ID   SPN90_HUMAN             Reviewed;         722 AA.
AC   Q9NZQ3; B4DFL5; Q6GU34; Q6SPF3; Q8TC10; Q9UGM8;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   29-MAY-2024, entry version 197.
DE   RecName: Full=NCK-interacting protein with SH3 domain;
DE   AltName: Full=54 kDa VacA-interacting protein;
DE   AltName: Full=54 kDa vimentin-interacting protein;
DE            Short=VIP54;
DE   AltName: Full=90 kDa SH3 protein interacting with Nck;
DE   AltName: Full=AF3p21;
DE   AltName: Full=Dia-interacting protein 1;
DE            Short=DIP-1;
DE   AltName: Full=Diaphanous protein-interacting protein;
DE   AltName: Full=SH3 adapter protein SPIN90;
DE   AltName: Full=WASP-interacting SH3-domain protein;
DE            Short=WISH;
DE   AltName: Full=Wiskott-Aldrich syndrome protein-interacting protein;
GN   Name=NCKIPSD; Synonyms=AF3P21, SPIN90;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION WITH
RP   KMT2A/MLL1.
RC   TISSUE=Leukemia;
RX   PubMed=10648423;
RA   Sano K., Hayakawa A., Piao J.-H., Kosaka Y., Nakamura H.;
RT   "Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage
RT   leukemia protein in a therapy-related leukemia with t(3;11)(p21;q23).";
RL   Blood 95:1066-1068(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH VACA, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=10619843; DOI=10.1093/emboj/19.1.48;
RA   de Bernard M., Moschioni M., Napolitani G., Rappuoli R., Montecucco C.;
RT   "The VacA toxin of Helicobacter pylori identifies a new intermediate
RT   filament-interacting protein.";
RL   EMBO J. 19:48-56(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC   TISSUE=Cervix carcinoma;
RX   PubMed=11241789; DOI=10.1002/gcc.1102;
RA   Hayakawa A., Matsuda Y., Daibata M., Nakamura H., Sano K.;
RT   "Genomic organization, tissue expression and cellular localization of
RT   AF3p21, a fusion partner of MLL in therapy-related leukemia.";
RL   Genes Chromosomes Cancer 30:364-374(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   PubMed=11278500; DOI=10.1074/jbc.m009411200;
RA   Lim C.S., Park E.S., Kim D.J., Song Y.H., Eom S.H., Chun J.-S., Kim J.H.,
RA   Kim J.-K., Park D., Song W.K.;
RT   "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adapter protein that
RT   is developmentally regulated during cardiac myocyte differentiation.";
RL   J. Biol. Chem. 276:12871-12878(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP   2).
RC   TISSUE=Brain, and Placenta;
RX   PubMed=11509578; DOI=10.1074/jbc.m107026200;
RA   Satoh S., Tominaga T.;
RT   "mDia-interacting protein acts downstream of rho-mDia and modifies src
RT   activation and stress fiber formation.";
RL   J. Biol. Chem. 276:39290-39294(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH FHOD1.
RC   TISSUE=Bone marrow;
RX   PubMed=15095401; DOI=10.1002/jcb.20031;
RA   Westendorf J.J., Koka S.;
RT   "Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated
RT   actin dynamics.";
RL   J. Cell. Biochem. 92:29-41(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT SER-660.
RC   TISSUE=Placenta, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-722 (ISOFORM 5).
RC   TISSUE=Brain cortex;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [11]
RP   INTERACTION WITH FASLG.
RX   PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA   Voss M., Lettau M., Janssen O.;
RT   "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT   phage display screening.";
RL   BMC Immunol. 10:53-53(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   FUNCTION IN ANGIOGENESIS, AND INTERACTION WITH TMIGD2.
RX   PubMed=22419821; DOI=10.1091/mbc.e11-11-0934;
RA   Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.;
RT   "Identification of IGPR-1 as a novel adhesion molecule involved in
RT   angiogenesis.";
RL   Mol. Biol. Cell 23:1646-1656(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Has an important role in stress fiber formation induced by
CC       active diaphanous protein homolog 1 (DRF1). Induces microspike
CC       formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced
CC       ARP2/3 complex activation in the absence of CDC42 (By similarity). May
CC       play an important role in the maintenance of sarcomeres and/or in the
CC       assembly of myofibrils into sarcomeres. Implicated in regulation of
CC       actin polymerization and cell adhesion. Plays a role in angiogenesis.
CC       {ECO:0000250, ECO:0000269|PubMed:22419821}.
CC   -!- SUBUNIT: Associates with the intermediate filaments, vimentin and
CC       desmin. Binds the first and third SH3 domains of NCK. Binds the
CC       proline-rich domains of N-WASP through its SH3 domain (By similarity).
CC       Similarly, binds diaphanous protein homolog 1 (DRF1). Binds the SH3
CC       domains of GRB2 through its proline-rich domains. Interacts with
CC       Helicobacter pylori toxin vacA. Isoform 4 interacts with FHOD1.
CC       Interacts with FASLG. Interacts with TMIGD2. {ECO:0000250,
CC       ECO:0000269|PubMed:10619843, ECO:0000269|PubMed:15095401,
CC       ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:22419821}.
CC   -!- INTERACTION:
CC       Q9NZQ3; Q9UQB8: BAIAP2; NbExp=2; IntAct=EBI-745080, EBI-525456;
CC       Q9NZQ3; P06241: FYN; NbExp=2; IntAct=EBI-745080, EBI-515315;
CC       Q9NZQ3; O00233: PSMD9; NbExp=4; IntAct=EBI-745080, EBI-750973;
CC       Q9NZQ3; O60504: SORBS3; NbExp=3; IntAct=EBI-745080, EBI-741237;
CC       Q9NZQ3; Q60437: BAIAP2; Xeno; NbExp=3; IntAct=EBI-745080, EBI-7010040;
CC       Q9NZQ3; Q9Z0W5: Pacsin1; Xeno; NbExp=6; IntAct=EBI-745080, EBI-1550185;
CC       Q9NZQ3; Q9QY17: Pacsin2; Xeno; NbExp=2; IntAct=EBI-745080, EBI-491201;
CC       Q9NZQ3-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-10963850, EBI-11096309;
CC       Q9NZQ3-3; Q96FN4: CPNE2; NbExp=3; IntAct=EBI-10963850, EBI-7097057;
CC       Q9NZQ3-3; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-10963850, EBI-744099;
CC       Q9NZQ3-3; O60861-1: GAS7; NbExp=5; IntAct=EBI-10963850, EBI-11745923;
CC       Q9NZQ3-3; P56470: LGALS4; NbExp=3; IntAct=EBI-10963850, EBI-720805;
CC       Q9NZQ3-3; Q71SY5: MED25; NbExp=3; IntAct=EBI-10963850, EBI-394558;
CC       Q9NZQ3-3; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-10963850, EBI-14086479;
CC       Q9NZQ3-3; O43639: NCK2; NbExp=3; IntAct=EBI-10963850, EBI-713635;
CC       Q9NZQ3-3; Q13526: PIN1; NbExp=3; IntAct=EBI-10963850, EBI-714158;
CC       Q9NZQ3-3; Q99959-2: PKP2; NbExp=3; IntAct=EBI-10963850, EBI-10987518;
CC       Q9NZQ3-3; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-10963850, EBI-5452779;
CC       Q9NZQ3-3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-10963850, EBI-1567797;
CC       Q9NZQ3-3; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-10963850, EBI-11974061;
CC       Q9NZQ3-3; Q9NW64: RBM22; NbExp=5; IntAct=EBI-10963850, EBI-2602260;
CC       Q9NZQ3-3; Q96R05: RBP7; NbExp=3; IntAct=EBI-10963850, EBI-2856326;
CC       Q9NZQ3-3; P09234: SNRPC; NbExp=3; IntAct=EBI-10963850, EBI-766589;
CC       Q9NZQ3-3; Q99469: STAC; NbExp=3; IntAct=EBI-10963850, EBI-2652799;
CC       Q9NZQ3-3; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-10963850, EBI-2559824;
CC       Q9NZQ3-3; Q14119: VEZF1; NbExp=3; IntAct=EBI-10963850, EBI-11980193;
CC       Q9NZQ3-3; Q9UFB7: ZBTB47; NbExp=3; IntAct=EBI-10963850, EBI-7781767;
CC       Q9NZQ3-3; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-10963850, EBI-14104088;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with DRF1 at membrane
CC       ruffles, and with Nck at Z-disks in mature cardiac myocytes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9NZQ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NZQ3-2; Sequence=VSP_003971;
CC       Name=3;
CC         IsoId=Q9NZQ3-3; Sequence=VSP_039422;
CC       Name=4; Synonyms=WISH-B;
CC         IsoId=Q9NZQ3-4; Sequence=VSP_039422, VSP_039425, VSP_039426;
CC       Name=5;
CC         IsoId=Q9NZQ3-5; Sequence=VSP_039423, VSP_039424;
CC   -!- TISSUE SPECIFICITY: Highest expression in heart, brain, skeletal
CC       muscle, kidney and liver. Lower levels in placenta, lung, small
CC       intestine and leukocytes. Weak expression in colon, thymus and spleen.
CC       {ECO:0000269|PubMed:10619843}.
CC   -!- DISEASE: Note=A chromosomal aberration involving NCKIPSD/AF3p21 is
CC       found in therapy-related leukemia. Translocation t(3;11)(p21;q23) with
CC       KMT2A/MLL1. {ECO:0000269|PubMed:10648423}.
CC   -!- MISCELLANEOUS: [Isoform 5]: Found in a brain affected by Alzheimer
CC       disease. May be due to intron retention. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG57476.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/228/AF3p21";
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DR   EMBL; AF178432; AAF35985.1; -; mRNA.
DR   EMBL; AJ242655; CAB65089.2; -; mRNA.
DR   EMBL; AF303581; AAK09094.1; -; mRNA.
DR   EMBL; AB069981; BAB63204.1; -; Genomic_DNA.
DR   EMBL; AB069982; BAB63205.1; -; Genomic_DNA.
DR   EMBL; AY453794; AAR83735.1; -; mRNA.
DR   EMBL; AC141002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016052; AAH16052.1; -; mRNA.
DR   EMBL; BC026280; AAH26280.1; -; mRNA.
DR   EMBL; AK294151; BAG57476.1; ALT_INIT; mRNA.
DR   CCDS; CCDS2776.1; -. [Q9NZQ3-1]
DR   CCDS; CCDS46827.1; -. [Q9NZQ3-3]
DR   RefSeq; NP_057537.1; NM_016453.3. [Q9NZQ3-1]
DR   RefSeq; NP_909119.1; NM_184231.2. [Q9NZQ3-3]
DR   PDB; 6DEC; X-ray; 4.60 A; M/P=269-722.
DR   PDB; 6DED; X-ray; 2.20 A; A/B=350-722.
DR   PDB; 6DEE; X-ray; 3.04 A; A=306-722.
DR   PDBsum; 6DEC; -.
DR   PDBsum; 6DED; -.
DR   PDBsum; 6DEE; -.
DR   AlphaFoldDB; Q9NZQ3; -.
DR   SMR; Q9NZQ3; -.
DR   BioGRID; 119583; 126.
DR   IntAct; Q9NZQ3; 100.
DR   MINT; Q9NZQ3; -.
DR   STRING; 9606.ENSP00000294129; -.
DR   GlyCosmos; Q9NZQ3; 1 site, 1 glycan.
DR   GlyGen; Q9NZQ3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NZQ3; -.
DR   MetOSite; Q9NZQ3; -.
DR   PhosphoSitePlus; Q9NZQ3; -.
DR   BioMuta; NCKIPSD; -.
DR   DMDM; 17433253; -.
DR   EPD; Q9NZQ3; -.
DR   jPOST; Q9NZQ3; -.
DR   MassIVE; Q9NZQ3; -.
DR   MaxQB; Q9NZQ3; -.
DR   PaxDb; 9606-ENSP00000294129; -.
DR   PeptideAtlas; Q9NZQ3; -.
DR   ProteomicsDB; 83478; -. [Q9NZQ3-1]
DR   ProteomicsDB; 83479; -. [Q9NZQ3-2]
DR   ProteomicsDB; 83480; -. [Q9NZQ3-3]
DR   ProteomicsDB; 83481; -. [Q9NZQ3-4]
DR   ProteomicsDB; 83482; -. [Q9NZQ3-5]
DR   Pumba; Q9NZQ3; -.
DR   Antibodypedia; 30227; 158 antibodies from 28 providers.
DR   DNASU; 51517; -.
DR   Ensembl; ENST00000294129.7; ENSP00000294129.2; ENSG00000213672.8. [Q9NZQ3-1]
DR   Ensembl; ENST00000416649.6; ENSP00000389059.2; ENSG00000213672.8. [Q9NZQ3-3]
DR   GeneID; 51517; -.
DR   KEGG; hsa:51517; -.
DR   MANE-Select; ENST00000294129.7; ENSP00000294129.2; NM_016453.4; NP_057537.1.
DR   UCSC; uc003cum.5; human. [Q9NZQ3-1]
DR   AGR; HGNC:15486; -.
DR   CTD; 51517; -.
DR   DisGeNET; 51517; -.
DR   GeneCards; NCKIPSD; -.
DR   HGNC; HGNC:15486; NCKIPSD.
DR   HPA; ENSG00000213672; Tissue enhanced (parathyroid).
DR   MIM; 606671; gene.
DR   neXtProt; NX_Q9NZQ3; -.
DR   OpenTargets; ENSG00000213672; -.
DR   PharmGKB; PA134872724; -.
DR   VEuPathDB; HostDB:ENSG00000213672; -.
DR   eggNOG; KOG4035; Eukaryota.
DR   GeneTree; ENSGT00390000015725; -.
DR   HOGENOM; CLU_012978_1_0_1; -.
DR   InParanoid; Q9NZQ3; -.
DR   OMA; CFARIFC; -.
DR   OrthoDB; 2915651at2759; -.
DR   PhylomeDB; Q9NZQ3; -.
DR   TreeFam; TF324522; -.
DR   PathwayCommons; Q9NZQ3; -.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR   SignaLink; Q9NZQ3; -.
DR   SIGNOR; Q9NZQ3; -.
DR   BioGRID-ORCS; 51517; 12 hits in 1156 CRISPR screens.
DR   ChiTaRS; NCKIPSD; human.
DR   GeneWiki; NCKIPSD; -.
DR   GenomeRNAi; 51517; -.
DR   Pharos; Q9NZQ3; Tbio.
DR   PRO; PR:Q9NZQ3; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9NZQ3; Protein.
DR   Bgee; ENSG00000213672; Expressed in right frontal lobe and 183 other cell types or tissues.
DR   ExpressionAtlas; Q9NZQ3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR   GO; GO:0008092; F:cytoskeletal protein binding; NAS:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0000147; P:actin cortical patch assembly; IEA:TreeGrafter.
DR   GO; GO:0051666; P:actin cortical patch localization; IEA:TreeGrafter.
DR   GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   CDD; cd11849; SH3_SPIN90; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR030125; SPIN90/Ldb17.
DR   InterPro; IPR018556; SPIN90/Ldb17_LRD.
DR   InterPro; IPR035514; SPIN90_SH3.
DR   PANTHER; PTHR13357:SF1; NCK-INTERACTING PROTEIN WITH SH3 DOMAIN; 1.
DR   PANTHER; PTHR13357; SH3 ADAPTER PROTEIN SPIN90 NCK INTERACTING PROTEIN WITH SH3 DOMAIN; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF09431; SPIN90_LRD; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromosomal rearrangement; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; SH3 domain;
KW   SH3-binding.
FT   CHAIN           1..722
FT                   /note="NCK-interacting protein with SH3 domain"
FT                   /id="PRO_0000072130"
FT   DOMAIN          1..58
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          101..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           175..192
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        107..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..184
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            57..58
FT                   /note="Breakpoint for translocation to form KMT2A/MLL1-
FT                   AF3P21 oncogene"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ESJ4"
FT   MOD_RES         181
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ESJ4"
FT   VAR_SEQ         165..171
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15095401,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_039422"
FT   VAR_SEQ         567..596
FT                   /note="AADQNVIMAALSKHANVKIFSEKLLLLLNR -> GGVGPGWAVAEHMVALRL
FT                   STLSIPMSFLSC (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039423"
FT   VAR_SEQ         597..722
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039424"
FT   VAR_SEQ         656..722
FT                   /note="LRMEYLSLMHAIVRTTPYLQHRHRLPDLQAILRRILNEEETSPQCQMDRMIV
FT                   REMCKEFLVLGEAPS -> GPFGAGQRPWPGVPRLLEPGSTPSREPHPVERSGVPALTS
FT                   SWASGCPRPLHPALQLVIDSAFGGRSV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10619843"
FT                   /id="VSP_003971"
FT   VAR_SEQ         656..658
FT                   /note="LRM -> GVH (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15095401"
FT                   /id="VSP_039425"
FT   VAR_SEQ         659..722
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15095401"
FT                   /id="VSP_039426"
FT   VARIANT         324
FT                   /note="T -> S (in dbSNP:rs6785620)"
FT                   /id="VAR_051378"
FT   VARIANT         660
FT                   /note="Y -> S (in dbSNP:rs17855516)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_063400"
FT   HELIX           312..324
FT                   /evidence="ECO:0007829|PDB:6DEE"
FT   HELIX           328..345
FT                   /evidence="ECO:0007829|PDB:6DEE"
FT   HELIX           350..359
FT                   /evidence="ECO:0007829|PDB:6DEE"
FT   HELIX           377..390
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           401..404
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           407..423
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           426..450
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           454..470
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           472..480
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           483..493
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           498..511
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   TURN            512..514
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           520..524
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           528..539
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           550..562
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   STRAND          568..570
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           572..578
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           584..596
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           613..621
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           625..628
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           633..649
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           657..670
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           673..676
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           680..691
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           698..713
FT                   /evidence="ECO:0007829|PDB:6DED"
FT   HELIX           715..717
FT                   /evidence="ECO:0007829|PDB:6DED"
SQ   SEQUENCE   722 AA;  78960 MW;  7683046B94647332 CRC64;
     MYRALYAFRS AEPNALAFAA GETFLVLERS SAHWWLAARA RSGETGYVPP AYLRRLQGLE
     QDVLQAIDRA IEAVHNTAMR DGGKYSLEQR GVLQKLIHHR KETLSRRGPS ASSVAVMTSS
     TSDHHLDAAA ARQPNGVCRA GFERQHSLPS SEHLGADGGL YQIPLPSSQI PPQPRRAAPT
     TPPPPVKRRD REALMASGSG GHNTMPSGGN SVSSGSSVSS TSLDTLYTSS SPSEPGSSCS
     PTPPPVPRRG THTTVSQVQP PPSKASAPEP PAEEEVATGT TSASDDLEAL GTLSLGTTEE
     KAAAEAAVPR TIGAELMELV RRNTGLSHEL CRVAIGIIVG HIQASVPASS PVMEQVLLSL
     VEGKDLSMAL PSGQVCHDQQ RLEVIFADLA RRKDDAQQRS WALYEDEGVI RCYLEELLHI
     LTDADPEVCK KMCKRNEFES VLALVAYYQM EHRASLRLLL LKCFGAMCSL DAAIISTLVS
     SVLPVELARD MQTDTQDHQK LCYSALILAM VFSMGEAVPY AHYEHLGTPF AQFLLNIVED
     GLPLDTTEQL PDLCVNLLLA LNLHLPAADQ NVIMAALSKH ANVKIFSEKL LLLLNRGDDP
     VRIFKHEPQP PHSVLKFLQD VFGSPATAAI FYHTDMMALI DITVRHIADL SPGDKLRMEY
     LSLMHAIVRT TPYLQHRHRL PDLQAILRRI LNEEETSPQC QMDRMIVREM CKEFLVLGEA
     PS
//