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Protein

E3 ubiquitin-protein ligase MARCH2

Gene

MARCH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 STX6.3 Publications

Pathwayi

Regions

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

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • endocytosis Source: UniProtKB-KW
  • protein ubiquitination Source: UniProtKB
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
RING finger protein 172
Gene namesi
Name:MARCH2
Synonyms:RNF172
ORF Names:HSPC240
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:28038. MARCH2.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • cytoplasmic vesicle Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • endosome membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134993565.

Polymorphism and mutation databases

BioMutaiMARCH2.
DMDMi57012977.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246E3 ubiquitin-protein ligase MARCH2PRO_0000055925Add
BLAST

Proteomic databases

PaxDbiQ9P0N8.
PRIDEiQ9P0N8.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Gene expression databases

BgeeiQ9P0N8.
CleanExiHS_MARCH2.
ExpressionAtlasiQ9P0N8. baseline and differential.
GenevestigatoriQ9P0N8.

Organism-specific databases

HPAiHPA014063.

Interactioni

Subunit structurei

Interacts with STX6 (By similarity). Interacts with MARCH3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC155Q8N6L03EBI-10317612,EBI-749265
FATE1Q969F03EBI-10317612,EBI-743099
LDLRAD1Q5T7003EBI-10317612,EBI-10173166
SYNE4Q8N2053EBI-10317612,EBI-7131783

Protein-protein interaction databases

BioGridi119413. 13 interactions.
IntActiQ9P0N8. 4 interactions.
STRINGi9606.ENSP00000215555.

Structurei

3D structure databases

ProteinModelPortaliQ9P0N8.
SMRiQ9P0N8. Positions 57-118.
ModBaseiSearch...
MobiDBiSearch...

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 fingeri56 – 11661RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiCOG5183.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000293394.
HOVERGENiHBG052411.
InParanoidiQ9P0N8.
KOiK10657.
OMAiICHEGAG.
OrthoDBiEOG7B05F1.
PhylomeDBiQ9P0N8.
TreeFamiTF319557.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P0N8-1) [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
MTTGDCCHLP GSLCDCSGSP AFSKVVEATG LGPPQYVAQV TSRDGRLLST
60 70 80 90 100
VIRALDTPSD GPFCRICHEG ANGECLLSPC GCTGTLGAVH KSCLEKWLSS
110 120 130 140 150
SNTSYCELCH TEFAVEKRPR PLTEWLKDPG PRTEKRTLCC DMVCFLFITP
160 170 180 190 200
LAAISGWLCL RGAQDHLRLH SQLEAVGLIA LTIALFTIYV LWTLVSFRYH
210 220 230 240
CQLYSEWRKT NQKVRLKIRE ADSPEGPQHS PLAAGLLKKV AEETPV
Length:246
Mass (Da):26,995
Last modified:October 1, 2000 - v1
Checksum:iFBD877D55211C929
GO
Isoform 2 (identifier: Q9P0N8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-194: Missing.

Note: No experimental confirmation available.

Show »
Length:176
Mass (Da):19,099
Checksum:i1AA18937FB6F7652
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541A → T.1 Publication
Corresponds to variant rs1133893 [ dbSNP | Ensembl ].
VAR_030303
Natural varianti219 – 2191R → P.
Corresponds to variant rs34099346 [ dbSNP | Ensembl ].
VAR_053638

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei125 – 19470Missing in isoform 2. CuratedVSP_041478Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB197929 mRNA. Translation: BAD89359.1.
AF151074 mRNA. Translation: AAF36160.1.
AC136469 Genomic DNA. No translation available.
BC032624 mRNA. Translation: AAH32624.1.
BC015910 mRNA. Translation: AAH15910.1.
BC111388 mRNA. Translation: AAI11389.1.
CCDSiCCDS12202.1. [Q9P0N8-1]
CCDS32894.1. [Q9P0N8-2]
RefSeqiNP_001005415.1. NM_001005415.1. [Q9P0N8-1]
NP_001005416.1. NM_001005416.1. [Q9P0N8-2]
NP_057580.3. NM_016496.4. [Q9P0N8-1]
XP_006722826.1. XM_006722763.2. [Q9P0N8-2]
UniGeneiHs.631861.

Genome annotation databases

EnsembliENST00000215555; ENSP00000215555; ENSG00000099785. [Q9P0N8-1]
ENST00000381035; ENSP00000370423; ENSG00000099785. [Q9P0N8-2]
ENST00000602117; ENSP00000471536; ENSG00000099785. [Q9P0N8-1]
GeneIDi51257.
KEGGihsa:51257.
UCSCiuc002mjv.3. human. [Q9P0N8-1]
uc002mjx.3. human. [Q9P0N8-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB197929 mRNA. Translation: BAD89359.1.
AF151074 mRNA. Translation: AAF36160.1.
AC136469 Genomic DNA. No translation available.
BC032624 mRNA. Translation: AAH32624.1.
BC015910 mRNA. Translation: AAH15910.1.
BC111388 mRNA. Translation: AAI11389.1.
CCDSiCCDS12202.1. [Q9P0N8-1]
CCDS32894.1. [Q9P0N8-2]
RefSeqiNP_001005415.1. NM_001005415.1. [Q9P0N8-1]
NP_001005416.1. NM_001005416.1. [Q9P0N8-2]
NP_057580.3. NM_016496.4. [Q9P0N8-1]
XP_006722826.1. XM_006722763.2. [Q9P0N8-2]
UniGeneiHs.631861.

3D structure databases

ProteinModelPortaliQ9P0N8.
SMRiQ9P0N8. Positions 57-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119413. 13 interactions.
IntActiQ9P0N8. 4 interactions.
STRINGi9606.ENSP00000215555.

Polymorphism and mutation databases

BioMutaiMARCH2.
DMDMi57012977.

Proteomic databases

PaxDbiQ9P0N8.
PRIDEiQ9P0N8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215555; ENSP00000215555; ENSG00000099785. [Q9P0N8-1]
ENST00000381035; ENSP00000370423; ENSG00000099785. [Q9P0N8-2]
ENST00000602117; ENSP00000471536; ENSG00000099785. [Q9P0N8-1]
GeneIDi51257.
KEGGihsa:51257.
UCSCiuc002mjv.3. human. [Q9P0N8-1]
uc002mjx.3. human. [Q9P0N8-2]

Organism-specific databases

CTDi51257.
GeneCardsiGC19P008478.
H-InvDBHIX0022474.
HGNCiHGNC:28038. MARCH2.
HPAiHPA014063.
MIMi613332. gene.
neXtProtiNX_Q9P0N8.
PharmGKBiPA134993565.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5183.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000293394.
HOVERGENiHBG052411.
InParanoidiQ9P0N8.
KOiK10657.
OMAiICHEGAG.
OrthoDBiEOG7B05F1.
PhylomeDBiQ9P0N8.
TreeFamiTF319557.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GeneWikiiMARCH2.
GenomeRNAii51257.
NextBioi54414.
PROiQ9P0N8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0N8.
CleanExiHS_MARCH2.
ExpressionAtlasiQ9P0N8. baseline and differential.
GenevestigatoriQ9P0N8.

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

« Hide 'large scale' publications
  1. "MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking."
    Nakamura N., Fukuda H., Kato A., Hirose S.
    Mol. Biol. Cell 16:1696-1710(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANT THR-54.
    Tissue: Brain and Skin.
  5. "Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins."
    Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.
    J. Virol. 78:1109-1120(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. "MARCH-III is a novel component of endosomes with properties similar to those of MARCH-II."
    Fukuda H., Nakamura N., Hirose S.
    J. Biochem. 139:137-145(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MARCH3.

Entry informationi

Entry nameiMARH2_HUMAN
AccessioniPrimary (citable) accession number: Q9P0N8
Secondary accession number(s): A6NP10
, Q5H785, Q8N5A3, Q96B78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 119 of the entry and version 1 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 19
    Human chromosome 19: 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

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.