Q8N2K1 (UB2J2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 J2
EC=6.3.2.19

Alternative name(s):
Non-canonical ubiquitin-conjugating enzyme 2
Short name=NCUBE-2

Gene names

Name:	UBE2J2
Synonyms:	NCUBE2

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	259 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD) By similarity.
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 By similarity.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.
Sequence caution	The sequence BM544827 differs from that shown. Reason: Frameshift at several positions. The sequence BM544827 differs from that shown. Reason:

Ontologies

Keywords
Biological process	Ubl conjugation pathway Unfolded protein response
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to unfolded protein Inferred from electronic annotation. Source: UniProtKB-KW
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...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N2K1-1)

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: Q8N2K1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MSSTSSKRAPTTATQRLKQDYLRIKKDPVPYICAEPLPSNILEW → MWPQDIAGR

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8N2K1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     44-44: W → WFKRFSWLSLLSSWDYR

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 259

259

Ubiquitin-conjugating enzyme E2 J2

PRO_0000082596

Regions

Topological domain

1 – 226

226

Cytoplasmic Potential

Transmembrane

227 – 247

21

Helical; Anchor for type IV membrane protein; Potential

Topological domain

248 – 259

12

Lumenal Potential

Sites

Active site

94

1

Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence

1 – 44

44

MSSTS…NILEW → MWPQDIAGR in isoform 2.

VSP_011572

Alternative sequence

44

1

W → WFKRFSWLSLLSSWDYR in isoform 3.

VSP_045219

Experimental info

Sequence conflict

2

1

S → N in BAC11355. Ref.2

Sequence conflict

100

1

F → S in BAC11355. Ref.2

Sequence conflict

214 – 238

25

PNLAG…ANLFV → QTSQGSSRPTGTTDSGWRPG ELVC in AAK52609. Ref.1

Secondary structure

1

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259

Helix Strand Turn

Details...

Helix

13 – 26

14

Beta strand

32 – 37

6

Beta strand

40 – 49

10

Turn

55 – 58

4

Beta strand

60 – 66

7

Turn

69 – 72

4

Beta strand

77 – 80

4

Beta strand

85 – 87

3

Helix

111 – 123

13

Helix

136 – 151

16

Helix

154 – 159

6

Helix

161 – 167

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 7, 2009. Version 3. Checksum: 7DB5280D2947CE7E	FASTA	259	28,898
	10 20 30 40 50 60 MSSTSSKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG PEMTPYEGGY 70 80 90 100 110 120 YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF HPDTWNPAWS VSTILTGLLS 130 140 150 160 170 180 FMVEKGPTLG SIETSDFTKR QLAVQSLAFN LKDKVFCELF PEVVEEIKQK QKAQDELSSR 190 200 210 220 230 240 PQTLPLPDVV PDGETHLVQN GIQLLNGHAP GAVPNLAGLQ QANRHHGLLG GALANLFVIV 250 GFAAFAYTVK YVLRSIAQE
	Isoform 2 [UniParc]. Checksum: D5E649B09D7CC30E	FASTA	224	24,937
	10 20 30 40 50 60 MWPQDIAGRH YVVRGPEMTP YEGGYYHGKL IFPREFPFKP PSIYMITPNG RFKCNTRLCL 70 80 90 100 110 120 SITDFHPDTW NPAWSVSTIL TGLLSFMVEK GPTLGSIETS DFTKRQLAVQ SLAFNLKDKV 130 140 150 160 170 180 FCELFPEVVE EIKQKQKAQD ELSSRPQTLP LPDVVPDGET HLVQNGIQLL NGHAPGAVPN 190 200 210 220 LAGLQQANRH HGLLGGALAN LFVIVGFAAF AYTVKYVLRS IAQE
	Isoform 3 [UniParc]. Checksum: 602B2575ABC79E4E	FASTA	275	30,972
	10 20 30 40 50 60 MSSTSSKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWFKRFSW LSLLSSWDYR 70 80 90 100 110 120 HYVVRGPEMT PYEGGYYHGK LIFPREFPFK PPSIYMITPN GRFKCNTRLC LSITDFHPDT 130 140 150 160 170 180 WNPAWSVSTI LTGLLSFMVE KGPTLGSIET SDFTKRQLAV QSLAFNLKDK VFCELFPEVV 190 200 210 220 230 240 EEIKQKQKAQ DELSSRPQTL PLPDVVPDGE THLVQNGIQL LNGHAPGAVP NLAGLQQANR 250 260 270 HHGLLGGALA NLFVIVGFAA FAYTVKYVLR SIAQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)." Tiwari S., Weissman A.M. J. Biol. Chem. 276:16193-16200(2001) [PubMed] [Europe PMC] [Abstract] 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. , 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] (ISOFORMS 1 AND 2). Tissue: Ovary.
[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. , 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. , 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 (JUL-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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-205 (ISOFORM 3). Tissue: Brain, Hippocampus and Placenta.
[6]	"Structure of the endoplasmic reticulum (ER)-associated human ubiquitin-conjugating enzyme E2 J2." Structural genomics consortium (SGC) Submitted (NOV-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-185.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF296658 mRNA. Translation: AAK52609.1.
AK056065 mRNA. Translation: BAB71086.1.
AK075017 mRNA. Translation: BAC11355.1.
AK291935 mRNA. Translation: BAF84624.1.
AL162741 Genomic DNA. Translation: CAI23257.1.
CH471183 Genomic DNA. Translation: EAW56256.1.
CH471183 Genomic DNA. Translation: EAW56259.1.
BC094777 mRNA. Translation: AAH94777.1.
BC104890 mRNA. Translation: AAI04891.1.
BC113430 mRNA. Translation: AAI13431.1.
BC143657 mRNA. Translation: AAI43658.1.
BM544827 mRNA. No translation available.

IPI

IPI00455911.
IPI00514050.
IPI00873186.

RefSeq

NP_477515.2. NM_058167.2.
NP_919296.1. NM_194315.1.
NP_919440.1. NM_194458.1.

UniGene

Hs.191987.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F4W	X-ray	2.00	A/B	1-185	[»]

ProteinModelPortal

Q8N2K1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8N2K1. 4 interactions.

STRING

9606.ENSP00000383719.

Polymorphism databases

DMDM

251757431.

Proteomic databases

PaxDb

Q8N2K1.

PRIDE

Q8N2K1.

Protocols and materials databases

DNASU

118424.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000339385; ENSP00000340197; ENSG00000160087.
ENST00000349431; ENSP00000305826; ENSG00000160087.
ENST00000360466; ENSP00000353653; ENSG00000160087.
ENST00000400930; ENSP00000383719; ENSG00000160087.

GeneID

118424.

KEGG

hsa:118424.

UCSC

uc001adm.3. human.
uc001adp.3. human.

Organism-specific databases

CTD

118424.

GeneCards

GC01M001182.

H-InvDB

HIX0000017.

HGNC

HGNC:19268. UBE2J2.

HPA

HPA051399.

neXtProt

NX_Q8N2K1.

PharmGKB

PA134882268.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000170330.

HOVERGEN

HBG058434.

KO

K04554.

OMA

TSDYTKR.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q8N2K1.

Bgee

Q8N2K1.

CleanEx

HS_UBE2J2.

Genevestigator

Q8N2K1.

GermOnline

ENSG00000160087. 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

ChiTaRS

UBE2J2. human.

EvolutionaryTrace

Q8N2K1.

GenomeRNAi

118424.

NextBio

80253.

Entry information

Entry name

UB2J2_HUMAN

Accession

Primary (citable) accession number: Q8N2K1
Secondary accession number(s): A8MYC7 , Q504T9, Q96N26, Q96T84

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	July 7, 2009
Last modified:	May 1, 2013
This is version 99 of the entry and version 3 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.