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Protein

Ubiquitin-conjugating enzyme E2 J1

Gene

UBE2J1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD).PROSITE-ProRule annotation2 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911Glycyl thioester intermediate

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin conjugating enzyme activity Source: MGI
  4. ubiquitin-like protein transferase activity Source: GO_Central
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  2. protein N-linked glycosylation via asparagine Source: UniProtKB
  3. protein ubiquitination Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9Y385.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:UBE2J1
Synonyms:NCUBE1
ORF Names:CGI-76, HSPC153, HSPC205
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17598. UBE2J1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Single-pass type IV membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 282282CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei283 – 30321Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini304 – 31815LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911C → S: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER. 1 Publication

Organism-specific databases

PharmGKBiPA134906541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Ubiquitin-conjugating enzyme E2 J1PRO_0000082594Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661Phosphoserine3 Publications
Modified residuei268 – 2681Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y385.
PaxDbiQ9Y385.
PeptideAtlasiQ9Y385.
PRIDEiQ9Y385.

2D gel databases

OGPiQ9Y385.

PTM databases

PhosphoSiteiQ9Y385.

Expressioni

Gene expression databases

BgeeiQ9Y385.
CleanExiHS_UBE2J1.
GenevestigatoriQ9Y385.

Organism-specific databases

HPAiCAB073419.
HPA003509.

Interactioni

Protein-protein interaction databases

BioGridi119555. 31 interactions.
DIPiDIP-45598N.
IntActiQ9Y385. 13 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9Y385.
SMRiQ9Y385. Positions 9-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00530000063379.
HOVERGENiHBG058959.
InParanoidiQ9Y385.
KOiK10578.
OMAiDFCCEMC.
OrthoDBiEOG7HB59N.
PhylomeDBiQ9Y385.
TreeFamiTF101124.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METRYNLKSP AVKRLMKEAA ELKDPTDHYH AQPLEDNLFE WHFTVRGPPD
60 70 80 90 100
SDFDGGVYHG RIVLPPEYPM KPPSIILLTA NGRFEVGKKI CLSISGHHPE
110 120 130 140 150
TWQPSWSIRT ALLAIIGFMP TKGEGAIGSL DYTPEERRAL AKKSQDFCCE
160 170 180 190 200
GCGSAMKDVL LPLKSGSDSS QADQEAKELA RQISFKAEVN SSGKTISESD
210 220 230 240 250
LNHSFSLTDL QDDIPTTFQG ATASTSYGLQ NSSAASFHQP TQPVAKNTSM
260 270 280 290 300
SPRQRRAQQQ SQRRLSTSPD VIQGHQPRDN HTDHGGSAVL IVILTLALAA
310
LIFRRIYLAN EYIFDFEL
Length:318
Mass (Da):35,199
Last modified:September 12, 2004 - v2
Checksum:iCFF5FE00C2BBD39E
GO

Sequence cautioni

The sequence AAD34071.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAF36125.1 differs from that shown. Reason: Frameshift at position 119. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 332QP → HA in AAD34071 (PubMed:10810093).Curated
Sequence conflicti276 – 2761Q → H in AAF21505 (PubMed:12082160).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551G → V.1 Publication
Corresponds to variant rs8099 [ dbSNP | Ensembl ].
VAR_019689
Natural varianti229 – 2291L → V.4 Publications
Corresponds to variant rs10502 [ dbSNP | Ensembl ].
VAR_019690

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5021.1.
RefSeqiNP_057105.2. NM_016021.2.
UniGeneiHs.163776.

Genome annotation databases

EnsembliENST00000435041; ENSP00000451261; ENSG00000198833.
GeneIDi51465.
KEGGihsa:51465.
UCSCiuc003pnc.3. human.

Polymorphism databases

DMDMi52000881.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5021.1.
RefSeqiNP_057105.2. NM_016021.2.
UniGeneiHs.163776.

3D structure databases

ProteinModelPortaliQ9Y385.
SMRiQ9Y385. Positions 9-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119555. 31 interactions.
DIPiDIP-45598N.
IntActiQ9Y385. 13 interactions.

PTM databases

PhosphoSiteiQ9Y385.

Polymorphism databases

DMDMi52000881.

2D gel databases

OGPiQ9Y385.

Proteomic databases

MaxQBiQ9Y385.
PaxDbiQ9Y385.
PeptideAtlasiQ9Y385.
PRIDEiQ9Y385.

Protocols and materials databases

DNASUi51465.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000435041; ENSP00000451261; ENSG00000198833.
GeneIDi51465.
KEGGihsa:51465.
UCSCiuc003pnc.3. human.

Organism-specific databases

CTDi51465.
GeneCardsiGC06M090037.
HGNCiHGNC:17598. UBE2J1.
HPAiCAB073419.
HPA003509.
neXtProtiNX_Q9Y385.
PharmGKBiPA134906541.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00530000063379.
HOVERGENiHBG058959.
InParanoidiQ9Y385.
KOiK10578.
OMAiDFCCEMC.
OrthoDBiEOG7HB59N.
PhylomeDBiQ9Y385.
TreeFamiTF101124.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9Y385.

Miscellaneous databases

ChiTaRSiUBE2J1. human.
GeneWikiiUBE2J1.
GenomeRNAii51465.
NextBioi55093.
PROiQ9Y385.

Gene expression databases

BgeeiQ9Y385.
CleanExiHS_UBE2J1.
GenevestigatoriQ9Y385.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(2001) [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(1999) [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(1999) [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(2003) [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 (MAR-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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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(2003) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. 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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ERAD PATHWAY.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiUB2J1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y385
Secondary accession number(s): A8K3F9
, Q53F25, Q5W0N4, Q9BZ32, Q9NQL3, Q9NY66, Q9P011, Q9P0S0, Q9UF10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 12, 2004
Last sequence update: September 12, 2004
Last modified: March 31, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.