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O60337

- MARH6_HUMAN

UniProt

O60337 - MARH6_HUMAN

Protein

E3 ubiquitin-protein ligase MARCH6

Gene

MARCH6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that promotes ubiquitination of DIO2, leading to its degradation. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May cooperate with UBE2G1.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 6262RING-CH-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. ubiquitin conjugating enzyme binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. protein K48-linked ubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase MARCH6 (EC:6.3.2.-)
    Alternative name(s):
    Doa10 homolog
    Membrane-associated RING finger protein 6
    Membrane-associated RING-CH protein VI
    Short name:
    MARCH-VI
    Protein TEB-4
    RING finger protein 176
    Gene namesi
    Name:MARCH6
    Synonyms:KIAA0597, RNF176, TEB4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:30550. MARCH6.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. integral component of endoplasmic reticulum membrane Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91C → A: Abolishes auto-ubiquitination. 1 Publication

    Organism-specific databases

    PharmGKBiPA134869368.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 910910E3 ubiquitin-protein ligase MARCH6PRO_0000274298Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Post-translational modificationi

    Auto-ubiquitinated, which results in proteasomal degradation.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiO60337.
    PaxDbiO60337.
    PRIDEiO60337.

    PTM databases

    PhosphoSiteiO60337.

    Expressioni

    Tissue specificityi

    Present in brain (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO60337.
    BgeeiO60337.
    CleanExiHS_MARCH6.
    GenevestigatoriO60337.

    Interactioni

    Subunit structurei

    Interacts with DIO2.1 Publication

    Protein-protein interaction databases

    BioGridi115587. 8 interactions.
    IntActiO60337. 1 interaction.
    STRINGi9606.ENSP00000274140.

    Structurei

    3D structure databases

    ProteinModelPortaliO60337.
    SMRiO60337. Positions 4-59.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 9191CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini113 – 14230ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini164 – 283120CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini305 – 33632ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini358 – 37619CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini398 – 42124ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini443 – 48038CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini502 – 51918ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini541 – 63292CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini654 – 67825ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini700 – 72122CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini743 – 76422ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini786 – 81530CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini837 – 84812ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini870 – 91041CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei92 – 11221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei143 – 16321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei284 – 30421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei337 – 35721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei377 – 39721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei422 – 44221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei481 – 50121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei520 – 54021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei633 – 65321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei679 – 69921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei722 – 74221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei765 – 78521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei816 – 83621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei849 – 86921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domaini

    The RING-CH-type zinc finger domain is required for E3 ligase activity.

    Sequence similaritiesi

    Contains 1 RING-CH-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 6262RING-CH-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5183.
    HOGENOMiHOG000286005.
    HOVERGENiHBG080753.
    InParanoidiO60337.
    KOiK10661.
    OMAiDNLLADC.
    OrthoDBiEOG7J4464.
    PhylomeDBiO60337.
    TreeFamiTF105777.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR011016. Znf_RING-CH.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF12906. RINGv. 1 hit.
    [Graphical view]
    SMARTiSM00744. RINGv. 1 hit.
    [Graphical view]
    PROSITEiPS51292. ZF_RING_CH. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60337-4) [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

    MDTAEEDICR VCRSEGTPEK PLYHPCVCTG SIKFIHQECL VQWLKHSRKE    50
    YCELCKHRFA FTPIYSPDMP SRLPIQDIFA GLVTSIGTAI RYWFHYTLVA 100
    FAWLGVVPLT ACRIYKCLFT GSVSSLLTLP LDMLSTENLL ADCLQGCFVV 150
    TCTLCAFISL VWLREQIVHG GAPIWLEHAA PPFNAAGHHQ NEAPAGGNGA 200
    ENVAADQPAN PPAENAVVGE NPDAQDDQAE EEEEDNEEED DAGVEDAADA 250
    NNGAQDDMNW NALEWDRAAE ELTWERMLGL DGSLVFLEHV FWVVSLNTLF 300
    ILVFAFCPYH IGHFSLVGLG FEEHVQASHF EGLITTIVGY ILLAITLIIC 350
    HGLATLVKFH RSRRLLGVCY IVVKVSLLVV VEIGVFPLIC GWWLDICSLE 400
    MFDATLKDRE LSFQSAPGTT MFLHWLVGMV YVFYFASFIL LLREVLRPGV 450
    LWFLRNLNDP DFNPVQEMIH LPIYRHLRRF ILSVIVFGSI VLLMLWLPIR 500
    IIKSVLPNFL PYNVMLYSDA PVSELSLELL LLQVVLPALL EQGHTRQWLK 550
    GLVRAWTVTA GYLLDLHSYL LGDQEENENS ANQQVNNNQH ARNNNAIPVV 600
    GEGLHAAHQA ILQQGGPVGF QPYRRPLNFP LRIFLLIVFM CITLLIASLI 650
    CLTLPVFAGR WLMSFWTGTA KIHELYTAAC GLYVCWLTIR AVTVMVAWMP 700
    QGRRVIFQKV KEWSLMIMKT LIVAVLLAGV VPLLLGLLFE LVIVAPLRVP 750
    LDQTPLFYPW QDWALGVLHA KIIAAITLMG PQWWLKTVIE QVYANGIRNI 800
    DLHYIVRKLA APVISVLLLS LCVPYVIASG VVPLLGVTAE MQNLVHRRIY 850
    PFLLMVVVLM AILSFQVRQF KRLYEHIKND KYLVGQRLVN YERKSGKQGS 900
    SPPPPQSSQE 910
    Length:910
    Mass (Da):102,545
    Last modified:February 6, 2007 - v2
    Checksum:iC7A96FEA45B5CA8D
    GO
    Isoform 2 (identifier: O60337-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         64-112: IYSPDMPSRLPIQDIFAGLVTSIGTAIRYWFHYTLVAFAWLGVVPLTAC → S

    Show »
    Length:862
    Mass (Da):97,178
    Checksum:iE05382BAE7E49AF3
    GO
    Isoform 3 (identifier: O60337-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         7-112: DICRVCRSEG...WLGVVPLTAC → G

    Show »
    Length:805
    Mass (Da):90,413
    Checksum:i1DC90D272E92EDD9
    GO

    Sequence cautioni

    The sequence AAB66840.1 differs from that shown. Reason: Frameshift at positions 381, 382, 383, 385, 391, 396 and 418.
    The sequence AAB66840.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA25523.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti380 – 3801V → VG in AAB66840. 1 PublicationCurated
    Sequence conflicti384 – 3841G → GS in AAB66840. 1 PublicationCurated
    Sequence conflicti390 – 3901C → WW in AAB66840. 1 PublicationCurated
    Sequence conflicti395 – 3951D → G in AAB66840. 1 PublicationCurated
    Sequence conflicti399 – 3991L → LG in AAB66840. 1 PublicationCurated
    Sequence conflicti546 – 5461R → K in AAB66840. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti622 – 6221P → L.1 Publication
    Corresponds to variant rs1062914 [ dbSNP | Ensembl ].
    VAR_030251

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei7 – 112106DICRV…PLTAC → G in isoform 3. 1 PublicationVSP_047035Add
    BLAST
    Alternative sequencei64 – 11249IYSPD…PLTAC → S in isoform 2. 1 PublicationVSP_047036Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011169 mRNA. Translation: BAA25523.1. Different initiation.
    AK296585 mRNA. Translation: BAG59204.1.
    AK300034 mRNA. Translation: BAG61845.1.
    AC012640 Genomic DNA. No translation available.
    AC092336 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08065.1.
    CH471102 Genomic DNA. Translation: EAX08066.1.
    BC046148 mRNA. Translation: AAH46148.1.
    BC136461 mRNA. Translation: AAI36462.1.
    BC136462 mRNA. Translation: AAI36463.1.
    BC142679 mRNA. Translation: AAI42680.1.
    BC142694 mRNA. Translation: AAI42695.1.
    AF009301 mRNA. Translation: AAB66840.1. Sequence problems.
    CCDSiCCDS34135.1. [O60337-4]
    CCDS59487.1. [O60337-5]
    CCDS59488.1. [O60337-6]
    PIRiT00268.
    RefSeqiNP_001257589.1. NM_001270660.1. [O60337-5]
    NP_001257590.1. NM_001270661.1. [O60337-6]
    NP_005876.2. NM_005885.3. [O60337-4]
    UniGeneiHs.432862.

    Genome annotation databases

    EnsembliENST00000274140; ENSP00000274140; ENSG00000145495. [O60337-4]
    ENST00000449913; ENSP00000414643; ENSG00000145495. [O60337-5]
    ENST00000503788; ENSP00000425930; ENSG00000145495. [O60337-6]
    GeneIDi10299.
    KEGGihsa:10299.
    UCSCiuc003jet.2. human. [O60337-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011169 mRNA. Translation: BAA25523.1 . Different initiation.
    AK296585 mRNA. Translation: BAG59204.1 .
    AK300034 mRNA. Translation: BAG61845.1 .
    AC012640 Genomic DNA. No translation available.
    AC092336 Genomic DNA. No translation available.
    CH471102 Genomic DNA. Translation: EAX08065.1 .
    CH471102 Genomic DNA. Translation: EAX08066.1 .
    BC046148 mRNA. Translation: AAH46148.1 .
    BC136461 mRNA. Translation: AAI36462.1 .
    BC136462 mRNA. Translation: AAI36463.1 .
    BC142679 mRNA. Translation: AAI42680.1 .
    BC142694 mRNA. Translation: AAI42695.1 .
    AF009301 mRNA. Translation: AAB66840.1 . Sequence problems.
    CCDSi CCDS34135.1. [O60337-4 ]
    CCDS59487.1. [O60337-5 ]
    CCDS59488.1. [O60337-6 ]
    PIRi T00268.
    RefSeqi NP_001257589.1. NM_001270660.1. [O60337-5 ]
    NP_001257590.1. NM_001270661.1. [O60337-6 ]
    NP_005876.2. NM_005885.3. [O60337-4 ]
    UniGenei Hs.432862.

    3D structure databases

    ProteinModelPortali O60337.
    SMRi O60337. Positions 4-59.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115587. 8 interactions.
    IntActi O60337. 1 interaction.
    STRINGi 9606.ENSP00000274140.

    PTM databases

    PhosphoSitei O60337.

    Proteomic databases

    MaxQBi O60337.
    PaxDbi O60337.
    PRIDEi O60337.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274140 ; ENSP00000274140 ; ENSG00000145495 . [O60337-4 ]
    ENST00000449913 ; ENSP00000414643 ; ENSG00000145495 . [O60337-5 ]
    ENST00000503788 ; ENSP00000425930 ; ENSG00000145495 . [O60337-6 ]
    GeneIDi 10299.
    KEGGi hsa:10299.
    UCSCi uc003jet.2. human. [O60337-4 ]

    Organism-specific databases

    CTDi 10299.
    GeneCardsi GC05P010353.
    HGNCi HGNC:30550. MARCH6.
    MIMi 613297. gene.
    neXtProti NX_O60337.
    PharmGKBi PA134869368.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5183.
    HOGENOMi HOG000286005.
    HOVERGENi HBG080753.
    InParanoidi O60337.
    KOi K10661.
    OMAi DNLLADC.
    OrthoDBi EOG7J4464.
    PhylomeDBi O60337.
    TreeFami TF105777.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi MARCH6. human.
    GeneWikii MARCH6.
    GenomeRNAii 10299.
    NextBioi 35472800.
    PROi O60337.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60337.
    Bgeei O60337.
    CleanExi HS_MARCH6.
    Genevestigatori O60337.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR011016. Znf_RING-CH.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF12906. RINGv. 1 hit.
    [Graphical view ]
    SMARTi SM00744. RINGv. 1 hit.
    [Graphical view ]
    PROSITEi PS51292. ZF_RING_CH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORMS 2 AND 3).
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [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 1).
      Tissue: Pancreas.
    6. "High resolution physical and transcription maps of the Cri-du-chat critical region."
      Simmons A.D., Lovett M.L.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-910 (ISOFORM 1), VARIANT LEU-622.
    7. "A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation."
      Swanson R., Locher M., Hochstrasser M.
      Genes Dev. 15:2660-2674(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    8. "TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum."
      Hassink G., Kikkert M., van Voorden S., Lee S.-J., Spaapen R., van Laar T., Coleman C.S., Bartee E., Frueh K., Chau V., Wiertz E.
      Biochem. J. 388:647-655(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-9.
    9. "Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)."
      Kreft S.G., Wang L., Hochstrasser M.
      J. Biol. Chem. 281:4646-4653(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    10. "The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase."
      Zavacki A.M., Arrojo E Drigo R., Freitas B.C., Chung M., Harney J.W., Egri P., Wittmann G., Fekete C., Gereben B., Bianco A.C.
      Mol. Cell. Biol. 29:5339-5347(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE FOR DIO2, INTERACTION WITH DIO2.
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMARH6_HUMAN
    AccessioniPrimary (citable) accession number: O60337
    Secondary accession number(s): A5PKZ4
    , B4DKJ2, B4DT33, D3DTC8, O14670, Q86X77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2007
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 107 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 5
      Human chromosome 5: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3