ID   SKAP2_PONAB             Reviewed;         359 AA.
AC   Q5RDS2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Src kinase-associated phosphoprotein 2;
DE   AltName: Full=Src family-associated phosphoprotein 2;
GN   Name=SKAP2; Synonyms=SCAP2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR857829; CAH90085.1; -; mRNA.
DR   AlphaFoldDB; Q5RDS2; -.
DR   SMR; Q5RDS2; -.
DR   STRING; 9601.ENSPPYP00000019851; -.
DR   PRIDE; Q5RDS2; -.
DR   eggNOG; ENOG502QVFD; Eukaryota.
DR   InParanoid; Q5RDS2; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
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..359
FT                   /note="Src kinase-associated phosphoprotein 2"
FT                   /id="PRO_0000270181"
FT   DOMAIN          116..219
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          297..358
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          67..88
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         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q920G0"
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         261
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UND0"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q920G0"
FT   CONFLICT        1
FT                   /note="M -> V (in Ref. 1; CAH90085)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  41159 MW;  2AEEE9F9313EACAE CRC64;
     MPNPSSTSSP YPLPEEIRNL LADVETFVAD ILKGENLSKK AKEKRESLIK KIKDVKSIYL
     QEFRDKGDAE DGEEYDDPFA GPPDTISLAS ERYDKDDEAT SDGAQFPPIA AQDLPFVLKA
     GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYS VRMNNALRKD
     GKKDCCFEIS APDKRIYQFT AASPKDAEEW VQQLKFVLQD MESDIIPEDY DERGELYDDV
     DHPLPISNLP TSSQPIDDEI YEELPEEEED SAPVKVVEQR KMGQDSVHHT SGDKSTDYAN
     FYQGLWDCTG AFSDELSFKR GDVIYILSKE YNRYGWWVGE MKGAIGLVPK AYIMEMYDI