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UBC12_HUMAN
ID   UBC12_HUMAN             Reviewed;         183 AA.
AC   P61081; O76069; Q8VC50;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=NEDD8-conjugating enzyme Ubc12;
DE            EC=2.3.2.34 {ECO:0000269|PubMed:15361859};
DE   AltName: Full=NEDD8 carrier protein;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 M;
GN   Name=UBE2M; Synonyms=UBC12;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9694792; DOI=10.1101/gad.12.15.2263;
RA   Osaka F., Kawasaki H., Aida N., Saeki M., Chiba T., Kawashima S.,
RA   Tanaka K., Kato S.;
RT   "A new NEDD8-ligating system for cullin-4A.";
RL   Genes Dev. 12:2263-2268(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Placenta;
RX   PubMed=10207026; DOI=10.1074/jbc.274.17.12036;
RA   Gong L., Yeh E.T.H.;
RT   "Identification of the activating and conjugating enzymes of the NEDD8
RT   conjugation pathway.";
RL   J. Biol. Chem. 274:12036-12042(1999).
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 vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   MUTAGENESIS OF CYS-111.
RX   PubMed=10828074; DOI=10.1074/jbc.275.22.17008;
RA   Wada H., Yeh E.T.H., Kamitani T.;
RT   "A dominant-negative UBC12 mutant sequesters NEDD8 and inhibits NEDD8
RT   conjugation in vivo.";
RL   J. Biol. Chem. 275:17008-17015(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   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   [7]
RP   INTERACTION WITH RBX1.
RX   PubMed=19250909; DOI=10.1016/j.molcel.2009.01.011;
RA   Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C.,
RA   Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.;
RT   "E2-RING expansion of the NEDD8 cascade confers specificity to cullin
RT   modification.";
RL   Mol. Cell 33:483-495(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
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., Buerckstuemmer T.,
RA   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   [10]
RP   INTERACTION WITH DCUN1D5.
RX   PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252;
RA   Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M.,
RA   Goenen M., Ghossein R., Ramanathan S.Y., Singh B.;
RT   "Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity
RT   and nuclear localization.";
RL   Clin. Cancer Res. 20:372-381(2014).
RN   [11]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-169, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   INTERACTION WITH DCUN1D1.
RX   PubMed=28581483; DOI=10.1038/nchembio.2386;
RA   Scott D.C., Hammill J.T., Min J., Rhee D.Y., Connelly M., Sviderskiy V.O.,
RA   Bhasin D., Chen Y., Ong S.S., Chai S.C., Goktug A.N., Huang G., Monda J.K.,
RA   Low J., Kim H.S., Paulo J.A., Cannon J.R., Shelat A.A., Chen T.,
RA   Kelsall I.R., Alpi A.F., Pagala V., Wang X., Peng J., Singh B.,
RA   Harper J.W., Schulman B.A., Guy R.K.;
RT   "Blocking an N-terminal acetylation-dependent protein interaction inhibits
RT   an E3 ligase.";
RL   Nat. Chem. Biol. 13:850-857(2017).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-26 IN COMPLEX WITH UBA3 AND
RP   NAE1, MUTAGENESIS OF MET-1; LEU-4; PHE-5; SER-6; LEU-7; GLN-9; GLN-10;
RP   LYS-11 AND LYS-12, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15361859; DOI=10.1038/nsmb826;
RA   Huang D.T., Miller D.W., Mathew R., Cassell R., Holton J.M., Roussel M.F.,
RA   Schulman B.A.;
RT   "A unique E1-E2 interaction required for optimal conjugation of the
RT   ubiquitin-like protein NEDD8.";
RL   Nat. Struct. Mol. Biol. 11:927-935(2004).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 27-183 IN COMPLEX WITH UBA3 AND
RP   NAE1, AND MUTAGENESIS OF LEU-32; GLN-35; LYS-36; ILE-38; ASN-39; LEU-41;
RP   PHE-51; ASP-55 AND LEU-57.
RX   PubMed=15694336; DOI=10.1016/j.molcel.2004.12.020;
RA   Huang D.T., Paydar A., Zhuang M., Waddell M.B., Holton J.M., Schulman B.A.;
RT   "Structural basis for recruitment of Ubc12 by an E2 binding domain in
RT   NEDD8's E1.";
RL   Mol. Cell 17:341-350(2005).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-15 IN COMPLEX WITH CUL1 AND
RP   DCUN1D1, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-12 IN COMPLEX WITH CUL1
RP   AND DCUN1D1, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21940857; DOI=10.1126/science.1209307;
RA   Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.;
RT   "N-terminal acetylation acts as an avidity enhancer within an
RT   interconnected multiprotein complex.";
RL   Science 334:674-678(2011).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (3.28 ANGSTROMS) OF 1-12 IN COMPLEX WITH DCUN1D2,
RP   ACETYLATION AT MET-1, AND INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3;
RP   DCUN1D4 AND DCUN1D5.
RX   PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
RA   Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
RA   Bennett E.J., Schulman B.A.;
RT   "Structural conservation of distinctive N-terminal acetylation-dependent
RT   interactions across a family of mammalian NEDD8 ligation enzymes.";
RL   Structure 21:42-53(2013).
CC   -!- FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1
CC       E1 complex and catalyzes its covalent attachment to other proteins. The
CC       specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2,
CC       suggests that the RBX1-UBE2M complex neddylates specific target
CC       proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell
CC       proliferation. {ECO:0000269|PubMed:10207026,
CC       ECO:0000269|PubMed:15361859}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine +
CC         [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating
CC         enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-
CC         yl-L-cysteine.; EC=2.3.2.34; Evidence={ECO:0000269|PubMed:15361859};
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Interacts with UBA3 and RBX1. Interacts (N-terminally
CC       acetylated form) with (via DCUN1 domain) DCUN1D1, DCUN1D2, DCUN1D3,
CC       DCUN1D4 and DCUN1D5 (PubMed:23201271, PubMed:28581483).
CC       {ECO:0000269|PubMed:15361859, ECO:0000269|PubMed:15694336,
CC       ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:21940857,
CC       ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:28581483}.
CC   -!- INTERACTION:
CC       P61081; Q13616: CUL1; NbExp=5; IntAct=EBI-1041660, EBI-359390;
CC       P61081; Q96GG9: DCUN1D1; NbExp=4; IntAct=EBI-1041660, EBI-740086;
CC       P61081; P62879: GNB2; NbExp=3; IntAct=EBI-1041660, EBI-356942;
CC       P61081; Q15843: NEDD8; NbExp=8; IntAct=EBI-1041660, EBI-716247;
CC       P61081; O60260-5: PRKN; NbExp=3; IntAct=EBI-1041660, EBI-21251460;
CC       P61081; P62877: RBX1; NbExp=7; IntAct=EBI-1041660, EBI-398523;
CC       P61081; Q8TBC4: UBA3; NbExp=2; IntAct=EBI-1041660, EBI-717567;
CC   -!- DOMAIN: Both the N-terminal docking peptide and the catalytic core
CC       domain must bind the UBA3-NAE1 complex simultaneously for optimal
CC       transfer of NEDD8.
CC   -!- PTM: The acetylation of Met-1 increases affinity for DCUN1D1 by about 2
CC       orders of magnitude and is crucial for NEDD8 transfer to cullins.
CC       {ECO:0000269|PubMed:21940857, ECO:0000269|PubMed:23201271}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBC12
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AB012191; BAA33145.1; -; mRNA.
DR   EMBL; AF075599; AAC26141.1; -; mRNA.
DR   EMBL; BT006754; AAP35400.1; -; mRNA.
DR   EMBL; BC058924; AAH58924.1; -; mRNA.
DR   CCDS; CCDS12987.1; -.
DR   RefSeq; NP_003960.1; NM_003969.3.
DR   PDB; 1TT5; X-ray; 2.60 A; E/F=1-26.
DR   PDB; 1Y8X; X-ray; 2.40 A; A=27-183.
DR   PDB; 2NVU; X-ray; 2.80 A; C=1-178.
DR   PDB; 3TDU; X-ray; 1.50 A; E/F=1-15.
DR   PDB; 3TDZ; X-ray; 2.00 A; E/F=2-12.
DR   PDB; 4GAO; X-ray; 3.28 A; C/E/F/H=1-12.
DR   PDB; 4P5O; X-ray; 3.11 A; G/I=2-183.
DR   PDBsum; 1TT5; -.
DR   PDBsum; 1Y8X; -.
DR   PDBsum; 2NVU; -.
DR   PDBsum; 3TDU; -.
DR   PDBsum; 3TDZ; -.
DR   PDBsum; 4GAO; -.
DR   PDBsum; 4P5O; -.
DR   AlphaFoldDB; P61081; -.
DR   SMR; P61081; -.
DR   BioGRID; 114504; 607.
DR   DIP; DIP-35679N; -.
DR   IntAct; P61081; 63.
DR   MINT; P61081; -.
DR   STRING; 9606.ENSP00000253023; -.
DR   BindingDB; P61081; -.
DR   ChEMBL; CHEMBL4295787; -.
DR   GlyGen; P61081; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61081; -.
DR   PhosphoSitePlus; P61081; -.
DR   SwissPalm; P61081; -.
DR   BioMuta; UBE2M; -.
DR   DMDM; 46577655; -.
DR   REPRODUCTION-2DPAGE; IPI00022597; -.
DR   UCD-2DPAGE; P61081; -.
DR   EPD; P61081; -.
DR   jPOST; P61081; -.
DR   MassIVE; P61081; -.
DR   MaxQB; P61081; -.
DR   PaxDb; P61081; -.
DR   PeptideAtlas; P61081; -.
DR   PRIDE; P61081; -.
DR   ProteomicsDB; 57261; -.
DR   Antibodypedia; 3333; 203 antibodies from 34 providers.
DR   DNASU; 9040; -.
DR   Ensembl; ENST00000253023.8; ENSP00000253023.2; ENSG00000130725.8.
DR   GeneID; 9040; -.
DR   KEGG; hsa:9040; -.
DR   MANE-Select; ENST00000253023.8; ENSP00000253023.2; NM_003969.4; NP_003960.1.
DR   UCSC; uc002qtl.5; human.
DR   CTD; 9040; -.
DR   DisGeNET; 9040; -.
DR   GeneCards; UBE2M; -.
DR   HGNC; HGNC:12491; UBE2M.
DR   HPA; ENSG00000130725; Low tissue specificity.
DR   MIM; 603173; gene.
DR   neXtProt; NX_P61081; -.
DR   OpenTargets; ENSG00000130725; -.
DR   PharmGKB; PA37140; -.
DR   VEuPathDB; HostDB:ENSG00000130725; -.
DR   eggNOG; KOG0420; Eukaryota.
DR   GeneTree; ENSGT00940000162814; -.
DR   HOGENOM; CLU_030988_6_0_1; -.
DR   InParanoid; P61081; -.
DR   OMA; GYPHDAP; -.
DR   OrthoDB; 1302735at2759; -.
DR   PhylomeDB; P61081; -.
DR   TreeFam; TF101125; -.
DR   BioCyc; MetaCyc:HS05432-MON; -.
DR   BRENDA; 2.3.2.34; 2681.
DR   PathwayCommons; P61081; -.
DR   Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; P61081; -.
DR   UniPathway; UPA00885; -.
DR   BioGRID-ORCS; 9040; 739 hits in 1054 CRISPR screens.
DR   ChiTaRS; UBE2M; human.
DR   EvolutionaryTrace; P61081; -.
DR   GeneWiki; UBE2M; -.
DR   GenomeRNAi; 9040; -.
DR   Pharos; P61081; Tchem.
DR   PRO; PR:P61081; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P61081; protein.
DR   Bgee; ENSG00000130725; Expressed in right frontal lobe and 184 other tissues.
DR   ExpressionAtlas; P61081; baseline and differential.
DR   Genevisible; P61081; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019788; F:NEDD8 transferase activity; IDA:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036211; P:protein modification process; IMP:UniProtKB.
DR   GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
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; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..183
FT                   /note="NEDD8-conjugating enzyme Ubc12"
FT                   /id="PRO_0000082488"
FT   DOMAIN          29..173
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..57
FT                   /note="Interaction with UBA3"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        111
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:21940857,
FT                   ECO:0000269|PubMed:23201271"
FT   MOD_RES         3
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         169
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P61082"
FT   MOD_RES         169
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MUTAGEN         1
FT                   /note="M->A: No effect on thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         4
FT                   /note="L->A: Impairs thioester intermediate formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         5
FT                   /note="F->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         6
FT                   /note="S->A: Slightly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         7
FT                   /note="L->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         9
FT                   /note="Q->A: Impairs thioester intermediate formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         10
FT                   /note="Q->A: No effect on thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         11
FT                   /note="K->A: No effect on thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         12
FT                   /note="K->A: Impairs thioester intermediate formation."
FT                   /evidence="ECO:0000269|PubMed:15361859"
FT   MUTAGEN         32
FT                   /note="L->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         35
FT                   /note="Q->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         36
FT                   /note="K->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         38
FT                   /note="I->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         39
FT                   /note="N->A: No effect on thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         41
FT                   /note="L->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         51
FT                   /note="F->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         55
FT                   /note="D->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         57
FT                   /note="L->A: Strongly impairs thioester intermediate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:15694336"
FT   MUTAGEN         111
FT                   /note="C->S: Forms a stable complex with NEDD8, which
FT                   prevents subsequent NEDD8 conjugation to cullins."
FT                   /evidence="ECO:0000269|PubMed:10828074"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:3TDU"
FT   HELIX           29..39
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          59..64
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   TURN            70..73
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   TURN            84..88
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:2NVU"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   HELIX           125..137
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   HELIX           147..154
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   HELIX           157..169
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          170..173
FT                   /evidence="ECO:0007829|PDB:1Y8X"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:1Y8X"
SQ   SEQUENCE   183 AA;  20900 MW;  E3C288CA6A98BC5C CRC64;
     MIKLFSLKQQ KKEEESAGGT KGSSKKASAA QLRIQKDINE LNLPKTCDIS FSDPDDLLNF
     KLVICPDEGF YKSGKFVFSF KVGQGYPHDP PKVKCETMVY HPNIDLEGNV CLNILREDWK
     PVLTINSIIY GLQYLFLEPN PEDPLNKEAA EVLQNNRRLF EQNVQRSMRG GYIGSTYFER
     CLK
 
 
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