Full text data of UBE2H
UBE2H
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-conjugating enzyme E2 H; 6.3.2.19 (UbcH2; Ubiquitin carrier protein H; Ubiquitin-conjugating enzyme E2-20K; Ubiquitin-protein ligase H)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-conjugating enzyme E2 H; 6.3.2.19 (UbcH2; Ubiquitin carrier protein H; Ubiquitin-conjugating enzyme E2-20K; Ubiquitin-protein ligase H)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62256
ID UBE2H_HUMAN Reviewed; 183 AA.
AC P62256; A4D1L6; C9JY93; P37286; Q7Z6F4;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 H;
DE EC=6.3.2.19;
DE AltName: Full=UbcH2;
DE AltName: Full=Ubiquitin carrier protein H;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-20K;
DE AltName: Full=Ubiquitin-protein ligase H;
GN Name=UBE2H;
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] (ISOFORM 1), AND FUNCTION.
RX PubMed=8132613;
RA Kaiser P., Seufert W., Hoefferer L., Kofler B., Sachsenmaier C.,
RA Herzog H., Jentsch S., Schweiger M., Schneider R.;
RT "A human ubiquitin-conjugating enzyme homologous to yeast UBC8.";
RL J. Biol. Chem. 269:8797-8802(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Lin L., Li S., Li H., Zhou G., Shen C., Zheng G., Ke R., Zhong G.,
RA Yu R., Yang S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [8]
RP FUNCTION.
RX PubMed=20061386; DOI=10.1074/jbc.M109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-
CC 11'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to
CC ubiquitinate histone H2A.
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC P43356:MAGEA2B; NbExp=2; IntAct=EBI-2129909, EBI-5650739;
CC Q9UBF1:MAGEC2; NbExp=3; IntAct=EBI-2129909, EBI-5651487;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62256-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62256-2; Sequence=VSP_044580;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z29328; CAA82525.1; -; mRNA.
DR EMBL; Z29330; CAA82527.1; -; mRNA.
DR EMBL; Z29331; CAA82528.1; -; mRNA.
DR EMBL; AY302138; AAP57630.1; -; mRNA.
DR EMBL; BT006756; AAP35402.1; -; mRNA.
DR EMBL; AC073320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24099.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83736.1; -; Genomic_DNA.
DR EMBL; BC006277; AAH06277.1; -; mRNA.
DR PIR; A53516; A53516.
DR RefSeq; NP_001189427.1; NM_001202498.1.
DR RefSeq; NP_003335.1; NM_003344.3.
DR RefSeq; NP_874356.1; NM_182697.2.
DR UniGene; Hs.643548; -.
DR PDB; 2Z5D; X-ray; 2.10 A; A/B=1-160.
DR PDBsum; 2Z5D; -.
DR ProteinModelPortal; P62256; -.
DR SMR; P62256; 4-155.
DR IntAct; P62256; 43.
DR STRING; 9606.ENSP00000347836; -.
DR PhosphoSite; P62256; -.
DR DMDM; 51338683; -.
DR PaxDb; P62256; -.
DR PRIDE; P62256; -.
DR DNASU; 7328; -.
DR Ensembl; ENST00000355621; ENSP00000347836; ENSG00000186591.
DR Ensembl; ENST00000473814; ENSP00000419097; ENSG00000186591.
DR GeneID; 7328; -.
DR KEGG; hsa:7328; -.
DR UCSC; uc003vpg.2; human.
DR CTD; 7328; -.
DR GeneCards; GC07M129470; -.
DR H-InvDB; HIX0123428; -.
DR HGNC; HGNC:12484; UBE2H.
DR HPA; HPA003302; -.
DR MIM; 601082; gene.
DR neXtProt; NX_P62256; -.
DR PharmGKB; PA37133; -.
DR eggNOG; COG5078; -.
DR HOGENOM; HOG000233452; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; P62256; -.
DR KO; K10576; -.
DR OMA; CIESKHE; -.
DR OrthoDB; EOG7Z3F66; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P62256; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2H; human.
DR EvolutionaryTrace; P62256; -.
DR GeneWiki; UBE2H; -.
DR GenomeRNAi; 7328; -.
DR NextBio; 28676; -.
DR PRO; PR:P62256; -.
DR ArrayExpress; P62256; -.
DR Bgee; P62256; -.
DR CleanEx; HS_UBE2H; -.
DR Genevestigator; P62256; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 183 Ubiquitin-conjugating enzyme E2 H.
FT /FTId=PRO_0000082486.
FT ACT_SITE 87 87 Glycyl thioester intermediate (By
FT similarity).
FT VAR_SEQ 69 99 Missing (in isoform 2).
FT /FTId=VSP_044580.
FT CONFLICT 165 165 S -> P (in Ref. 2; AAP57630).
FT HELIX 6 20
FT STRAND 21 23
FT STRAND 25 30
FT STRAND 33 39
FT TURN 45 48
FT STRAND 50 56
FT TURN 59 63
FT STRAND 67 72
FT TURN 81 83
FT HELIX 88 94
FT HELIX 103 106
FT HELIX 108 114
FT HELIX 124 132
FT HELIX 134 148
FT HELIX 151 154
SQ 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
//
ID UBE2H_HUMAN Reviewed; 183 AA.
AC P62256; A4D1L6; C9JY93; P37286; Q7Z6F4;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-JUL-2004, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 H;
DE EC=6.3.2.19;
DE AltName: Full=UbcH2;
DE AltName: Full=Ubiquitin carrier protein H;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-20K;
DE AltName: Full=Ubiquitin-protein ligase H;
GN Name=UBE2H;
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] (ISOFORM 1), AND FUNCTION.
RX PubMed=8132613;
RA Kaiser P., Seufert W., Hoefferer L., Kofler B., Sachsenmaier C.,
RA Herzog H., Jentsch S., Schweiger M., Schneider R.;
RT "A human ubiquitin-conjugating enzyme homologous to yeast UBC8.";
RL J. Biol. Chem. 269:8797-8802(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Lin L., Li S., Li H., Zhou G., Shen C., Zheng G., Ke R., Zhong G.,
RA Yu R., Yang S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [8]
RP FUNCTION.
RX PubMed=20061386; DOI=10.1074/jbc.M109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-
CC 11'- and 'Lys-48'-linked polyubiquitination. Capable, in vitro, to
CC ubiquitinate histone H2A.
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC P43356:MAGEA2B; NbExp=2; IntAct=EBI-2129909, EBI-5650739;
CC Q9UBF1:MAGEC2; NbExp=3; IntAct=EBI-2129909, EBI-5651487;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62256-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62256-2; Sequence=VSP_044580;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z29328; CAA82525.1; -; mRNA.
DR EMBL; Z29330; CAA82527.1; -; mRNA.
DR EMBL; Z29331; CAA82528.1; -; mRNA.
DR EMBL; AY302138; AAP57630.1; -; mRNA.
DR EMBL; BT006756; AAP35402.1; -; mRNA.
DR EMBL; AC073320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24099.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83736.1; -; Genomic_DNA.
DR EMBL; BC006277; AAH06277.1; -; mRNA.
DR PIR; A53516; A53516.
DR RefSeq; NP_001189427.1; NM_001202498.1.
DR RefSeq; NP_003335.1; NM_003344.3.
DR RefSeq; NP_874356.1; NM_182697.2.
DR UniGene; Hs.643548; -.
DR PDB; 2Z5D; X-ray; 2.10 A; A/B=1-160.
DR PDBsum; 2Z5D; -.
DR ProteinModelPortal; P62256; -.
DR SMR; P62256; 4-155.
DR IntAct; P62256; 43.
DR STRING; 9606.ENSP00000347836; -.
DR PhosphoSite; P62256; -.
DR DMDM; 51338683; -.
DR PaxDb; P62256; -.
DR PRIDE; P62256; -.
DR DNASU; 7328; -.
DR Ensembl; ENST00000355621; ENSP00000347836; ENSG00000186591.
DR Ensembl; ENST00000473814; ENSP00000419097; ENSG00000186591.
DR GeneID; 7328; -.
DR KEGG; hsa:7328; -.
DR UCSC; uc003vpg.2; human.
DR CTD; 7328; -.
DR GeneCards; GC07M129470; -.
DR H-InvDB; HIX0123428; -.
DR HGNC; HGNC:12484; UBE2H.
DR HPA; HPA003302; -.
DR MIM; 601082; gene.
DR neXtProt; NX_P62256; -.
DR PharmGKB; PA37133; -.
DR eggNOG; COG5078; -.
DR HOGENOM; HOG000233452; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; P62256; -.
DR KO; K10576; -.
DR OMA; CIESKHE; -.
DR OrthoDB; EOG7Z3F66; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P62256; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2H; human.
DR EvolutionaryTrace; P62256; -.
DR GeneWiki; UBE2H; -.
DR GenomeRNAi; 7328; -.
DR NextBio; 28676; -.
DR PRO; PR:P62256; -.
DR ArrayExpress; P62256; -.
DR Bgee; P62256; -.
DR CleanEx; HS_UBE2H; -.
DR Genevestigator; P62256; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Ligase; Nucleotide-binding; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 183 Ubiquitin-conjugating enzyme E2 H.
FT /FTId=PRO_0000082486.
FT ACT_SITE 87 87 Glycyl thioester intermediate (By
FT similarity).
FT VAR_SEQ 69 99 Missing (in isoform 2).
FT /FTId=VSP_044580.
FT CONFLICT 165 165 S -> P (in Ref. 2; AAP57630).
FT HELIX 6 20
FT STRAND 21 23
FT STRAND 25 30
FT STRAND 33 39
FT TURN 45 48
FT STRAND 50 56
FT TURN 59 63
FT STRAND 67 72
FT TURN 81 83
FT HELIX 88 94
FT HELIX 103 106
FT HELIX 108 114
FT HELIX 124 132
FT HELIX 134 148
FT HELIX 151 154
SQ 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
//
MIM
601082
*RECORD*
*FIELD* NO
601082
*FIELD* TI
*601082 UBIQUITIN-CONJUGATING ENZYME E2H; UBE2H
;;UBIQUITIN-CONJUGATING ENZYME UBC8, YEAST, HOMOLOG OF
read more*FIELD* TX
Ubiquitin-conjugating enzymes catalyze the covalent attachment of
ubiquitin to cellular substrates. Kaiser et al. (1994) isolated a novel
ubiquitin-conjugating enzyme from human placenta and cloned the
corresponding cDNA. DNA sequencing revealed that this gene, symbolized
UBCH2 by them, encodes a protein with significant sequence similarity to
yeast UBC8. They discovered that yeast UBC8 is interrupted by a single
intron bearing an unusual branch point sequence. The authors noted that
yeast UBC8 exhibited 54% amino acid sequence identity to human UBCH2.
Moreover, full-length yeast and human enzymes expressed from the cDNAs
showed similar enzymatic activities in vitro by catalyzing the
ubiquitination of histones, suggesting that the 2 enzymes may fulfill
similar functions in vivo.
By study of hamster/human hybrid cell DNAs, Kaiser et al. (1994)
demonstrated that the human UBC8 gene is located on chromosome 7.
Hayashida et al. (2000) constructed a 1-Mb physical and transcript map
of 7q32 and mapped UBE2H to a region between D7S530 and D7S649.
*FIELD* RF
1. Hayashida, S.; Yamasaki, K.; Asada, Y.; Soeda, E.; Niikawa, N.;
Kishino, T.: Construction of a physical and transcript map flanking
the imprinted MEST/PEG1 region at 7q32. Genomics 66: 221-225, 2000.
2. Kaiser, P.; Seufert, W.; Hofferer, L.; Kofler, B.; Sachsenmaier,
C.; Herzog, H.; Jentsch, S.; Schweiger, M.; Schneider, R.: Human
ubiquitin-conjugating enzyme homologous to yeast UBC8. J. Biol. Chem. 269:
8797-8802, 1994.
*FIELD* CN
Joanna S. Amberger - updated: 4/19/2001
*FIELD* CD
Victor A. McKusick: 2/20/1996
*FIELD* ED
terry: 04/20/2001
joanna: 4/19/2001
carol: 7/8/1998
jenny: 4/4/1997
mark: 2/20/1996
*RECORD*
*FIELD* NO
601082
*FIELD* TI
*601082 UBIQUITIN-CONJUGATING ENZYME E2H; UBE2H
;;UBIQUITIN-CONJUGATING ENZYME UBC8, YEAST, HOMOLOG OF
read more*FIELD* TX
Ubiquitin-conjugating enzymes catalyze the covalent attachment of
ubiquitin to cellular substrates. Kaiser et al. (1994) isolated a novel
ubiquitin-conjugating enzyme from human placenta and cloned the
corresponding cDNA. DNA sequencing revealed that this gene, symbolized
UBCH2 by them, encodes a protein with significant sequence similarity to
yeast UBC8. They discovered that yeast UBC8 is interrupted by a single
intron bearing an unusual branch point sequence. The authors noted that
yeast UBC8 exhibited 54% amino acid sequence identity to human UBCH2.
Moreover, full-length yeast and human enzymes expressed from the cDNAs
showed similar enzymatic activities in vitro by catalyzing the
ubiquitination of histones, suggesting that the 2 enzymes may fulfill
similar functions in vivo.
By study of hamster/human hybrid cell DNAs, Kaiser et al. (1994)
demonstrated that the human UBC8 gene is located on chromosome 7.
Hayashida et al. (2000) constructed a 1-Mb physical and transcript map
of 7q32 and mapped UBE2H to a region between D7S530 and D7S649.
*FIELD* RF
1. Hayashida, S.; Yamasaki, K.; Asada, Y.; Soeda, E.; Niikawa, N.;
Kishino, T.: Construction of a physical and transcript map flanking
the imprinted MEST/PEG1 region at 7q32. Genomics 66: 221-225, 2000.
2. Kaiser, P.; Seufert, W.; Hofferer, L.; Kofler, B.; Sachsenmaier,
C.; Herzog, H.; Jentsch, S.; Schweiger, M.; Schneider, R.: Human
ubiquitin-conjugating enzyme homologous to yeast UBC8. J. Biol. Chem. 269:
8797-8802, 1994.
*FIELD* CN
Joanna S. Amberger - updated: 4/19/2001
*FIELD* CD
Victor A. McKusick: 2/20/1996
*FIELD* ED
terry: 04/20/2001
joanna: 4/19/2001
carol: 7/8/1998
jenny: 4/4/1997
mark: 2/20/1996