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Q8N668

- COMD1_HUMAN

UniProt

Q8N668 - COMD1_HUMAN

Protein

COMM domain-containing protein 1

Gene

COMMD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes.7 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi101 – 1011CopperSequence Analysis
    Metal bindingi110 – 1101CopperSequence Analysis
    Metal bindingi134 – 1341CopperSequence Analysis

    GO - Molecular functioni

    1. copper ion binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. copper ion homeostasis Source: UniProtKB
    2. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    3. positive regulation of protein ubiquitination Source: UniProtKB
    4. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    COMM domain-containing protein 1
    Alternative name(s):
    Protein Murr1
    Gene namesi
    Name:COMMD1
    Synonyms:C2orf5, MURR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:23024. COMMD1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins.

    GO - Cellular componenti

    1. Cul2-RING ubiquitin ligase complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi110 – 1101M → A: Reduces copper-induced fluorescence change. 1 Publication
    Mutagenesisi134 – 1341H → A: Reduces copper-induced fluorescence change. 1 Publication

    Organism-specific databases

    PharmGKBiPA134891368.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 190189COMM domain-containing protein 1PRO_0000077384Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Post-translational modificationi

    Ubiquitinated; undergoes both 'Lys-63'- and 'Lys-48'-linked polyubiquitination. Ubiquitinated by XIAP, leading to its proteasomal degradation.3 Publications

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ8N668.
    PaxDbiQ8N668.
    PRIDEiQ8N668.

    PTM databases

    PhosphoSiteiQ8N668.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest expression in the liver, with lower expression in brain, lung, placenta, pancreas, small intestine, heart, skeletal muscle, kidney and placenta.3 Publications

    Gene expression databases

    ArrayExpressiQ8N668.
    BgeeiQ8N668.
    CleanExiHS_COMMD1.
    GenevestigatoriQ8N668.

    Organism-specific databases

    HPAiHPA034633.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts (via COMM domain) with COMMD2, COMMD3, COMMD4, COMMD5, COMMD6, COMMD7, COMMD8 and COMMD10 (via COMM domain). Identified in a complex with an E3 ubiquitin ligase complex composed of TCEB1/elongin C, CUL2, SOCS1 and RBX1. Interacts directly with SOCS1 and CUL2. Interacts directly the N-terminal region of ATP7B. Interacts with CCS, CDKN2A, RELA and NFKBIB. Identified in a complex with NF-kappa-B. Interacts with CLU.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1550112,EBI-1550112
    COMMD3Q9UBI13EBI-1550112,EBI-714979
    COMMD4Q9H0A82EBI-1550112,EBI-1550064
    COMMD6Q7Z4G12EBI-1550112,EBI-1550081
    CUL2Q136173EBI-1550112,EBI-456179
    NFKBIAP259633EBI-1550112,EBI-307386
    RELQ048643EBI-1550112,EBI-307352
    RELAQ042067EBI-1550112,EBI-73886
    RELBQ012012EBI-1550112,EBI-357837
    SCNN1DP511723EBI-1550112,EBI-2547114
    SOCS1O155243EBI-1550112,EBI-968198

    Protein-protein interaction databases

    BioGridi127317. 51 interactions.
    IntActiQ8N668. 25 interactions.
    MINTiMINT-4140741.
    STRINGi9606.ENSP00000308236.

    Structurei

    Secondary structure

    1
    190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi9 – 135
    Helixi15 – 184
    Beta strandi23 – 253
    Helixi32 – 398
    Beta strandi41 – 433
    Helixi48 – 525
    Turni53 – 553
    Helixi59 – 624
    Turni63 – 653
    Turni69 – 713
    Turni73 – 753
    Helixi76 – 794
    Beta strandi82 – 843
    Helixi88 – 947
    Turni95 – 1017
    Beta strandi102 – 1065

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H2MNMR-A1-108[»]
    ProteinModelPortaliQ8N668.
    SMRiQ8N668. Positions 1-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N668.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini118 – 18669COMMPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 COMM domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG46398.
    HOGENOMiHOG000236295.
    HOVERGENiHBG051067.
    InParanoidiQ8N668.
    OMAiLLAQSRW.
    PhylomeDBiQ8N668.
    TreeFamiTF332823.

    Family and domain databases

    InterProiIPR017920. COMM.
    IPR009886. HCaRG.
    [Graphical view]
    PfamiPF07258. HCaRG. 1 hit.
    [Graphical view]
    PROSITEiPS51269. COMM. 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: Q8N668-1) [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

    MAAGELEGGK PLSGLLNALA QDTFHGYPGI TEELLRSQLY PEVPPEEFRP    50
    FLAKMRGILK SIASADMDFN QLEAFLTAQT KKQGGITSDQ AAVISKFWKS 100
    HKTKIRESLM NQSRWNSGLR GLSWRVDGKS QSRHSAQIHT PVAIIELELG 150
    KYGQESEFLC LEFDEVKVNQ ILKTLSEVEE SISTLISQPN 190
    Length:190
    Mass (Da):21,178
    Last modified:October 1, 2002 - v1
    Checksum:i9C810AECA67011DC
    GO
    Isoform 2 (identifier: Q8N668-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-190: ESEFLCLEFDEVKVNQILKTLSEVEESISTLISQPN → VHCNQ

    Note: No experimental confirmation available.

    Show »
    Length:159
    Mass (Da):17,665
    Checksum:i3914BE73CBDD80F8
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei155 – 19036ESEFL…ISQPN → VHCNQ in isoform 2. 1 PublicationVSP_055532Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB178811 mRNA. Translation: BAD18972.1.
    AK294203 mRNA. Translation: BAG57515.1.
    AC018462 Genomic DNA. No translation available.
    AC107081 Genomic DNA. No translation available.
    AC116652 Genomic DNA. No translation available.
    BC009266 mRNA. Translation: AAH09266.2.
    BC022046 mRNA. Translation: AAH22046.1.
    CCDSiCCDS1869.1.
    RefSeqiNP_689729.1. NM_152516.2.
    UniGeneiHs.468702.

    Genome annotation databases

    EnsembliENST00000311832; ENSP00000308236; ENSG00000173163. [Q8N668-1]
    GeneIDi150684.
    KEGGihsa:150684.
    UCSCiuc002sbp.3. human.

    Polymorphism databases

    DMDMi51316026.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB178811 mRNA. Translation: BAD18972.1 .
    AK294203 mRNA. Translation: BAG57515.1 .
    AC018462 Genomic DNA. No translation available.
    AC107081 Genomic DNA. No translation available.
    AC116652 Genomic DNA. No translation available.
    BC009266 mRNA. Translation: AAH09266.2 .
    BC022046 mRNA. Translation: AAH22046.1 .
    CCDSi CCDS1869.1.
    RefSeqi NP_689729.1. NM_152516.2.
    UniGenei Hs.468702.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H2M NMR - A 1-108 [» ]
    ProteinModelPortali Q8N668.
    SMRi Q8N668. Positions 1-108.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127317. 51 interactions.
    IntActi Q8N668. 25 interactions.
    MINTi MINT-4140741.
    STRINGi 9606.ENSP00000308236.

    PTM databases

    PhosphoSitei Q8N668.

    Polymorphism databases

    DMDMi 51316026.

    Proteomic databases

    MaxQBi Q8N668.
    PaxDbi Q8N668.
    PRIDEi Q8N668.

    Protocols and materials databases

    DNASUi 150684.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311832 ; ENSP00000308236 ; ENSG00000173163 . [Q8N668-1 ]
    GeneIDi 150684.
    KEGGi hsa:150684.
    UCSCi uc002sbp.3. human.

    Organism-specific databases

    CTDi 150684.
    GeneCardsi GC02P062115.
    HGNCi HGNC:23024. COMMD1.
    HPAi HPA034633.
    MIMi 607238. gene.
    neXtProti NX_Q8N668.
    PharmGKBi PA134891368.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG46398.
    HOGENOMi HOG000236295.
    HOVERGENi HBG051067.
    InParanoidi Q8N668.
    OMAi LLAQSRW.
    PhylomeDBi Q8N668.
    TreeFami TF332823.

    Miscellaneous databases

    ChiTaRSi COMMD1. human.
    EvolutionaryTracei Q8N668.
    GeneWikii COMMD1.
    GenomeRNAii 150684.
    NextBioi 86500.
    PROi Q8N668.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N668.
    Bgeei Q8N668.
    CleanExi HS_COMMD1.
    Genevestigatori Q8N668.

    Family and domain databases

    InterProi IPR017920. COMM.
    IPR009886. HCaRG.
    [Graphical view ]
    Pfami PF07258. HCaRG. 1 hit.
    [Graphical view ]
    PROSITEi PS51269. COMM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Analysis of the human homologue of the canine copper toxicosis gene MURR1 in Wilson disease patients."
      Stuehler B., Reichert J., Stremmel W., Schaefer M.
      J. Mol. Med. 82:629-634(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Comparative analyses of gene imprinting and CpG island methylation around mouse Murr1 and human syntenic region identify the 5'-portion of U2af1-rs1 CpG island as an imprinting control region."
      Zhang Z., Yatsuki H., Wang Y., Joh K., Nabetani A., Hatada I., Soejima H., Iwasaka T., Mukai T.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    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] (ISOFORM 2).
      Tissue: Amygdala.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Ovary and Skin.
    7. "Identification of a new copper metabolism gene by positional cloning in a purebred dog population."
      van De Sluis B.A.J., Rothuizen J., Pearson P.L., van Oost B.A., Wijmenga C.
      Hum. Mol. Genet. 11:165-173(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein."
      Tao T.Y., Liu F., Klomp L., Wijmenga C., Gitlin J.D.
      J. Biol. Chem. 278:41593-41596(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATP7B.
    9. Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH XIAP.
    10. Cited for: FUNCTION, INTERACTION WITH RELA; COMMD2; COMMD3; COMMD4; COMMD5; COMMD6; COMMD7; COMMD8 AND COMMD10, IDENTIFICATION IN A COMPLEX WITH NF-KAPPA-B, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Characterization of COMMD protein-protein interactions in NF-kappaB signalling."
      de Bie P., van de Sluis B., Burstein E., Duran K.J., Berger R., Duckett C.S., Wijmenga C., Klomp L.W.
      Biochem. J. 398:63-71(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH COMMD6 AND NFKBIB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    12. "Characterization and copper binding properties of human COMMD1 (MURR1)."
      Narindrasorasak S., Kulkarni P., Deschamps P., She Y.M., Sarkar B.
      Biochemistry 46:3116-3128(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF MET-110 AND HIS-134, COPPER-BINDING.
    13. "COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase."
      Maine G.N., Mao X., Komarck C.M., Burstein E.
      EMBO J. 26:436-447(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, INTERACTION WITH SOCS1 AND CUL2, IDENTIFICATION IN AN E3 UBIQUITIN LIGASE COMPLEX COMPOSED OF TCEB1/ELONGIN C; CUL2; SOCS1 AND RBX1.
    14. "Tumor suppressor ARF promotes non-classic proteasome-independent polyubiquitination of COMMD1."
      Huang Y., Wu M., Li H.Y.
      J. Biol. Chem. 283:11453-11460(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH CDKN2A.
    15. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Nucleolar targeting of RelA(p65) is regulated by COMMD1-dependent ubiquitination."
      Thoms H.C., Loveridge C.J., Simpson J., Clipson A., Reinhardt K., Dunlop M.G., Stark L.A.
      Cancer Res. 70:139-149(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1."
      Vonk W.I., Wijmenga C., Berger R., van de Sluis B., Klomp L.W.
      J. Biol. Chem. 285:28991-29000(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCS.
    18. "Clusterin facilitates COMMD1 and I-kappaB degradation to enhance NF-kappaB activity in prostate cancer cells."
      Zoubeidi A., Ettinger S., Beraldi E., Hadaschik B., Zardan A., Klomp L.W., Nelson C.C., Rennie P.S., Gleave M.E.
      Mol. Cancer Res. 8:119-130(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, PROTEASOMAL DEGRADATION, INTERACTION WITH CLU.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Solution structure of the COMMD1 N-terminal domain."
      Sommerhalter M., Zhang Y., Rosenzweig A.C.
      J. Mol. Biol. 365:715-721(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-108.

    Entry informationi

    Entry nameiCOMD1_HUMAN
    AccessioniPrimary (citable) accession number: Q8N668
    Secondary accession number(s): B4DFQ4, Q96GS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 95 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 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    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