Q9Y385 (UB2J1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 J1
EC=6.3.2.19

Alternative name(s):
Non-canonical ubiquitin-conjugating enzyme 1
Short name=NCUBE-1
Yeast ubiquitin-conjugating enzyme UBC6 homolog E
Short name=HsUBC6e

Gene names

Name:	UBE2J1
Synonyms:	NCUBE1
ORF Names:	CGI-76, HSPC153, HSPC205

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). Ref.2 Ref.15
Catalytic activity	ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
Pathway	Protein modification; protein ubiquitination.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type IV membrane protein Ref.2.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.
Sequence caution	The sequence AAD34071.1 differs from that shown. Reason: Erroneous initiation. The sequence AAF36125.1 differs from that shown. Reason: Frameshift at position 119.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.15. Source: UniProtKB protein N-linked glycosylation via asparagine Inferred from mutant phenotype Ref.15. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 318	318	Ubiquitin-conjugating enzyme E2 J1		PRO_0000082594
Regions
	Topological domain	1 – 282	282	Cytoplasmic Potential
	Transmembrane	283 – 303	21	Helical; Anchor for type IV membrane protein; Potential
	Topological domain	304 – 318	15	Lumenal Potential
Sites
	Active site	91	1	Glycyl thioester intermediate
Amino acid modifications
	Modified residue	266	1	Phosphoserine Ref.12 Ref.14
	Modified residue	268	1	Phosphoserine Ref.11
Natural variations
	Natural variant	55	1	G → V. Ref.2 Corresponds to variant rs8099 [ dbSNP | Ensembl ].		VAR_019689
	Natural variant	229	1	L → V. Ref.4 Ref.6 Ref.8 Ref.9 Corresponds to variant rs10502 [ dbSNP | Ensembl ].		VAR_019690
Experimental info
	Mutagenesis	91	1	C → S: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER. Ref.2
	Sequence conflict	32 – 33	2	QP → HA in AAD34071. Ref.3
	Sequence conflict	276	1	Q → H in AAF21505. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y385 [UniParc]. Last modified September 13, 2004. Version 2. Checksum: CFF5FE00C2BBD39E	FASTA	318	35,199
	10 20 30 40 50 60 METRYNLKSP AVKRLMKEAA ELKDPTDHYH AQPLEDNLFE WHFTVRGPPD SDFDGGVYHG 70 80 90 100 110 120 RIVLPPEYPM KPPSIILLTA NGRFEVGKKI CLSISGHHPE TWQPSWSIRT ALLAIIGFMP 130 140 150 160 170 180 TKGEGAIGSL DYTPEERRAL AKKSQDFCCE GCGSAMKDVL LPLKSGSDSS QADQEAKELA 190 200 210 220 230 240 RQISFKAEVN SSGKTISESD LNHSFSLTDL QDDIPTTFQG ATASTSYGLQ NSSAASFHQP 250 260 270 280 290 300 TQPVAKNTSM SPRQRRAQQQ SQRRLSTSPD VIQGHQPRDN HTDHGGSAVL IVILTLALAA 310 LIFRRIYLAN EYIFDFEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a family of non-canonical ubiquitin-conjugating enzymes structurally related to yeast UBC6." Lester D.H., Farquharson C., Russell G.C., Houston B. Biochem. Biophys. Res. Commun. 269:474-480(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A role for mammalian Ubc6 homologues in ER-associated protein degradation." Lenk U., Yu H., Walter J., Gelman M.S., Hartmann E., Kopito R.R., Sommer T. J. Cell Sci. 115:3007-3014(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-55, FUNCTION, MUTAGENESIS OF CYS-91, SUBCELLULAR LOCATION.
[3]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-229. Tissue: Umbilical cord blood.
[5]	"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. , 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].
[6]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-229. Tissue: Spleen.
[7]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-229.
[9]	"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], VARIANT VAL-229. Tissue: Muscle.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, MASS SPECTROMETRY.
[15]	"STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein." Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T., Morino-Koga S., Wada I., Kai H. Mol. Cell 47:99-110(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ERAD PATHWAY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ245898 mRNA. Translation: CAB83212.1. U93243 mRNA. Translation: AAF21505.1. AF151834 mRNA. Translation: AAD34071.1. Different initiation. AF151039 mRNA. Translation: AAF36125.1. Frameshift. AF161502 mRNA. Translation: AAF29117.1. AK290574 mRNA. Translation: BAF83263.1. AK223464 mRNA. Translation: BAD97184.1. AL138717, AL139804 Genomic DNA. Translation: CAH70228.1. AL139804, AL138717 Genomic DNA. Translation: CAI19635.1. CH471051 Genomic DNA. Translation: EAW48555.1. CH471051 Genomic DNA. Translation: EAW48556.1. BC013973 mRNA. Translation: AAH13973.1.
IPI	IPI00006937.
RefSeq	NP_057105.2. NM_016021.2.
UniGene	Hs.163776.
3D structure databases
ProteinModelPortal	Q9Y385.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-45598N.
IntAct	Q9Y385. 11 interactions.
PTM databases
PhosphoSite	Q9Y385.
Polymorphism databases
DMDM	52000881.
2D gel databases
OGP	Q9Y385.
Proteomic databases
PaxDb	Q9Y385.
PeptideAtlas	Q9Y385.
PRIDE	Q9Y385.
Protocols and materials databases
DNASU	51465.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000435041; ENSP00000451261; ENSG00000198833.
GeneID	51465.
KEGG	hsa:51465.
UCSC	uc003pnc.3. human.
Organism-specific databases
CTD	51465.
GeneCards	GC06M090093.
HGNC	HGNC:17598. UBE2J1.
HPA	HPA003509.
neXtProt	NX_Q9Y385.
PharmGKB	PA134906541.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5078.
HOVERGEN	HBG058959.
InParanoid	Q9Y385.
KO	K10578.
OMA	CCEGCGC.
OrthoDB	EOG4G7BZW.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q9Y385.
Bgee	Q9Y385.
CleanEx	HS_UBE2J1.
Genevestigator	Q9Y385.
GermOnline	ENSG00000198833. Homo sapiens.
Family and domain databases
Gene3D	3.10.110.10. 1 hit.
InterPro	IPR000608. UBQ-conjugat_E2. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view]
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
SUPFAM	SSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. False negative. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	51465.
NextBio	55093.

Entry information

Entry name

UB2J1_HUMAN

Accession

Primary (citable) accession number: Q9Y385
Secondary accession number(s): A8K3F9 , Q53F25, Q5W0N4, Q9BZ32, Q9NQL3, Q9NY66, Q9P011, Q9P0S0, Q9UF10

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	September 13, 2004
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.