ID   STRP2_HUMAN             Reviewed;         834 AA.
AC   Q9ULQ0; Q8WUZ4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Striatin-interacting protein 2;
DE   AltName: Full=Protein FAM40B;
GN   Name=STRIP2; Synonyms=FAM40B, KIAA1170;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
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   [4]
RP   INTERACTION WITH CTTNBP2NL.
RX   PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA   Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA   Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA   Aebersold R., Raught B., Gingras A.C.;
RT   "A PP2A phosphatase high density interaction network identifies a novel
RT   striatin-interacting phosphatase and kinase complex linked to the cerebral
RT   cavernous malformation 3 (CCM3) protein.";
RL   Mol. Cell. Proteomics 8:157-171(2009).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA   Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA   Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT   "Identification and characterization of a set of conserved and new
RT   regulators of cytoskeletal organisation, cell morphology and migration.";
RL   BMC Biol. 9:54-54(2011).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318; SER-329 AND SER-354, AND
RP   IDENTIFICATION BY 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).
CC   -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC       cytoskeletal organization. Required in the control of cell shape.
CC       {ECO:0000269|PubMed:21834987}.
CC   -!- SUBUNIT: Component of striatin-interacting phosphatase and kinase
CC       (STRIPAK) complex (By similarity). Interacts with CTTNBP2NL.
CC       {ECO:0000250, ECO:0000269|PubMed:18782753}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21834987}.
CC       Note=Enriched in lamellipodia.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ULQ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ULQ0-2; Sequence=VSP_014867, VSP_014868;
CC   -!- SIMILARITY: Belongs to the STRIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86484.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB032996; BAA86484.1; ALT_INIT; mRNA.
DR   EMBL; AC009244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC019064; AAH19064.1; -; mRNA.
DR   CCDS; CCDS34752.1; -. [Q9ULQ0-1]
DR   CCDS; CCDS47709.1; -. [Q9ULQ0-2]
DR   RefSeq; NP_001127808.1; NM_001134336.1. [Q9ULQ0-2]
DR   RefSeq; NP_065755.1; NM_020704.2. [Q9ULQ0-1]
DR   AlphaFoldDB; Q9ULQ0; -.
DR   SMR; Q9ULQ0; -.
DR   BioGRID; 121534; 36.
DR   DIP; DIP-51635N; -.
DR   IntAct; Q9ULQ0; 25.
DR   MINT; Q9ULQ0; -.
DR   STRING; 9606.ENSP00000249344; -.
DR   iPTMnet; Q9ULQ0; -.
DR   PhosphoSitePlus; Q9ULQ0; -.
DR   SwissPalm; Q9ULQ0; -.
DR   BioMuta; STRIP2; -.
DR   DMDM; 71151881; -.
DR   EPD; Q9ULQ0; -.
DR   jPOST; Q9ULQ0; -.
DR   MassIVE; Q9ULQ0; -.
DR   MaxQB; Q9ULQ0; -.
DR   PaxDb; 9606-ENSP00000249344; -.
DR   PeptideAtlas; Q9ULQ0; -.
DR   ProteomicsDB; 85092; -. [Q9ULQ0-1]
DR   ProteomicsDB; 85093; -. [Q9ULQ0-2]
DR   Pumba; Q9ULQ0; -.
DR   Antibodypedia; 17893; 63 antibodies from 20 providers.
DR   DNASU; 57464; -.
DR   Ensembl; ENST00000249344.7; ENSP00000249344.2; ENSG00000128578.10. [Q9ULQ0-1]
DR   Ensembl; ENST00000435494.2; ENSP00000392393.2; ENSG00000128578.10. [Q9ULQ0-2]
DR   GeneID; 57464; -.
DR   KEGG; hsa:57464; -.
DR   MANE-Select; ENST00000249344.7; ENSP00000249344.2; NM_020704.3; NP_065755.1.
DR   UCSC; uc003vow.5; human. [Q9ULQ0-1]
DR   AGR; HGNC:22209; -.
DR   CTD; 57464; -.
DR   DisGeNET; 57464; -.
DR   GeneCards; STRIP2; -.
DR   HGNC; HGNC:22209; STRIP2.
DR   HPA; ENSG00000128578; Tissue enhanced (brain, choroid plexus, skeletal muscle).
DR   MIM; 617919; gene.
DR   neXtProt; NX_Q9ULQ0; -.
DR   OpenTargets; ENSG00000128578; -.
DR   PharmGKB; PA134923427; -.
DR   VEuPathDB; HostDB:ENSG00000128578; -.
DR   eggNOG; KOG3680; Eukaryota.
DR   GeneTree; ENSGT00400000022095; -.
DR   HOGENOM; CLU_011008_1_0_1; -.
DR   InParanoid; Q9ULQ0; -.
DR   OMA; KMTRAMR; -.
DR   OrthoDB; 5491701at2759; -.
DR   PhylomeDB; Q9ULQ0; -.
DR   TreeFam; TF314205; -.
DR   PathwayCommons; Q9ULQ0; -.
DR   SignaLink; Q9ULQ0; -.
DR   BioGRID-ORCS; 57464; 9 hits in 1152 CRISPR screens.
DR   ChiTaRS; STRIP2; human.
DR   GenomeRNAi; 57464; -.
DR   Pharos; Q9ULQ0; Tbio.
DR   PRO; PR:Q9ULQ0; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9ULQ0; Protein.
DR   Bgee; ENSG00000128578; Expressed in pigmented layer of retina and 143 other cell types or tissues.
DR   Genevisible; Q9ULQ0; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR   InterPro; IPR040185; Far11/STRP.
DR   InterPro; IPR021819; Far11/STRP_C.
DR   InterPro; IPR012486; Far11/STRP_N.
DR   PANTHER; PTHR13239; PROTEIN REQUIRED FOR HYPHAL ANASTOMOSIS HAM-2; 1.
DR   PANTHER; PTHR13239:SF6; STRIATIN-INTERACTING PROTEIN 2; 1.
DR   Pfam; PF11882; DUF3402; 2.
DR   Pfam; PF07923; N1221; 1.
DR   SMART; SM01293; DUF3402; 1.
DR   SMART; SM01292; N1221; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..834
FT                   /note="Striatin-interacting protein 2"
FT                   /id="PRO_0000187022"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         752..758
FT                   /note="DIDARPW -> GESSQSS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014867"
FT   VAR_SEQ         759..834
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014868"
FT   VARIANT         383
FT                   /note="R -> Q (in dbSNP:rs2242030)"
FT                   /id="VAR_049021"
SQ   SEQUENCE   834 AA;  95360 MW;  3DAF1DA8FD6E4C4D CRC64;
     MEDPAAPGTG GPPANGNGNG GGKGKQAAPK GREAFRSQRR ESEGSVDCPT LEFEYGDADG
     HAAELSELYS YTENLEFTNN RRCFEEDFKT QVQGKEWLEL EEDAQKAYIM GLLDRLEVVS
     RERRLKVARA VLYLAQGTFG ECDSEVDVLH WSRYNCFLLY QMGTFSTFLE LLHMEIDNSQ
     ACSSALRKPA VSIADSTELR VLLSVMYLMV ENIRLERETD PCGWRTARET FRTELSFSMH
     NEEPFALLLF SMVTKFCSGL APHFPIKKVL LLLWKVVMFT LGGFEHLQTL KVQKRAELGL
     PPLAEDSIQV VKSMRAASPP SYTLDLGESQ LAPPPSKLRG RRGSRRQLLT KQDSLDIYNE
     RDLFKTEEPA TEEEEESAGD GERTLDGELD LLEQDPLVPP PPSQAPLSAE RVAFPKGLPW
     APKVRQKDIE HFLEMSRNKF IGFTLGQDTD TLVGLPRPIH ESVKTLKQHK YISIADVQIK
     NEEELEKCPM SLGEEVVPET PCEILYQGML YSLPQYMIAL LKILLAAAPT SKAKTDSINI
     LADVLPEEMP ITVLQSMKLG IDVNRHKEII VKSISTLLLL LLKHFKLNHI YQFEYVSQHL
     VFANCIPLIL KFFNQNILSY ITAKNSISVL DYPCCTIQDL PELTTESLEA GDNSQFCWRN
     LFSCINLLRL LNKLTKWKHS RTMMLVVFKS APILKRALKV KQAMLQLYVL KLLKLQTKYL
     GRQWRKSNMK TMSAIYQKVR HRMNDDWAYG NDIDARPWDF QAEECTLRAN IEAFNSRRYD
     RPQDSEFSPV DNCLQSVLGQ RLDLPEDFHY SYELWLEREV FSQPICWEEL LQNH
//