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Protein

E3 ubiquitin-protein ligase MARCH2

Gene

March2

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 may mediate ubiquitination of TFRC and CD86, and promote their subsequent endocytosis and sorting to lysosomes via multivesicular bodies. 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 be involved in endosomal trafficking through interaction with STX6 (By similarity).By similarity

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri56 – 11661RING-CH-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Endocytosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MARCH2 (EC:6.3.2.-)
Alternative name(s):
Membrane-associated RING finger protein 2
Membrane-associated RING-CH protein II
Short name:
MARCH-II
Gene namesi
Name:March2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1925915. March2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei138 – 15821HelicalSequence AnalysisAdd
BLAST
Transmembranei175 – 19521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246E3 ubiquitin-protein ligase MARCH2PRO_0000055926Add
BLAST

Proteomic databases

MaxQBiQ99M02.
PRIDEiQ99M02.

Expressioni

Gene expression databases

BgeeiQ99M02.
CleanExiMM_MARCH2.
ExpressionAtlasiQ99M02. baseline and differential.
GenevisibleiQ99M02. MM.

Interactioni

Subunit structurei

Interacts with STX6 and MARCH3.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065225.

Structurei

3D structure databases

ProteinModelPortaliQ99M02.
SMRiQ99M02. Positions 64-118.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri56 – 11661RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5183.
GeneTreeiENSGT00730000110355.
HOVERGENiHBG052411.
InParanoidiQ99M02.
KOiK10657.
PhylomeDBiQ99M02.

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]

Sequencei

Sequence statusi: Complete.

Q99M02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTGDCCHLP GSLCDCSSSP AFSKVVEATG LGPPQYVAQV TSRDGRLLST
60 70 80 90 100
VIRALDSQSD CPFCRICHEG ANGENLLSPC GCTGTLGAVH KSCLEKWLSS
110 120 130 140 150
SNTSYCELCH TEFAVEKRPR PLTEWLKDPG PRTEKRTLCC DMVCFVFITP
160 170 180 190 200
LAAISGWLCL RGAQDHLRLH SRLEAVGLIA LTIALFTIYV LWTLVSFRYH
210 220 230 240
CQLYSEWRKT NQKVRLKIRE ADGSEDPHHS LLATGLLKKV AEETPV
Length:246
Mass (Da):27,186
Last modified:June 1, 2001 - v1
Checksum:iDC4A6EE34B8AE897
GO

Sequence cautioni

The sequence BAC38235.1 differs from that shown. Reason: Frameshift at position 172. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK079234 mRNA. Translation: BAC37584.1.
AK081495 mRNA. Translation: BAC38235.1. Frameshift.
BC002144 mRNA. Translation: AAH02144.1.
CCDSiCCDS57064.1.
RefSeqiNP_001239409.1. NM_001252480.1.
UniGeneiMm.311439.
Mm.374865.

Genome annotation databases

EnsembliENSMUST00000172767; ENSMUSP00000134220; ENSMUSG00000079557.
GeneIDi224703.
KEGGimmu:224703.
UCSCiuc008bzk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK079234 mRNA. Translation: BAC37584.1.
AK081495 mRNA. Translation: BAC38235.1. Frameshift.
BC002144 mRNA. Translation: AAH02144.1.
CCDSiCCDS57064.1.
RefSeqiNP_001239409.1. NM_001252480.1.
UniGeneiMm.311439.
Mm.374865.

3D structure databases

ProteinModelPortaliQ99M02.
SMRiQ99M02. Positions 64-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065225.

Proteomic databases

MaxQBiQ99M02.
PRIDEiQ99M02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000172767; ENSMUSP00000134220; ENSMUSG00000079557.
GeneIDi224703.
KEGGimmu:224703.
UCSCiuc008bzk.2. mouse.

Organism-specific databases

CTDi51257.
MGIiMGI:1925915. March2.

Phylogenomic databases

eggNOGiCOG5183.
GeneTreeiENSGT00730000110355.
HOVERGENiHBG052411.
InParanoidiQ99M02.
KOiK10657.
PhylomeDBiQ99M02.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiMarch2. mouse.
NextBioi377316.
PROiQ99M02.
SOURCEiSearch...

Gene expression databases

BgeeiQ99M02.
CleanExiMM_MARCH2.
ExpressionAtlasiQ99M02. baseline and differential.
GenevisibleiQ99M02. MM.

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].
    Strain: C57BL/6J.
    Tissue: Head and Urinary bladder.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiMARH2_MOUSE
AccessioniPrimary (citable) accession number: Q99M02
Secondary accession number(s): Q8C4Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 117 of the entry and version 1 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.