MARHA_HUMAN
ID MARHA_HUMAN Reviewed; 808 AA.
AC Q8NA82; D3DU09; Q8IYS7; Q8N7Z7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable E3 ubiquitin-protein ligase MARCHF10;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 10;
DE AltName: Full=Membrane-associated RING-CH protein X;
DE Short=MARCH-X;
DE AltName: Full=RING finger protein 190;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCHF10 {ECO:0000305};
GN Name=MARCHF10 {ECO:0000312|HGNC:HGNC:26655}; Synonyms=MARCH10, RNF190;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-319.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-241.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (Probable). E3 ubiquitin ligases
CC accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of
CC a thioester and then directly transfer the ubiquitin to targeted
CC substrates. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INTERACTION:
CC Q8NA82; Q9NQW6-2: ANLN; NbExp=3; IntAct=EBI-2341554, EBI-10312488;
CC Q8NA82; O43464: HTRA2; NbExp=3; IntAct=EBI-2341554, EBI-517086;
CC Q8NA82; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2341554, EBI-1055254;
CC Q8NA82; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2341554, EBI-741158;
CC Q8NA82; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2341554, EBI-5235340;
CC Q8NA82; Q9H3U1: UNC45A; NbExp=7; IntAct=EBI-2341554, EBI-1048763;
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase
CC activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35021.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC05079.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK093076; BAC04044.1; -; mRNA.
DR EMBL; AK097506; BAC05079.1; ALT_INIT; mRNA.
DR EMBL; AC005821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94337.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94338.1; -; Genomic_DNA.
DR EMBL; BC035021; AAH35021.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11635.1; -.
DR RefSeq; NP_001094345.1; NM_001100875.2.
DR RefSeq; NP_001275708.1; NM_001288779.1.
DR RefSeq; NP_001275709.1; NM_001288780.1.
DR RefSeq; NP_689811.2; NM_152598.3.
DR AlphaFoldDB; Q8NA82; -.
DR SMR; Q8NA82; -.
DR BioGRID; 127813; 8.
DR IntAct; Q8NA82; 10.
DR MINT; Q8NA82; -.
DR STRING; 9606.ENSP00000463080; -.
DR GlyGen; Q8NA82; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NA82; -.
DR PhosphoSitePlus; Q8NA82; -.
DR BioMuta; MARCH10; -.
DR DMDM; 296439307; -.
DR MassIVE; Q8NA82; -.
DR PaxDb; Q8NA82; -.
DR PeptideAtlas; Q8NA82; -.
DR PRIDE; Q8NA82; -.
DR ProteomicsDB; 72656; -.
DR Antibodypedia; 18645; 200 antibodies from 25 providers.
DR DNASU; 162333; -.
DR Ensembl; ENST00000311269.10; ENSP00000311496.5; ENSG00000173838.12.
DR Ensembl; ENST00000456609.6; ENSP00000416177.2; ENSG00000173838.12.
DR GeneID; 162333; -.
DR KEGG; hsa:162333; -.
DR MANE-Select; ENST00000311269.10; ENSP00000311496.5; NM_152598.4; NP_689811.2.
DR UCSC; uc002jag.6; human.
DR CTD; 162333; -.
DR DisGeNET; 162333; -.
DR GeneCards; MARCHF10; -.
DR HGNC; HGNC:26655; MARCHF10.
DR HPA; ENSG00000173838; Tissue enriched (testis).
DR MIM; 613337; gene.
DR neXtProt; NX_Q8NA82; -.
DR OpenTargets; ENSG00000173838; -.
DR VEuPathDB; HostDB:ENSG00000173838; -.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT00530000063836; -.
DR HOGENOM; CLU_021725_0_0_1; -.
DR InParanoid; Q8NA82; -.
DR OMA; HDYERDW; -.
DR OrthoDB; 517602at2759; -.
DR PhylomeDB; Q8NA82; -.
DR TreeFam; TF330816; -.
DR PathwayCommons; Q8NA82; -.
DR SignaLink; Q8NA82; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 162333; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; MARCH10; human.
DR GenomeRNAi; 162333; -.
DR Pharos; Q8NA82; Tdark.
DR PRO; PR:Q8NA82; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8NA82; protein.
DR Bgee; ENSG00000173838; Expressed in left testis and 112 other tissues.
DR ExpressionAtlas; Q8NA82; baseline and differential.
DR Genevisible; Q8NA82; HS.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16813; RING_CH-C4HC3_MARCH10; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042583; MARCH10_RING_CH-C4HC3.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..808
FT /note="Probable E3 ubiquitin-protein ligase MARCHF10"
FT /id="PRO_0000261626"
FT ZN_FING 651..721
FT /note="RING-CH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT REGION 33..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 659
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 711
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00623"
FT VARIANT 241
FT /note="G -> E (in dbSNP:rs17853369)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029461"
FT VARIANT 319
FT /note="F -> S (in dbSNP:rs9891498)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_029462"
FT VARIANT 742
FT /note="E -> K (in dbSNP:rs16946335)"
FT /id="VAR_029463"
FT CONFLICT 734
FT /note="H -> Y (in Ref. 1; BAC05079)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="N -> S (in Ref. 4; AAH35021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 808 AA; 90511 MW; 456C2D2A93AAE8B1 CRC64;
MLHDARDRQK FFSDVQYLRD MQHKVDSEYQ ACLRRQEYRR DPNEKKRDQF WGQETSFERS
RFSSRSSSKQ SSSEEDALTE PRSSIKISAF KCDSKLPAID QTSVKQKHKS TMTVRKAEKV
DPSEPSPADQ APMVLLRKRK PNLRRFTVSP ESHSPRASGD RSRQKQQWPA KVPVPRGADQ
VVQQEGLMCN TKLKRPNQER RNLVPSSQPM TENAPDRAKK GDPSAPSQSE LHPALSQAFQ
GKNSPQVLSE FSGPPLTPTT VGGPRKASFR FRDEDFYSIL SLNSRRESDD TEEETQSEEC
LWVGVRSPCS PSHHKRSRFG GTSTPQAKNK NFEENAENCR GHSSRRSEPS HGSLRISNAM
EPATERPSAG QRLSQDPGLP DRESATEKDR GGSENAKKSP LSWDTKSEPR QEVGVNAENV
WSDCISVEHR PGTHDSEGYW KDYLNSSQNS LDYFISGRPI SPRSSVNSSY NPPASFMHSA
LRDDIPVDLS MSSTSVHSSD SEGNSGFHVC QPLSPIRNRT PFASAENHNY FPVNSAHEFA
VREAEDTTLT SQPQGAPLYT DLLLNPQGNL SLVDSSSSSP SRMNSEGHLH VSGSLQENTP
FTFFAVSHFP NQNDNGSRMA ASGFTDEKET SKIKADPEKL KKLQESLLEE DSEEEGDLCR
ICQIAGGSPS NPLLEPCGCV GSLQFVHQEC LKKWLKVKIT SGADLGAVKT CEMCKQGLLV
DLGDFNMIEF YQKHQQSQAQ NELMNSGLYL VLLLHLYEQR FAELMRLNHN QVERERLSRN
YPQPRTEENE NSELGDGNEG SISQSQVV
