SKAP2_BOVIN
ID SKAP2_BOVIN Reviewed; 358 AA.
AC Q32LP7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Src kinase-associated phosphoprotein 2;
DE AltName: Full=Src family-associated phosphoprotein 2;
GN Name=SKAP2; Synonyms=SCAP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in B-cell and macrophage adhesion processes.
CC In B-cells, may act by coupling the B-cell receptor (BCR) to integrin
CC activation. May play a role in src signaling pathway (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FYB1, which is required for SKAP2 protein
CC stability. Interacts with PTPNS1. Part of a complex consisting of
CC SKAP2, FYB1 and PTPNS1. Part of a complex consisting of SKAP2, FYB1 and
CC LILRB3. Interacts with LAT, GRB2, PTK2B and PRAM1. May interact with
CC actin. May interact with FYN, HCK and LYN. Interacts with FASLG (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain interacts with FYB1 and PTK2B. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SKAP family. {ECO:0000305}.
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DR EMBL; BC109480; AAI09481.1; -; mRNA.
DR RefSeq; NP_001033303.1; NM_001038214.1.
DR AlphaFoldDB; Q32LP7; -.
DR SMR; Q32LP7; -.
DR STRING; 9913.ENSBTAP00000043366; -.
DR PaxDb; Q32LP7; -.
DR PRIDE; Q32LP7; -.
DR Ensembl; ENSBTAT00000046037; ENSBTAP00000043366; ENSBTAG00000005650.
DR GeneID; 616545; -.
DR KEGG; bta:616545; -.
DR CTD; 8935; -.
DR VEuPathDB; HostDB:ENSBTAG00000005650; -.
DR VGNC; VGNC:34646; SKAP2.
DR eggNOG; ENOG502QVFD; Eukaryota.
DR GeneTree; ENSGT00390000017856; -.
DR HOGENOM; CLU_062032_0_0_1; -.
DR InParanoid; Q32LP7; -.
DR OMA; KQGFPQD; -.
DR OrthoDB; 767446at2759; -.
DR TreeFam; TF331055; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000005650; Expressed in monocyte and 104 other tissues.
DR ExpressionAtlas; Q32LP7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037781; SKAP_fam.
DR PANTHER; PTHR15129; PTHR15129; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW B-cell activation; Cytoplasm; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..358
FT /note="Src kinase-associated phosphoprotein 2"
FT /id="PRO_0000270178"
FT DOMAIN 116..219
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 296..357
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 62..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75563"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75563"
FT MOD_RES 75
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75563"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UND0"
FT MOD_RES 197
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75563"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 260
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UND0"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920G0"
SQ SEQUENCE 358 AA; 40839 MW; 38815A683AC81908 CRC64;
MPNPSSISAP YPLPEEIRNL LADVETFVAD ILRGENLSKK AKEKRDALVK KIKDVKSIYL
QESQDKGDAE DGEEYDDPFA GPPDTISLAS ERYDKDDEAP SDGNQFPPIA AQDLPFVLKA
GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYN VRMNNTLRKD
GKKDCCFEIS APDKRIYQFT AASPKDAEEW VQQLNFVLQD MGSDVIPEDD EERGELYDDV
DHPLPSSSPT RSLPIDDEIY EELPEEEEDG ALVKVEGQRK MSQDSVHHTT GDKSTNYANF
YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA YVMEMYDI
