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3BP5L_PONAB
ID   3BP5L_PONAB             Reviewed;         393 AA.
AC   Q5R9X9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=SH3 domain-binding protein 5-like;
DE            Short=SH3BP-5-like;
GN   Name=SH3BP5L;
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: Functions as guanine nucleotide exchange factor (GEF) for
CC       RAB11A. {ECO:0000250|UniProtKB:Q7L8J4}.
CC   -!- SIMILARITY: Belongs to the SH3BP5 family. {ECO:0000305}.
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DR   EMBL; CR859251; CAH91431.1; -; mRNA.
DR   RefSeq; NP_001125840.1; NM_001132368.2.
DR   AlphaFoldDB; Q5R9X9; -.
DR   SMR; Q5R9X9; -.
DR   STRING; 9601.ENSPPYP00000000006; -.
DR   GeneID; 100172769; -.
DR   KEGG; pon:100172769; -.
DR   CTD; 80851; -.
DR   eggNOG; KOG2008; Eukaryota.
DR   InParanoid; Q5R9X9; -.
DR   OrthoDB; 566222at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   InterPro; IPR007940; SH3BP5.
DR   PANTHER; PTHR19423; PTHR19423; 1.
DR   Pfam; PF05276; SH3BP5; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..393
FT                   /note="SH3 domain-binding protein 5-like"
FT                   /id="PRO_0000317510"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          59..140
FT                   /evidence="ECO:0000255"
FT   COILED          169..272
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        17..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L8J4"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L8J4"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LH9"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L8J4"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L8J4"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L8J4"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7L8J4"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99LH9"
SQ   SEQUENCE   393 AA;  43449 MW;  B1E021EDF0E581B4 CRC64;
     MAELRQVPGG RETPQGELRP EVVEDEVPRS PVAEEPGGGG SSSSEAKLSP REEEELDPRI
     QEELEHLNQA SEEINQVELQ LDEARTTYRR ILQESARKLN TQGSHLGSCI EKARPYYEAR
     RLAKEAQQET QKAALRYERA VSMHNAAREM VLVAEQGVMA DKNRLDPTWQ EMLNHATCKV
     NEAEEERLRG EREHQRVTRL CQQAEARVQA LQKTLRRAIG KSRPYFELKA QFSQILEEHK
     AKVTELEQQV AQAKTRYSVA LRNLEQISEQ IHARRRGDLP PHPLGPRRSS PVGAEAGPED
     TGDGDSGIEG AEGAGLEEGS SLGPGPAPDT DTLSLLSLRT VASDLQKCDS VEHLRGLSDH
     VSLDGQELGT RSGGRRGSDG GVRGGRHQRS VSL
 
 
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