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Protein

E3 ubiquitin-protein ligase MARCH3

Gene

March3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

E3 ubiquitin-protein ligase which may be involved in endosomal trafficking. 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 (By similarity).By similarity

Pathwayi: protein 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 fingeri63 – 12361RING-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 MARCH3 (EC:6.3.2.-)
Alternative name(s):
Membrane-associated RING finger protein 3
Membrane-associated RING-CH protein III
Short name:
MARCH-III
Gene namesi
Name:March3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:2443667. March3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei145 – 16521HelicalSequence analysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218E3 ubiquitin-protein ligase MARCH3PRO_0000055928Add
BLAST

Proteomic databases

MaxQBiQ8BRX9.
PaxDbiQ8BRX9.
PRIDEiQ8BRX9.

PTM databases

iPTMnetiQ8BRX9.
PhosphoSiteiQ8BRX9.

Expressioni

Gene expression databases

BgeeiQ8BRX9.
CleanExiMM_MARCH3.
ExpressionAtlasiQ8BRX9. baseline and differential.

Interactioni

Subunit structurei

Interacts with MARCH2 and STX6.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099976.

Structurei

3D structure databases

ProteinModelPortaliQ8BRX9.
SMRiQ8BRX9. Positions 70-125.
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 fingeri63 – 12361RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000293394.
HOVERGENiHBG052411.
InParanoidiQ8BRX9.
KOiK10658.
OrthoDBiEOG7B05F1.
TreeFamiTF319557.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
PfamiPF12906. RINGv. 1 hit.
[Graphical view]
SMARTiSM00744. RINGv. 1 hit.
[Graphical view]
PROSITEiPS51292. ZF_RING_CH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BRX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSRCSHLP EVLPDCTSSA APVVKTVEDC GSLVNGQPQY VMQVSAKDGQ
60 70 80 90 100
LLSTVVRTLA TQSPFNDRPM CRICHEGSSQ EDLLSPCECT GTLGTIHRSC
110 120 130 140 150
LEHWLSSSNT SYCELCHFRF AVERKPRPLV EWLRNPGPQH EKRTLFGDMV
160 170 180 190 200
CFLFITPLAT ISGWLCLRGA VDHLHFSSRL EAVGLIALTV ALFTIYLFWT
210
LRRYGHQSKP FWNQSSRS
Length:218
Mass (Da):24,491
Last modified:March 1, 2003 - v1
Checksum:i098C2028247ECE19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041088 mRNA. Translation: BAC30814.1.
BC107233 mRNA. Translation: AAI07234.1.
BC107232 mRNA. Translation: AAI07233.1.
CCDSiCCDS29262.1.
RefSeqiNP_796089.1. NM_177115.2.
UniGeneiMm.312623.

Genome annotation databases

EnsembliENSMUST00000102912; ENSMUSP00000099976; ENSMUSG00000032656.
GeneIDi320253.
KEGGimmu:320253.
UCSCiuc008eyv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK041088 mRNA. Translation: BAC30814.1.
BC107233 mRNA. Translation: AAI07234.1.
BC107232 mRNA. Translation: AAI07233.1.
CCDSiCCDS29262.1.
RefSeqiNP_796089.1. NM_177115.2.
UniGeneiMm.312623.

3D structure databases

ProteinModelPortaliQ8BRX9.
SMRiQ8BRX9. Positions 70-125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099976.

PTM databases

iPTMnetiQ8BRX9.
PhosphoSiteiQ8BRX9.

Proteomic databases

MaxQBiQ8BRX9.
PaxDbiQ8BRX9.
PRIDEiQ8BRX9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102912; ENSMUSP00000099976; ENSMUSG00000032656.
GeneIDi320253.
KEGGimmu:320253.
UCSCiuc008eyv.1. mouse.

Organism-specific databases

CTDi115123.
MGIiMGI:2443667. March3.

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000293394.
HOVERGENiHBG052411.
InParanoidiQ8BRX9.
KOiK10658.
OrthoDBiEOG7B05F1.
TreeFamiTF319557.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi396359.
PROiQ8BRX9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BRX9.
CleanExiMM_MARCH3.
ExpressionAtlasiQ8BRX9. baseline and differential.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
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: Aorta and Vein.
  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].

Entry informationi

Entry nameiMARH3_MOUSE
AccessioniPrimary (citable) accession number: Q8BRX9
Secondary accession number(s): Q3KNK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 96 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

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 one 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.