SKA3_HUMAN
ID SKA3_HUMAN Reviewed; 412 AA.
AC Q8IX90; A2A330; A2A331; B2RBY2; Q5VZV5; Q86WR2; Q8NBG1; Q96D22;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Spindle and kinetochore-associated protein 3;
GN Name=SKA3; Synonyms=C13orf3, RAMA1;
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 VARIANT GLU-335.
RA Panvichian R., Ratanavila A., Ratanatharathorn V.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
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] (ISOFORMS 1 AND 2), AND VARIANTS
RP ILE-58 AND ALA-254.
RC TISSUE=Testis, and Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-119; SER-155 AND
RP THR-384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP IDENTIFICATION IN THE SKA1 COMPLEX, AND INTERACTION WITH SKA1.
RX PubMed=19289083; DOI=10.1016/j.devcel.2009.01.011;
RA Welburn J.P.I., Grishchuk E.L., Backer C.B., Wilson-Kubalek E.M.,
RA Yates J.R. III, Cheeseman I.M.;
RT "The human kinetochore Ska1 complex facilitates microtubule
RT depolymerization-coupled motility.";
RL Dev. Cell 16:374-385(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE SKA1 COMPLEX.
RX PubMed=19360002; DOI=10.1038/emboj.2009.96;
RA Gaitanos T.N., Santamaria A., Jeyaprakash A.A., Wang B., Conti E.,
RA Nigg E.A.;
RT "Stable kinetochore-microtubule interactions depend on the Ska complex and
RT its new component Ska3/C13Orf3.";
RL EMBO J. 28:1442-1452(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-318, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-152; SER-155; THR-265
RP AND SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH SKA1 AND MICROTUBULES.
RX PubMed=23085020; DOI=10.1016/j.devcel.2012.09.012;
RA Schmidt J.C., Arthanari H., Boeszoermenyi A., Dashkevich N.M.,
RA Wilson-Kubalek E.M., Monnier N., Markus M., Oberer M., Milligan R.A.,
RA Bathe M., Wagner G., Grishchuk E.L., Cheeseman I.M.;
RT "The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and
RT binds to curved protofilaments.";
RL Dev. Cell 23:968-980(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-119; SER-139;
RP SER-155; SER-159 AND SER-267, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Component of the SKA1 complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation (PubMed:19289083, PubMed:19360002,
CC PubMed:23085020). The SKA1 complex is a direct component of the
CC kinetochore-microtubule interface and directly associates with
CC microtubules as oligomeric assemblies (PubMed:19289083,
CC PubMed:19360002). The complex facilitates the processive movement of
CC microspheres along a microtubule in a depolymerization-coupled manner
CC (PubMed:19289083). In the complex, it mediates the microtubule-
CC stimulated oligomerization (PubMed:19289083). Affinity for microtubules
CC is synergistically enhanced in the presence of the ndc-80 complex and
CC may allow the ndc-80 complex to track depolymerizing microtubules
CC (PubMed:23085020). {ECO:0000269|PubMed:19289083,
CC ECO:0000269|PubMed:19360002, ECO:0000269|PubMed:23085020}.
CC -!- SUBUNIT: Component of the SKA1 complex, composed of SKA1, SKA2 and SKA3
CC (PubMed:19289083, PubMed:19360002). The core SKA1 complex is composed
CC of 2 SKA1-SKA2 heterodimers, each heterodimer interacting with a
CC molecule of the SKA3 homodimer (PubMed:19289083, PubMed:19360002). The
CC core SKA1 complex associates with microtubules and forms oligomeric
CC assemblies (PubMed:19289083, PubMed:19360002, PubMed:23085020).
CC Interacts with SKA1; the interaction is direct (PubMed:19289083,
CC PubMed:23085020). {ECO:0000269|PubMed:19289083,
CC ECO:0000269|PubMed:19360002, ECO:0000269|PubMed:23085020}.
CC -!- INTERACTION:
CC Q8IX90; O94818-2: NOL4; NbExp=3; IntAct=EBI-1773976, EBI-10190763;
CC Q8IX90; Q96BD8: SKA1; NbExp=11; IntAct=EBI-1773976, EBI-741854;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:19289083,
CC ECO:0000269|PubMed:19360002, ECO:0000269|PubMed:20813266}.
CC Note=Localizes to the outer kinetochore and spindle microtubules during
CC mitosis in a NDC80 complex-dependent manner.
CC {ECO:0000269|PubMed:19360002}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IX90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IX90-2; Sequence=VSP_040527, VSP_040528;
CC Name=3;
CC IsoId=Q8IX90-3; Sequence=VSP_037245;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SKA3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13418.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAG37379.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG37379.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAX08294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF361358; AAO13796.1; -; mRNA.
DR EMBL; AK090584; BAC03484.1; -; mRNA.
DR EMBL; AK314864; BAG37379.1; ALT_SEQ; mRNA.
DR EMBL; AL158032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08293.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08294.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471075; EAX08295.1; -; Genomic_DNA.
DR EMBL; BC013418; AAH13418.1; ALT_SEQ; mRNA.
DR EMBL; BC048988; AAH48988.1; -; mRNA.
DR CCDS; CCDS31946.1; -. [Q8IX90-1]
DR CCDS; CCDS53856.1; -. [Q8IX90-3]
DR RefSeq; NP_001159489.1; NM_001166017.1. [Q8IX90-3]
DR RefSeq; NP_659498.4; NM_145061.5. [Q8IX90-1]
DR RefSeq; XP_005266345.1; XM_005266288.3.
DR PDB; 4AJ5; X-ray; 3.32 A; 1/2/3/4/U/V/W/X/Y/Z=1-101.
DR PDBsum; 4AJ5; -.
DR AlphaFoldDB; Q8IX90; -.
DR SMR; Q8IX90; -.
DR BioGRID; 128691; 176.
DR ComplexPortal; CPX-5642; Kinetochore SKA complex.
DR IntAct; Q8IX90; 38.
DR MINT; Q8IX90; -.
DR STRING; 9606.ENSP00000319417; -.
DR GlyGen; Q8IX90; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IX90; -.
DR PhosphoSitePlus; Q8IX90; -.
DR BioMuta; SKA3; -.
DR DMDM; 73620123; -.
DR EPD; Q8IX90; -.
DR jPOST; Q8IX90; -.
DR MassIVE; Q8IX90; -.
DR MaxQB; Q8IX90; -.
DR PaxDb; Q8IX90; -.
DR PeptideAtlas; Q8IX90; -.
DR PRIDE; Q8IX90; -.
DR ProteomicsDB; 70973; -. [Q8IX90-1]
DR ProteomicsDB; 70974; -. [Q8IX90-2]
DR ProteomicsDB; 70975; -. [Q8IX90-3]
DR Antibodypedia; 22379; 191 antibodies from 27 providers.
DR DNASU; 221150; -.
DR Ensembl; ENST00000298260.8; ENSP00000298260.4; ENSG00000165480.16. [Q8IX90-2]
DR Ensembl; ENST00000314759.6; ENSP00000319417.5; ENSG00000165480.16. [Q8IX90-1]
DR Ensembl; ENST00000400018.7; ENSP00000382896.3; ENSG00000165480.16. [Q8IX90-3]
DR GeneID; 221150; -.
DR KEGG; hsa:221150; -.
DR MANE-Select; ENST00000314759.6; ENSP00000319417.5; NM_145061.6; NP_659498.4.
DR UCSC; uc001unt.3; human. [Q8IX90-1]
DR CTD; 221150; -.
DR DisGeNET; 221150; -.
DR GeneCards; SKA3; -.
DR HGNC; HGNC:20262; SKA3.
DR HPA; ENSG00000165480; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 619247; gene.
DR neXtProt; NX_Q8IX90; -.
DR OpenTargets; ENSG00000165480; -.
DR PharmGKB; PA165505498; -.
DR VEuPathDB; HostDB:ENSG00000165480; -.
DR eggNOG; ENOG502QSTX; Eukaryota.
DR GeneTree; ENSGT00500000045005; -.
DR HOGENOM; CLU_033334_1_0_1; -.
DR InParanoid; Q8IX90; -.
DR OMA; ERYMIPQ; -.
DR OrthoDB; 1070468at2759; -.
DR PhylomeDB; Q8IX90; -.
DR TreeFam; TF332721; -.
DR PathwayCommons; Q8IX90; -.
DR SignaLink; Q8IX90; -.
DR SIGNOR; Q8IX90; -.
DR BioGRID-ORCS; 221150; 543 hits in 1098 CRISPR screens.
DR ChiTaRS; SKA3; human.
DR GenomeRNAi; 221150; -.
DR Pharos; Q8IX90; Tbio.
DR PRO; PR:Q8IX90; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8IX90; protein.
DR Bgee; ENSG00000165480; Expressed in ventricular zone and 107 other tissues.
DR ExpressionAtlas; Q8IX90; baseline and differential.
DR Genevisible; Q8IX90; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0000940; C:outer kinetochore; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IDA:UniProtKB.
DR InterPro; IPR033341; SKA3.
DR PANTHER; PTHR48118; PTHR48118; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..412
FT /note="Spindle and kinetochore-associated protein 3"
FT /id="PRO_0000089878"
FT REGION 132..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 384
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 35
FT /note="D -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040527"
FT VAR_SEQ 36..412
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040528"
FT VAR_SEQ 374..412
FT /note="LLSKYNSNLATPIAIKAVPPSKRFLKHGQNIRDVSNKEN -> KFQWIYPTQ
FT KLNKMR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037245"
FT VARIANT 58
FT /note="V -> I (in dbSNP:rs11546983)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_057831"
FT VARIANT 254
FT /note="T -> A (in dbSNP:rs17345690)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_023113"
FT VARIANT 335
FT /note="D -> E (in dbSNP:rs17279819)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_057832"
FT HELIX 3..30
FT /evidence="ECO:0007829|PDB:4AJ5"
FT HELIX 35..66
FT /evidence="ECO:0007829|PDB:4AJ5"
FT HELIX 68..99
FT /evidence="ECO:0007829|PDB:4AJ5"
SQ SEQUENCE 412 AA; 46359 MW; BCC48E527DD8AA84 CRC64;
MDPIRSFCGK LRSLASTLDC ETARLQRALD GEESDFEDYP MRILYDLHSE VQTLKDDVNI
LLDKARLENQ EGIDFIKATK VLMEKNSMDI MKIREYFQKY GYSPRVKKNS VHEQEAINSD
PELSNCENFQ KTDVKDDLSD PPVASSCISE KSPRSPQLSD FGLERYIVSQ VLPNPPQAVN
NYKEEPVIVT PPTKQSLVKV LKTPKCALKM DDFECVTPKL EHFGISEYTM CLNEDYTMGL
KNARNNKSEE AIDTESRLND NVFATPSPII QQLEKSDAEY TNSPLVPTFC TPGLKIPSTK
NSIALVSTNY PLSKTNSSSN DLEVEDRTSL VLNSDTCFEN LTDPSSPTIS SYENLLRTPT
PPEVTKIPED ILQLLSKYNS NLATPIAIKA VPPSKRFLKH GQNIRDVSNK EN
