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Protein

Small kinetochore-associated protein

Gene

KNSTRN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the mitotic spindle required for faithful chromosome segregation and progression into anaphase (PubMed:19667759). Promotes the metaphase-to-anaphase transition and is required for chromosome alignment, normal timing of sister chromatid segregation, and maintenance of spindle pole architecture (PubMed:19667759, PubMed:22110139). The astrin (SPAG5)-kinastrin (SKAP) complex promotes stable microtubule-kinetochore attachments (PubMed:21402792). Required for kinetochore oscillations and dynamics of microtubule plus-ends during live cell mitosis, possibly by forming a link between spindle microtubule plus-ends and mitotic chromosomes to achieve faithful cell division (PubMed:23035123). May be involved in UV-induced apoptosis via its interaction with PRPF19; however, these results need additional evidences (PubMed:24718257).1 Publication4 Publications

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromosome segregation Source: UniProtKB
  • mitotic sister chromatid segregation Source: UniProtKB
  • regulation of attachment of spindle microtubules to kinetochore Source: UniProtKB
  • spindle organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Small kinetochore-associated protein1 Publication
Short name:
SKAP1 Publication
Alternative name(s):
Kinetochore-localized astrin-binding protein1 Publication
Short name:
Kinastrin1 Publication
Kinetochore-localized astrin/SPAG5-binding protein
TRAF4-associated factor 1
Gene namesi
Name:KNSTRNImported
Synonyms:C15orf23Imported, SKAP1 Publication, TRAF4AF1
ORF Names:HSD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30767. KNSTRN.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • kinetochore Source: UniProtKB
  • microtubule cytoskeleton Source: HPA
  • microtubule plus-end Source: UniProtKB
  • mitotic spindle Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cutaneous squamous cell carcinomas (SCC): A malignancy of the skin. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes. Disease susceptibility is associated with variations affecting the gene represented in this entry. Variant Phe-24 appears specific for UV-associated malignancies (PubMed:25194279).

Keywords - Diseasei

Disease mutation

Organism-specific databases

PharmGKBiPA134895025.

Polymorphism and mutation databases

BioMutaiKNSTRN.
DMDMi125991199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Small kinetochore-associated proteinPRO_0000274512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y448.
MaxQBiQ9Y448.
PaxDbiQ9Y448.
PeptideAtlasiQ9Y448.
PRIDEiQ9Y448.

PTM databases

iPTMnetiQ9Y448.
PhosphoSiteiQ9Y448.

Expressioni

Tissue specificityi

Widely expressed, including in skin.1 Publication

Inductioni

Degraded at the end of mitosis. Down-regulated upon exposure to nitric oxide.2 Publications

Gene expression databases

BgeeiQ9Y448.
CleanExiHS_C15orf23.
ExpressionAtlasiQ9Y448. baseline and differential.
GenevisibleiQ9Y448. HS.

Organism-specific databases

HPAiHPA042027.

Interactioni

Subunit structurei

Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. Interacts with SPAG5. Directly binds to microtubules, although at relatively low affinity. Interacts with CENPE; this interaction greatly favors microtubule-binding. Interacts with DSN1/MIS13; leading to localization to kinetochores. Interacts with MAPRE1/EB1; leading to localization to the microtubule plus ends. Interacts with PRPF19.3 Publications

Protein-protein interaction databases

BioGridi124714. 44 interactions.
DIPiDIP-31247N.
IntActiQ9Y448. 22 interactions.
MINTiMINT-4832111.
STRINGi9606.ENSP00000249776.

Structurei

3D structure databases

ProteinModelPortaliQ9Y448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni159 – 316158Interaction with SPAG51 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili166 – 21651Sequence analysisAdd
BLAST
Coiled coili248 – 31669Sequence analysisAdd
BLAST

Domaini

The coiled coil regions mediate binding to kinetochores.1 Publication

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IKUT. Eukaryota.
ENOG4111DW5. LUCA.
GeneTreeiENSGT00390000010376.
HOVERGENiHBG083924.
InParanoidiQ9Y448.
OMAiLCNNQVN.
OrthoDBiEOG7N0C5M.
PhylomeDBiQ9Y448.
TreeFamiTF336302.

Family and domain databases

InterProiIPR033373. SKAP.
[Graphical view]
PANTHERiPTHR31940. PTHR31940. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y448-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAPEAPPLD RVFRTTWLST ECDSHPLPPS YRKFLFETQA ADLAGGTTVA
60 70 80 90 100
AGNLLNESEK DCGQDRRAPG VQPCRLVTMT SVVKTVYSLQ PPSALSGGQP
110 120 130 140 150
ADTQTRATSK SLLPVRSKEV DVSKQLHSGG PENDVTKITK LRRENGQMKA
160 170 180 190 200
TDTATRRNVR KGYKPLSKQK SEEELKDKNQ LLEAVNKQLH QKLTETQGEL
210 220 230 240 250
KDLTQKVELL EKFRDNCLAI LESKGLDPAL GSETLASRQE STTDHMDSML
260 270 280 290 300
LLETLQEELK LFNETAKKQM EELQALKVKL EMKEERVRFL EQQTLCNNQV
310
NDLTTALKEM EQLLEM
Length:316
Mass (Da):35,438
Last modified:February 6, 2007 - v2
Checksum:i6FC6745DBA6B70D8
GO
Isoform 2 (identifier: Q9Y448-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     275-316: ALKVKLEMKEERVRFLEQQTLCNNQVNDLTTALKEMEQLLEM → IAWMNHGILHQM

Show »
Length:286
Mass (Da):31,880
Checksum:i8EE608F67306D3DC
GO
Isoform 3 (identifier: Q9Y448-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-316: ALGSETLASR...LKEMEQLLEM → VAVRNFARGAEAF

Show »
Length:241
Mass (Da):26,586
Checksum:iF55DD94EF9CD69FE
GO

Sequence cautioni

The sequence AAH04543.1 differs from that shown. Reason: Erroneous termination at position 174. Translated as Glu.Curated
The sequence AAH14060.1 differs from that shown. Reason: Erroneous termination at position 174. Translated as Glu.Curated
The sequence AAI07803.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471T → K in AAH45739 (PubMed:15489334).Curated
Sequence conflicti232 – 2321S → G in AAI18640 (PubMed:15489334).Curated
Sequence conflicti236 – 2361A → S in AAD24201 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241S → F in SCC; impaired chromatid cohesion. 1 Publication
VAR_071857
Natural varianti40 – 401A → E.1 Publication
Corresponds to variant rs7164132 [ dbSNP | Ensembl ].
VAR_030304
Natural varianti75 – 751R → L.1 Publication
Corresponds to variant rs7169404 [ dbSNP | Ensembl ].
VAR_030305
Natural varianti92 – 921P → S.1 Publication
Corresponds to variant rs7169262 [ dbSNP | Ensembl ].
VAR_030306

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei229 – 31688ALGSE…QLLEM → VAVRNFARGAEAF in isoform 3. 1 PublicationVSP_041069Add
BLAST
Alternative sequencei275 – 31642ALKVK…QLLEM → IAWMNHGILHQM in isoform 2. 1 PublicationVSP_041070Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY652615 mRNA. Translation: AAT66172.1.
AK301887 mRNA. Translation: BAG63319.1.
AC013356 Genomic DNA. No translation available.
BC004543 mRNA. Translation: AAH04543.1. Different termination.
BC014060 mRNA. Translation: AAH14060.1. Different termination.
BC045739 mRNA. Translation: AAH45739.1.
BC064344 mRNA. Translation: AAH64344.1.
BC107802 mRNA. Translation: AAI07803.1. Different initiation.
BC118559 mRNA. Translation: AAI18560.1.
BC118639 mRNA. Translation: AAI18640.1.
CR602848 mRNA. No translation available.
CR611451 mRNA. No translation available.
U81002 mRNA. Translation: AAD24201.1.
CCDSiCCDS42021.1. [Q9Y448-1]
CCDS45226.1. [Q9Y448-2]
CCDS45227.1. [Q9Y448-3]
RefSeqiNP_001136233.1. NM_001142761.1. [Q9Y448-2]
NP_001136234.1. NM_001142762.1. [Q9Y448-3]
NP_150628.3. NM_033286.3. [Q9Y448-1]
UniGeneiHs.525796.

Genome annotation databases

EnsembliENST00000249776; ENSP00000249776; ENSG00000128944. [Q9Y448-1]
ENST00000416151; ENSP00000391233; ENSG00000128944. [Q9Y448-2]
ENST00000448395; ENSP00000393001; ENSG00000128944. [Q9Y448-3]
GeneIDi90417.
KEGGihsa:90417.
UCSCiuc001zll.4. human. [Q9Y448-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY652615 mRNA. Translation: AAT66172.1.
AK301887 mRNA. Translation: BAG63319.1.
AC013356 Genomic DNA. No translation available.
BC004543 mRNA. Translation: AAH04543.1. Different termination.
BC014060 mRNA. Translation: AAH14060.1. Different termination.
BC045739 mRNA. Translation: AAH45739.1.
BC064344 mRNA. Translation: AAH64344.1.
BC107802 mRNA. Translation: AAI07803.1. Different initiation.
BC118559 mRNA. Translation: AAI18560.1.
BC118639 mRNA. Translation: AAI18640.1.
CR602848 mRNA. No translation available.
CR611451 mRNA. No translation available.
U81002 mRNA. Translation: AAD24201.1.
CCDSiCCDS42021.1. [Q9Y448-1]
CCDS45226.1. [Q9Y448-2]
CCDS45227.1. [Q9Y448-3]
RefSeqiNP_001136233.1. NM_001142761.1. [Q9Y448-2]
NP_001136234.1. NM_001142762.1. [Q9Y448-3]
NP_150628.3. NM_033286.3. [Q9Y448-1]
UniGeneiHs.525796.

3D structure databases

ProteinModelPortaliQ9Y448.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124714. 44 interactions.
DIPiDIP-31247N.
IntActiQ9Y448. 22 interactions.
MINTiMINT-4832111.
STRINGi9606.ENSP00000249776.

PTM databases

iPTMnetiQ9Y448.
PhosphoSiteiQ9Y448.

Polymorphism and mutation databases

BioMutaiKNSTRN.
DMDMi125991199.

Proteomic databases

EPDiQ9Y448.
MaxQBiQ9Y448.
PaxDbiQ9Y448.
PeptideAtlasiQ9Y448.
PRIDEiQ9Y448.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249776; ENSP00000249776; ENSG00000128944. [Q9Y448-1]
ENST00000416151; ENSP00000391233; ENSG00000128944. [Q9Y448-2]
ENST00000448395; ENSP00000393001; ENSG00000128944. [Q9Y448-3]
GeneIDi90417.
KEGGihsa:90417.
UCSCiuc001zll.4. human. [Q9Y448-1]

Organism-specific databases

CTDi90417.
GeneCardsiKNSTRN.
HGNCiHGNC:30767. KNSTRN.
HPAiHPA042027.
MIMi614718. gene.
neXtProtiNX_Q9Y448.
PharmGKBiPA134895025.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKUT. Eukaryota.
ENOG4111DW5. LUCA.
GeneTreeiENSGT00390000010376.
HOVERGENiHBG083924.
InParanoidiQ9Y448.
OMAiLCNNQVN.
OrthoDBiEOG7N0C5M.
PhylomeDBiQ9Y448.
TreeFamiTF336302.

Miscellaneous databases

GenomeRNAii90417.
PROiQ9Y448.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y448.
CleanExiHS_C15orf23.
ExpressionAtlasiQ9Y448. baseline and differential.
GenevisibleiQ9Y448. HS.

Family and domain databases

InterProiIPR033373. SKAP.
[Graphical view]
PANTHERiPTHR31940. PTHR31940. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A spermatogenesis related gene expressed in nucleus."
    Cai C.L., Liu N., Lin W., Miao S.Y., Wang L.F.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLU-40; LEU-75 AND SER-92.
    Tissue: Kidney, Ovary and Testis.
  5. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-316 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-316 (ISOFORM 2).
    Tissue: Neuroblastoma.
  6. Touji S., Yano M., Kobayasi A., Tamai K.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-316 (ISOFORM 1).
  7. "Analysis of differentially expressed genes in nitric oxide-exposed human monocytic cells."
    Turpaev K., Bouton C., Diet A., Glatigny A., Drapier J.-C.
    Free Radic. Biol. Med. 38:1392-1400(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY NITRIC OXIDE.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "SKAP associates with kinetochores and promotes the metaphase-to-anaphase transition."
    Fang L., Seki A., Fang G.
    Cell Cycle 8:2819-2827(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment."
    Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.
    J. Cell Biol. 192:959-968(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH SPAG5; PLK1; DYNLL1 AND SGO2, INTERACTION WITH SPAG5.
  12. "CENP-E kinesin interacts with SKAP protein to orchestrate accurate chromosome segregation in mitosis."
    Huang Y., Wang W., Yao P., Wang X., Liu X., Zhuang X., Yan F., Zhou J., Du J., Ward T., Zou H., Zhang J., Fang G., Ding X., Dou Z., Yao X.
    J. Biol. Chem. 287:1500-1509(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CENPE, BINDING TO MICROTUBULES, SUBCELLULAR LOCATION, INDUCTION.
  13. "Mitotic regulator SKAP forms a link between kinetochore core complex KMN and dynamic spindle microtubules."
    Wang X., Zhuang X., Cao D., Chu Y., Yao P., Liu W., Liu L., Adams G., Fang G., Dou Z., Ding X., Huang Y., Wang D., Yao X.
    J. Biol. Chem. 287:39380-39390(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DSN1 AND MAPRE1.
  14. "Recurrent point mutations in the kinetochore gene KNSTRN in cutaneous squamous cell carcinoma."
    Lee C.S., Bhaduri A., Mah A., Johnson W.L., Ungewickell A., Aros C.J., Nguyen C.B., Rios E.J., Siprashvili Z., Straight A., Kim J., Aasi S.Z., Khavari P.A.
    Nat. Genet. 46:1060-1062(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SCC, VARIANT SCC PHE-24, FUNCTION, TISSUE SPECIFICITY.
  15. "Small kinetochore associated protein (SKAP) promotes UV-induced cell apoptosis through negatively regulating pre-mRNA processing factor 19 (Prp19)."
    Lu S., Wang R., Cai C., Liang J., Xu L., Miao S., Wang L., Song W.
    PLoS ONE 9:E92712-E92712(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRPF19, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSKAP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y448
Secondary accession number(s): B4DXA7
, Q147U5, Q32Q57, Q5ISJ0, Q6P2S5, Q6PJM0, Q86XB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: July 6, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.