SKAP2_RAT
ID SKAP2_RAT Reviewed; 358 AA.
AC Q920G0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Src kinase-associated phosphoprotein 2;
DE AltName: Full=SKAP55 homolog;
DE Short=SKAP-55HOM;
DE Short=SKAP-HOM;
DE Short=SKAP55-HOM;
DE AltName: Full=Src family-associated phosphoprotein 2;
DE AltName: Full=Src kinase-associated phosphoprotein 55-related protein;
GN Name=Skap2; Synonyms=Scap2, Skap55r;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RA Sada K., Hong S., Siraganian R.;
RT "Src kinase-associated phosphoprotein homolog (SKAP55-HOM) in signaling
RT from the high affinity IgE receptor aggregation.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-9; SER-87; SER-90;
RP SER-223; SER-272; SER-282 AND SER-285, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; AF302132; AAK97262.1; -; mRNA.
DR EMBL; BC070949; AAH70949.1; -; mRNA.
DR RefSeq; NP_569097.1; NM_130413.1.
DR RefSeq; XP_006236539.1; XM_006236477.3.
DR RefSeq; XP_006236540.1; XM_006236478.3.
DR AlphaFoldDB; Q920G0; -.
DR SMR; Q920G0; -.
DR STRING; 10116.ENSRNOP00000016608; -.
DR iPTMnet; Q920G0; -.
DR PhosphoSitePlus; Q920G0; -.
DR PaxDb; Q920G0; -.
DR PRIDE; Q920G0; -.
DR Ensembl; ENSRNOT00000016608; ENSRNOP00000016608; ENSRNOG00000012228.
DR GeneID; 155183; -.
DR KEGG; rno:155183; -.
DR CTD; 8935; -.
DR RGD; 620159; Skap2.
DR eggNOG; ENOG502QVFD; Eukaryota.
DR GeneTree; ENSGT00390000017856; -.
DR HOGENOM; CLU_062032_0_0_1; -.
DR InParanoid; Q920G0; -.
DR OMA; KQGFPQD; -.
DR OrthoDB; 767446at2759; -.
DR PhylomeDB; Q920G0; -.
DR TreeFam; TF331055; -.
DR Reactome; R-RNO-391160; Signal regulatory protein family interactions.
DR PRO; PR:Q920G0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000012228; Expressed in lung and 19 other tissues.
DR Genevisible; Q920G0; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
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 1: Evidence at protein 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_0000270182"
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 60..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O75563"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 260
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UND0"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 358 AA; 40717 MW; B2E5374860C9D9EE CRC64;
MPNPGSTSSP GSIPEEIRNL LADVETFVAD TLKGENLSKK AKEKRDSLIK KIKDVKSVYP
QEFQDKGDAE EGDEYDDPFA GPPDTISLAS ERYDKDDDGP SDGNQFPPIA AQDLSFVIKA
GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIEGYD VRMNNTLRKD
AKKDCCFEIC APDKRIYQFT AASPKDAEEW VQQLKFILQD MGSDVIPEDE DEKGDLYDDV
DHPVPVSSPQ RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVQHPS GDKSTDYANF
YQGLWDCTGS LSDELSFKRG DVIYILSKEY NRYGWWVGEM QGAIGLVPKA YLMEMYDI
