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Q7Z7E8 (UB2Q1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 Q1

EC=6.3.2.19
Alternative name(s):
Protein NICE-5
Ubiquitin carrier protein Q1
Ubiquitin-protein ligase Q1
Gene names
Name:UBE2Q1
Synonyms:NICE5, UBE2Q
ORF Names:PRO3094
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins By similarity.

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Tissue specificity

Widely expressed. Ref.6

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAF71141.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH61583.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH87836.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI07058.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB71173.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB65097.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16275660. Source: IntAct

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STUB1Q9UNE73EBI-1783287,EBI-357085

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z7E8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q7Z7E8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Ubiquitin-conjugating enzyme E2 Q1
PRO_0000223876

Regions

Compositional bias8 – 3831Gly-rich

Sites

Active site3511Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.11

Natural variations

Alternative sequence1 – 169169Missing in isoform 2.
VSP_017296

Experimental info

Sequence conflict2871N → Y Ref.6

Secondary structure

................................ 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 106FF7E59DF65555

FASTA42246,127
        10         20         30         40         50         60 
MQQPQPQGQQ QPGPGQQLGG QGAAPGAGGG PGGGPGPGPC LRRELKLLES IFHRGHERFR 

        70         80         90        100        110        120 
IASACLDELS CEFLLAGAGG AGAGAAPGPH LPPRGSVPGD PVRIHCNITE SYPAVPPIWS 

       130        140        150        160        170        180 
VESDDPNLAA VLERLVDIKK GNTLLLQHLK RIISDLCKLY NLPQHPDVEM LDQPLPAEQC 

       190        200        210        220        230        240 
TQEDVSSEDE DEEMPEDTED LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD 

       250        260        270        280        290        300 
YLNGAVSGSV QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH 

       310        320        330        340        350        360 
NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI CMELLTKQGW 

       370        380        390        400        410        420 
SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ SYKSLVQIHE KNGWYTPPKE 


DG 

« Hide

Isoform 2 [UniParc].

Checksum: 63C896449FD35EF2
Show »

FASTA25328,473

References

« Hide 'large scale' references
[1]"Isolation and characterization of the human UBE2Q gene and its murine ortholog."
Altmann M.E., Schulze E., Adham I.M., Koehler M., Engel W.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-422.
Tissue: Cerebellum.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-422 (ISOFORM 1).
Tissue: Cervix and Uterus.
[6]"Identification of human epidermal differentiation complex (EDC)-encoded genes by subtractive hybridization of entire YACs to a gridded keratinocyte cDNA library."
Marenholz I., Zirra M., Fischer D.F., Backendorf C., Ziegler A., Mischke D.
Genome Res. 11:341-355(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 282-422, TISSUE SPECIFICITY.
Tissue: Keratinocyte.
[7]"Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., Liu M., He F.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-386.
Tissue: Fetal liver.
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-422.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY112698 mRNA. Translation: AAM60814.1.
AK056388 mRNA. Translation: BAB71173.1. Different initiation.
AK293986 mRNA. Translation: BAG57353.1.
AL592078 Genomic DNA. Translation: CAI16186.1.
CH471121 Genomic DNA. Translation: EAW53193.1.
BC000848 mRNA. Translation: AAH00848.1.
BC015316 mRNA. Translation: AAH15316.2.
BC061583 mRNA. Translation: AAH61583.1. Different initiation.
BC070158 mRNA. Translation: AAH70158.1.
BC087836 mRNA. Translation: AAH87836.1. Different initiation.
BC107057 mRNA. Translation: AAI07058.1. Different initiation.
AJ243666 mRNA. Translation: CAB65097.1. Different initiation.
AF116721 mRNA. Translation: AAF71141.1. Different initiation.
CR457219 mRNA. Translation: CAG33500.1.
CCDSCCDS1069.1. [Q7Z7E8-1]
RefSeqNP_060052.3. NM_017582.6. [Q7Z7E8-1]
UniGeneHs.607928.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QGXX-ray2.56A/B/C/D247-414[»]
ProteinModelPortalQ7Z7E8.
SMRQ7Z7E8. Positions 249-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120732. 6 interactions.
IntActQ7Z7E8. 6 interactions.
MINTMINT-7944200.

PTM databases

PhosphoSiteQ7Z7E8.

Polymorphism databases

DMDM74750234.

Proteomic databases

MaxQBQ7Z7E8.
PaxDbQ7Z7E8.
PRIDEQ7Z7E8.

Protocols and materials databases

DNASU55585.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292211; ENSP00000292211; ENSG00000160714. [Q7Z7E8-1]
GeneID55585.
KEGGhsa:55585.
UCSCuc001fff.1. human. [Q7Z7E8-1]

Organism-specific databases

CTD55585.
GeneCardsGC01M154521.
H-InvDBHIX0001106.
HGNCHGNC:15698. UBE2Q1.
neXtProtNX_Q7Z7E8.
PharmGKBPA38029.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320521.
HOVERGENHBG061368.
InParanoidQ7Z7E8.
KOK10582.
OMANQYSLTR.
OrthoDBEOG76DTSS.
PhylomeDBQ7Z7E8.
TreeFamTF313338.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ7Z7E8.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ7Z7E8.
BgeeQ7Z7E8.
CleanExHS_UBE2Q1.
GenevestigatorQ7Z7E8.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 2 hits.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2Q1. human.
EvolutionaryTraceQ7Z7E8.
GenomeRNAi55585.
NextBio60100.
PROQ7Z7E8.

Entry information

Entry nameUB2Q1_HUMAN
AccessionPrimary (citable) accession number: Q7Z7E8
Secondary accession number(s): B4DF92 expand/collapse secondary AC list , Q3B841, Q5I0X2, Q6IS04, Q6P7P2, Q96MV4, Q9BVX5, Q9UGL6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM