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Protein

Probable E3 ubiquitin-protein ligase MARCH10

Gene

MARCH10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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 fingeri651 – 72171RING-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:26655. MARCH10.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162395028.

Polymorphism and mutation databases

BioMutaiMARK10.
DMDMi296439307.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 808808Probable E3 ubiquitin-protein ligase MARCH10PRO_0000261626Add
BLAST

Proteomic databases

EPDiQ8NA82.
PaxDbiQ8NA82.
PRIDEiQ8NA82.

PTM databases

PhosphoSiteiQ8NA82.

Expressioni

Gene expression databases

BgeeiQ8NA82.
CleanExiHS_MARCH10.
ExpressionAtlasiQ8NA82. baseline and differential.
GenevisibleiQ8NA82. HS.

Organism-specific databases

HPAiHPA023316.
HPA023322.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ANLNQ9NQW6-23EBI-2341554,EBI-10312488
UNC45AQ9H3U13EBI-2341554,EBI-1048763
WDYHV1Q96HA83EBI-2341554,EBI-741158

Protein-protein interaction databases

BioGridi127813. 8 interactions.
IntActiQ8NA82. 6 interactions.
MINTiMINT-7969464.
STRINGi9606.ENSP00000311496.

Structurei

3D structure databases

ProteinModelPortaliQ8NA82.
SMRiQ8NA82. Positions 657-721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi575 – 5817Poly-Ser

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 fingeri651 – 72171RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00530000063836.
HOGENOMiHOG000113485.
HOVERGENiHBG087265.
InParanoidiQ8NA82.
KOiK10665.
PhylomeDBiQ8NA82.
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.

Q8NA82-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHDARDRQK FFSDVQYLRD MQHKVDSEYQ ACLRRQEYRR DPNEKKRDQF
60 70 80 90 100
WGQETSFERS RFSSRSSSKQ SSSEEDALTE PRSSIKISAF KCDSKLPAID
110 120 130 140 150
QTSVKQKHKS TMTVRKAEKV DPSEPSPADQ APMVLLRKRK PNLRRFTVSP
160 170 180 190 200
ESHSPRASGD RSRQKQQWPA KVPVPRGADQ VVQQEGLMCN TKLKRPNQER
210 220 230 240 250
RNLVPSSQPM TENAPDRAKK GDPSAPSQSE LHPALSQAFQ GKNSPQVLSE
260 270 280 290 300
FSGPPLTPTT VGGPRKASFR FRDEDFYSIL SLNSRRESDD TEEETQSEEC
310 320 330 340 350
LWVGVRSPCS PSHHKRSRFG GTSTPQAKNK NFEENAENCR GHSSRRSEPS
360 370 380 390 400
HGSLRISNAM EPATERPSAG QRLSQDPGLP DRESATEKDR GGSENAKKSP
410 420 430 440 450
LSWDTKSEPR QEVGVNAENV WSDCISVEHR PGTHDSEGYW KDYLNSSQNS
460 470 480 490 500
LDYFISGRPI SPRSSVNSSY NPPASFMHSA LRDDIPVDLS MSSTSVHSSD
510 520 530 540 550
SEGNSGFHVC QPLSPIRNRT PFASAENHNY FPVNSAHEFA VREAEDTTLT
560 570 580 590 600
SQPQGAPLYT DLLLNPQGNL SLVDSSSSSP SRMNSEGHLH VSGSLQENTP
610 620 630 640 650
FTFFAVSHFP NQNDNGSRMA ASGFTDEKET SKIKADPEKL KKLQESLLEE
660 670 680 690 700
DSEEEGDLCR ICQIAGGSPS NPLLEPCGCV GSLQFVHQEC LKKWLKVKIT
710 720 730 740 750
SGADLGAVKT CEMCKQGLLV DLGDFNMIEF YQKHQQSQAQ NELMNSGLYL
760 770 780 790 800
VLLLHLYEQR FAELMRLNHN QVERERLSRN YPQPRTEENE NSELGDGNEG

SISQSQVV
Length:808
Mass (Da):90,511
Last modified:May 18, 2010 - v3
Checksum:i456C2D2A93AAE8B1
GO

Sequence cautioni

The sequence AAH35021.1 differs from that shown. Reason: Erroneous termination at position 658. Translated as Leu.Curated
The sequence BAC05079.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti734 – 7341H → Y in BAC05079 (PubMed:14702039).Curated
Sequence conflicti791 – 7911N → S in AAH35021 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti241 – 2411G → E.1 Publication
Corresponds to variant rs17853369 [ dbSNP | Ensembl ].
VAR_029461
Natural varianti319 – 3191F → S.1 Publication
Corresponds to variant rs9891498 [ dbSNP | Ensembl ].
VAR_029462
Natural varianti742 – 7421E → K.
Corresponds to variant rs16946335 [ dbSNP | Ensembl ].
VAR_029463

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK093076 mRNA. Translation: BAC04044.1.
AK097506 mRNA. Translation: BAC05079.1. Different initiation.
AC005821 Genomic DNA. No translation available.
AC068512 Genomic DNA. No translation available.
AC080038 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94337.1.
CH471109 Genomic DNA. Translation: EAW94338.1.
BC035021 mRNA. Translation: AAH35021.1. Sequence problems.
CCDSiCCDS11635.1.
RefSeqiNP_001094345.1. NM_001100875.2.
NP_001275708.1. NM_001288779.1.
NP_001275709.1. NM_001288780.1.
NP_689811.2. NM_152598.3.
UniGeneiHs.665663.

Genome annotation databases

EnsembliENST00000311269; ENSP00000311496; ENSG00000173838.
ENST00000456609; ENSP00000416177; ENSG00000173838.
GeneIDi162333.
KEGGihsa:162333.
UCSCiuc002jag.6. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK093076 mRNA. Translation: BAC04044.1.
AK097506 mRNA. Translation: BAC05079.1. Different initiation.
AC005821 Genomic DNA. No translation available.
AC068512 Genomic DNA. No translation available.
AC080038 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94337.1.
CH471109 Genomic DNA. Translation: EAW94338.1.
BC035021 mRNA. Translation: AAH35021.1. Sequence problems.
CCDSiCCDS11635.1.
RefSeqiNP_001094345.1. NM_001100875.2.
NP_001275708.1. NM_001288779.1.
NP_001275709.1. NM_001288780.1.
NP_689811.2. NM_152598.3.
UniGeneiHs.665663.

3D structure databases

ProteinModelPortaliQ8NA82.
SMRiQ8NA82. Positions 657-721.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127813. 8 interactions.
IntActiQ8NA82. 6 interactions.
MINTiMINT-7969464.
STRINGi9606.ENSP00000311496.

PTM databases

PhosphoSiteiQ8NA82.

Polymorphism and mutation databases

BioMutaiMARK10.
DMDMi296439307.

Proteomic databases

EPDiQ8NA82.
PaxDbiQ8NA82.
PRIDEiQ8NA82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311269; ENSP00000311496; ENSG00000173838.
ENST00000456609; ENSP00000416177; ENSG00000173838.
GeneIDi162333.
KEGGihsa:162333.
UCSCiuc002jag.6. human.

Organism-specific databases

CTDi162333.
GeneCardsiMARCH10.
HGNCiHGNC:26655. MARCH10.
HPAiHPA023316.
HPA023322.
MIMi613337. gene.
neXtProtiNX_Q8NA82.
PharmGKBiPA162395028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00530000063836.
HOGENOMiHOG000113485.
HOVERGENiHBG087265.
InParanoidiQ8NA82.
KOiK10665.
PhylomeDBiQ8NA82.
TreeFamiTF330816.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GenomeRNAii162333.
NextBioi88152.
PROiQ8NA82.
SOURCEiSearch...

Gene expression databases

BgeeiQ8NA82.
CleanExiHS_MARCH10.
ExpressionAtlasiQ8NA82. baseline and differential.
GenevisibleiQ8NA82. HS.

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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-319.
    Tissue: Testis.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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], VARIANT GLU-241.
    Tissue: Testis.

Entry informationi

Entry nameiMARHA_HUMAN
AccessioniPrimary (citable) accession number: Q8NA82
Secondary accession number(s): D3DU09, Q8IYS7, Q8N7Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 18, 2010
Last modified: May 11, 2016
This is version 117 of the entry and version 3 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 17
    Human chromosome 17: 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

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.