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Protein

E3 ubiquitin-protein ligase MARCH6

Gene

March6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Pathwayi

Regions

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

GO - Molecular functioni

GO - Biological processi

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):
Membrane-associated RING finger protein 6
Membrane-associated RING-CH protein VI
Short name:
MARCH-VI
Gene namesi
Name:March6
Synonyms:Kiaa0597
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2442773. March6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9191CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei92 – 11221HelicalSequence AnalysisAdd
BLAST
Topological domaini113 – 14230ExtracellularSequence AnalysisAdd
BLAST
Transmembranei143 – 16321HelicalSequence AnalysisAdd
BLAST
Topological domaini164 – 283120CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei284 – 30421HelicalSequence AnalysisAdd
BLAST
Topological domaini305 – 33632ExtracellularSequence AnalysisAdd
BLAST
Transmembranei337 – 35721HelicalSequence AnalysisAdd
BLAST
Topological domaini358 – 37619CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei377 – 39721HelicalSequence AnalysisAdd
BLAST
Topological domaini398 – 42124ExtracellularSequence AnalysisAdd
BLAST
Transmembranei422 – 44221HelicalSequence AnalysisAdd
BLAST
Topological domaini443 – 48038CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei481 – 50121HelicalSequence AnalysisAdd
BLAST
Topological domaini502 – 51918ExtracellularSequence AnalysisAdd
BLAST
Transmembranei520 – 54021HelicalSequence AnalysisAdd
BLAST
Topological domaini541 – 63191CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei632 – 65221HelicalSequence AnalysisAdd
BLAST
Topological domaini653 – 67725ExtracellularSequence AnalysisAdd
BLAST
Transmembranei678 – 69821HelicalSequence AnalysisAdd
BLAST
Topological domaini699 – 72022CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei721 – 74121HelicalSequence AnalysisAdd
BLAST
Topological domaini742 – 76322ExtracellularSequence AnalysisAdd
BLAST
Transmembranei764 – 78421HelicalSequence AnalysisAdd
BLAST
Topological domaini785 – 81430CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei815 – 83521HelicalSequence AnalysisAdd
BLAST
Topological domaini836 – 84712ExtracellularSequence AnalysisAdd
BLAST
Transmembranei848 – 86821HelicalSequence AnalysisAdd
BLAST
Topological domaini869 – 90941CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 909909E3 ubiquitin-protein ligase MARCH6PRO_0000274299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Post-translational modificationi

Auto-ubiquitinated, which results in proteasomal degradation.By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ6ZQ89.
PaxDbiQ6ZQ89.
PRIDEiQ6ZQ89.

PTM databases

PhosphoSiteiQ6ZQ89.

Expressioni

Gene expression databases

BgeeiQ6ZQ89.
CleanExiMM_MARCH6.
ExpressionAtlasiQ6ZQ89. baseline and differential.
GenevestigatoriQ6ZQ89.

Interactioni

Subunit structurei

Interacts with DIO2.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6ZQ89.
SMRiQ6ZQ89. Positions 4-59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the DOA10/MARCH6 family.Curated
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.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000286005.
HOVERGENiHBG080753.
InParanoidiQ6ZQ89.
KOiK10661.
OMAiDNLLADC.
OrthoDBiEOG7J4464.
PhylomeDBiQ6ZQ89.
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. AlignAdd to basket

Isoform 1 (identifier: Q6ZQ89-1) [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

        10         20         30         40         50
MDTAEEDICR VCRSEGTPEK PLYHPCVCTG SIKFIHQECL VQWLKHSRKE
60 70 80 90 100
YCELCKHRFA FTPIYSPDMP SRLPIQDIFA GLVTSIGTAI RYWFHYTLVA
110 120 130 140 150
FAWLGVVPLT ACRIYKCLFT GSVSSLLTLP LDMLSTENLL ADCLQGCFVV
160 170 180 190 200
TCTLCAFISL VWLREQIVHG GAPIWLEHAA PPFNAAGHHQ NEAPVGGNGA
210 220 230 240 250
ENPAADQPAN PAGENAVLGE NPDAQDGQAE EEEEDNEEED DAGVEDAADA
260 270 280 290 300
NNGAQDDMNW NALEWDRAAE ELTWERMLGL DGSLVFLEHV FWVVSLNTLF
310 320 330 340 350
ILVFAFCPYH IGHFSLVGLG FEEHVQASHF EGLITTIVGY ILLAITLIIC
360 370 380 390 400
HALATLVKFH RSRRLLGVCY IVVKVSLLVV VEIGVFPLIC GWWLDICSLE
410 420 430 440 450
MFDATLKDRE LSFQSAPGTT MFLHWLVGMV YVFYFASFIL LLREVLRPGV
460 470 480 490 500
LWFLRNLNDP DFNPVQEMIH LPIYRHLRRF ILSVIVFGSI VLLMLWLPIR
510 520 530 540 550
IIKSLLPNFL PYNVMLYSDA PVSELSLELL LLQVVLPALL EQGHTRQWLK
560 570 580 590 600
GLVRAWTVTA GYLLDLHSYL LGDQEENENS ANQQVNNNQP ARNNNAVPAG
610 620 630 640 650
EGLHAAHQAI LQQGGPVGFQ PYRRPLNFPL RIFLLIVFMC ITLLIASLIC
660 670 680 690 700
LTLPVFAGRW LMSFWTGTAK IHELYTAACG LYVCWLTIRA VTVLVAWMPQ
710 720 730 740 750
GRRVIFQKVK EWSLMIMKTL IVAVLLAGVV PLLLGLLFEL VIVAPLRVPL
760 770 780 790 800
DQTPLFYPWQ DWALGVLHAK IIAAITLMGP QWWLKTVIEQ VYANGIRNID
810 820 830 840 850
LHYIIRKLAA PVISVLLLSL CVPYVIASGA VPLLGVTAEM QNLVHRRIYP
860 870 880 890 900
FLLMVVVLMG ILSFQVRQFK RLYEHIKNDK YLVGQRLVNY ERKSGKQGPS

TPPPVSSQE
Length:909
Mass (Da):102,273
Last modified:February 6, 2007 - v2
Checksum:iDC46CB2A34B6F749
GO
Isoform 2 (identifier: Q6ZQ89-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     625-821: PLNFPLRIFL...VISVLLLSLC → LPRWAPSHWQ...SWGFIVHNIC
     822-909: Missing.

Note: No experimental confirmation available.

Show »
Length:661
Mass (Da):74,274
Checksum:iC73C562C44B0DAF4
GO
Isoform 3 (identifier: Q6ZQ89-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     683-708: Missing.

Note: No experimental confirmation available.

Show »
Length:883
Mass (Da):99,219
Checksum:i5DB1C80612C77827
GO

Sequence cautioni

The sequence AAH37454.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti476 – 4761H → N in BAC31427 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei625 – 821197PLNFP…LLSLC → LPRWAPSHWQGLLSCVLCPV AFRKMMSSWGFIVHNIC in isoform 2. 1 PublicationVSP_022702Add
BLAST
Alternative sequencei683 – 70826Missing in isoform 3. 1 PublicationVSP_022704Add
BLAST
Alternative sequencei822 – 90988Missing in isoform 2. 1 PublicationVSP_022703Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042980 mRNA. Translation: BAC31427.1.
AK089827 mRNA. Translation: BAC40971.1.
AK129169 Transcribed RNA. Translation: BAC97979.1.
BC037454 mRNA. Translation: AAH37454.1. Different initiation.
BC048816 mRNA. Translation: AAH48816.1.
BC059190 mRNA. Translation: AAH59190.2.
CCDSiCCDS37054.1. [Q6ZQ89-1]
RefSeqiNP_766194.2. NM_172606.2. [Q6ZQ89-1]
UniGeneiMm.272185.

Genome annotation databases

EnsembliENSMUST00000090227; ENSMUSP00000087694; ENSMUSG00000039100. [Q6ZQ89-1]
GeneIDi223455.
KEGGimmu:223455.
UCSCiuc007vkh.1. mouse. [Q6ZQ89-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK042980 mRNA. Translation: BAC31427.1.
AK089827 mRNA. Translation: BAC40971.1.
AK129169 Transcribed RNA. Translation: BAC97979.1.
BC037454 mRNA. Translation: AAH37454.1. Different initiation.
BC048816 mRNA. Translation: AAH48816.1.
BC059190 mRNA. Translation: AAH59190.2.
CCDSiCCDS37054.1. [Q6ZQ89-1]
RefSeqiNP_766194.2. NM_172606.2. [Q6ZQ89-1]
UniGeneiMm.272185.

3D structure databases

ProteinModelPortaliQ6ZQ89.
SMRiQ6ZQ89. Positions 4-59.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ6ZQ89.

Proteomic databases

MaxQBiQ6ZQ89.
PaxDbiQ6ZQ89.
PRIDEiQ6ZQ89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090227; ENSMUSP00000087694; ENSMUSG00000039100. [Q6ZQ89-1]
GeneIDi223455.
KEGGimmu:223455.
UCSCiuc007vkh.1. mouse. [Q6ZQ89-1]

Organism-specific databases

CTDi10299.
MGIiMGI:2442773. March6.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG5183.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000286005.
HOVERGENiHBG080753.
InParanoidiQ6ZQ89.
KOiK10661.
OMAiDNLLADC.
OrthoDBiEOG7J4464.
PhylomeDBiQ6ZQ89.
TreeFamiTF105777.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiMarch6. mouse.
NextBioi376726.
PROiQ6ZQ89.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZQ89.
CleanExiMM_MARCH6.
ExpressionAtlasiQ6ZQ89. baseline and differential.
GenevestigatoriQ6ZQ89.

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]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 476-909 (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum and Spleen.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 348-883 (ISOFORM 3).
    Tissue: Brain.
  3. "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] OF 383-909 (ISOFORM 1).
    Strain: Czech II and FVB/N.
    Tissue: Mammary gland.

Entry informationi

Entry nameiMARH6_MOUSE
AccessioniPrimary (citable) accession number: Q6ZQ89
Secondary accession number(s): Q6PCS1
, Q80V02, Q80VC7, Q8BJA0, Q8BXX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: March 4, 2015
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.