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Q9Y385

- UB2J1_HUMAN

UniProt

Q9Y385 - UB2J1_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 J1

Gene

UBE2J1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (13 Sep 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD).2 PublicationsPROSITE-ProRule annotation

    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. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW

    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: UniProtKB-UniPathway

    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17598. UBE2J1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    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 – 2661Phosphoserine2 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

    HPAiHPA003509.

    Interactioni

    Protein-protein interaction databases

    BioGridi119555. 29 interactions.
    DIPiDIP-45598N.
    IntActiQ9Y385. 12 interactions.

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 282282CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini304 – 31815LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei283 – 30321Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5078.
    HOVERGENiHBG058959.
    InParanoidiQ9Y385.
    KOiK10578.
    OMAiCCEGCGC.
    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

    METRYNLKSP AVKRLMKEAA ELKDPTDHYH AQPLEDNLFE WHFTVRGPPD    50
    SDFDGGVYHG RIVLPPEYPM KPPSIILLTA NGRFEVGKKI CLSISGHHPE 100
    TWQPSWSIRT ALLAIIGFMP TKGEGAIGSL DYTPEERRAL AKKSQDFCCE 150
    GCGSAMKDVL LPLKSGSDSS QADQEAKELA RQISFKAEVN SSGKTISESD 200
    LNHSFSLTDL QDDIPTTFQG ATASTSYGLQ NSSAASFHQP TQPVAKNTSM 250
    SPRQRRAQQQ SQRRLSTSPD VIQGHQPRDN HTDHGGSAVL IVILTLALAA 300
    LIFRRIYLAN EYIFDFEL 318
    Length:318
    Mass (Da):35,199
    Last modified:September 13, 2004 - v2
    Checksum:iCFF5FE00C2BBD39E
    GO

    Sequence cautioni

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

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5021.1.
    RefSeqi NP_057105.2. NM_016021.2.
    UniGenei Hs.163776.

    3D structure databases

    ProteinModelPortali Q9Y385.
    SMRi Q9Y385. Positions 9-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119555. 29 interactions.
    DIPi DIP-45598N.
    IntActi Q9Y385. 12 interactions.

    PTM databases

    PhosphoSitei Q9Y385.

    Polymorphism databases

    DMDMi 52000881.

    2D gel databases

    OGPi Q9Y385.

    Proteomic databases

    MaxQBi Q9Y385.
    PaxDbi Q9Y385.
    PeptideAtlasi Q9Y385.
    PRIDEi Q9Y385.

    Protocols and materials databases

    DNASUi 51465.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000435041 ; ENSP00000451261 ; ENSG00000198833 .
    GeneIDi 51465.
    KEGGi hsa:51465.
    UCSCi uc003pnc.3. human.

    Organism-specific databases

    CTDi 51465.
    GeneCardsi GC06M090093.
    HGNCi HGNC:17598. UBE2J1.
    HPAi HPA003509.
    neXtProti NX_Q9Y385.
    PharmGKBi PA134906541.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5078.
    HOVERGENi HBG058959.
    InParanoidi Q9Y385.
    KOi K10578.
    OMAi CCEGCGC.
    OrthoDBi EOG7HB59N.
    PhylomeDBi Q9Y385.
    TreeFami TF101124.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9Y385.

    Miscellaneous databases

    GeneWikii UBE2J1.
    GenomeRNAii 51465.
    NextBioi 55093.
    PROi Q9Y385.

    Gene expression databases

    Bgeei Q9Y385.
    CleanExi HS_UBE2J1.
    Genevestigatori Q9Y385.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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(2010) [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(2011) [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(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ERAD PATHWAY.

    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 13, 2004
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 125 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