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Q86WV1

- SKAP1_HUMAN

UniProt

Q86WV1 - SKAP1_HUMAN

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Protein
Src kinase-associated phosphoprotein 1
Gene
SKAP1, SCAP1, SKAP55
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Positively regulates T-cell receptor signaling by enhancing the MAP kinase pathway. Required for optimal conjugation between T-cells and antigen-presenting cells by promoting the clustering of integrin ITGAL on the surface of T-cells. May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.5 Publications

GO - Molecular functioni

  1. SH2 domain binding Source: UniProtKB
  2. SH3 domain binding Source: BHF-UCL
  3. SH3/SH2 adaptor activity Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein kinase binding Source: UniProtKB
  6. protein phosphatase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. T cell receptor signaling pathway Source: UniProtKB
  2. positive regulation of signal transduction Source: GOC
  3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. positive regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

SignaLinkiQ86WV1.

Names & Taxonomyi

Protein namesi
Recommended name:
Src kinase-associated phosphoprotein 1
Alternative name(s):
Src family-associated phosphoprotein 1
Src kinase-associated phosphoprotein of 55 kDa
Short name:
SKAP-55
Short name:
pp55
Gene namesi
Name:SKAP1
Synonyms:SCAP1, SKAP55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:15605. SKAP1.

Subcellular locationi

Cytoplasm. Nucleus. Cell membrane
Note: Upon T-cell stimulation, translocates to lipid rafts at the cell membrane.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: HPA
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi219 – 2191Y → F: Impairs interaction with PTPRC. No effect on interaction with FYN or GRB2. 2 Publications
Mutagenesisi232 – 2321Y → F: Abolishes interaction with PTPRC, translocation to cell membrane upon T-cell stimulation and activation of the MAP kinase pathway. No effect on interaction with FYN or GRB2. 2 Publications
Mutagenesisi271 – 2711Y → F: No effect on interaction with PTPRC and translocation to cell membrane upon T-cell stimulation. Abolishes interaction with FYN and GRB2 and activation of the MAP kinase pathway. 2 Publications
Mutagenesisi295 – 2951Y → F: Abolishes FYB-dependent activation of ITGAL clustering. 1 Publication
Mutagenesisi298 – 2981Y → F: Impairs interaction with FYB. 1 Publication
Mutagenesisi333 – 3331W → R: Abolishes homodimerization, interaction with FYB and activation of the MAP kinase pathway. 3 Publications

Organism-specific databases

PharmGKBiPA162403362.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Src kinase-associated phosphoprotein 1
PRO_0000270173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421Phosphotyrosine By similarity
Modified residuei219 – 2191Phosphotyrosine Inferred
Modified residuei232 – 2321Phosphotyrosine Inferred
Modified residuei271 – 2711Phosphotyrosine; by FYN1 Publication
Modified residuei295 – 2951Phosphotyrosine; by FYN Inferred

Post-translational modificationi

Phosphorylated on tyrosines. Phosphorylation by FYN on Tyr-271 is required for GRB2 interaction. Phosphorylation by FYN on Tyr-295 abolishes interaction with FYB. Tyr-232 is dephosphorylated by PTPRC Inferred.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86WV1.
PaxDbiQ86WV1.
PRIDEiQ86WV1.

PTM databases

PhosphoSiteiQ86WV1.

Expressioni

Tissue specificityi

Highly expressed in thymocytes and peripheral blood lymphocytes. Also expressed in spleen cells and testis. Present in T-cells (at protein level).1 Publication

Gene expression databases

ArrayExpressiQ86WV1.
BgeeiQ86WV1.
CleanExiHS_SKAP1.
GenevestigatoriQ86WV1.

Organism-specific databases

HPAiCAB025882.
HPA002969.

Interactioni

Subunit structurei

Homodimer. Interacts with FYN and PTPRC. Interacts with GRB2 when phosphorylated on Tyr-271. Interacts with FYB, which is required for SKAP2 protein stability. Part of a complex consisting of SKAP1, FYB and CLNK. Interacts with RASGRP1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FYBO151176EBI-2477305,EBI-1753267

Protein-protein interaction databases

BioGridi114184. 11 interactions.
IntActiQ86WV1. 3 interactions.
MINTiMINT-6939971.
STRINGi9606.ENSP00000338171.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi108 – 11912
Beta strandi121 – 1244
Beta strandi126 – 13611
Beta strandi139 – 1457
Beta strandi152 – 1565
Beta strandi161 – 1644
Helixi166 – 1683
Helixi172 – 1765
Beta strandi177 – 1815
Beta strandi183 – 1853
Beta strandi188 – 1914
Helixi195 – 21218

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5DX-ray1.70A/B/C/D108-213[»]
ProteinModelPortaliQ86WV1.
SMRiQ86WV1. Positions 7-213, 301-351.

Miscellaneous databases

EvolutionaryTraceiQ86WV1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini107 – 210104PH
Add
BLAST
Domaini294 – 35562SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 2956Interaction with FYB

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi220 – 23011Poly-Glu
Add
BLAST

Domaini

The SH3 domain interacts with FYB.

Sequence similaritiesi

Belongs to the SKAP family.
Contains 1 PH domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG76786.
HOGENOMiHOG000231109.
HOVERGENiHBG052827.
InParanoidiQ86WV1.
KOiK17699.
OMAiHLRRDSK.
OrthoDBiEOG7K6PVB.
PhylomeDBiQ86WV1.
TreeFamiTF331055.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86WV1-1) [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

MQAAALPEEI RWLLEDAEEF LAEGLRNENL SAVARDHRDH ILRGFQQIKA    50
RYYWDFQPQG GDIGQDSSDD NHSGTLGLSL TSDAPFLSDY QDEGMEDIVK 100
GAQELDNVIK QGYLEKKSKD HSFFGSEWQK RWCVVSRGLF YYYANEKSKQ 150
PKGTFLIKGY GVRMAPHLRR DSKKESCFEL TSQDRRSYEF TATSPAEARD 200
WVDQISFLLK DLSSLTIPYE EDEEEEEKEE TYDDIDGFDS PSCGSQCRPT 250
ILPGSVGIKE PTEEKEEEDI YEVLPDEEHD LEEDESGTRR KGVDYASYYQ 300
GLWDCHGDQP DELSFQRGDL IRILSKEYNM YGWWVGELNS LVGIVPKEYL 350
TTAFEVEER 359
Length:359
Mass (Da):41,432
Last modified:November 24, 2009 - v3
Checksum:i630FE4C17295BD6D
GO
Isoform 2 (identifier: Q86WV1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-293: Missing.

Show »
Length:358
Mass (Da):41,333
Checksum:i158BBE1D48539DAC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti161 – 1611G → S.1 Publication
Corresponds to variant rs2278868 [ dbSNP | Ensembl ].
VAR_029811
Natural varianti242 – 2421S → G.
Corresponds to variant rs35288886 [ dbSNP | Ensembl ].
VAR_035343

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei293 – 2931Missing in isoform 2.
VSP_022179

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871S → T in CAA72101. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11215 mRNA. Translation: CAA72101.1.
AC006468 Genomic DNA. No translation available.
AC027152 Genomic DNA. No translation available.
AC036222 Genomic DNA. No translation available.
AC090627 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94749.1.
CH471109 Genomic DNA. Translation: EAW94750.1.
BC047870 mRNA. Translation: AAH47870.1.
CCDSiCCDS32674.1. [Q86WV1-1]
RefSeqiNP_001068567.1. NM_001075099.1. [Q86WV1-2]
NP_003717.3. NM_003726.3. [Q86WV1-1]
UniGeneiHs.316931.

Genome annotation databases

EnsembliENST00000336915; ENSP00000338171; ENSG00000141293. [Q86WV1-1]
ENST00000584924; ENSP00000464311; ENSG00000141293. [Q86WV1-1]
GeneIDi8631.
KEGGihsa:8631.
UCSCiuc002ini.1. human. [Q86WV1-1]
uc002inj.1. human. [Q86WV1-2]

Polymorphism databases

DMDMi269849660.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11215 mRNA. Translation: CAA72101.1 .
AC006468 Genomic DNA. No translation available.
AC027152 Genomic DNA. No translation available.
AC036222 Genomic DNA. No translation available.
AC090627 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94749.1 .
CH471109 Genomic DNA. Translation: EAW94750.1 .
BC047870 mRNA. Translation: AAH47870.1 .
CCDSi CCDS32674.1. [Q86WV1-1 ]
RefSeqi NP_001068567.1. NM_001075099.1. [Q86WV1-2 ]
NP_003717.3. NM_003726.3. [Q86WV1-1 ]
UniGenei Hs.316931.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U5D X-ray 1.70 A/B/C/D 108-213 [» ]
ProteinModelPortali Q86WV1.
SMRi Q86WV1. Positions 7-213, 301-351.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114184. 11 interactions.
IntActi Q86WV1. 3 interactions.
MINTi MINT-6939971.
STRINGi 9606.ENSP00000338171.

PTM databases

PhosphoSitei Q86WV1.

Polymorphism databases

DMDMi 269849660.

Proteomic databases

MaxQBi Q86WV1.
PaxDbi Q86WV1.
PRIDEi Q86WV1.

Protocols and materials databases

DNASUi 8631.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336915 ; ENSP00000338171 ; ENSG00000141293 . [Q86WV1-1 ]
ENST00000584924 ; ENSP00000464311 ; ENSG00000141293 . [Q86WV1-1 ]
GeneIDi 8631.
KEGGi hsa:8631.
UCSCi uc002ini.1. human. [Q86WV1-1 ]
uc002inj.1. human. [Q86WV1-2 ]

Organism-specific databases

CTDi 8631.
GeneCardsi GC17M046210.
HGNCi HGNC:15605. SKAP1.
HPAi CAB025882.
HPA002969.
MIMi 604969. gene.
neXtProti NX_Q86WV1.
PharmGKBi PA162403362.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG76786.
HOGENOMi HOG000231109.
HOVERGENi HBG052827.
InParanoidi Q86WV1.
KOi K17699.
OMAi HLRRDSK.
OrthoDBi EOG7K6PVB.
PhylomeDBi Q86WV1.
TreeFami TF331055.

Enzyme and pathway databases

SignaLinki Q86WV1.

Miscellaneous databases

EvolutionaryTracei Q86WV1.
GeneWikii SKAP1.
GenomeRNAii 8631.
NextBioi 32353.
PROi Q86WV1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q86WV1.
Bgeei Q86WV1.
CleanExi HS_SKAP1.
Genevestigatori Q86WV1.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00233. PH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of SKAP55, a novel protein that associates with p59fyn in human T-lymphocytes."
    Marie-Cardine A., Bruyns E., Eckerskorn C., Kirchgessner H., Meuer S., Schraven B.
    J. Biol. Chem. 272:16077-16080(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 101-110; 120-130 AND 153-158, PHOSPHORYLATION, INTERACTION WITH FYN, TISSUE SPECIFICITY, VARIANT SER-161.
    Tissue: Blood.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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 2).
    Tissue: Pancreas.
  5. "Molecular interaction between the Fyn-associated protein SKAP55 and the SLP-76-associated phosphoprotein SLAP-130."
    Marie-Cardine A., Hendricks-Taylor L.R., Boerth N.J., Zhao H., Schraven B., Koretzky G.A.
    J. Biol. Chem. 273:25789-25795(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYB, MUTAGENESIS OF TRP-333.
  6. "FYB (FYN binding protein) serves as a binding partner for lymphoid protein and FYN kinase substrate SKAP55 and a SKAP55-related protein in T cells."
    Liu J., Kang H., Raab M., da Silva A.J., Kraeft S.-K., Rudd C.E.
    Proc. Natl. Acad. Sci. U.S.A. 95:8779-8784(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYB, SUBCELLULAR LOCATION.
  7. "SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55."
    Kang H., Freund C., Duke-Cohan J.S., Musacchio A., Wagner G., Rudd C.E.
    EMBO J. 19:2889-2899(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYB, MUTAGENESIS OF TYR-295 AND TYR-298, FUNCTION.
  8. "SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation."
    Wu L., Yu Z., Shen S.-H.
    J. Biol. Chem. 277:40420-40427(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, MUTAGENESIS OF TYR-219; TYR-232; TYR-271 AND TRP-333, PHOSPHORYLATION, INTERACTION WITH GRB2.
  9. "SKAP55 coupled with CD45 positively regulates T-cell receptor-mediated gene transcription."
    Wu L., Fu J., Shen S.-H.
    Mol. Cell. Biol. 22:2673-2686(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-219 AND TYR-232, DEPHOSPHORYLATION BY PTPRC, MUTAGENESIS OF TYR-219; TYR-232 AND TYR-271, SUBCELLULAR LOCATION, FUNCTION.
  10. "SKAP-55 regulates integrin adhesion and formation of T cell-APC conjugates."
    Wang H., Moon E.-Y., Azouz A., Wu X., Smith A., Schneider H., Hogg N., Rudd C.E.
    Nat. Immunol. 4:366-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells."
    Huang Y., Norton D.D., Precht P., Martindale J.L., Burkhardt J.K., Wange R.L.
    J. Biol. Chem. 280:23576-23583(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FYB, MUTAGENESIS OF TRP-333.
  12. "An essential role for SKAP-55 in LFA-1 clustering on T cells that cannot be substituted by SKAP-55R."
    Jo E.-K., Wang H., Rudd C.E.
    J. Exp. Med. 201:1733-1739(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Regulation and function of SKAP-55 non-canonical motif binding to the SH3c domain of adhesion and degranulation-promoting adaptor protein."
    Duke-Cohan J.S., Kang H., Liu H., Rudd C.E.
    J. Biol. Chem. 281:13743-13750(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH FYB.
  14. "The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1."
    Kliche S., Breitling D., Togni M., Pusch R., Heuer K., Wang X., Freund C., Kasirer-Friede A., Menasche G., Koretzky G.A., Schraven B.
    Mol. Cell. Biol. 26:7130-7144(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "SKAP55 modulates T cell antigen receptor-induced activation of the Ras-Erk-AP1 pathway by binding RasGRP1."
    Kosco K.A., Cerignoli F., Williams S., Abraham R.T., Mustelin T.
    Mol. Immunol. 45:510-522(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASGRP1.
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Structural basis for the dimerization and phosphoinositide specificity of the Src kinase-associated phosphoproteins SKAP55 and SKAP-HOM."
    Tang Y., Swanson K.D., Neel B.G., Eck M.J.
    Submitted (JUL-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 108-213.

Entry informationi

Entry nameiSKAP1_HUMAN
AccessioniPrimary (citable) accession number: Q86WV1
Secondary accession number(s): D3DTV1, O15268
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 24, 2009
Last modified: September 3, 2014
This is version 100 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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