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API5_PONAB
ID   API5_PONAB              Reviewed;         504 AA.
AC   Q5R644;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Apoptosis inhibitor 5;
DE            Short=API-5;
GN   Name=API5;
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: Antiapoptotic factor that may have a role in protein
CC       assembly. Negatively regulates ACIN1. By binding to ACIN1, it
CC       suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA
CC       fragmentation. Also known to efficiently suppress E2F1-induced
CC       apoptosis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Interacts with FGF2 and ACIN1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Mainly nuclear.
CC   -!- PTM: Acetylation at Lys-251 impairs antiapoptotic function.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the API5 family. {ECO:0000305}.
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DR   EMBL; CR860652; CAH92772.1; -; mRNA.
DR   RefSeq; NP_001126616.1; NM_001133144.1.
DR   AlphaFoldDB; Q5R644; -.
DR   SMR; Q5R644; -.
DR   STRING; 9601.ENSPPYP00000003839; -.
DR   GeneID; 100173613; -.
DR   KEGG; pon:100173613; -.
DR   CTD; 8539; -.
DR   eggNOG; KOG2213; Eukaryota.
DR   InParanoid; Q5R644; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR008383; API5.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   PANTHER; PTHR12758; PTHR12758; 1.
DR   Pfam; PF05918; API5; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Apoptosis; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..504
FT                   /note="Apoptosis inhibitor 5"
FT                   /id="PRO_0000064636"
FT   REGION          1..360
FT                   /note="ARM-like and Heat-like helical repeats"
FT                   /evidence="ECO:0000250"
FT   REGION          370..391
FT                   /note="Leucine-zipper"
FT   REGION          452..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           454..475
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        483..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         251
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZZ5"
FT   MOD_RES         399
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZZ5"
FT   MOD_RES         462
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZZ5"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZZ5"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35841"
SQ   SEQUENCE   504 AA;  56770 MW;  D4A0D283CDFC4A87 CRC64;
     MPTVEELYRN YGILADATEQ VGQHKDAYQV ILDGVKGGTK EKRLAAQFIP KFFKHFPELA
     DSAINAQLDL CEDEDVSIRR QAIKELPQFA TGENLPRVAD ILTQLLQTDD SAEFNLVNNA
     LLSIFKMDAK GTLGGLFSQI LQGEDIVRER AIKFLSTKLK TLPDEVLTKE VEELILTESK
     KVLEDVTGEE FVLFMKILSG LKSLQTVSGR QQLVELVAEQ ADLEQTFNPS DPDCVDRLLQ
     CTRQAVPLFS KNVHSTRFVT YFCEQVLPNL GTLTTPVEGL DIQLEVLKLL AEMSSFCGDM
     EKLETNLRKL FDKLLEYMPL PPEEAENGEN AGNEEPKLQF SYVECLLYSF HQLGRKLPDF
     LTAKLNAEKL KDFKIRLQYF ARGLQVYIRQ LRLALQGKTG EALKTEENKI KVVALKITNN
     INVLIKDLFH IPPSYKSTVT LSWKPVQKVE IGQKRASEDT TSGSPPKKSS AGPKRDARQI
     YNPPSGKYSS NLGNFNYERS LQGK
 
 
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