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Protein

E3 ubiquitin-protein ligase MARCH7

Gene

MARCH7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. 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.1 Publication

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 fingeri544 – 61471RING-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

BRENDAi6.3.2.19. 2681.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MARCH7 (EC:6.3.2.-)
Alternative name(s):
Axotrophin
Membrane-associated RING finger protein 7
Membrane-associated RING-CH protein VII
Short name:
MARCH-VII
RING finger protein 177
Gene namesi
Name:MARCH7
Synonyms:AXOT, RNF177
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:17393. MARCH7.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25198.

Polymorphism and mutation databases

BioMutaiMARK7.
DMDMi74762745.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 704704E3 ubiquitin-protein ligase MARCH7PRO_0000274415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei686 – 6861PhosphothreonineCombined sources
Modified residuei687 – 6871PhosphoserineCombined sources
Modified residuei691 – 6911PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9H992.
MaxQBiQ9H992.
PaxDbiQ9H992.
PRIDEiQ9H992.

PTM databases

iPTMnetiQ9H992.
PhosphoSiteiQ9H992.

Expressioni

Gene expression databases

BgeeiQ9H992.
CleanExiHS_MARCH7.
ExpressionAtlasiQ9H992. baseline and differential.
GenevisibleiQ9H992. HS.

Organism-specific databases

HPAiHPA014275.
HPA022152.

Interactioni

Protein-protein interaction databases

BioGridi122319. 25 interactions.
IntActiQ9H992. 7 interactions.
MINTiMINT-2876071.
STRINGi9606.ENSP00000259050.

Structurei

3D structure databases

ProteinModelPortaliQ9H992.
SMRiQ9H992. Positions 550-608.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 421409Ser-richAdd
BLAST

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 fingeri544 – 61471RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00530000063836.
HOGENOMiHOG000232048.
HOVERGENiHBG080528.
InParanoidiQ9H992.
KOiK10662.
OMAiPDNRASE.
OrthoDBiEOG7K3TM7.
PhylomeDBiQ9H992.
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]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9H992-1) [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
MESKPSRIPR RISVQPSSSL SARMMSGSRG SSLNDTYHSR DSSFRLDSEY
60 70 80 90 100
QSTSASASAS PFQSAWYSES EITQGARSRS QNQQRDHDSK RPKLSCTNCT
110 120 130 140 150
TSAGRNVGNG LNTLSDSSWR HSQVPRSSSM VLGSFGTDLM RERRDLERRT
160 170 180 190 200
DSSISNLMDY SHRSGDFTTS SYVQDRVPSY SQGARPKENS MSTLQLNTSS
210 220 230 240 250
TNHQLPSEHQ TILSSRDSRN SLRSNFSSRE SESSRSNTQP GFSYSSSRDE
260 270 280 290 300
APIISNSERV VSSQRPFQES SDNEGRRTTR RLLSRIASSM SSTFFSRRSS
310 320 330 340 350
QDSLNTRSLN SENSYVSPRI LTASQSRSNV PSASEVPDNR ASEASQGFRF
360 370 380 390 400
LRRRWGLSSL SHNHSSESDS ENFNQESEGR NTGPWLSSSL RNRCTPLFSR
410 420 430 440 450
RRREGRDESS RIPTSDTSSR SHIFRRESNE VVHLEAQNDP LGAAANRPQA
460 470 480 490 500
SAASSSATTG GSTSDSAQGG RNTGISGILP GSLFRFAVPP ALGSNLTDNV
510 520 530 540 550
MITVDIIPSG WNSADGKSDK TKSAPSRDPE RLQKIKESLL LEDSEEEEGD
560 570 580 590 600
LCRICQMAAA SSSNLLIEPC KCTGSLQYVH QDCMKKWLQA KINSGSSLEA
610 620 630 640 650
VTTCELCKEK LELNLEDFDI HELHRAHANE QAEYEFISSG LYLVVLLHLC
660 670 680 690 700
EQSFSDMMGN TNEPSTRVRF INLARTLQAH MEDLETSEDD SEEDGDHNRT

FDIA
Length:704
Mass (Da):78,051
Last modified:March 1, 2001 - v1
Checksum:i1271F74D7F389130
GO
Isoform 2 (identifier: Q9H992-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: MESKPSRIPRRISVQPSSSLSARMMSGSRGSSLNDTYHSRDSSFRLDSEYQ → MIGNYDHLMSLVT

Note: No experimental confirmation available.
Show »
Length:666
Mass (Da):73,778
Checksum:iA553FF5F219A65D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti376 – 3761E → G in BAD96600 (Ref. 2) Curated
Sequence conflicti412 – 4121I → V in BAD96600 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001T → S.
Corresponds to variant rs17813964 [ dbSNP | Ensembl ].
VAR_030284
Natural varianti193 – 1931T → I.
Corresponds to variant rs16844275 [ dbSNP | Ensembl ].
VAR_030285
Natural varianti379 – 3791G → S.1 Publication
Corresponds to variant rs13024801 [ dbSNP | Ensembl ].
VAR_030286

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5151MESKP…DSEYQ → MIGNYDHLMSLVT in isoform 2. 1 PublicationVSP_054406Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022973 mRNA. Translation: BAB14340.1.
AK292836 mRNA. Translation: BAF85525.1.
AK302347 mRNA. Translation: BAH13681.1.
AK222880 mRNA. Translation: BAD96600.1.
AC009961 Genomic DNA. Translation: AAY14941.1.
CH471058 Genomic DNA. Translation: EAX11402.1.
BC003404 mRNA. Translation: AAH03404.1.
BC065014 mRNA. Translation: AAH65014.1.
CCDSiCCDS2210.1. [Q9H992-1]
CCDS63039.1. [Q9H992-2]
RefSeqiNP_001269734.1. NM_001282805.1. [Q9H992-1]
NP_001269735.1. NM_001282806.1.
NP_001269736.1. NM_001282807.1. [Q9H992-2]
NP_073737.1. NM_022826.3. [Q9H992-1]
XP_005246830.1. XM_005246773.1. [Q9H992-1]
UniGeneiHs.529272.

Genome annotation databases

EnsembliENST00000259050; ENSP00000259050; ENSG00000136536. [Q9H992-1]
ENST00000409175; ENSP00000386830; ENSG00000136536. [Q9H992-1]
ENST00000409591; ENSP00000387238; ENSG00000136536. [Q9H992-2]
GeneIDi64844.
KEGGihsa:64844.
UCSCiuc002uax.5. human. [Q9H992-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022973 mRNA. Translation: BAB14340.1.
AK292836 mRNA. Translation: BAF85525.1.
AK302347 mRNA. Translation: BAH13681.1.
AK222880 mRNA. Translation: BAD96600.1.
AC009961 Genomic DNA. Translation: AAY14941.1.
CH471058 Genomic DNA. Translation: EAX11402.1.
BC003404 mRNA. Translation: AAH03404.1.
BC065014 mRNA. Translation: AAH65014.1.
CCDSiCCDS2210.1. [Q9H992-1]
CCDS63039.1. [Q9H992-2]
RefSeqiNP_001269734.1. NM_001282805.1. [Q9H992-1]
NP_001269735.1. NM_001282806.1.
NP_001269736.1. NM_001282807.1. [Q9H992-2]
NP_073737.1. NM_022826.3. [Q9H992-1]
XP_005246830.1. XM_005246773.1. [Q9H992-1]
UniGeneiHs.529272.

3D structure databases

ProteinModelPortaliQ9H992.
SMRiQ9H992. Positions 550-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122319. 25 interactions.
IntActiQ9H992. 7 interactions.
MINTiMINT-2876071.
STRINGi9606.ENSP00000259050.

PTM databases

iPTMnetiQ9H992.
PhosphoSiteiQ9H992.

Polymorphism and mutation databases

BioMutaiMARK7.
DMDMi74762745.

Proteomic databases

EPDiQ9H992.
MaxQBiQ9H992.
PaxDbiQ9H992.
PRIDEiQ9H992.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259050; ENSP00000259050; ENSG00000136536. [Q9H992-1]
ENST00000409175; ENSP00000386830; ENSG00000136536. [Q9H992-1]
ENST00000409591; ENSP00000387238; ENSG00000136536. [Q9H992-2]
GeneIDi64844.
KEGGihsa:64844.
UCSCiuc002uax.5. human. [Q9H992-1]

Organism-specific databases

CTDi64844.
GeneCardsiMARCH7.
HGNCiHGNC:17393. MARCH7.
HPAiHPA014275.
HPA022152.
MIMi613334. gene.
neXtProtiNX_Q9H992.
PharmGKBiPA25198.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00530000063836.
HOGENOMiHOG000232048.
HOVERGENiHBG080528.
InParanoidiQ9H992.
KOiK10662.
OMAiPDNRASE.
OrthoDBiEOG7K3TM7.
PhylomeDBiQ9H992.
TreeFamiTF330816.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.

Miscellaneous databases

ChiTaRSiMARCH7. human.
GeneWikiiMARCH7.
GenomeRNAii64844.
PROiQ9H992.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H992.
CleanExiHS_MARCH7.
ExpressionAtlasiQ9H992. baseline and differential.
GenevisibleiQ9H992. 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

« Hide 'large scale' publications
  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] (ISOFORMS 1 AND 2).
    Tissue: Testis and Trachea.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-379.
    Tissue: Liver.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Placenta and Skin.
  6. "Leukaemia inhibitory factor (LIF) is functionally linked to axotrophin and both LIF and axotrophin are linked to regulatory immune tolerance."
    Metcalfe S.M., Muthukumarana P.A.D.S., Thompson H.L., Haendel M.A., Lyons G.E.
    FEBS Lett. 579:609-614(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system."
    Flierman D., Coleman C.S., Pickart C.M., Rapoport T.A., Chau V.
    Proc. Natl. Acad. Sci. U.S.A. 103:11589-11594(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-686; SER-687 AND SER-691, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMARH7_HUMAN
AccessioniPrimary (citable) accession number: Q9H992
Secondary accession number(s): A8K9X1
, B7Z7P5, D3DPB0, Q53GQ1, Q9BTR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 126 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 2
    Human chromosome 2: 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.