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Database: UniProt
Entry: A7MAZ3
LinkDB: A7MAZ3
Original site: A7MAZ3 
ID   UBA5_BOVIN              Reviewed;         404 AA.
AC   A7MAZ3;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   16-JAN-2019, entry version 76.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE            Short=Ubiquitin-activating enzyme 5;
DE   AltName: Full=UFM1-activating enzyme;
DE   AltName: Full=Ubiquitin-activating enzyme E1 domain-containing protein 1;
GN   Name=UBA5; Synonyms=UBE1DC1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E1-like enzyme which activates UFM1 and SUMO2.
CC       {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with UFC1. Interacts with
CC       UFM1. {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ9}.
CC       Nucleus {ECO:0000250|UniProtKB:Q9GZZ9}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9GZZ9}. Note=Localizes mainly in the
CC       cytoplasm, while it localizes to the nucleus in presence of SUMO2.
CC       {ECO:0000250|UniProtKB:Q9GZZ9}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000305}.
DR   EMBL; BC151254; AAI51255.1; -; mRNA.
DR   RefSeq; NP_001094537.1; NM_001101067.2.
DR   UniGene; Bt.17929; -.
DR   ProteinModelPortal; A7MAZ3; -.
DR   SMR; A7MAZ3; -.
DR   STRING; 9913.ENSBTAP00000005894; -.
DR   PaxDb; A7MAZ3; -.
DR   PeptideAtlas; A7MAZ3; -.
DR   PRIDE; A7MAZ3; -.
DR   Ensembl; ENSBTAT00000005894; ENSBTAP00000005894; ENSBTAG00000004495.
DR   GeneID; 509292; -.
DR   KEGG; bta:509292; -.
DR   CTD; 79876; -.
DR   VGNC; VGNC:36564; UBA5.
DR   eggNOG; KOG2336; Eukaryota.
DR   eggNOG; COG0476; LUCA.
DR   GeneTree; ENSGT00940000156177; -.
DR   HOGENOM; HOG000256352; -.
DR   HOVERGEN; HBG056496; -.
DR   InParanoid; A7MAZ3; -.
DR   KO; K12164; -.
DR   OMA; ETHNYNI; -.
DR   OrthoDB; 1092362at2759; -.
DR   TreeFam; TF314168; -.
DR   Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000004495; Expressed in 10 organ(s), highest expression level in spleen.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071566; F:UFM1 activating enzyme activity; ISS:UniProtKB.
DR   GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR   GO; GO:1990592; P:protein K69-linked ufmylation; ISS:UniProtKB.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0071569; P:protein ufmylation; ISS:UniProtKB.
DR   GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Golgi apparatus;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation pathway; Zinc.
FT   CHAIN         1    404       Ubiquitin-like modifier-activating enzyme
FT                                5.
FT                                /FTId=PRO_0000391931.
FT   ACT_SITE    250    250       Glycyl thioester intermediate.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       226    226       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       229    229       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       303    303       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   METAL       308    308       Zinc. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING      83     83       ATP; via amide nitrogen.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     104    104       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     127    127       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     150    150       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   BINDING     184    184       ATP. {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   MOD_RES      45     45       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   MOD_RES     358    358       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9GZZ9}.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8VE47}.
SQ   SEQUENCE   404 AA;  44697 MW;  F1FD2BB9A5D1BC6B CRC64;
     MAESVERLQQ RVEELERELA QERSRRALGS GDGGGGRARI EKMSSEVVDS NPYSRLMALK
     RMGIVSDYEK IRTFTVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP
     HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFEHF MNRISNGGLE EGKPVDLVLS
     CVDNFEARMT INTACNELGQ TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID
     EKTLKREGVC AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN
     PQCDDRNCRK QQKEYKKKVA ALPKQEVIQE EGEIIHEDNE WGIELVSEIS EEELKKSSGP
     IPDLPEGIIV AYTVPQKQED SVPEVTVEDS GESLEDLMAK MKNI
//
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