ID   UB2D1_HUMAN             Reviewed;         147 AA.
AC   P51668;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   07-JUL-2009, entry version 83.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 D1;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase D1;
DE   AltName: Full=Ubiquitin carrier protein D1;
DE   AltName: Full=UbcH5;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 1;
DE   AltName: Full=E2(17)KB 1;
DE   AltName: Full=UBC4/5 homolog;
DE   AltName: Full=Stimulator of Fe transport;
DE            Short=SFT;
GN   Name=UBE2D1; Synonyms=SFT, UBCH5, UBCH5A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94377440; PubMed=8090726; DOI=10.1073/pnas.91.19.8797;
RA   Scheffner M., Huibregtse J.M., Howley P.M.;
RT   "Identification of a human ubiquitin-conjugating enzyme that mediates
RT   the E6-AP-dependent ubiquitination of p53.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:8797-8801(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12480712; DOI=10.1182/blood-2002-07-2192;
RA   Gehrke S.G., Riedel H.-D., Herrmann T., Hadaschik B., Bents K.,
RA   Veltkamp C., Stremmel W.;
RT   "UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is
RT   closely related to SFT, a stimulator of iron transport, and is up-
RT   regulated in hereditary hemochromatosis.";
RL   Blood 101:3288-3293(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 134-147, AND TISSUE SPECIFICITY.
RX   MEDLINE=98031921; PubMed=9362508; DOI=10.1083/jcb.139.4.895;
RA   Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
RT   "Functional expression cloning and characterization of SFT, a
RT   stimulator of Fe transport.";
RL   J. Cell Biol. 139:895-905(1997).
RN   [6]
RP   ERRATUM.
RA   Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
RL   J. Cell Biol. 147:205-205(1999).
RN   [7]
RP   SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; SKP1; APC AND TBL1X.
RX   MEDLINE=21286882; PubMed=11389839; DOI=10.1016/S1097-2765(01)00242-8;
RA   Matsuzawa S., Reed J.C.;
RT   "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
RT   degradation linked to p53 responses.";
RL   Mol. Cell 7:915-926(2001).
RN   [8]
RP   INTERACTION WITH RNF11.
RX   PubMed=14562029; DOI=10.1038/sj.bjc.6601301;
RA   Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J.,
RA   Zubovits J., Burger A.M., Seth A.K.;
RT   "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a
RT   target of Smurf2 E3 ligase.";
RL   Br. J. Cancer 89:1538-1544(2003).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Mediates the selective degradation of short-lived and
CC       abnormal proteins. Functions in the E6/E6-AP-induced
CC       ubiquitination of p53/TP53.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of a E3 ubiquitin ligase complex containing
CC       UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with
CC       RNF11.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Up-regulated in livers of iron-
CC       overloaded patients with hereditary hemochromatosis.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC   -!- CAUTION: PubMed:9362508 cloned and sequenced SFT which consisted
CC       of UBE2D1 last coding exon along with intronic sequences on the
CC       5'-end of this exon. A function in iron transport has been
CC       described.
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DR   EMBL; X78140; CAA55019.1; -; mRNA.
DR   EMBL; AF257220; AAM81086.1; -; mRNA.
DR   EMBL; AJ272367; CAC82177.1; -; mRNA.
DR   EMBL; AJ293565; CAC82097.1; -; Genomic_DNA.
DR   EMBL; BT007041; AAP35690.1; -; mRNA.
DR   EMBL; BC005980; AAH05980.1; -; mRNA.
DR   EMBL; BC015997; AAH15997.1; -; mRNA.
DR   EMBL; AF020761; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00019930; -.
DR   PIR; I39202; I39202.
DR   RefSeq; NP_003329.1; -.
DR   UniGene; Hs.129683; -.
DR   PDB; 2C4P; X-ray; 2.35 A; A/B=1-147.
DR   PDBsum; 2C4P; -.
DR   IntAct; P51668; 3.
DR   PRIDE; P51668; -.
DR   Ensembl; ENSG00000072401; Homo sapiens.
DR   GeneID; 7321; -.
DR   KEGG; hsa:7321; -.
DR   UCSC; uc001jke.1; human.
DR   GeneCards; GC10P059764; -.
DR   H-InvDB; HIX0008841; -.
DR   HGNC; HGNC:12474; UBE2D1.
DR   HPA; HPA003920; -.
DR   MIM; 602961; gene.
DR   PharmGKB; PA37124; -.
DR   HOGENOM; P51668; -.
DR   HOVERGEN; P51668; -.
DR   OMA; P51668; NDLQRDP.
DR   BRENDA; 6.3.2.19; 247.
DR   Reactome; REACT_12034; Signaling by BMP.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_6844; Signaling by TGF beta.
DR   Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
DR   NextBio; 28626; -.
DR   ArrayExpress; P51668; -.
DR   Bgee; P51668; -.
DR   CleanEx; HS_UBE2D1; -.
DR   GermOnline; ENSG00000072401; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent protea...; EXP:Reactome.
DR   GO; GO:0030509; P:BMP signaling pathway; EXP:Reactome.
DR   GO; GO:0051436; P:negative regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN         1    147       Ubiquitin-conjugating enzyme E2 D1.
FT                                /FTId=PRO_0000082460.
FT   ACT_SITE     85     85       Glycyl thioester intermediate (By
FT                                similarity).
FT   HELIX         1     11
FT   TURN         12     15
FT   STRAND       19     26
FT   STRAND       29     38
FT   TURN         44     47
FT   STRAND       49     55
FT   TURN         58     61
FT   STRAND       66     69
FT   HELIX        87     89
FT   TURN         90     92
FT   HELIX        99    111
FT   HELIX       121    129
FT   HELIX       131    145
SQ   SEQUENCE   147 AA;  16602 MW;  2E96FD0179EE119D CRC64;
     MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF FLTVHFPTDY
     PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV
     PDIAQIYKSD KEKYNRHARE WTQKYAM
//