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Ubiquitin-conjugating enzyme E2 H (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme H) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme H) (UbcH2) (Ubiquitin carrier protein H) (Ubiquitin-conjugating enzyme E2-20K) (Ubiquitin-protein ligase H)

 UBE2H_HUMAN             Reviewed;         183 AA.
P62256; A4D1L6; C9JY93; P37286; Q7Z6F4;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
18-JUL-2018, entry version 146.
RecName: Full=Ubiquitin-conjugating enzyme E2 H;
EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme H;
EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
AltName: Full=E2 ubiquitin-conjugating enzyme H;
AltName: Full=UbcH2;
AltName: Full=Ubiquitin carrier protein H;
AltName: Full=Ubiquitin-conjugating enzyme E2-20K;
AltName: Full=Ubiquitin-protein ligase H;
Name=UBE2H;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=8132613;
Kaiser P., Seufert W., Hoefferer L., Kofler B., Sachsenmaier C.,
Herzog H., Jentsch S., Schweiger M., Schneider R.;
"A human ubiquitin-conjugating enzyme homologous to yeast UBC8.";
J. Biol. Chem. 269:8797-8802(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Lin L., Li S., Li H., Zhou G., Shen C., Zheng G., Ke R., Zhong G.,
Yu R., Yang S.;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME.
PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014;
Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.;
"E3-independent monoubiquitination of ubiquitin-binding proteins.";
Mol. Cell 26:891-898(2007).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11] {ECO:0000244|PDB:2Z5D}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-160, AND
AUTOUBIQUITINATION.
PubMed=22496338; DOI=10.1074/mcp.O111.013706;
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J.,
Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K.,
Arrowsmith C.H., Raught B., Dhe-Paganon S.;
"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
function screen.";
Mol. Cell. Proteomics 11:329-341(2012).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In vitro catalyzes 'Lys-
11'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to
ubiquitinate histone H2A. {ECO:0000269|PubMed:20061386,
ECO:0000269|PubMed:8132613}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:20061386}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-
activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:17588522}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- INTERACTION:
P43356:MAGEA2B; NbExp=2; IntAct=EBI-2129909, EBI-5650739;
Q9UBF1:MAGEC2; NbExp=3; IntAct=EBI-2129909, EBI-5651487;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62256-1; Sequence=Displayed;
Name=2;
IsoId=P62256-2; Sequence=VSP_044580;
Note=No experimental confirmation available.;
-!- PTM: Autoubiquitinated in vitro in the presence of NEDD4L.
{ECO:0000269|PubMed:22496338}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; Z29328; CAA82525.1; -; mRNA.
EMBL; Z29330; CAA82527.1; -; mRNA.
EMBL; Z29331; CAA82528.1; -; mRNA.
EMBL; AY302138; AAP57630.1; -; mRNA.
EMBL; BT006756; AAP35402.1; -; mRNA.
EMBL; AC073320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236950; EAL24099.1; -; Genomic_DNA.
EMBL; CH471070; EAW83736.1; -; Genomic_DNA.
EMBL; BC006277; AAH06277.1; -; mRNA.
CCDS; CCDS47710.1; -. [P62256-2]
CCDS; CCDS5814.1; -. [P62256-1]
PIR; A53516; A53516.
RefSeq; NP_001189427.1; NM_001202498.1.
RefSeq; NP_003335.1; NM_003344.3. [P62256-1]
RefSeq; NP_874356.1; NM_182697.2. [P62256-2]
UniGene; Hs.643548; -.
PDB; 2Z5D; X-ray; 2.10 A; A/B=1-160.
PDBsum; 2Z5D; -.
ProteinModelPortal; P62256; -.
SMR; P62256; -.
BioGrid; 113176; 89.
IntAct; P62256; 51.
STRING; 9606.ENSP00000347836; -.
MoonDB; P62256; Predicted.
iPTMnet; P62256; -.
PhosphoSitePlus; P62256; -.
BioMuta; UBE2H; -.
DMDM; 51338683; -.
EPD; P62256; -.
MaxQB; P62256; -.
PaxDb; P62256; -.
PeptideAtlas; P62256; -.
PRIDE; P62256; -.
ProteomicsDB; 57376; -.
DNASU; 7328; -.
Ensembl; ENST00000355621; ENSP00000347836; ENSG00000186591. [P62256-1]
Ensembl; ENST00000473814; ENSP00000419097; ENSG00000186591. [P62256-2]
GeneID; 7328; -.
KEGG; hsa:7328; -.
UCSC; uc003vpf.3; human. [P62256-1]
CTD; 7328; -.
DisGeNET; 7328; -.
EuPathDB; HostDB:ENSG00000186591.11; -.
GeneCards; UBE2H; -.
H-InvDB; HIX0123428; -.
HGNC; HGNC:12484; UBE2H.
HPA; HPA003302; -.
MIM; 601082; gene.
neXtProt; NX_P62256; -.
OpenTargets; ENSG00000186591; -.
PharmGKB; PA37133; -.
eggNOG; KOG0416; Eukaryota.
eggNOG; ENOG410XRC5; LUCA.
GeneTree; ENSGT00390000004852; -.
HOGENOM; HOG000233452; -.
HOVERGEN; HBG063308; -.
InParanoid; P62256; -.
KO; K10576; -.
OMA; NLVNDNM; -.
OrthoDB; EOG091G0RI1; -.
PhylomeDB; P62256; -.
TreeFam; TF101121; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P62256; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2H; human.
EvolutionaryTrace; P62256; -.
GeneWiki; UBE2H; -.
GenomeRNAi; 7328; -.
PRO; PR:P62256; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000186591; -.
CleanEx; HS_UBE2H; -.
ExpressionAtlas; P62256; baseline and differential.
Genevisible; P62256; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Nucleotide-binding; Reference proteome;
Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 183 Ubiquitin-conjugating enzyme E2 H.
/FTId=PRO_0000082486.
ACT_SITE 87 87 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62257}.
VAR_SEQ 69 99 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_044580.
CONFLICT 165 165 S -> P (in Ref. 2; AAP57630).
{ECO:0000305}.
HELIX 6 20 {ECO:0000244|PDB:2Z5D}.
STRAND 21 23 {ECO:0000244|PDB:2Z5D}.
STRAND 25 30 {ECO:0000244|PDB:2Z5D}.
STRAND 33 39 {ECO:0000244|PDB:2Z5D}.
TURN 45 48 {ECO:0000244|PDB:2Z5D}.
STRAND 50 56 {ECO:0000244|PDB:2Z5D}.
TURN 59 63 {ECO:0000244|PDB:2Z5D}.
STRAND 67 72 {ECO:0000244|PDB:2Z5D}.
TURN 81 83 {ECO:0000244|PDB:2Z5D}.
HELIX 88 94 {ECO:0000244|PDB:2Z5D}.
HELIX 103 106 {ECO:0000244|PDB:2Z5D}.
HELIX 108 114 {ECO:0000244|PDB:2Z5D}.
HELIX 124 132 {ECO:0000244|PDB:2Z5D}.
HELIX 134 148 {ECO:0000244|PDB:2Z5D}.
HELIX 151 154 {ECO:0000244|PDB:2Z5D}.
SEQUENCE 183 AA; 20655 MW; 3DD5D365945F708C CRC64;
MSSPSPGKRR MDTDVVKLIE SKHEVTILGG LNEFVVKFYG PQGTPYEGGV WKVRVDLPDK
YPFKSPSIGF MNKIFHPNID EASGTVCLDV INQTWTALYD LTNIFESFLP QLLAYPNPID
PLNGDAAAMY LHRPEEYKQK IKEYIQKYAT EEALKEQEEG TGDSSSESSM SDFSEDEAQD
MEL


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U1063Rb CLIA HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T


 

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