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O60337

- MARH6_HUMAN

UniProt

O60337 - MARH6_HUMAN

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Protein
E3 ubiquitin-protein ligase MARCH6
Gene
MARCH6, KIAA0597, RNF176, TEB4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-type
Add
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
Complete GO annotation...

GO - Biological processi

  1. protein K48-linked ubiquitination Source: UniProtKB
Complete GO annotation...

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; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9191Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei92 – 11221Helical; Reviewed prediction
Add
BLAST
Topological domaini113 – 14230Extracellular Reviewed prediction
Add
BLAST
Transmembranei143 – 16321Helical; Reviewed prediction
Add
BLAST
Topological domaini164 – 283120Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei284 – 30421Helical; Reviewed prediction
Add
BLAST
Topological domaini305 – 33632Extracellular Reviewed prediction
Add
BLAST
Transmembranei337 – 35721Helical; Reviewed prediction
Add
BLAST
Topological domaini358 – 37619Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei377 – 39721Helical; Reviewed prediction
Add
BLAST
Topological domaini398 – 42124Extracellular Reviewed prediction
Add
BLAST
Transmembranei422 – 44221Helical; Reviewed prediction
Add
BLAST
Topological domaini443 – 48038Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei481 – 50121Helical; Reviewed prediction
Add
BLAST
Topological domaini502 – 51918Extracellular Reviewed prediction
Add
BLAST
Transmembranei520 – 54021Helical; Reviewed prediction
Add
BLAST
Topological domaini541 – 63292Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei633 – 65321Helical; Reviewed prediction
Add
BLAST
Topological domaini654 – 67825Extracellular Reviewed prediction
Add
BLAST
Transmembranei679 – 69921Helical; Reviewed prediction
Add
BLAST
Topological domaini700 – 72122Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei722 – 74221Helical; Reviewed prediction
Add
BLAST
Topological domaini743 – 76422Extracellular Reviewed prediction
Add
BLAST
Transmembranei765 – 78521Helical; Reviewed prediction
Add
BLAST
Topological domaini786 – 81530Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei816 – 83621Helical; Reviewed prediction
Add
BLAST
Topological domaini837 – 84812Extracellular Reviewed prediction
Add
BLAST
Transmembranei849 – 86921Helical; Reviewed prediction
Add
BLAST
Topological domaini870 – 91041Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of endoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

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 MARCH6
PRO_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.

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. 6 interactions.
IntActiO60337. 1 interaction.
STRINGi9606.ENSP00000274140.

Structurei

3D structure databases

ProteinModelPortaliO60337.
SMRiO60337. Positions 4-59.

Family & Domainsi

Domaini

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

Sequence similaritiesi

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.

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.
VSP_047035Add
BLAST
Alternative sequencei64 – 11249IYSPD…PLTAC → S in isoform 2.
VSP_047036Add
BLAST

Sequence conflict

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

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...

Protein-protein interaction databases

BioGridi 115587. 6 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 106 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

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