Full text data of UBA5
UBA5
(UBE1DC1)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-like modifier-activating enzyme 5; Ubiquitin-activating enzyme 5 (ThiFP1; UFM1-activating enzyme; Ubiquitin-activating enzyme E1 domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-like modifier-activating enzyme 5; Ubiquitin-activating enzyme 5 (ThiFP1; UFM1-activating enzyme; Ubiquitin-activating enzyme E1 domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9GZZ9
ID UBA5_HUMAN Reviewed; 404 AA.
AC Q9GZZ9; A6NJL3; D3DNC8; Q96ST1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
DE AltName: Full=ThiFP1;
DE AltName: Full=UFM1-activating enzyme;
DE AltName: Full=Ubiquitin-activating enzyme E1 domain-containing protein 1;
GN Name=UBA5; Synonyms=UBE1DC1;
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), FUNCTION, AND MUTAGENESIS OF
RP CYS-250.
RX PubMed=15071506; DOI=10.1038/sj.emboj.7600205;
RA Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N.,
RA Ueno T., Kominami E., Natsume T., Tanaka K.;
RT "A novel protein-conjugating system for Ufm1, a ubiquitin-fold
RT modifier.";
RL EMBO J. 23:1977-1986(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=16328888; DOI=10.1007/s11033-005-4822-y;
RA Dou T., Gu S., Liu J., Chen F., Zeng L., Guo L., Xie Y., Mao Y.;
RT "Isolation and characterization of ubiquitin-activating enzyme E1-
RT domain containing 1, UBE1DC1.";
RL Mol. Biol. Rep. 32:265-271(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND SUBCELLULAR
RP LOCATION.
RX PubMed=18442052; DOI=10.1002/jcb.21791;
RA Zheng M., Gu X., Zheng D., Yang Z., Li F., Zhao J., Xie Y., Ji C.,
RA Mao Y.;
RT "UBE1DC1, an ubiquitin-activating enzyme, activates two different
RT ubiquitin-like proteins.";
RL J. Cell. Biochem. 104:2324-2334(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-329 IN COMPLEX WITH ATP
RP AND ZINC, FUNCTION, AND ACTIVE SITE.
RX PubMed=20368332; DOI=10.1074/jbc.M110.102921;
RA Bacik J.P., Walker J.R., Ali M., Schimmer A.D., Dhe-Paganon S.;
RT "Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5)
RT bound to ATP: mechanistic insights into a minimalistic E1 enzyme.";
RL J. Biol. Chem. 285:20273-20280(2010).
CC -!- FUNCTION: E1-like enzyme which activates UFM1 and SUMO2.
CC -!- INTERACTION:
CC O95166:GABARAP; NbExp=2; IntAct=EBI-747805, EBI-712001;
CC Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-747805, EBI-746969;
CC P60520:GABARAPL2; NbExp=10; IntAct=EBI-747805, EBI-720116;
CC Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-747805, EBI-373144;
CC Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-747805, EBI-2603996;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes mainly in
CC cytoplasm, while it mainly localizes to the nucleus in presence of
CC SUMO2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=UBE1DC1A;
CC IsoId=Q9GZZ9-1; Sequence=Displayed;
CC Name=2; Synonyms=UBE1DC1B;
CC IsoId=Q9GZZ9-2; Sequence=VSP_038528;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily.
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; AB154406; BAD15375.1; -; mRNA.
DR EMBL; AY253672; AAP79600.1; -; mRNA.
DR EMBL; AL136757; CAB66691.1; -; mRNA.
DR EMBL; AK026904; BAB15587.1; -; mRNA.
DR EMBL; AK027563; BAB55199.1; -; mRNA.
DR EMBL; AC020632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79192.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79189.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79191.1; -; Genomic_DNA.
DR EMBL; BC009737; AAH09737.1; -; mRNA.
DR RefSeq; NP_079094.1; NM_024818.3.
DR RefSeq; NP_938143.1; NM_198329.2.
DR RefSeq; XP_005247844.1; XM_005247787.1.
DR UniGene; Hs.170737; -.
DR PDB; 3GUC; X-ray; 2.25 A; A/B=57-329.
DR PDB; 3H8V; X-ray; 2.00 A; A/B=57-329.
DR PDBsum; 3GUC; -.
DR PDBsum; 3H8V; -.
DR ProteinModelPortal; Q9GZZ9; -.
DR SMR; Q9GZZ9; 43-329.
DR IntAct; Q9GZZ9; 37.
DR MINT; MINT-1475093; -.
DR STRING; 9606.ENSP00000348565; -.
DR ChEMBL; CHEMBL2016429; -.
DR PhosphoSite; Q9GZZ9; -.
DR DMDM; 74733510; -.
DR PaxDb; Q9GZZ9; -.
DR PRIDE; Q9GZZ9; -.
DR DNASU; 79876; -.
DR Ensembl; ENST00000264991; ENSP00000264991; ENSG00000081307.
DR Ensembl; ENST00000356232; ENSP00000348565; ENSG00000081307.
DR Ensembl; ENST00000494238; ENSP00000418807; ENSG00000081307.
DR GeneID; 79876; -.
DR KEGG; hsa:79876; -.
DR UCSC; uc003epa.4; human.
DR CTD; 79876; -.
DR GeneCards; GC03P132373; -.
DR HGNC; HGNC:23230; UBA5.
DR HPA; HPA017235; -.
DR MIM; 610552; gene.
DR neXtProt; NX_Q9GZZ9; -.
DR PharmGKB; PA162407661; -.
DR eggNOG; COG0476; -.
DR HOGENOM; HOG000256352; -.
DR HOVERGEN; HBG056496; -.
DR InParanoid; Q9GZZ9; -.
DR KO; K12164; -.
DR OMA; NYNITTM; -.
DR OrthoDB; EOG7N63MX; -.
DR PhylomeDB; Q9GZZ9; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q9GZZ9; -.
DR GeneWiki; UBE1DC1; -.
DR GenomeRNAi; 79876; -.
DR NextBio; 69659; -.
DR PRO; PR:Q9GZZ9; -.
DR ArrayExpress; Q9GZZ9; -.
DR Bgee; Q9GZZ9; -.
DR CleanEx; HS_UBA5; -.
DR Genevestigator; Q9GZZ9; -.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; IDA:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR InterPro; IPR009036; Molybdenum_cofac_synth_MoeB.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Cytoplasm; 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_0000194970.
FT ACT_SITE 250 250 Glycyl thioester intermediate.
FT METAL 226 226 Zinc.
FT METAL 229 229 Zinc.
FT METAL 303 303 Zinc.
FT METAL 308 308 Zinc.
FT BINDING 83 83 ATP; via amide nitrogen.
FT BINDING 104 104 ATP.
FT BINDING 127 127 ATP.
FT BINDING 150 150 ATP.
FT BINDING 184 184 ATP.
FT MOD_RES 45 45 Phosphoserine.
FT MOD_RES 358 358 Phosphoserine.
FT VAR_SEQ 1 56 Missing (in isoform 2).
FT /FTId=VSP_038528.
FT MUTAGEN 250 250 C->S: Forms a stable intermediate
FT complex.
FT CONFLICT 403 403 N -> S (in Ref. 4; BAB55199).
FT HELIX 70 73
FT STRAND 75 79
FT HELIX 83 95
FT STRAND 98 103
FT HELIX 120 122
FT HELIX 127 138
FT STRAND 142 147
FT HELIX 154 166
FT STRAND 167 170
FT STRAND 176 180
FT HELIX 185 198
FT STRAND 202 207
FT STRAND 211 219
FT TURN 221 223
FT STRAND 229 231
FT HELIX 247 274
FT STRAND 281 286
FT TURN 287 290
FT HELIX 306 317
SQ SEQUENCE 404 AA; 44863 MW; 02F0F64FEAA1E880 CRC64;
MAESVERLQQ RVQELERELA QERSLQVPRS GDGGGGRVRI EKMSSEVVDS NPYSRLMALK
RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP
HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFQHF MDRISNGGLE EGKPVDLVLS
CVDNFEARMT INTACNELGQ TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID
EKTLKREGVC AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN
PQCDDRNCRK QQEEYKKKVA ALPKQEVIQE EEEIIHEDNE WGIELVSEVS EEELKNFSGP
VPDLPEGITV AYTIPKKQED SVTELTVEDS GESLEDLMAK MKNM
//
ID UBA5_HUMAN Reviewed; 404 AA.
AC Q9GZZ9; A6NJL3; D3DNC8; Q96ST1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5;
DE Short=Ubiquitin-activating enzyme 5;
DE AltName: Full=ThiFP1;
DE AltName: Full=UFM1-activating enzyme;
DE AltName: Full=Ubiquitin-activating enzyme E1 domain-containing protein 1;
GN Name=UBA5; Synonyms=UBE1DC1;
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), FUNCTION, AND MUTAGENESIS OF
RP CYS-250.
RX PubMed=15071506; DOI=10.1038/sj.emboj.7600205;
RA Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N.,
RA Ueno T., Kominami E., Natsume T., Tanaka K.;
RT "A novel protein-conjugating system for Ufm1, a ubiquitin-fold
RT modifier.";
RL EMBO J. 23:1977-1986(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=16328888; DOI=10.1007/s11033-005-4822-y;
RA Dou T., Gu S., Liu J., Chen F., Zeng L., Guo L., Xie Y., Mao Y.;
RT "Isolation and characterization of ubiquitin-activating enzyme E1-
RT domain containing 1, UBE1DC1.";
RL Mol. Biol. Rep. 32:265-271(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND SUBCELLULAR
RP LOCATION.
RX PubMed=18442052; DOI=10.1002/jcb.21791;
RA Zheng M., Gu X., Zheng D., Yang Z., Li F., Zhao J., Xie Y., Ji C.,
RA Mao Y.;
RT "UBE1DC1, an ubiquitin-activating enzyme, activates two different
RT ubiquitin-like proteins.";
RL J. Cell. Biochem. 104:2324-2334(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 57-329 IN COMPLEX WITH ATP
RP AND ZINC, FUNCTION, AND ACTIVE SITE.
RX PubMed=20368332; DOI=10.1074/jbc.M110.102921;
RA Bacik J.P., Walker J.R., Ali M., Schimmer A.D., Dhe-Paganon S.;
RT "Crystal structure of the human ubiquitin-activating enzyme 5 (UBA5)
RT bound to ATP: mechanistic insights into a minimalistic E1 enzyme.";
RL J. Biol. Chem. 285:20273-20280(2010).
CC -!- FUNCTION: E1-like enzyme which activates UFM1 and SUMO2.
CC -!- INTERACTION:
CC O95166:GABARAP; NbExp=2; IntAct=EBI-747805, EBI-712001;
CC Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-747805, EBI-746969;
CC P60520:GABARAPL2; NbExp=10; IntAct=EBI-747805, EBI-720116;
CC Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-747805, EBI-373144;
CC Q9BXW4:MAP1LC3C; NbExp=2; IntAct=EBI-747805, EBI-2603996;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes mainly in
CC cytoplasm, while it mainly localizes to the nucleus in presence of
CC SUMO2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=UBE1DC1A;
CC IsoId=Q9GZZ9-1; Sequence=Displayed;
CC Name=2; Synonyms=UBE1DC1B;
CC IsoId=Q9GZZ9-2; Sequence=VSP_038528;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily.
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; AB154406; BAD15375.1; -; mRNA.
DR EMBL; AY253672; AAP79600.1; -; mRNA.
DR EMBL; AL136757; CAB66691.1; -; mRNA.
DR EMBL; AK026904; BAB15587.1; -; mRNA.
DR EMBL; AK027563; BAB55199.1; -; mRNA.
DR EMBL; AC020632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79192.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79189.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79191.1; -; Genomic_DNA.
DR EMBL; BC009737; AAH09737.1; -; mRNA.
DR RefSeq; NP_079094.1; NM_024818.3.
DR RefSeq; NP_938143.1; NM_198329.2.
DR RefSeq; XP_005247844.1; XM_005247787.1.
DR UniGene; Hs.170737; -.
DR PDB; 3GUC; X-ray; 2.25 A; A/B=57-329.
DR PDB; 3H8V; X-ray; 2.00 A; A/B=57-329.
DR PDBsum; 3GUC; -.
DR PDBsum; 3H8V; -.
DR ProteinModelPortal; Q9GZZ9; -.
DR SMR; Q9GZZ9; 43-329.
DR IntAct; Q9GZZ9; 37.
DR MINT; MINT-1475093; -.
DR STRING; 9606.ENSP00000348565; -.
DR ChEMBL; CHEMBL2016429; -.
DR PhosphoSite; Q9GZZ9; -.
DR DMDM; 74733510; -.
DR PaxDb; Q9GZZ9; -.
DR PRIDE; Q9GZZ9; -.
DR DNASU; 79876; -.
DR Ensembl; ENST00000264991; ENSP00000264991; ENSG00000081307.
DR Ensembl; ENST00000356232; ENSP00000348565; ENSG00000081307.
DR Ensembl; ENST00000494238; ENSP00000418807; ENSG00000081307.
DR GeneID; 79876; -.
DR KEGG; hsa:79876; -.
DR UCSC; uc003epa.4; human.
DR CTD; 79876; -.
DR GeneCards; GC03P132373; -.
DR HGNC; HGNC:23230; UBA5.
DR HPA; HPA017235; -.
DR MIM; 610552; gene.
DR neXtProt; NX_Q9GZZ9; -.
DR PharmGKB; PA162407661; -.
DR eggNOG; COG0476; -.
DR HOGENOM; HOG000256352; -.
DR HOVERGEN; HBG056496; -.
DR InParanoid; Q9GZZ9; -.
DR KO; K12164; -.
DR OMA; NYNITTM; -.
DR OrthoDB; EOG7N63MX; -.
DR PhylomeDB; Q9GZZ9; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q9GZZ9; -.
DR GeneWiki; UBE1DC1; -.
DR GenomeRNAi; 79876; -.
DR NextBio; 69659; -.
DR PRO; PR:Q9GZZ9; -.
DR ArrayExpress; Q9GZZ9; -.
DR Bgee; Q9GZZ9; -.
DR CleanEx; HS_UBA5; -.
DR Genevestigator; Q9GZZ9; -.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0071566; F:UFM1 activating enzyme activity; IDA:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR InterPro; IPR009036; Molybdenum_cofac_synth_MoeB.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Cytoplasm; 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_0000194970.
FT ACT_SITE 250 250 Glycyl thioester intermediate.
FT METAL 226 226 Zinc.
FT METAL 229 229 Zinc.
FT METAL 303 303 Zinc.
FT METAL 308 308 Zinc.
FT BINDING 83 83 ATP; via amide nitrogen.
FT BINDING 104 104 ATP.
FT BINDING 127 127 ATP.
FT BINDING 150 150 ATP.
FT BINDING 184 184 ATP.
FT MOD_RES 45 45 Phosphoserine.
FT MOD_RES 358 358 Phosphoserine.
FT VAR_SEQ 1 56 Missing (in isoform 2).
FT /FTId=VSP_038528.
FT MUTAGEN 250 250 C->S: Forms a stable intermediate
FT complex.
FT CONFLICT 403 403 N -> S (in Ref. 4; BAB55199).
FT HELIX 70 73
FT STRAND 75 79
FT HELIX 83 95
FT STRAND 98 103
FT HELIX 120 122
FT HELIX 127 138
FT STRAND 142 147
FT HELIX 154 166
FT STRAND 167 170
FT STRAND 176 180
FT HELIX 185 198
FT STRAND 202 207
FT STRAND 211 219
FT TURN 221 223
FT STRAND 229 231
FT HELIX 247 274
FT STRAND 281 286
FT TURN 287 290
FT HELIX 306 317
SQ SEQUENCE 404 AA; 44863 MW; 02F0F64FEAA1E880 CRC64;
MAESVERLQQ RVQELERELA QERSLQVPRS GDGGGGRVRI EKMSSEVVDS NPYSRLMALK
RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP
HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFQHF MDRISNGGLE EGKPVDLVLS
CVDNFEARMT INTACNELGQ TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID
EKTLKREGVC AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN
PQCDDRNCRK QQEEYKKKVA ALPKQEVIQE EEEIIHEDNE WGIELVSEVS EEELKNFSGP
VPDLPEGITV AYTIPKKQED SVTELTVEDS GESLEDLMAK MKNM
//
MIM
610552
*RECORD*
*FIELD* NO
610552
*FIELD* TI
*610552 UBIQUITIN-ACTIVATING ENZYME E1 DOMAIN-CONTAINING 1; UBE1DC1
;;UBA5
*FIELD* TX
read more
DESCRIPTION
UBE1DC1 is an E1-like activating enzyme for ubiquitin-fold modifier-1
(UFM1; 610553) (Komatsu et al., 2004).
CLONING
Using yeast 2-hybrid analysis with GATE16 (GABARAPL2; 607452), a human
homolog of yeast Atg8p, as bait, followed by PCR of human liver cDNA,
Komatsu et al. (2004) cloned UBE1DC1, which they called UBA5. The
deduced 404-amino acid protein shares similarity with members of the
E1-like enzyme family of ubiquitin-like posttranslational modifiers.
Using large-scale cDNA sequencing of human fetal brain cDNAs, Dou et al.
(2005) cloned UBE1DC1. The deduced protein has a predicted molecular
mass of 43.9 kD and contains a conserved ThiF domain with a nearby
cysteine residue similar to ubiquitin activating enzyme E1C (UBE1C;
603172). RT-PCR analysis detected highest UBE1DC1 expression in spleen,
high expression in most other tissues examined, and low expression in
colon, prostate, brain, and ovary.
GENE FUNCTION
Using immunoprecipitation of intermediates formed from FLAG-tagged
UBE1DC1 and mutant constructs coexpressed with Myc-tagged UFM1 in HEK293
cells as well as an in vitro UFM1 conjugation assay, Komatsu et al.
(2004) showed that UBE1DC1 is a UFM1-activating enzyme with the active
site at cys250.
GENE STRUCTURE
Dou et al. (2005) determined that the UBE1DC1 gene contains 12 exons and
spans 17.4 kb.
MAPPING
By genomic sequence analysis, Dou et al. (2005) mapped the UBE1DC1 gene
to chromosome 3q22.
*FIELD* RF
1. Dou, T.; Gu, S.; Liu, J.; Chen, F.; Zeng, L.; Guo, L.; Xie, Y.;
Mao, Y.: Isolation and characterization of ubiquitin-activating enzyme
E1-domain containing 1, UBE1DC1. Molec. Biol. Rep. 32: 265-271,
2005.
2. Komatsu, M.; Chiba, T.; Tatsumi, K.; Iemura, S.; Tanida, I.; Okazaki,
N.; Ueno, T.; Kominami, E.; Natsume, T.; Tanaka, K.: A novel protein-conjugating
system for Ufm1, a ubiquitin-fold modifier. EMBO J. 23: 1977-1986,
2004.
*FIELD* CD
Dorothy S. Reilly: 11/7/2006
*FIELD* ED
carol: 11/07/2006
carol: 11/7/2006
*RECORD*
*FIELD* NO
610552
*FIELD* TI
*610552 UBIQUITIN-ACTIVATING ENZYME E1 DOMAIN-CONTAINING 1; UBE1DC1
;;UBA5
*FIELD* TX
read more
DESCRIPTION
UBE1DC1 is an E1-like activating enzyme for ubiquitin-fold modifier-1
(UFM1; 610553) (Komatsu et al., 2004).
CLONING
Using yeast 2-hybrid analysis with GATE16 (GABARAPL2; 607452), a human
homolog of yeast Atg8p, as bait, followed by PCR of human liver cDNA,
Komatsu et al. (2004) cloned UBE1DC1, which they called UBA5. The
deduced 404-amino acid protein shares similarity with members of the
E1-like enzyme family of ubiquitin-like posttranslational modifiers.
Using large-scale cDNA sequencing of human fetal brain cDNAs, Dou et al.
(2005) cloned UBE1DC1. The deduced protein has a predicted molecular
mass of 43.9 kD and contains a conserved ThiF domain with a nearby
cysteine residue similar to ubiquitin activating enzyme E1C (UBE1C;
603172). RT-PCR analysis detected highest UBE1DC1 expression in spleen,
high expression in most other tissues examined, and low expression in
colon, prostate, brain, and ovary.
GENE FUNCTION
Using immunoprecipitation of intermediates formed from FLAG-tagged
UBE1DC1 and mutant constructs coexpressed with Myc-tagged UFM1 in HEK293
cells as well as an in vitro UFM1 conjugation assay, Komatsu et al.
(2004) showed that UBE1DC1 is a UFM1-activating enzyme with the active
site at cys250.
GENE STRUCTURE
Dou et al. (2005) determined that the UBE1DC1 gene contains 12 exons and
spans 17.4 kb.
MAPPING
By genomic sequence analysis, Dou et al. (2005) mapped the UBE1DC1 gene
to chromosome 3q22.
*FIELD* RF
1. Dou, T.; Gu, S.; Liu, J.; Chen, F.; Zeng, L.; Guo, L.; Xie, Y.;
Mao, Y.: Isolation and characterization of ubiquitin-activating enzyme
E1-domain containing 1, UBE1DC1. Molec. Biol. Rep. 32: 265-271,
2005.
2. Komatsu, M.; Chiba, T.; Tatsumi, K.; Iemura, S.; Tanida, I.; Okazaki,
N.; Ueno, T.; Kominami, E.; Natsume, T.; Tanaka, K.: A novel protein-conjugating
system for Ufm1, a ubiquitin-fold modifier. EMBO J. 23: 1977-1986,
2004.
*FIELD* CD
Dorothy S. Reilly: 11/7/2006
*FIELD* ED
carol: 11/07/2006
carol: 11/7/2006