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Q9Y6X9

- MORC2_HUMAN

UniProt

Q9Y6X9 - MORC2_HUMAN

Protein

MORC family CW-type zinc finger protein 2

Gene

MORC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    May act as a transcriptional repressor. Down-regulates CA9 expression.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri490 – 54455CW-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. zinc ion binding Source: InterPro

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MORC family CW-type zinc finger protein 2
    Alternative name(s):
    Zinc finger CW-type coiled-coil domain protein 1
    Gene namesi
    Name:MORC2
    Synonyms:KIAA0852, ZCWCC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:23573. MORC2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytosol 1 Publication
    Note: Mainly located in the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB-SubCell
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134986990.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 10321031MORC family CW-type zinc finger protein 2PRO_0000096537Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei615 – 6151Phosphoserine3 Publications
    Modified residuei696 – 6961Phosphoserine1 Publication
    Modified residuei705 – 7051Phosphoserine1 Publication
    Modified residuei725 – 7251Phosphoserine1 Publication
    Modified residuei730 – 7301Phosphoserine1 Publication
    Modified residuei733 – 7331Phosphothreonine1 Publication
    Modified residuei739 – 7391Phosphoserine2 Publications
    Modified residuei743 – 7431Phosphoserine3 Publications
    Modified residuei777 – 7771Phosphoserine3 Publications
    Modified residuei779 – 7791Phosphoserine3 Publications
    Modified residuei856 – 8561PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6X9.
    PaxDbiQ9Y6X9.
    PRIDEiQ9Y6X9.

    PTM databases

    PhosphoSiteiQ9Y6X9.

    Expressioni

    Tissue specificityi

    Highly expressed in smooth muscle, pancreas and testis.

    Gene expression databases

    ArrayExpressiQ9Y6X9.
    BgeeiQ9Y6X9.
    CleanExiHS_MORC2.
    GenevestigatoriQ9Y6X9.

    Organism-specific databases

    HPAiHPA000436.

    Interactioni

    Subunit structurei

    Interacts with HDAC4.1 Publication

    Protein-protein interaction databases

    BioGridi116547. 6 interactions.
    MINTiMINT-4995722.
    STRINGi9606.ENSP00000215862.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y6X9.
    SMRiQ9Y6X9. Positions 27-86, 494-542.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili282 – 36281Sequence AnalysisAdd
    BLAST
    Coiled coili547 – 58438Sequence AnalysisAdd
    BLAST
    Coiled coili741 – 76121Sequence AnalysisAdd
    BLAST
    Coiled coili966 – 101651Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CW-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri490 – 54455CW-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG308593.
    HOGENOMiHOG000060084.
    HOVERGENiHBG056877.
    InParanoidiQ9Y6X9.
    OMAiRNCLRYF.
    OrthoDBiEOG71ZP0X.
    PhylomeDBiQ9Y6X9.
    TreeFamiTF329118.

    Family and domain databases

    Gene3Di3.30.565.10. 2 hits.
    InterProiIPR003594. HATPase_ATP-bd.
    IPR011124. Znf_CW.
    [Graphical view]
    PfamiPF07496. zf-CW. 1 hit.
    [Graphical view]
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF55874. SSF55874. 2 hits.
    PROSITEiPS51050. ZF_CW. 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: Q9Y6X9-1) [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

    MAFTNYSSLN RAQLTFEYLH TNSTTHEFLF GALAELVDNA RDADATRIDI     50
    YAERREDLRG GFMLCFLDDG AGMDPSDAAS VIQFGKSAKR TPESTQIGQY 100
    GNGLKSGSMR IGKDFILFTK KEDTMTCLFL SRTFHEEEGI DEVIVPLPTW 150
    NARTREPVTD NVEKFAIETE LIYKYSPFRT EEEVMTQFMK IPGDSGTLVI 200
    IFNLKLMDNG EPELDIISNP RDIQMAETSP EGTKPERRSF RAYAAVLYID 250
    PRMRIFIHGH KVQTKRLSCC LYKPRMYKYT SSRFKTRAEQ EVKKAEHVAR 300
    IAEEKAREAE SKARTLEVRL GGDLTRDSRV MLRQVQNRAI TLRREADVKK 350
    RIKEAKQRAL KEPKELNFVF GVNIEHRDLD GMFIYNCSRL IKMYEKVGPQ 400
    LEGGMACGGV VGVVDVPYLV LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY 450
    WKDIAIAQRG IIKFWDEFGY LSANWNQPPS SELRYKRRRA MEIPTTIQCD 500
    LCLKWRTLPF QLSSVEKDYP DTWVCSMNPD PEQDRCEASE QKQKVPLGTF 550
    RKDMKTQEEK QKQLTEKIRQ QQEKLEALQK TTPIRSQADL KKLPLEVTTR 600
    PSTEEPVRRP QRPRSPPLPA VIRNAPSRPP SLPTPRPASQ PRKAPVISST 650
    PKLPALAARE EASTSRLLQP PEAPRKPANT LVKTASRPAP LVQQLSPSLL 700
    PNSKSPREVP SPKVIKTPVV KKTESPIKLS PATPSRKRSV AVSDEEEVEE 750
    EAERRKERCK RGRFVVKEEK KDSNELSDSA GEEDSADLKR AQKDKGLHVE 800
    VRVNREWYTG RVTAVEVGKH VVRWKVKFDY VPTDTTPRDR WVEKGSEDVR 850
    LMKPPSPEHQ SLDTQQEGGE EEVGPVAQQA IAVAEPSTSE CLRIEPDTTA 900
    LSTNHETIDL LVQILRNCLR YFLPPSFPIS KKQLSAMNSD ELISFPLKEY 950
    FKQYEVGLQN LCNSYQSRAD SRAKASEESL RTSERKLRET EEKLQKLRTN 1000
    IVALLQKVQE DIDINTDDEL DAYIEDLITK GD 1032

    Note: No experimental confirmation available.

    Length:1,032
    Mass (Da):117,823
    Last modified:September 5, 2006 - v2
    Checksum:i7BEFA46E4150ABF5
    GO
    Isoform 2 (identifier: Q9Y6X9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:970
    Mass (Da):110,724
    Checksum:i459161807B8B53F6
    GO

    Sequence cautioni

    The sequence BAA74875.2 differs from that shown. Reason: Intron retention.
    The sequence AAC12954.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6262Missing in isoform 2. 2 PublicationsVSP_041759Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020659 mRNA. Translation: BAA74875.2. Sequence problems.
    CR456469 mRNA. Translation: CAG30355.1.
    AC004542 Genomic DNA. Translation: AAC12954.1. Sequence problems.
    AL133637 mRNA. Translation: CAB63760.1.
    CH471095 Genomic DNA. Translation: EAW59921.1.
    BC019257 mRNA. Translation: AAH19257.3.
    BC136782 mRNA. Translation: AAI36783.1.
    CCDSiCCDS33636.1. [Q9Y6X9-2]
    PIRiT02436.
    T43455.
    RefSeqiNP_055756.1. NM_014941.1. [Q9Y6X9-2]
    XP_005261448.1. XM_005261391.1. [Q9Y6X9-1]
    UniGeneiHs.555918.

    Genome annotation databases

    EnsembliENST00000215862; ENSP00000215862; ENSG00000133422. [Q9Y6X9-2]
    ENST00000397641; ENSP00000380763; ENSG00000133422. [Q9Y6X9-1]
    GeneIDi22880.
    KEGGihsa:22880.
    UCSCiuc003aje.1. human. [Q9Y6X9-1]

    Polymorphism databases

    DMDMi114152840.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020659 mRNA. Translation: BAA74875.2 . Sequence problems.
    CR456469 mRNA. Translation: CAG30355.1 .
    AC004542 Genomic DNA. Translation: AAC12954.1 . Sequence problems.
    AL133637 mRNA. Translation: CAB63760.1 .
    CH471095 Genomic DNA. Translation: EAW59921.1 .
    BC019257 mRNA. Translation: AAH19257.3 .
    BC136782 mRNA. Translation: AAI36783.1 .
    CCDSi CCDS33636.1. [Q9Y6X9-2 ]
    PIRi T02436.
    T43455.
    RefSeqi NP_055756.1. NM_014941.1. [Q9Y6X9-2 ]
    XP_005261448.1. XM_005261391.1. [Q9Y6X9-1 ]
    UniGenei Hs.555918.

    3D structure databases

    ProteinModelPortali Q9Y6X9.
    SMRi Q9Y6X9. Positions 27-86, 494-542.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116547. 6 interactions.
    MINTi MINT-4995722.
    STRINGi 9606.ENSP00000215862.

    PTM databases

    PhosphoSitei Q9Y6X9.

    Polymorphism databases

    DMDMi 114152840.

    Proteomic databases

    MaxQBi Q9Y6X9.
    PaxDbi Q9Y6X9.
    PRIDEi Q9Y6X9.

    Protocols and materials databases

    DNASUi 22880.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215862 ; ENSP00000215862 ; ENSG00000133422 . [Q9Y6X9-2 ]
    ENST00000397641 ; ENSP00000380763 ; ENSG00000133422 . [Q9Y6X9-1 ]
    GeneIDi 22880.
    KEGGi hsa:22880.
    UCSCi uc003aje.1. human. [Q9Y6X9-1 ]

    Organism-specific databases

    CTDi 22880.
    GeneCardsi GC22M031322.
    HGNCi HGNC:23573. MORC2.
    HPAi HPA000436.
    neXtProti NX_Q9Y6X9.
    PharmGKBi PA134986990.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG308593.
    HOGENOMi HOG000060084.
    HOVERGENi HBG056877.
    InParanoidi Q9Y6X9.
    OMAi RNCLRYF.
    OrthoDBi EOG71ZP0X.
    PhylomeDBi Q9Y6X9.
    TreeFami TF329118.

    Miscellaneous databases

    GeneWikii MORC2.
    GenomeRNAii 22880.
    NextBioi 43453.
    PROi Q9Y6X9.

    Gene expression databases

    ArrayExpressi Q9Y6X9.
    Bgeei Q9Y6X9.
    CleanExi HS_MORC2.
    Genevestigatori Q9Y6X9.

    Family and domain databases

    Gene3Di 3.30.565.10. 2 hits.
    InterProi IPR003594. HATPase_ATP-bd.
    IPR011124. Znf_CW.
    [Graphical view ]
    Pfami PF07496. zf-CW. 1 hit.
    [Graphical view ]
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55874. SSF55874. 2 hits.
    PROSITEi PS51050. ZF_CW. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [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).
      Tissue: Cerebellum and Neuroblastoma.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 712-1032.
      Tissue: Testis.
    7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-705; SER-725; SER-730; THR-733; SER-777 AND SER-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739 AND SER-743, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Identification and expression analysis of a novel CW-type zinc finger protein MORC2 in cancer cells."
      Wang G.L., Wang C.Y., Cai X.Z., Chen W., Wang X.H., Li F.
      Anat. Rec. 293:1002-1009(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "Involvement of histone deacetylation in MORC2-mediated down-regulation of carbonic anhydrase IX."
      Shao Y., Li Y., Zhang J., Liu D., Liu F., Zhao Y., Shen T., Li F.
      Nucleic Acids Res. 38:2813-2824(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HDAC4.
    13. "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-615; SER-743; SER-777 AND SER-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-615; SER-739; SER-743; SER-777 AND SER-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMORC2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6X9
    Secondary accession number(s): B2RNB1, Q9UF28, Q9Y6V2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 26, 2002
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 123 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 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3