SKAP_HUMAN
ID SKAP_HUMAN Reviewed; 316 AA.
AC Q9Y448; B4DXA7; Q147U5; Q32Q57; Q5ISJ0; Q6P2S5; Q6PJM0; Q86XB4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Small kinetochore-associated protein {ECO:0000303|PubMed:19667759};
DE Short=SKAP {ECO:0000303|PubMed:19667759};
DE AltName: Full=Kinetochore-localized astrin-binding protein {ECO:0000303|PubMed:21402792};
DE Short=Kinastrin {ECO:0000303|PubMed:21402792};
DE AltName: Full=Kinetochore-localized astrin/SPAG5-binding protein;
DE AltName: Full=TRAF4-associated factor 1;
GN Name=KNSTRN {ECO:0000312|HGNC:HGNC:30767};
GN Synonyms=C15orf23 {ECO:0000312|HGNC:HGNC:30767},
GN SKAP {ECO:0000303|PubMed:19667759}, TRAF4AF1; ORFNames=HSD11;
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=Testis;
RA Cai C.L., Liu N., Lin W., Miao S.Y., Wang L.F.;
RT "A spermatogenesis related gene expressed in nucleus.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-40;
RP LEU-75 AND SER-92.
RC TISSUE=Kidney, Ovary, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-316 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-316 (ISOFORM 2).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-316 (ISOFORM 1).
RA Touji S., Yano M., Kobayasi A., Tamai K.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION BY NITRIC OXIDE.
RX PubMed=15855057; DOI=10.1016/j.freeradbiomed.2005.02.002;
RA Turpaev K., Bouton C., Diet A., Glatigny A., Drapier J.-C.;
RT "Analysis of differentially expressed genes in nitric oxide-exposed human
RT monocytic cells.";
RL Free Radic. Biol. Med. 38:1392-1400(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19667759; DOI=10.4161/cc.8.17.9514;
RA Fang L., Seki A., Fang G.;
RT "SKAP associates with kinetochores and promotes the metaphase-to-anaphase
RT transition.";
RL Cell Cycle 8:2819-2827(2009).
RN [10]
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH SPAG5;
RP PLK1; DYNLL1 AND SGO2, AND INTERACTION WITH SPAG5.
RX PubMed=21402792; DOI=10.1083/jcb.201008023;
RA Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.;
RT "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and
RT facilitates chromosome alignment.";
RL J. Cell Biol. 192:959-968(2011).
RN [12]
RP FUNCTION, INTERACTION WITH CENPE, BINDING TO MICROTUBULES, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=22110139; DOI=10.1074/jbc.m111.277194;
RA Huang Y., Wang W., Yao P., Wang X., Liu X., Zhuang X., Yan F., Zhou J.,
RA Du J., Ward T., Zou H., Zhang J., Fang G., Ding X., Dou Z., Yao X.;
RT "CENP-E kinesin interacts with SKAP protein to orchestrate accurate
RT chromosome segregation in mitosis.";
RL J. Biol. Chem. 287:1500-1509(2012).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DSN1 AND MAPRE1.
RX PubMed=23035123; DOI=10.1074/jbc.m112.406652;
RA Wang X., Zhuang X., Cao D., Chu Y., Yao P., Liu W., Liu L., Adams G.,
RA Fang G., Dou Z., Ding X., Huang Y., Wang D., Yao X.;
RT "Mitotic regulator SKAP forms a link between kinetochore core complex KMN
RT and dynamic spindle microtubules.";
RL J. Biol. Chem. 287:39380-39390(2012).
RN [14]
RP INTERACTION WITH DYNLL1.
RX PubMed=22965910; DOI=10.1083/jcb.201202112;
RA Dunsch A.K., Hammond D., Lloyd J., Schermelleh L., Gruneberg U., Barr F.A.;
RT "Dynein light chain 1 and a spindle-associated adaptor promote dynein
RT asymmetry and spindle orientation.";
RL J. Cell Biol. 198:1039-1054(2012).
RN [15]
RP INVOLVEMENT IN SCC, VARIANT SCC PHE-24, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25194279; DOI=10.1038/ng.3091;
RA Lee C.S., Bhaduri A., Mah A., Johnson W.L., Ungewickell A., Aros C.J.,
RA Nguyen C.B., Rios E.J., Siprashvili Z., Straight A., Kim J., Aasi S.Z.,
RA Khavari P.A.;
RT "Recurrent point mutations in the kinetochore gene KNSTRN in cutaneous
RT squamous cell carcinoma.";
RL Nat. Genet. 46:1060-1062(2014).
RN [16]
RP INTERACTION WITH PRPF19, AND SUBCELLULAR LOCATION.
RX PubMed=24718257; DOI=10.1371/journal.pone.0092712;
RA Lu S., Wang R., Cai C., Liang J., Xu L., Miao S., Wang L., Song W.;
RT "Small kinetochore associated protein (SKAP) promotes UV-induced cell
RT apoptosis through negatively regulating pre-mRNA processing factor 19
RT (Prp19).";
RL PLoS ONE 9:E92712-E92712(2014).
RN [17]
RP INVOLVEMENT IN ROCHIS, SUBCELLULAR LOCATION, AND INTERACTION WITH MAP4.
RX PubMed=29180244; DOI=10.1016/j.jaci.2017.10.033;
RA Sharfe N., Karanxha A., Dadi H., Merico D., Chitayat D., Herbrick J.A.,
RA Freeman S., Grinstein S., Roifman C.M.;
RT "Dual loss of p110delta PI3-kinase and SKAP (KNSTRN) expression leads to
RT combined immunodeficiency and multisystem syndromic features.";
RL J. Allergy Clin. Immunol. 142:618-629(2018).
CC -!- FUNCTION: Essential component of the mitotic spindle required for
CC faithful chromosome segregation and progression into anaphase
CC (PubMed:19667759). Promotes the metaphase-to-anaphase transition and is
CC required for chromosome alignment, normal timing of sister chromatid
CC segregation, and maintenance of spindle pole architecture
CC (PubMed:19667759, PubMed:22110139). The astrin (SPAG5)-kinastrin (SKAP)
CC complex promotes stable microtubule-kinetochore attachments
CC (PubMed:21402792). Required for kinetochore oscillations and dynamics
CC of microtubule plus-ends during live cell mitosis, possibly by forming
CC a link between spindle microtubule plus-ends and mitotic chromosomes to
CC achieve faithful cell division (PubMed:23035123). May be involved in
CC UV-induced apoptosis via its interaction with PRPF19; however, these
CC results need additional evidences (PubMed:24718257).
CC {ECO:0000269|PubMed:19667759, ECO:0000269|PubMed:21402792,
CC ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:23035123,
CC ECO:0000305|PubMed:24718257}.
CC -!- SUBUNIT: Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing
CC KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2 (PubMed:21402792). Interacts with
CC SPAG5 (PubMed:21402792). Directly binds to microtubules, although at
CC relatively low affinity (PubMed:21402792). Interacts with CENPE; this
CC interaction greatly favors microtubule-binding (PubMed:22110139).
CC Interacts with DSN1/MIS13; leading to localization to kinetochores
CC (PubMed:23035123). Interacts with MAPRE1/EB1; leading to localization
CC to the microtubule plus ends (PubMed:23035123). Interacts with PRPF19
CC (PubMed:24718257). Interacts with DYNLL1 (PubMed:22965910). Interacts
CC with MAP4 (PubMed:29180244). {ECO:0000269|PubMed:21402792,
CC ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:22965910,
CC ECO:0000269|PubMed:23035123, ECO:0000269|PubMed:24718257,
CC ECO:0000269|PubMed:29180244}.
CC -!- INTERACTION:
CC Q9Y448; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-373334, EBI-11096309;
CC Q9Y448; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-373334, EBI-745073;
CC Q9Y448; P42858: HTT; NbExp=3; IntAct=EBI-373334, EBI-466029;
CC Q9Y448; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-373334, EBI-9091197;
CC Q9Y448; Q15691: MAPRE1; NbExp=4; IntAct=EBI-373334, EBI-1004115;
CC Q9Y448; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-373334, EBI-726739;
CC Q9Y448; O43482: OIP5; NbExp=3; IntAct=EBI-373334, EBI-536879;
CC Q9Y448; O60437: PPL; NbExp=3; IntAct=EBI-373334, EBI-368321;
CC Q9Y448; Q96ES7: SGF29; NbExp=5; IntAct=EBI-373334, EBI-743117;
CC Q9Y448; Q9Y3C0: WASHC3; NbExp=6; IntAct=EBI-373334, EBI-712969;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24718257}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19667759,
CC ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22110139,
CC ECO:0000269|PubMed:23035123}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:19667759}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000269|PubMed:29180244}. Note=Colocalizes with
CC microtubules around centrosomes in prophase and with the mitotic
CC spindle at prometaphase and metaphase. From late prometaphase to
CC anaphase, is highly concentrated on kinetochores. Located at the
CC kinetochore-microtubule interface. The astrin (SPAG5)-kinastrin (SKAP)
CC complex localizes to the microtubule plus ends (PubMed:23035123).
CC {ECO:0000269|PubMed:19667759, ECO:0000269|PubMed:21402792,
CC ECO:0000269|PubMed:22110139, ECO:0000269|PubMed:23035123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y448-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y448-2; Sequence=VSP_041070;
CC Name=3;
CC IsoId=Q9Y448-3; Sequence=VSP_041069;
CC -!- TISSUE SPECIFICITY: Widely expressed, including in skin.
CC {ECO:0000269|PubMed:25194279}.
CC -!- INDUCTION: Degraded at the end of mitosis. Down-regulated upon exposure
CC to nitric oxide. {ECO:0000269|PubMed:15855057,
CC ECO:0000269|PubMed:22110139}.
CC -!- DOMAIN: The coiled coil regions mediate binding to kinetochores.
CC {ECO:0000269|PubMed:23035123}.
CC -!- DISEASE: Roifman-Chitayat syndrome (ROCHIS) [MIM:613328]: An autosomal
CC recessive digenic disorder characterized by global developmental delay,
CC variable neurologic features such as seizures and ataxia, optic
CC atrophy, dysmorphic facial features, distal skeletal anomalies, and
CC recurrent invasive infections due to combined immunodeficiency.
CC {ECO:0000269|PubMed:29180244}. Note=The disease is caused by variants
CC affecting distinct genetic loci, including the gene represented in this
CC entry. Caused by the simultaneous occurrence of homozygous mutations in
CC PIK3CD and KNSTRN. {ECO:0000269|PubMed:29180244}.
CC -!- DISEASE: Note=Cutaneous squamous cell carcinomas (SCC): A malignancy of
CC the skin. The hallmark of cutaneous SCC is malignant transformation of
CC normal epidermal keratinocytes. Disease susceptibility is associated
CC with variants affecting the gene represented in this entry. Variant
CC Phe-24 appears specific for UV-associated malignancies
CC (PubMed:25194279). {ECO:0000269|PubMed:25194279}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04543.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH14060.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI07803.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY652615; AAT66172.1; -; mRNA.
DR EMBL; AK301887; BAG63319.1; -; mRNA.
DR EMBL; AC013356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004543; AAH04543.1; ALT_TERM; mRNA.
DR EMBL; BC014060; AAH14060.1; ALT_TERM; mRNA.
DR EMBL; BC045739; AAH45739.1; -; mRNA.
DR EMBL; BC064344; AAH64344.1; -; mRNA.
DR EMBL; BC107802; AAI07803.1; ALT_INIT; mRNA.
DR EMBL; BC118559; AAI18560.1; -; mRNA.
DR EMBL; BC118639; AAI18640.1; -; mRNA.
DR EMBL; CR602848; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR611451; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U81002; AAD24201.1; -; mRNA.
DR CCDS; CCDS42021.1; -. [Q9Y448-1]
DR CCDS; CCDS45226.1; -. [Q9Y448-2]
DR CCDS; CCDS45227.1; -. [Q9Y448-3]
DR RefSeq; NP_001136233.1; NM_001142761.1. [Q9Y448-2]
DR RefSeq; NP_001136234.1; NM_001142762.1. [Q9Y448-3]
DR RefSeq; NP_150628.3; NM_033286.3. [Q9Y448-1]
DR AlphaFoldDB; Q9Y448; -.
DR SMR; Q9Y448; -.
DR BioGRID; 124714; 92.
DR CORUM; Q9Y448; -.
DR DIP; DIP-31247N; -.
DR IntAct; Q9Y448; 48.
DR MINT; Q9Y448; -.
DR STRING; 9606.ENSP00000249776; -.
DR GlyConnect; 2078; 1 N-Linked glycan (1 site).
DR GlyGen; Q9Y448; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9Y448; -.
DR MetOSite; Q9Y448; -.
DR PhosphoSitePlus; Q9Y448; -.
DR BioMuta; KNSTRN; -.
DR DMDM; 125991199; -.
DR EPD; Q9Y448; -.
DR jPOST; Q9Y448; -.
DR MassIVE; Q9Y448; -.
DR MaxQB; Q9Y448; -.
DR PaxDb; Q9Y448; -.
DR PeptideAtlas; Q9Y448; -.
DR PRIDE; Q9Y448; -.
DR ProteomicsDB; 86099; -. [Q9Y448-1]
DR ProteomicsDB; 86100; -. [Q9Y448-2]
DR ProteomicsDB; 86101; -. [Q9Y448-3]
DR Antibodypedia; 52276; 52 antibodies from 16 providers.
DR DNASU; 90417; -.
DR Ensembl; ENST00000249776.13; ENSP00000249776.8; ENSG00000128944.14. [Q9Y448-1]
DR Ensembl; ENST00000416151.6; ENSP00000391233.2; ENSG00000128944.14. [Q9Y448-2]
DR Ensembl; ENST00000448395.6; ENSP00000393001.2; ENSG00000128944.14. [Q9Y448-3]
DR GeneID; 90417; -.
DR KEGG; hsa:90417; -.
DR MANE-Select; ENST00000249776.13; ENSP00000249776.8; NM_033286.4; NP_150628.3.
DR UCSC; uc001zll.4; human. [Q9Y448-1]
DR CTD; 90417; -.
DR DisGeNET; 90417; -.
DR GeneCards; KNSTRN; -.
DR HGNC; HGNC:30767; KNSTRN.
DR HPA; ENSG00000128944; Tissue enhanced (testis, thyroid gland).
DR MalaCards; KNSTRN; -.
DR MIM; 613328; phenotype.
DR MIM; 614718; gene.
DR neXtProt; NX_Q9Y448; -.
DR OpenTargets; ENSG00000128944; -.
DR Orphanet; 221139; Combined immunodeficiency with faciooculoskeletal anomalies.
DR PharmGKB; PA134895025; -.
DR VEuPathDB; HostDB:ENSG00000128944; -.
DR eggNOG; ENOG502S60X; Eukaryota.
DR GeneTree; ENSGT00390000010376; -.
DR InParanoid; Q9Y448; -.
DR OMA; QDSCLAI; -.
DR OrthoDB; 1460326at2759; -.
DR PhylomeDB; Q9Y448; -.
DR TreeFam; TF336302; -.
DR PathwayCommons; Q9Y448; -.
DR SignaLink; Q9Y448; -.
DR SIGNOR; Q9Y448; -.
DR BioGRID-ORCS; 90417; 18 hits in 1079 CRISPR screens.
DR GenomeRNAi; 90417; -.
DR Pharos; Q9Y448; Tbio.
DR PRO; PR:Q9Y448; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y448; protein.
DR Bgee; ENSG00000128944; Expressed in ventricular zone and 158 other tissues.
DR ExpressionAtlas; Q9Y448; baseline and differential.
DR Genevisible; Q9Y448; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001726; C:ruffle; IDA:ARUK-UCL.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:ARUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:ARUK-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IMP:ARUK-UCL.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:ARUK-UCL.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:ARUK-UCL.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR InterPro; IPR033373; SKAP.
DR PANTHER; PTHR31940; PTHR31940; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Kinetochore;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..316
FT /note="Small kinetochore-associated protein"
FT /id="PRO_0000274512"
FT REGION 159..316
FT /note="Interaction with SPAG5"
FT /evidence="ECO:0000269|PubMed:21402792"
FT COILED 166..216
FT /evidence="ECO:0000255"
FT COILED 248..316
FT /evidence="ECO:0000255"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 229..316
FT /note="ALGSETLASRQESTTDHMDSMLLLETLQEELKLFNETAKKQMEELQALKVKL
FT EMKEERVRFLEQQTLCNNQVNDLTTALKEMEQLLEM -> VAVRNFARGAEAF (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_041069"
FT VAR_SEQ 275..316
FT /note="ALKVKLEMKEERVRFLEQQTLCNNQVNDLTTALKEMEQLLEM -> IAWMNH
FT GILHQM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_041070"
FT VARIANT 24
FT /note="S -> F (in SCC; impaired chromatid cohesion;
FT dbSNP:rs868438023)"
FT /evidence="ECO:0000269|PubMed:25194279"
FT /id="VAR_071857"
FT VARIANT 40
FT /note="A -> E (in dbSNP:rs7164132)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030304"
FT VARIANT 75
FT /note="R -> L (in dbSNP:rs7169404)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030305"
FT VARIANT 92
FT /note="P -> S (in dbSNP:rs7169262)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030306"
FT CONFLICT 47
FT /note="T -> K (in Ref. 4; AAH45739)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="S -> G (in Ref. 4; AAI18640)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="A -> S (in Ref. 6; AAD24201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35438 MW; 6FC6745DBA6B70D8 CRC64;
MAAPEAPPLD RVFRTTWLST ECDSHPLPPS YRKFLFETQA ADLAGGTTVA AGNLLNESEK
DCGQDRRAPG VQPCRLVTMT SVVKTVYSLQ PPSALSGGQP ADTQTRATSK SLLPVRSKEV
DVSKQLHSGG PENDVTKITK LRRENGQMKA TDTATRRNVR KGYKPLSKQK SEEELKDKNQ
LLEAVNKQLH QKLTETQGEL KDLTQKVELL EKFRDNCLAI LESKGLDPAL GSETLASRQE
STTDHMDSML LLETLQEELK LFNETAKKQM EELQALKVKL EMKEERVRFL EQQTLCNNQV
NDLTTALKEM EQLLEM
