Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable E3 ubiquitin-protein ligase MARCH10

Gene

March10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase (Probable). 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.Curated

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 fingeri633 – 70371RING-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:
Probable E3 ubiquitin-protein ligase MARCH10 (EC:6.3.2.-)
Alternative name(s):
Membrane-associated RING finger protein 10
Membrane-associated RING-CH protein X
Short name:
MARCH-X
RING finger protein 190
Gene namesi
Name:March10
Synonyms:Rnf190
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1311692. March10.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 790790Probable E3 ubiquitin-protein ligase MARCH10PRO_0000261627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5XIV2.
PRIDEiQ5XIV2.

PTM databases

iPTMnetiQ5XIV2.
PhosphoSiteiQ5XIV2.

Expressioni

Gene expression databases

ExpressionAtlasiQ5XIV2. baseline.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009316.

Structurei

3D structure databases

ProteinModelPortaliQ5XIV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili284 – 30825Sequence analysisAdd
BLAST

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 fingeri633 – 70371RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00530000063836.
HOGENOMiHOG000113485.
HOVERGENiHBG087265.
InParanoidiQ5XIV2.
KOiK10665.
OMAiCQIAGGS.
OrthoDBiEOG7K3TM7.
PhylomeDBiQ5XIV2.
TreeFamiTF330816.

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.

Q5XIV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHEARDRQK FVSDVQYLRD MQHKVDSEYQ ACLKRQEHKK EPNEKKQEQL
60 70 80 90 100
WGKDTSDRSR FSSGSSCKQS SGEEDSLSEA RLATKAPTAK CEPKLPAIDQ
110 120 130 140 150
TSVKQKHKGT MTLKKPEKVS PSKPSAVAQA TKILSRKRRP NLGRLTVSPE
160 170 180 190 200
MHSPRLSGER SRQKAQLSTK TSGLLGADPV VQQDSLLSAN EMKLKRPARE
210 220 230 240 250
KRNLAPSSQL VRVAGKAPLE RQKKGDPSAR PQNEPHTALS QTFQPMSGSQ
260 270 280 290 300
VLTESSVPPF LPATVVGPRR APFRFHDEDF YSALSLNNEQ ENYDTEEETR
310 320 330 340 350
TEEELLLAGM RSPPSYKRSR FLGTSAAQNR NVEENAENLR GNSLRRSEPN
360 370 380 390 400
PGSPRKTSVT EPTTKQSSPG QRMLQDTRLP RELAKDNPSG DQDEKTPVPG
410 420 430 440 450
DAKSDGVTQV SAEDVSNNCA VEDRSAVHNC ERDWQRYLSG SRNSFDCLLS
460 470 480 490 500
GRPTAPRASV NPSYNAHGSL FHSAVIDDIP ASLSVSSILV PSAELEENLR
510 520 530 540 550
FNVRRPLSPI RNRNPSAASE SHSEDTQGEE ERASTSQAQE SPLLSDLPNP
560 570 580 590 600
QSSMALGDSP SSPTRRHLQG HFYMPGSLQE NIPFTFFAVS DFASQNDNGT
610 620 630 640 650
SVRVSGVMDE KATEIKADPE KLRKLQESLL EEDSEEEGDL CRICQIAGGS
660 670 680 690 700
PANPLLEPCG CVGSLQFVHQ ECLKKWLKVK ITSGADLSTV KTCEMCKQGL
710 720 730 740 750
LVDLDDFNMT EFYHKHQQSR AQSELMNSGL YLVLLLHLYE QRFAELMTLN
760 770 780 790
YRRASRERMS RNYPQPRPEE SESSESGDGN ESNVYPGRVI
Length:790
Mass (Da):87,886
Last modified:November 23, 2004 - v1
Checksum:iE5DAE696C792EA0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083567 mRNA. Translation: AAH83567.1.
RefSeqiNP_001013995.1. NM_001013973.1.
XP_006247641.1. XM_006247579.2.
XP_006247642.1. XM_006247580.2.
UniGeneiRn.160625.

Genome annotation databases

EnsembliENSRNOT00000009316; ENSRNOP00000009316; ENSRNOG00000007084.
GeneIDi303596.
KEGGirno:303596.
UCSCiRGD:1311692. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083567 mRNA. Translation: AAH83567.1.
RefSeqiNP_001013995.1. NM_001013973.1.
XP_006247641.1. XM_006247579.2.
XP_006247642.1. XM_006247580.2.
UniGeneiRn.160625.

3D structure databases

ProteinModelPortaliQ5XIV2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009316.

PTM databases

iPTMnetiQ5XIV2.
PhosphoSiteiQ5XIV2.

Proteomic databases

PaxDbiQ5XIV2.
PRIDEiQ5XIV2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009316; ENSRNOP00000009316; ENSRNOG00000007084.
GeneIDi303596.
KEGGirno:303596.
UCSCiRGD:1311692. rat.

Organism-specific databases

CTDi162333.
RGDi1311692. March10.

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00530000063836.
HOGENOMiHOG000113485.
HOVERGENiHBG087265.
InParanoidiQ5XIV2.
KOiK10665.
OMAiCQIAGGS.
OrthoDBiEOG7K3TM7.
PhylomeDBiQ5XIV2.
TreeFamiTF330816.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi651696.
PROiQ5XIV2.

Gene expression databases

ExpressionAtlasiQ5XIV2. baseline.

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 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].
    Tissue: Testis.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMARHA_RAT
AccessioniPrimary (citable) accession number: Q5XIV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 23, 2004
Last modified: January 20, 2016
This is version 99 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.