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Q9BUN8

- DERL1_HUMAN

UniProt

Q9BUN8 - DERL1_HUMAN

Protein

Derlin-1

Gene

DERL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In case of infection by cytomegaloviruses, it plays a central role in the export from the ER and subsequent degradation of MHC class I heavy chains via its interaction with US11 viral protein, which recognizes and associates with MHC class I heavy chains. Also participates in the degradation process of misfolded cytomegalovirus US2 protein.2 Publications

    GO - Molecular functioni

    1. MHC class I protein binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. receptor activity Source: UniProtKB

    GO - Biological processi

    1. endoplasmic reticulum unfolded protein response Source: UniProtKB
    2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    3. establishment of protein localization Source: UniProtKB
    4. intracellular transport of viral protein in host cell Source: UniProtKB
    5. response to unfolded protein Source: MGI
    6. retrograde protein transport, ER to cytosol Source: UniProtKB

    Keywords - Biological processi

    Host-virus interaction, Protein transport, Transport, Unfolded protein response

    Protein family/group databases

    TCDBi3.A.16.1.1. the endoplasmic reticular retrotranslocon (er-rt) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Derlin-1
    Alternative name(s):
    Degradation in endoplasmic reticulum protein 1
    Short name:
    DERtrin-1
    Der1-like protein 1
    Gene namesi
    Name:DERL1
    Synonyms:DER1
    ORF Names:UNQ243/PRO276
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:28454. DERL1.

    Subcellular locationi

    Endoplasmic reticulum membrane 4 Publications; Multi-pass membrane protein 4 Publications

    GO - Cellular componenti

    1. early endosome Source: Ensembl
    2. endoplasmic reticulum Source: UniProtKB
    3. Hrd1p ubiquitin ligase complex Source: UniProt
    4. integral component of endoplasmic reticulum membrane Source: UniProtKB
    5. integral component of membrane Source: MGI
    6. late endosome Source: Ensembl
    7. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134926638.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 251250Derlin-1PRO_0000219042Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei202 – 2021Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BUN8.
    PaxDbiQ9BUN8.
    PRIDEiQ9BUN8.

    PTM databases

    PhosphoSiteiQ9BUN8.

    Expressioni

    Tissue specificityi

    Ubiquitous.2 Publications

    Inductioni

    Up-regulated in response to endoplasmic reticulum stress via the ERN1-XBP1 pathway of the unfolded protein response (UPR).By similarity

    Gene expression databases

    ArrayExpressiQ9BUN8.
    BgeeiQ9BUN8.
    CleanExiHS_DERL1.
    GenevestigatoriQ9BUN8.

    Organism-specific databases

    HPAiHPA016562.

    Interactioni

    Subunit structurei

    Forms homo- and heterooligomers with DERL2 and DERL3; binding to DERL3 is poorer than that between DERL2 and DERL3. Interacts with AMFR, VIMP/SELS, SEL1L, SELK, SYVN1 and VCP, as well as with SEL1L-SYVN1 and VCP-VIMP protein complexes; this interaction is weaker than that observed between DERL2 and these complexes. Interacts with the cytomegalovirus US11 protein. Interacts with NGLY1 and YOD1. Does not bind to EDEM1. Interacts with DNAJB9 and RNF103. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, VIMP, STT3A AND VCP.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAP31P515723EBI-398977,EBI-77683
    CFTRP135692EBI-398977,EBI-349854

    Protein-protein interaction databases

    BioGridi122559. 42 interactions.
    IntActiQ9BUN8. 8 interactions.
    STRINGi9606.ENSP00000259512.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BUN8.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 2221CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini44 – 5916LumenalSequence AnalysisAdd
    BLAST
    Topological domaini81 – 10525CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini127 – 15428LumenalSequence AnalysisAdd
    BLAST
    Topological domaini176 – 25176CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 4321Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei60 – 8021Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei106 – 12621Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei155 – 17521Helical; Name=4Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the derlin family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5291.
    HOGENOMiHOG000200949.
    HOVERGENiHBG105143.
    InParanoidiQ9BUN8.
    KOiK11519.
    OMAiYIWCQLN.
    OrthoDBiEOG7353XM.
    PhylomeDBiQ9BUN8.
    TreeFamiTF354297.

    Family and domain databases

    InterProiIPR007599. DER1.
    [Graphical view]
    PANTHERiPTHR11009. PTHR11009. 1 hit.
    PfamiPF04511. DER1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BUN8-1) [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

    MSDIGDWFRS IPAITRYWFA ATVAVPLVGK LGLISPAYLF LWPEAFLYRF    50
    QIWRPITATF YFPVGPGTGF LYLVNLYFLY QYSTRLETGA FDGRPADYLF 100
    MLLFNWICIV ITGLAMDMQL LMIPLIMSVL YVWAQLNRDM IVSFWFGTRF 150
    KACYLPWVIL GFNYIIGGSV INELIGNLVG HLYFFLMFRY PMDLGGRNFL 200
    STPQFLYRWL PSRRGGVSGF GVPPASMRRA ADQNGGGGRH NWGQGFRLGD 250
    Q 251
    Length:251
    Mass (Da):28,801
    Last modified:June 1, 2001 - v1
    Checksum:i4A6E0DB68D9AF244
    GO
    Isoform 2 (identifier: Q9BUN8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         170-189: Missing.

    Show »
    Length:231
    Mass (Da):26,423
    Checksum:iE0D0982FDD620F1F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711I → V.
    Corresponds to variant rs2272722 [ dbSNP | Ensembl ].
    VAR_019516

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei170 – 18920Missing in isoform 2. 1 PublicationVSP_041329Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358818 mRNA. Translation: AAQ89177.1.
    AC104316 Genomic DNA. No translation available.
    BC002457 mRNA. Translation: AAH02457.1.
    AK124086 mRNA. Translation: BAG54003.1.
    CCDSiCCDS47915.1. [Q9BUN8-2]
    CCDS6337.1. [Q9BUN8-1]
    RefSeqiNP_001128143.1. NM_001134671.2. [Q9BUN8-2]
    NP_077271.1. NM_024295.5. [Q9BUN8-1]
    UniGeneiHs.241576.

    Genome annotation databases

    EnsembliENST00000259512; ENSP00000259512; ENSG00000136986. [Q9BUN8-1]
    ENST00000405944; ENSP00000384289; ENSG00000136986. [Q9BUN8-2]
    GeneIDi79139.
    KEGGihsa:79139.
    UCSCiuc003ypl.3. human. [Q9BUN8-1]
    uc003ypm.3. human. [Q9BUN8-2]

    Polymorphism databases

    DMDMi50400630.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY358818 mRNA. Translation: AAQ89177.1 .
    AC104316 Genomic DNA. No translation available.
    BC002457 mRNA. Translation: AAH02457.1 .
    AK124086 mRNA. Translation: BAG54003.1 .
    CCDSi CCDS47915.1. [Q9BUN8-2 ]
    CCDS6337.1. [Q9BUN8-1 ]
    RefSeqi NP_001128143.1. NM_001134671.2. [Q9BUN8-2 ]
    NP_077271.1. NM_024295.5. [Q9BUN8-1 ]
    UniGenei Hs.241576.

    3D structure databases

    ProteinModelPortali Q9BUN8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122559. 42 interactions.
    IntActi Q9BUN8. 8 interactions.
    STRINGi 9606.ENSP00000259512.

    Protein family/group databases

    TCDBi 3.A.16.1.1. the endoplasmic reticular retrotranslocon (er-rt) family.

    PTM databases

    PhosphoSitei Q9BUN8.

    Polymorphism databases

    DMDMi 50400630.

    Proteomic databases

    MaxQBi Q9BUN8.
    PaxDbi Q9BUN8.
    PRIDEi Q9BUN8.

    Protocols and materials databases

    DNASUi 79139.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259512 ; ENSP00000259512 ; ENSG00000136986 . [Q9BUN8-1 ]
    ENST00000405944 ; ENSP00000384289 ; ENSG00000136986 . [Q9BUN8-2 ]
    GeneIDi 79139.
    KEGGi hsa:79139.
    UCSCi uc003ypl.3. human. [Q9BUN8-1 ]
    uc003ypm.3. human. [Q9BUN8-2 ]

    Organism-specific databases

    CTDi 79139.
    GeneCardsi GC08M124094.
    HGNCi HGNC:28454. DERL1.
    HPAi HPA016562.
    MIMi 608813. gene.
    neXtProti NX_Q9BUN8.
    PharmGKBi PA134926638.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5291.
    HOGENOMi HOG000200949.
    HOVERGENi HBG105143.
    InParanoidi Q9BUN8.
    KOi K11519.
    OMAi YIWCQLN.
    OrthoDBi EOG7353XM.
    PhylomeDBi Q9BUN8.
    TreeFami TF354297.

    Miscellaneous databases

    GenomeRNAii 79139.
    NextBioi 68017.
    PROi Q9BUN8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BUN8.
    Bgeei Q9BUN8.
    CleanExi HS_DERL1.
    Genevestigatori Q9BUN8.

    Family and domain databases

    InterProi IPR007599. DER1.
    [Graphical view ]
    PANTHERi PTHR11009. PTHR11009. 1 hit.
    Pfami PF04511. DER1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    2. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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).
      Tissue: Lymph.
    4. "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] OF 47-131 (ISOFORM 2).
      Tissue: Esophagus.
    5. "A membrane protein required for dislocation of misfolded proteins from the ER."
      Lilley B.N., Ploegh H.L.
      Nature 429:834-840(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, TISSUE SPECIFICITY, INTERACTION WITH US11.
    6. "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol."
      Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.
      Nature 429:841-847(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH US11 AND VIMP.
    7. "The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway."
      Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., Koning F., Kloetzel P.-M., Seeger M.
      J. Mol. Biol. 354:1021-1027(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VCP AND SYVN1.
    8. "The retrotranslocation protein derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum."
      Katiyar S., Joshi S., Lennarz W.J.
      Mol. Biol. Cell 16:4584-4594(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NGLY1.
    9. "Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane."
      Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.
      Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMOOLIGOMERIZATION, INTERACTION WITH AMFR; SYVN1; VCP AND VIMP.
    10. "Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane."
      Lilley B.N., Ploegh H.L.
      Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, OLIGOMERIZATION, INTERACTION WITH VIMP; VCP; SEL1L AND SYVN1.
    11. "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation."
      Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.
      J. Cell Biol. 172:383-393(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH DERL3 AND VCP.
    12. "Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated degradation pathway."
      Maruyama Y., Yamada M., Takahashi K., Yamada M.
      Biochem. Biophys. Res. Commun. 374:737-741(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF103.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER."
      Ernst R., Mueller B., Ploegh H.L., Schlieker C.
      Mol. Cell 36:28-38(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YOD1.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis."
      Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 286:42937-42948(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SELK AND VIMP, IDENTIFICATION IN A COMPLEX WITH CANX; DERL2; DDOST; RPN1; RPN2; SELK; STT3A; VCP AND VIMP.
    17. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDERL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BUN8
    Secondary accession number(s): B3KW41, E9PH19
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 114 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3