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Database: UniProt
Entry: B4E3G5_HUMAN
LinkDB: B4E3G5_HUMAN
Original site: B4E3G5_HUMAN 
ID   B4E3G5_HUMAN            Unreviewed;       251 AA.
AC   B4E3G5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   22-FEB-2023, entry version 52.
DE   SubName: Full=cDNA FLJ55275, highly similar to Phosphatidylinositol 3-kinase regulatory subunit gamma {ECO:0000313|EMBL:BAG65477.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG65477.1};
RN   [1] {ECO:0000313|EMBL:BAG65477.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Uterus {ECO:0000313|EMBL:BAG65477.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC       {ECO:0000256|ARBA:ARBA00009442}.
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DR   EMBL; AK304713; BAG65477.1; -; mRNA.
DR   AlphaFoldDB; B4E3G5; -.
DR   SMR; B4E3G5; -.
DR   PeptideAtlas; B4E3G5; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd09930; SH2_cSH2_p85_like; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR032498; PI3K_P85_iSH2.
DR   InterPro; IPR035020; PI3kinase_P85_cSH2.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10155:SF10; PI3K21B, ISOFORM B; 1.
DR   Pfam; PF16454; PI3K_P85_iSH2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00678; PI3KINASEP85.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAG65477.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Transferase {ECO:0000313|EMBL:BAG65477.1}.
FT   DOMAIN          148..242
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   COILED          36..84
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   251 AA;  29737 MW;  4A26788C84EACD9C CRC64;
     MKRTAIEAFN ETIKIFEEQC HTQEQHSKEY IERFRREGNE KEIERIMMNY DKLKSRLGEI
     HDSKMRLEQD LKKQALDNRE IDKKMNSIKP DLIQLRKIRD QHLVWLNHKG VRQKRLNVWL
     GIKNEDADEN YFINEEDENL PHYDEKTWFV EDINRVQAED LLYGKPDGAF LIRESSKKGC
     YACSVVADGE VKHCVIYSTA RGYGFAEPYN LYSSLKELVL HYQQTSLVQH NDSLNVRLAY
     PVHAQMPSLC R
//
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