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Q96NY9

- MUS81_HUMAN

UniProt

Q96NY9 - MUS81_HUMAN

Protein

Crossover junction endonuclease MUS81

Gene

MUS81

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    Interacts with EME1 and EME2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks.9 Publications

    Cofactori

    Magnesium.1 Publication

    GO - Molecular functioni

    1. 3'-flap endonuclease activity Source: UniProtKB
    2. DNA binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA catabolic process, endonucleolytic Source: MGI
    2. DNA recombination Source: UniProtKB-KW
    3. DNA repair Source: UniProtKB
    4. response to intra-S DNA damage checkpoint signaling Source: MGI

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Crossover junction endonuclease MUS81 (EC:3.1.22.-)
    Gene namesi
    Name:MUS81
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:29814. MUS81.

    Subcellular locationi

    Nucleusnucleolus 4 Publications
    Note: Recruited to foci of DNA damage in S-phase cells.

    GO - Cellular componenti

    1. intercellular bridge Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi306 – 3072GD → AE: Loss of activity.
    Mutagenesisi333 – 3342ER → AG: Loss of activity.
    Mutagenesisi338 – 3392DD → AA: Loss of activity.

    Organism-specific databases

    PharmGKBiPA134881809.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 551551Crossover junction endonuclease MUS81PRO_0000198858Add
    BLAST

    Proteomic databases

    MaxQBiQ96NY9.
    PaxDbiQ96NY9.
    PRIDEiQ96NY9.

    PTM databases

    PhosphoSiteiQ96NY9.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Developmental stagei

    Expressed in S phase and G2 phase.1 Publication

    Inductioni

    Up-regulated in cells treated with agents that damage DNA or block replication. This up-regulation seems to be independent of transcription.1 Publication

    Gene expression databases

    ArrayExpressiQ96NY9.
    BgeeiQ96NY9.
    CleanExiHS_MUS81.
    GenevestigatoriQ96NY9.

    Organism-specific databases

    HPAiHPA050711.
    HPA059530.

    Interactioni

    Subunit structurei

    May self-associate. Interacts with EME1, EME2 and CHEK2. Interacts with BLM, and this interaction may stimulate the endonuclease activity of MUS81. Interacts with SLX4/BTBD12; this interaction is direct and links the MUS81-EME1 complex to SLX4, which may coordinate the action of the structure-specific endonuclease during DNA repair. Interacts with DCLRE1B/Apollo.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EME1Q96AY25EBI-2370806,EBI-2370825
    FEN1P397485EBI-2370806,EBI-707816
    SLX4Q8IY928EBI-2370806,EBI-2370740

    Protein-protein interaction databases

    BioGridi123170. 12 interactions.
    DIPiDIP-48630N.
    IntActiQ96NY9. 6 interactions.
    MINTiMINT-3056813.
    STRINGi9606.ENSP00000307853.

    Structurei

    Secondary structure

    1
    551
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi137 – 14913
    Helixi152 – 1543
    Helixi160 – 17011
    Helixi184 – 1907
    Beta strandi193 – 1953
    Beta strandi198 – 2003
    Beta strandi203 – 2053
    Helixi207 – 21913
    Turni220 – 2223
    Beta strandi224 – 2263
    Beta strandi275 – 2773
    Turni289 – 2913
    Helixi292 – 2943
    Beta strandi305 – 3095
    Beta strandi329 – 3324
    Turni337 – 3404
    Helixi341 – 3444
    Beta strandi345 – 3473
    Helixi348 – 3525
    Turni353 – 3564
    Turni358 – 3603
    Beta strandi362 – 3654
    Beta strandi373 – 3764
    Helixi381 – 39313
    Helixi405 – 4084
    Helixi410 – 4167
    Turni417 – 4215
    Turni458 – 4614
    Helixi462 – 4643
    Turni465 – 4673
    Turni471 – 4733
    Helixi474 – 4774
    Turni488 – 4925
    Beta strandi493 – 4975
    Helixi500 – 5089
    Helixi513 – 5153
    Turni516 – 5205
    Turni526 – 5294
    Helixi534 – 54411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2MC3NMR-A127-230[»]
    2ZIXX-ray3.50A246-551[»]
    4P0PX-ray2.80A246-551[»]
    4P0QX-ray2.85A246-551[»]
    4P0RX-ray6.50A/C246-551[»]
    4P0SX-ray6.00A/C/E/G246-551[»]
    ProteinModelPortaliQ96NY9.
    SMRiQ96NY9. Positions 11-90, 128-230, 259-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96NY9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini270 – 372103ERCC4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni125 – 244120Interaction with BLMAdd
    BLAST

    Sequence similaritiesi

    Belongs to the XPF family.Curated
    Contains 1 ERCC4 domain.Curated

    Phylogenomic databases

    eggNOGiCOG1948.
    HOGENOMiHOG000113699.
    HOVERGENiHBG052538.
    InParanoidiQ96NY9.
    KOiK08991.
    OMAiKCGRLQR.
    OrthoDBiEOG7TXKGV.
    PhylomeDBiQ96NY9.
    TreeFamiTF315113.

    Family and domain databases

    Gene3Di1.10.8.310. 1 hit.
    3.40.50.10130. 1 hit.
    InterProiIPR010996. DNA_pol_b-like_N.
    IPR020819. DNA_repair_nuc_XPF/helicase.
    IPR006166. ERCC4_domain.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR027420. PolB_N.
    IPR011335. Restrct_endonuc-II-like.
    [Graphical view]
    PfamiPF02732. ERCC4. 1 hit.
    [Graphical view]
    SMARTiSM00891. ERCC4. 1 hit.
    SM00278. HhH1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47802. SSF47802. 1 hit.
    SSF52980. SSF52980. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q96NY9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPVRLGRK RPLPACPNPL FVRWLTEWRD EATRSRRRTR FVFQKALRSL    50
    RRYPLPLRSG KEAKILQHFG DGLCRMLDER LQRHRTSGGD HAPDSPSGEN 100
    SPAPQGRLAE VQDSSMPVPA QPKAGGSGSY WPARHSGARV ILLVLYREHL 150
    NPNGHHFLTK EELLQRCAQK SPRVAPGSAR PWPALRSLLH RNLVLRTHQP 200
    ARYSLTPEGL ELAQKLAESE GLSLLNVGIG PKEPPGEETA VPGAASAELA 250
    SEAGVQQQPL ELRPGEYRVL LCVDIGETRG GGHRPELLRE LQRLHVTHTV 300
    RKLHVGDFVW VAQETNPRDP ANPGELVLDH IVERKRLDDL CSSIIDGRFR 350
    EQKFRLKRCG LERRVYLVEE HGSVHNLSLP ESTLLQAVTN TQVIDGFFVK 400
    RTADIKESAA YLALLTRGLQ RLYQGHTLRS RPWGTPGNPE SGAMTSPNPL 450
    CSLLTFSDFN AGAIKNKAQS VREVFARQLM QVRGVSGEKA AALVDRYSTP 500
    ASLLAAYDAC ATPKEQETLL STIKCGRLQR NLGPALSRTL SQLYCSYGPL 550
    T 551
    Length:551
    Mass (Da):61,173
    Last modified:February 5, 2008 - v3
    Checksum:iD0F331CC2269D847
    GO

    Sequence cautioni

    The sequence BAB14953.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371R → H.3 Publications
    Corresponds to variant rs13817 [ dbSNP | Ensembl ].
    VAR_025340
    Natural varianti115 – 1151S → F.
    Corresponds to variant rs34381357 [ dbSNP | Ensembl ].
    VAR_061988
    Natural varianti180 – 1801R → P.3 Publications
    Corresponds to variant rs545500 [ dbSNP | Ensembl ].
    VAR_038521
    Natural varianti189 – 1891L → F.
    Corresponds to variant rs2298447 [ dbSNP | Ensembl ].
    VAR_021990
    Natural varianti350 – 3501R → W.
    Corresponds to variant rs34891773 [ dbSNP | Ensembl ].
    VAR_038522
    Natural varianti481 – 4811Q → H.
    Corresponds to variant rs765593 [ dbSNP | Ensembl ].
    VAR_025341

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF425646 mRNA. Translation: AAL28065.1.
    BC009999 mRNA. Translation: AAH09999.2.
    AK024665 mRNA. Translation: BAB14953.1. Different initiation.
    CCDSiCCDS8115.1.
    RefSeqiNP_079404.3. NM_025128.4.
    UniGeneiHs.288798.

    Genome annotation databases

    EnsembliENST00000308110; ENSP00000307853; ENSG00000172732.
    GeneIDi80198.
    KEGGihsa:80198.
    UCSCiuc001ofv.4. human.

    Polymorphism databases

    DMDMi166898077.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF425646 mRNA. Translation: AAL28065.1 .
    BC009999 mRNA. Translation: AAH09999.2 .
    AK024665 mRNA. Translation: BAB14953.1 . Different initiation.
    CCDSi CCDS8115.1.
    RefSeqi NP_079404.3. NM_025128.4.
    UniGenei Hs.288798.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2MC3 NMR - A 127-230 [» ]
    2ZIX X-ray 3.50 A 246-551 [» ]
    4P0P X-ray 2.80 A 246-551 [» ]
    4P0Q X-ray 2.85 A 246-551 [» ]
    4P0R X-ray 6.50 A/C 246-551 [» ]
    4P0S X-ray 6.00 A/C/E/G 246-551 [» ]
    ProteinModelPortali Q96NY9.
    SMRi Q96NY9. Positions 11-90, 128-230, 259-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123170. 12 interactions.
    DIPi DIP-48630N.
    IntActi Q96NY9. 6 interactions.
    MINTi MINT-3056813.
    STRINGi 9606.ENSP00000307853.

    PTM databases

    PhosphoSitei Q96NY9.

    Polymorphism databases

    DMDMi 166898077.

    Proteomic databases

    MaxQBi Q96NY9.
    PaxDbi Q96NY9.
    PRIDEi Q96NY9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308110 ; ENSP00000307853 ; ENSG00000172732 .
    GeneIDi 80198.
    KEGGi hsa:80198.
    UCSCi uc001ofv.4. human.

    Organism-specific databases

    CTDi 80198.
    GeneCardsi GC11P065627.
    H-InvDB HIX0009809.
    HGNCi HGNC:29814. MUS81.
    HPAi HPA050711.
    HPA059530.
    MIMi 606591. gene.
    neXtProti NX_Q96NY9.
    PharmGKBi PA134881809.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1948.
    HOGENOMi HOG000113699.
    HOVERGENi HBG052538.
    InParanoidi Q96NY9.
    KOi K08991.
    OMAi KCGRLQR.
    OrthoDBi EOG7TXKGV.
    PhylomeDBi Q96NY9.
    TreeFami TF315113.

    Miscellaneous databases

    EvolutionaryTracei Q96NY9.
    GeneWikii MUS81.
    GenomeRNAii 80198.
    NextBioi 70556.
    PROi Q96NY9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96NY9.
    Bgeei Q96NY9.
    CleanExi HS_MUS81.
    Genevestigatori Q96NY9.

    Family and domain databases

    Gene3Di 1.10.8.310. 1 hit.
    3.40.50.10130. 1 hit.
    InterProi IPR010996. DNA_pol_b-like_N.
    IPR020819. DNA_repair_nuc_XPF/helicase.
    IPR006166. ERCC4_domain.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR027420. PolB_N.
    IPR011335. Restrct_endonuc-II-like.
    [Graphical view ]
    Pfami PF02732. ERCC4. 1 hit.
    [Graphical view ]
    SMARTi SM00891. ERCC4. 1 hit.
    SM00278. HhH1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47802. SSF47802. 1 hit.
    SSF52980. SSF52980. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-37 AND PRO-180, FUNCTION, COFACTOR, INTERACTION WITH CHEK2, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF 306-GLY-ASP-307; 333-GLU-ARG-334 AND 338-ASP-ASP-339.
      Tissue: Cerebellum.
    2. "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], VARIANTS HIS-37 AND PRO-180.
      Tissue: Brain.
    3. "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 24-551, VARIANTS HIS-37 AND PRO-180.
    4. "Holliday junction resolution in human cells: two junction endonucleases with distinct substrate specificities."
      Constantinou A., Chen X.-B., McGowan C.H., West S.C.
      EMBO J. 21:5577-5585(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Identification and characterization of human MUS81-MMS4 structure-specific endonuclease."
      Oegruenc M., Sancar A.
      J. Biol. Chem. 278:21715-21720(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EME1.
    6. "Identification and characterization of the human mus81-eme1 endonuclease."
      Ciccia A., Constantinou A., West S.C.
      J. Biol. Chem. 278:25172-25178(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EME1.
    7. "Mus81 endonuclease localizes to nucleoli and to regions of DNA damage in human S-phase cells."
      Gao H., Chen X.-B., McGowan C.H.
      Mol. Biol. Cell 14:4826-4834(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    8. "RNA interference inhibition of Mus81 reduces mitotic recombination in human cells."
      Blais V., Gao H., Elwell C.A., Boddy M.N., Gaillard P.-H.L., Russell P., McGowan C.H.
      Mol. Biol. Cell 15:552-562(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH EME1, SUBCELLULAR LOCATION, MUTAGENESIS OF 338-ASP-ASP-339.
    9. Cited for: FUNCTION, INTERACTION WITH BLM, SUBCELLULAR LOCATION.
    10. "Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM."
      Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R., Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C.
      Mol. Cell 25:331-343(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EME1 AND EME2.
    11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links."
      Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X., Shen X., Li L., Legerski R.J.
      Oncogene 27:5045-5056(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCLRE1B.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: FUNCTION, INTERACTION WITH SLX4.
    15. "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
      Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
      Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLX4.
    16. "Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases."
      Fekairi S., Scaglione S., Chahwan C., Taylor E.R., Tissier A., Coulon S., Dong M.-Q., Ruse C., Yates J.R. III, Russell P., Fuchs R.P., McGowan C.H., Gaillard P.-H.L.
      Cell 138:78-89(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLX4.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiMUS81_HUMAN
    AccessioniPrimary (citable) accession number: Q96NY9
    Secondary accession number(s): Q9H7D9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 119 of the entry and version 3 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 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3