ID   KNTC1_HUMAN             Reviewed;        2209 AA.
AC   P50748; A7E2C4; B3KSG2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 192.
DE   RecName: Full=Kinetochore-associated protein 1;
DE   AltName: Full=Rough deal homolog;
DE            Short=HsROD;
DE            Short=Rod;
DE            Short=hRod;
GN   Name=KNTC1; Synonyms=KIAA0166, ROD {ECO:0000303|PubMed:28441529};
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=Bone marrow;
RX   PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA   Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. V. The
RT   coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 3:17-24(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11146660; DOI=10.1038/35046598;
RA   Chan G.K.T., Jablonski S.A., Starr D.A., Goldberg M.L., Yen T.J.;
RT   "Human Zw10 and ROD are mitotic checkpoint proteins that bind to
RT   kinetochores.";
RL   Nat. Cell Biol. 2:944-947(2000).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11590237; DOI=10.1242/jcs.114.17.3103;
RA   Scaeerou F., Starr D.A., Piano F., Papoulas O., Karess R.E., Goldberg M.L.;
RT   "The ZW10 and Rough Deal checkpoint proteins function together in a large,
RT   evolutionarily conserved complex targeted to the kinetochore.";
RL   J. Cell Sci. 114:3103-3114(2001).
RN   [8]
RP   INTERACTION WITH ZWILCH AND ZW10.
RX   PubMed=12686595; DOI=10.1091/mbc.e02-09-0624;
RA   Williams B.C., Li Z., Liu S., Williams E.V., Leung G., Yen T.J.,
RA   Goldberg M.L.;
RT   "Zwilch, a new component of the ZW10/ROD complex required for kinetochore
RT   functions.";
RL   Mol. Biol. Cell 14:1379-1391(2003).
RN   [9]
RP   FUNCTION, AND IDENTIFICATION IN THE RZZ COMPLEX.
RX   PubMed=15824131; DOI=10.1083/jcb.200411118;
RA   Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I., Yates J.R. III,
RA   Tagaya M., Cleveland D.W.;
RT   "ZW10 links mitotic checkpoint signaling to the structural kinetochore.";
RL   J. Cell Biol. 169:49-60(2005).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
RP   INTERACTION WITH ZWILCH, AND IDENTIFICATION IN THE RRZ COMPLEX.
RX   PubMed=20462495; DOI=10.1016/j.str.2010.02.014;
RA   Civril F., Wehenkel A., Giorgi F.M., Santaguida S., Di Fonzo A.,
RA   Grigorean G., Ciccarelli F.D., Musacchio A.;
RT   "Structural analysis of the RZZ complex reveals common ancestry with
RT   multisubunit vesicle tethering machinery.";
RL   Structure 18:616-626(2010).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1035 AND SER-1045, 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).
RN   [14]
RP   PHOSPHORYLATION AT THR-13 AND SER-15.
RX   PubMed=28441529; DOI=10.1016/j.devcel.2017.03.025;
RA   Maciejowski J., Drechsler H., Grundner-Culemann K., Ballister E.R.,
RA   Rodriguez-Rodriguez J.A., Rodriguez-Bravo V., Jones M.J.K., Foley E.,
RA   Lampson M.A., Daub H., McAinsh A.D., Jallepalli P.V.;
RT   "Mps1 Regulates Kinetochore-Microtubule Attachment Stability via the Ska
RT   Complex to Ensure Error-Free Chromosome Segregation.";
RL   Dev. Cell 41:143-156(2017).
CC   -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC       cells from prematurely exiting mitosis. Required for the assembly of
CC       the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores
CC       (PubMed:11146660, PubMed:11590237, PubMed:15824131). Its function
CC       related to the spindle assembly machinery is proposed to depend on its
CC       association in the mitotic RZZ complex. {ECO:0000269|PubMed:11146660,
CC       ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15824131, ECO:0000305}.
CC   -!- SUBUNIT: Interacts with ZW10; the interaction is required for stable
CC       association with the kinetochore. Component of the RZZ complex composed
CC       of KNTC1/ROD, ZW10 and ZWILCH; in the complex interacts directly with
CC       ZWILCH. {ECO:0000269|PubMed:12686595, ECO:0000269|PubMed:15824131,
CC       ECO:0000269|PubMed:20462495}.
CC   -!- INTERACTION:
CC       P50748; Q9H900: ZWILCH; NbExp=2; IntAct=EBI-1001245, EBI-1001239;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere,
CC       kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Dynamic pattern of
CC       localization during the cell cycle. At interphase, uniformly
CC       distributed throughout the cytoplasm and nucleus. By prophase and until
CC       late stages of prometaphase, a fraction of the total pool is
CC       concentrated at kinetochores. By metaphase, detected at kinetochores,
CC       along spindle fibers and most prominently at the poles. By late
CC       anaphase until the end of telophase, no longer detectable on
CC       kinetochores or along spindle fibers, but still present at the spindle
CC       poles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P50748-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P50748-2; Sequence=VSP_057013, VSP_057014, VSP_057015;
CC   -!- TISSUE SPECIFICITY: High expression in testis.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA11483.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D79988; BAA11483.2; ALT_INIT; mRNA.
DR   EMBL; AK093470; BAG52724.1; -; mRNA.
DR   EMBL; AC026333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW98334.1; -; Genomic_DNA.
DR   EMBL; BC150278; AAI50279.1; -; mRNA.
DR   CCDS; CCDS45002.1; -. [P50748-1]
DR   RefSeq; NP_055523.1; NM_014708.6. [P50748-1]
DR   RefSeq; XP_006719769.1; XM_006719706.3. [P50748-1]
DR   RefSeq; XP_054229870.1; XM_054373895.1. [P50748-1]
DR   PDB; 7QPG; EM; 3.90 A; R/S=2-2209.
DR   AlphaFoldDB; P50748; -.
DR   EMDB; EMD-14120; -.
DR   SMR; P50748; -.
DR   BioGRID; 115084; 108.
DR   ComplexPortal; CPX-6017; RZZ complex.
DR   CORUM; P50748; -.
DR   DIP; DIP-36479N; -.
DR   FunCoup; P50748; 1813.
DR   IntAct; P50748; 93.
DR   NDEx; MUSIC2-C5180-KNTC1; Osteosarcoma (U2OS) cell map - C5180 (62 proteins).
DR   STRING; 9606.ENSP00000328236; -.
DR   BindingDB; P50748; -.
DR   ChEMBL; CHEMBL6066879; -.
DR   GlyGen; P50748; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P50748; -.
DR   PhosphoSitePlus; P50748; -.
DR   SwissPalm; P50748; -.
DR   BioMuta; KNTC1; -.
DR   DMDM; 1723117; -.
DR   jPOST; P50748; -.
DR   MassIVE; P50748; -.
DR   PaxDb; 9606-ENSP00000328236; -.
DR   PeptideAtlas; P50748; -.
DR   ProteomicsDB; 3637; -.
DR   ProteomicsDB; 56261; -. [P50748-1]
DR   Pumba; P50748; -.
DR   Antibodypedia; 9885; 128 antibodies from 20 providers.
DR   DNASU; 9735; -.
DR   Ensembl; ENST00000333479.12; ENSP00000328236.6; ENSG00000184445.12. [P50748-1]
DR   GeneID; 9735; -.
DR   KEGG; hsa:9735; -.
DR   MANE-Select; ENST00000333479.12; ENSP00000328236.6; NM_014708.6; NP_055523.1.
DR   UCSC; uc001ucv.4; human. [P50748-1]
DR   AGR; HGNC:17255; -.
DR   ClinPGx; PA30184; -.
DR   CTD; 9735; -.
DR   DisGeNET; 9735; -.
DR   GeneCards; KNTC1; -.
DR   HGNC; HGNC:17255; KNTC1.
DR   HPA; ENSG00000184445; Tissue enhanced (bone).
DR   MIM; 607363; gene.
DR   OpenTargets; ENSG00000184445; -.
DR   VEuPathDB; HostDB:ENSG00000184445; -.
DR   eggNOG; KOG4256; Eukaryota.
DR   GeneTree; ENSGT00390000007883; -.
DR   HOGENOM; CLU_231522_0_0_1; -.
DR   InParanoid; P50748; -.
DR   OMA; FYELYLC; -.
DR   OrthoDB; 343783at2759; -.
DR   PAN-GO; P50748; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; P50748; -.
DR   PathwayCommons; P50748; -.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   SignaLink; P50748; -.
DR   SIGNOR; P50748; -.
DR   Agora; ENSG00000184445; -.
DR   BioGRID-ORCS; 9735; 207 hits in 1168 CRISPR screens.
DR   ChiTaRS; KNTC1; human.
DR   GenomeRNAi; 9735; -.
DR   Pharos; P50748; Tbio.
DR   PRO; PR:P50748; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P50748; protein.
DR   Bgee; ENSG00000184445; Expressed in primordial germ cell in gonad and 146 other cell types or tissues.
DR   ExpressionAtlas; P50748; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:1990423; C:RZZ complex; IDA:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:UniProtKB.
DR   GO; GO:1903394; P:protein localization to kinetochore involved in kinetochore assembly; IBA:GO_Central.
DR   GO; GO:0065003; P:protein-containing complex assembly; NAS:UniProtKB.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; NAS:ComplexPortal.
DR   GO; GO:0007096; P:regulation of exit from mitosis; NAS:UniProtKB.
DR   InterPro; IPR055403; ARM_KNTC1_1st.
DR   InterPro; IPR055404; ARM_KNTC1_2nd.
DR   InterPro; IPR055405; ARM_KNTC1_3rd.
DR   InterPro; IPR052802; KNTC1.
DR   InterPro; IPR055402; KNTC1_N.
DR   InterPro; IPR019527; RZZ-complex_KNTC1/ROD_C.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR15688; KINETOCHORE-ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR15688:SF1; KINETOCHORE-ASSOCIATED PROTEIN 1; 1.
DR   Pfam; PF24520; ARM_KNTC1_1st; 1.
DR   Pfam; PF24516; ARM_KNTC1_2nd; 1.
DR   Pfam; PF24515; ARM_KNTC1_3rd; 1.
DR   Pfam; PF24506; KNTC1_N; 1.
DR   Pfam; PF10493; Rod_C; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PDBsum; 7QPG; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW   Chromosome; Cytoplasm; Cytoskeleton; Kinetochore; Mitosis; Nucleus;
KW   Phosphoprotein; Proteomics identification; Reference proteome.
FT   CHAIN           1..2209
FT                   /note="Kinetochore-associated protein 1"
FT                   /id="PRO_0000084312"
FT   MOD_RES         13
FT                   /note="Phosphothreonine; by TTK"
FT                   /evidence="ECO:0000269|PubMed:28441529"
FT   MOD_RES         15
FT                   /note="Phosphoserine; by TTK"
FT                   /evidence="ECO:0000269|PubMed:28441529"
FT   MOD_RES         1035
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1045
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..1575
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057013"
FT   VAR_SEQ         2011..2018
FT                   /note="VPYFSKAW -> RWRSCYVA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057014"
FT   VAR_SEQ         2019..2209
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_057015"
FT   VARIANT         245
FT                   /note="K -> N (in dbSNP:rs7968222)"
FT                   /id="VAR_051082"
FT   VARIANT         738
FT                   /note="E -> D (in dbSNP:rs17883249)"
FT                   /id="VAR_051083"
FT   VARIANT         1506
FT                   /note="T -> M (in dbSNP:rs35315099)"
FT                   /id="VAR_051084"
FT   VARIANT         1830
FT                   /note="P -> L (in dbSNP:rs7310898)"
FT                   /id="VAR_051085"
FT   VARIANT         2021
FT                   /note="V -> G (in dbSNP:rs11837038)"
FT                   /id="VAR_051086"
SQ   SEQUENCE   2209 AA;  250749 MW;  514C948733CBFDAC CRC64;
     MWNDIELLTN DDTGSGYLSV GSRKEHGTAL YQVDLLVKIS SEKASLNPKI QACSLSDGFI
     IVADQSVILL DSICRSLQLH LVFDTEVDVV GLCQEGKFLL VGERSGNLHL IHVTSKQTLL
     TNAFVQKAND ENRRTYQNLV IEKDGSNEGT YYMLLLTYSG FFCITNLQLL KIQQAIENVD
     FSTAKKLQGQ IKSSFISTEN YHTLGCLSLV AGDLASEVPV IIGGTGNCAF SKWEPDSSKK
     GMTVKNLIDA EIIKGAKKFQ LIDNLLFVLD TDNVLSLWDI YTLTPVWNWP SLHVEEFLLT
     TEADSPSSVT WQGITNLKLI ALTASANKKM KNLMVYSLPT MEILYSLEVS SVSSLVQTGI
     STDTIYLLEG VCKNDPKLSE DSVSVLVLRC LTEALPENRL SRLLHKHRFA EAESFAIQFG
     LDVELVYKVK SNHILEKLAL SSVDASEQTE WQQLVDDAKE NLHKIQDDEF VVNYCLKAQW
     ITYETTQEML NYAKTRLLKK EDKTALIYSD GLKEVLRAHA KLTTFYGAFG PEKFSGSSWI
     EFLNNEDDLK DIFLQLKEGN LVCAQYLWLR HRANFESRFD VKMLESLLNS MSASVSLQKL
     CPWFKNDVIP FVRRTVPEGQ IILAKWLEQA ARNLELTDKA NWPENGLQLA EIFFTAEKTD
     ELGLASSWHW ISLKDYQNTE EVCQLRTLVN NLRELITLHR KYNCKLALSD FEKENTTTIV
     FRMFDKVLAP ELIPSILEKF IRVYMREHDL QEEELLLLYI EDLLNRCSSK STSLFETAWE
     AKAMAVIACL SDTDLIFDAV LKIMYAAVVP WSAAVEQLVK QHLEMDHPKV KLLQESYKLM
     EMKKLLRGYG IREVNLLNKE IMRVVRYILK QDVPSSLEDA LKVAQAFMLS DDEIYSLRII
     DLIDREQGED CLLLLKSLPP AEAEKTAERV IIWARLALQE EPDHSKEGKA WRMSVAKTSV
     DILKILCDIQ KDNLQKKDEC EEMLKLFKEV ASLQENFEVF LSFEDYSNSS LVADLREQHI
     KAHEVAQAKH KPGSTPEPIA AEVRSPSMES KLHRQALALQ MSKQELEAEL TLRALKDGNI
     KTALKKCSDL FKYHCNADTG KLLFLTCQKL CQMLADNVPV TVPVGLNLPS MIHDLASQAA
     TICSPDFLLD ALELCKHTLM AVELSRQCQM DDCGILMKAS FGTHKDPYEE WSYSDFFSED
     GIVLESQMVL PVIYELISSL VPLAESKRYP LESTSLPYCS LNEGDGLVLP VINSISALLQ
     NLQESSQWEL ALRFVVGSFG TCLQHSVSNF MNATLSEKLF GETTLVKSRH VVMELKEKAV
     IFIRENATTL LHKVFNCRLV DLDLALGYCT LLPQKDVFEN LWKLIDKAWQ NYDKILAISL
     VGSELASLYQ EIEMGLKFRE LSTDAQWGIR LGKLGISFQP VFRQHFLTKK DLIKALVENI
     DMDTSLILEY CSTFQLDCDA VLQLFIETLL HNTNAGQGQG DASMDSAKRR HPKLLAKALE
     MVPLLTSTKD LVISLSGILH KLDPYDYEMI EVVLKVIERA DEKITNININ QALSILKHLK
     SYRRISPPVD LEYQYMLEHV ITLPSAAQTR LPFHLIFFGT AQNFWKILST ELSEESFPTL
     LLISKLMKFS LDTLYVSTAK HVFEKKLKPK LLKLTQAKSS TLINKEITKI TQTIESCLLS
     IVNPEWAVAI AISLAQDIPE GSFKISALKF CLYLAERWLQ NIPSQDEKRE KAEALLKKLH
     IQYRRSGTEA VLIAHKLNTE EYLRVIGKPA HLIVSLYEHP SINQRIQNSS GTDYPDIHAA
     AKEIAEVNEI NLEKVWDMLL EKWLCPSTKP GEKPSELFEL QEDEALRRVQ YLLLSRPIDY
     SSRMLFVFAT STTTTLGMHQ LTFAHRTRAL QCLFYLADKE TIESLFKKPI EEVKSYLRCI
     TFLASFETLN IPITYELFCS SPKEGMIKGL WKNHSHESMA VRLVTELCLE YKIYDLQLWN
     GLLQKLLGFN MIPYLRKVLK AISSIHSLWQ VPYFSKAWQR VIQIPLLSAS CPLSPDQLSD
     CSESLIAVLE CPVSGDLDLI GVARQYIQLE LPAFALACLM LMPHSEKRHQ QIKNFLGSCD
     PQVILKQLEE HMNTGQLAGF SHQIRSLILN NIINKKEFGI LAKTKYFQML KMHAMNTNNI
     TELVNYLAND LSLDEASVLI TEYSKHCGKP VPPDTAPCEI LKMFLSGLS
//