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Protein

Src kinase-associated phosphoprotein 2

Gene

Skap2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway.3 Publications

GO - Molecular functioni

GO - Biological processi

  • B cell activation Source: UniProtKB-KW
  • immune response-activating signal transduction Source: GO_Central
  • negative regulation of cell proliferation Source: MGI

Keywordsi

Biological processB-cell activation

Enzyme and pathway databases

ReactomeiR-MMU-391160 Signal regulatory protein family interactions

Names & Taxonomyi

Protein namesi
Recommended name:
Src kinase-associated phosphoprotein 2
Alternative name(s):
Pyk2/RAFTK-associated protein
SKAP55 homolog
Short name:
SKAP-HOM
Src family-associated phosphoprotein 2
Src kinase-associated phosphoprotein 55-related protein
Src-associated adapter protein with PH and SH3 domains
Gene namesi
Name:Skap2
Synonyms:Prap, Ra70, Saps, Scap2, Skap55r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1889206 Skap2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice are healthy and do not display any obvious abnormality. They have normal T-cell, platelet and macrophage function, but show reduced levels of spontaneous immunoglobulins in the serum, and defects in B-cell proliferation.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi260Y → F: Abolishes interaction with FYN, phosphorylation by FYN, and effects on cell growth. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002701801 – 358Src kinase-associated phosphoprotein 2Add BLAST358

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphoserineBy similarity1
Modified residuei9PhosphoserineBy similarity1
Modified residuei75PhosphotyrosineCombined sources1
Modified residuei87PhosphoserineBy similarity1
Modified residuei90PhosphoserineBy similarity1
Modified residuei151PhosphotyrosineCombined sources1
Modified residuei197PhosphotyrosineBy similarity1
Modified residuei223PhosphoserineBy similarity1
Modified residuei260Phosphotyrosine; by FYNCombined sources1 Publication1
Modified residuei272PhosphoserineBy similarity1
Modified residuei282PhosphoserineBy similarity1
Modified residuei285PhosphoserineBy similarity1

Post-translational modificationi

Dephosphorylated on Tyr-75 by PTPN22 (By similarity). Phosphorylated by FYN on Tyr-260. In case of infection with Y.pseudotuberculosis, dephosphorylated by bacterial phosphatase yopH.By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3UND0
PaxDbiQ3UND0
PeptideAtlasiQ3UND0
PRIDEiQ3UND0

PTM databases

iPTMnetiQ3UND0
PhosphoSitePlusiQ3UND0

Expressioni

Tissue specificityi

Expressed in kidney, lung, liver, spleen, bone marrow and testis. Present in T-cells, B-cells, and all cells of the myelomonocytic lineage. Present in all brain regions, with highest levels in neurons from the Purkinje cell layer, hippocampal gyrus, cortex and substantia nigra (at protein level).4 Publications

Inductioni

By IL-6 in myeloid cells.1 Publication

Gene expression databases

BgeeiENSMUSG00000059182
CleanExiMM_SKAP2
ExpressionAtlasiQ3UND0 baseline and differential
GenevisibleiQ3UND0 MM

Interactioni

Subunit structurei

Interacts with LAT, GRB2, PTK2B and PRAM1 (By similarity). Homodimer. Interacts with FYB1, which is required for SKAP2 protein stability. Interacts with PTPNS1. Part of a complex consisting of SKAP2, FYB1 and PTPNS1. Part of a complex consisting of SKAP2, FYB1 and LILRB3. May interact with actin. May interact with FYN, HCK and LYN. Interacts with FASLG (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN22Q9Y2R22EBI-642769,EBI-1211241From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207619, 1 interactor
CORUMiQ3UND0
IntActiQ3UND0, 3 interactors
MINTiQ3UND0
STRINGi10090.ENSMUSP00000077342

Structurei

Secondary structure

1358
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 29Combined sources15
Turni30 – 34Combined sources5
Helixi39 – 55Combined sources17
Helixi56 – 59Combined sources4
Helixi61 – 63Combined sources3
Helixi111 – 113Combined sources3
Beta strandi115 – 126Combined sources12
Beta strandi128 – 130Combined sources3
Turni132 – 134Combined sources3
Beta strandi136 – 145Combined sources10
Beta strandi148 – 154Combined sources7
Beta strandi161 – 165Combined sources5
Beta strandi170 – 173Combined sources4
Helixi175 – 177Combined sources3
Helixi183 – 185Combined sources3
Beta strandi186 – 190Combined sources5
Beta strandi192 – 194Combined sources3
Beta strandi196 – 200Combined sources5
Helixi204 – 217Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M0VNMR-B73-79[»]
1U5EX-ray2.60A/B14-222[»]
1U5FX-ray1.90A111-248[»]
1U5GX-ray2.10A/B/C/D103-222[»]
2OTXX-ray2.60A/B12-222[»]
ProteinModelPortaliQ3UND0
SMRiQ3UND0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3UND0

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini116 – 219PHPROSITE-ProRule annotationAdd BLAST104
Domaini296 – 357SH3PROSITE-ProRule annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 64HomodimerizationAdd BLAST51

Domaini

The SH3 domain interacts with FYB1 and PTK2B.By similarity

Sequence similaritiesi

Belongs to the SKAP family.Curated

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiENOG410IH8Q Eukaryota
ENOG410ZVZV LUCA
GeneTreeiENSGT00390000017856
HOGENOMiHOG000231109
HOVERGENiHBG052827
InParanoidiQ3UND0
OMAiWDCTGAL
OrthoDBiEOG091G0HBY
PhylomeDBiQ3UND0
TreeFamiTF331055

Family and domain databases

Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR037781 SKAP_fam
PANTHERiPTHR15129 PTHR15129, 1 hit
PfamiView protein in Pfam
PF00169 PH, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00452 SH3DOMAIN
SMARTiView protein in SMART
SM00233 PH, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS50003 PH_DOMAIN, 1 hit
PS50002 SH3, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UND0-1) [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
MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK
60 70 80 90 100
KIKDVKSVYL QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP
110 120 130 140 150
SDGNQFPPIA AQDLPFVIKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY
160 170 180 190 200
YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD GKKDCCFEIC APDKRIYQFT
210 220 230 240 250
AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV DHPAAVSSPQ
260 270 280 290 300
RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF
310 320 330 340 350
YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA

YLMEMYDI
Length:358
Mass (Da):40,712
Last modified:January 9, 2007 - v2
Checksum:iB66973A656E44E05
GO
Isoform 2 (identifier: Q3UND0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     22-28: Missing.

Note: No experimental confirmation available.
Show »
Length:351
Mass (Da):39,950
Checksum:iA6C08305272498D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16E → K in BAE25817 (PubMed:16141072).Curated1
Sequence conflicti104N → P AA sequence (PubMed:11207596).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02218422 – 28Missing in isoform 2. 1 Publication7

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051324 mRNA Translation: AAC99297.1
AB014485 mRNA Translation: BAA77253.1
AK076000 mRNA Translation: BAC36111.1
AK144289 mRNA Translation: BAE25817.1
BC003711 mRNA Translation: AAH03711.1
CCDSiCCDS20137.1 [Q3UND0-1]
RefSeqiNP_061243.1, NM_018773.2 [Q3UND0-1]
UniGeneiMm.221479
Mm.392558

Genome annotation databases

EnsembliENSMUST00000078214; ENSMUSP00000077342; ENSMUSG00000059182 [Q3UND0-2]
ENSMUST00000204778; ENSMUSP00000145462; ENSMUSG00000059182 [Q3UND0-1]
GeneIDi54353
KEGGimmu:54353
UCSCiuc009bxv.1 mouse [Q3UND0-1]
uc009bxw.1 mouse [Q3UND0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSKAP2_MOUSE
AccessioniPrimary (citable) accession number: Q3UND0
Secondary accession number(s): Q8BK74, Q9Z2K4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: May 23, 2018
This is version 117 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health