Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q7Z7E8

- UB2Q1_HUMAN

UniProt

Q7Z7E8 - UB2Q1_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 Q1

Gene

UBE2Q1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins.PROSITE-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 sitei351 – 3511Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. 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.
    SignaLinkiQ7Z7E8.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:UBE2Q1
    Synonyms:NICE5, UBE2Q
    ORF Names:PRO3094
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:15698. UBE2Q1.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38029.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 422422Ubiquitin-conjugating enzyme E2 Q1PRO_0000223876Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ7Z7E8.
    PaxDbiQ7Z7E8.
    PRIDEiQ7Z7E8.

    PTM databases

    PhosphoSiteiQ7Z7E8.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ7Z7E8.
    BgeeiQ7Z7E8.
    CleanExiHS_UBE2Q1.
    GenevestigatoriQ7Z7E8.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STUB1Q9UNE73EBI-1783287,EBI-357085

    Protein-protein interaction databases

    BioGridi120732. 6 interactions.
    IntActiQ7Z7E8. 6 interactions.
    MINTiMINT-7944200.

    Structurei

    Secondary structure

    1
    422
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi250 – 26415
    Helixi267 – 2704
    Beta strandi273 – 2786
    Helixi279 – 2813
    Beta strandi285 – 2917
    Helixi298 – 30912
    Beta strandi315 – 3206
    Turni325 – 3273
    Beta strandi331 – 3377
    Beta strandi339 – 3413
    Beta strandi348 – 3503
    Turni357 – 3593
    Helixi366 – 37914
    Beta strandi386 – 3883
    Helixi390 – 3923
    Helixi395 – 40511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QGXX-ray2.56A/B/C/D247-414[»]
    ProteinModelPortaliQ7Z7E8.
    SMRiQ7Z7E8. Positions 249-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z7E8.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi8 – 3831Gly-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG320521.
    HOVERGENiHBG061368.
    InParanoidiQ7Z7E8.
    KOiK10582.
    OMAiNQYSLTR.
    OrthoDBiEOG76DTSS.
    PhylomeDBiQ7Z7E8.
    TreeFamiTF313338.

    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. 2 hits.
    PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z7E8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MQQPQPQGQQ QPGPGQQLGG QGAAPGAGGG PGGGPGPGPC LRRELKLLES    50
    IFHRGHERFR IASACLDELS CEFLLAGAGG AGAGAAPGPH LPPRGSVPGD 100
    PVRIHCNITE SYPAVPPIWS VESDDPNLAA VLERLVDIKK GNTLLLQHLK 150
    RIISDLCKLY NLPQHPDVEM LDQPLPAEQC TQEDVSSEDE DEEMPEDTED 200
    LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD YLNGAVSGSV 250
    QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH 300
    NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI 350
    CMELLTKQGW SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ 400
    SYKSLVQIHE KNGWYTPPKE DG 422
    Length:422
    Mass (Da):46,127
    Last modified:October 1, 2003 - v1
    Checksum:i106FF7E59DF65555
    GO
    Isoform 2 (identifier: Q7Z7E8-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:253
    Mass (Da):28,473
    Checksum:i63C896449FD35EF2
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti287 – 2871N → Y(PubMed:11230159)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 169169Missing in isoform 2. 2 PublicationsVSP_017296Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1069.1. [Q7Z7E8-1]
    RefSeqiNP_060052.3. NM_017582.6. [Q7Z7E8-1]
    UniGeneiHs.607928.

    Genome annotation databases

    EnsembliENST00000292211; ENSP00000292211; ENSG00000160714. [Q7Z7E8-1]
    GeneIDi55585.
    KEGGihsa:55585.
    UCSCiuc001fff.1. human. [Q7Z7E8-1]

    Polymorphism databases

    DMDMi74750234.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1069.1. [Q7Z7E8-1 ]
    RefSeqi NP_060052.3. NM_017582.6. [Q7Z7E8-1 ]
    UniGenei Hs.607928.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QGX X-ray 2.56 A/B/C/D 247-414 [» ]
    ProteinModelPortali Q7Z7E8.
    SMRi Q7Z7E8. Positions 249-409.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120732. 6 interactions.
    IntActi Q7Z7E8. 6 interactions.
    MINTi MINT-7944200.

    PTM databases

    PhosphoSitei Q7Z7E8.

    Polymorphism databases

    DMDMi 74750234.

    Proteomic databases

    MaxQBi Q7Z7E8.
    PaxDbi Q7Z7E8.
    PRIDEi Q7Z7E8.

    Protocols and materials databases

    DNASUi 55585.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292211 ; ENSP00000292211 ; ENSG00000160714 . [Q7Z7E8-1 ]
    GeneIDi 55585.
    KEGGi hsa:55585.
    UCSCi uc001fff.1. human. [Q7Z7E8-1 ]

    Organism-specific databases

    CTDi 55585.
    GeneCardsi GC01M154521.
    H-InvDB HIX0001106.
    HGNCi HGNC:15698. UBE2Q1.
    neXtProti NX_Q7Z7E8.
    PharmGKBi PA38029.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320521.
    HOVERGENi HBG061368.
    InParanoidi Q7Z7E8.
    KOi K10582.
    OMAi NQYSLTR.
    OrthoDBi EOG76DTSS.
    PhylomeDBi Q7Z7E8.
    TreeFami TF313338.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q7Z7E8.

    Miscellaneous databases

    ChiTaRSi UBE2Q1. human.
    EvolutionaryTracei Q7Z7E8.
    GenomeRNAii 55585.
    NextBioi 60100.
    PROi Q7Z7E8.

    Gene expression databases

    ArrayExpressi Q7Z7E8.
    Bgeei Q7Z7E8.
    CleanExi HS_UBE2Q1.
    Genevestigatori Q7Z7E8.

    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. 2 hits.
    PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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].

    Entry informationi

    Entry nameiUB2Q1_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z7E8
    Secondary accession number(s): B4DF92
    , Q3B841, Q5I0X2, Q6IS04, Q6P7P2, Q96MV4, Q9BVX5, Q9UGL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3