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E3 ubiquitin-protein ligase MARCH8 (EC 2.3.2.27) (Cellular modulator of immune recognition) (c-MIR) (Membrane-associated RING finger protein 8) (Membrane-associated RING-CH protein VIII) (MARCH-VIII) (RING finger protein 178) (RING-type E3 ubiquitin transferase MARCH8)

 MARH8_HUMAN             Reviewed;         291 AA.
Q5T0T0; B2R8E7; H0Y7C6; Q5T0S8; Q8TC72;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 1.
30-AUG-2017, entry version 115.
RecName: Full=E3 ubiquitin-protein ligase MARCH8;
EC=2.3.2.27;
AltName: Full=Cellular modulator of immune recognition;
Short=c-MIR;
AltName: Full=Membrane-associated RING finger protein 8;
AltName: Full=Membrane-associated RING-CH protein VIII;
Short=MARCH-VIII;
AltName: Full=RING finger protein 178;
AltName: Full=RING-type E3 ubiquitin transferase MARCH8 {ECO:0000305};
Name=MARCH8; Synonyms=MIR, RNF178;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CD86, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12582153; DOI=10.1074/jbc.M211285200;
Goto E., Ishido S., Sato Y., Ohgimoto S., Ohgimoto K.,
Nagano-Fujii M., Hotta H.;
"c-MIR, a human E3 ubiquitin ligase, is a functional homolog of
herpesvirus proteins MIR1 and MIR2 and has similar activity.";
J. Biol. Chem. 278:14657-14668(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-266.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=14722266; DOI=10.1128/JVI.78.3.1109-1120.2004;
Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.;
"Downregulation of major histocompatibility complex class I by human
ubiquitin ligases related to viral immune evasion proteins.";
J. Virol. 78:1109-1120(2004).
[7]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR BETA.
PubMed=18389477; DOI=10.1002/eji.200737902;
Thibodeau J., Bourgeois-Daigneault M.C., Huppe G., Tremblay J.,
Aumont A., Houde M., Bartee E., Brunet A., Gauvreau M.E.,
de Gassart A., Gatti E., Baril M., Cloutier M., Bontron S., Fruh K.,
Lamarre D., Steimle V.;
"Interleukin-10-induced MARCH1 mediates intracellular sequestration of
MHC class II in monocytes.";
Eur. J. Immunol. 38:1225-1230(2008).
[8]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR ALPHA AND BETA, AND
SUBCELLULAR LOCATION.
PubMed=19117940; DOI=10.1074/jbc.M805736200;
Lapaque N., Jahnke M., Trowsdale J., Kelly A.P.;
"The HLA-DRalpha chain is modified by polyubiquitination.";
J. Biol. Chem. 284:7007-7016(2009).
[9]
FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR.
PubMed=19566897; DOI=10.1111/j.1600-0854.2009.00948.x;
Gauvreau M.E., Cote M.H., Bourgeois-Daigneault M.C., Rivard L.D.,
Xiu F., Brunet A., Shaw A., Steimle V., Thibodeau J.;
"Sorting of MHC class II molecules into exosomes through a ubiquitin-
independent pathway.";
Traffic 10:1518-1527(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
STRUCTURE BY NMR OF 65-136.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RING domain of the human cellular modulator
of immune recognition protein.";
Submitted (JUN-2006) to the PDB data bank.
-!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
of CD86 and MHC class II proteins, such as HLA-DR alpha and beta,
and promotes their subsequent endocytosis and sorting to lysosomes
via multivesicular bodies. May also promote ubiquitination and
endocytosis of TFRC and FAS. {ECO:0000269|PubMed:12582153,
ECO:0000269|PubMed:14722266, ECO:0000269|PubMed:18389477,
ECO:0000269|PubMed:19117940, ECO:0000269|PubMed:19566897}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with CD86. {ECO:0000269|PubMed:12582153}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:19117940}; Multi-pass membrane protein
{ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:14722266};
Multi-pass membrane protein {ECO:0000255}. Early endosome membrane
{ECO:0000269|PubMed:14722266}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5T0T0-1; Sequence=Displayed;
Name=2;
IsoId=Q5T0T0-2; Sequence=VSP_055697;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Broadly expressed. Present in immature
dendritic cells (at protein level). {ECO:0000269|PubMed:12582153,
ECO:0000269|PubMed:14722266}.
-!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
ligase activity.
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EMBL; AK313340; BAG36144.1; -; mRNA.
EMBL; AL445201; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL731567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471160; EAW86647.1; -; Genomic_DNA.
EMBL; CH471160; EAW86648.1; -; Genomic_DNA.
EMBL; BC025394; AAH25394.1; -; mRNA.
EMBL; BC066988; AAH66988.1; -; mRNA.
CCDS; CCDS60519.1; -. [Q5T0T0-2]
CCDS; CCDS7213.1; -. [Q5T0T0-1]
RefSeq; NP_001002266.1; NM_001002266.2. [Q5T0T0-1]
RefSeq; NP_001269795.1; NM_001282866.1. [Q5T0T0-2]
RefSeq; NP_659458.2; NM_145021.5. [Q5T0T0-1]
RefSeq; XP_005271861.1; XM_005271804.2. [Q5T0T0-2]
RefSeq; XP_006717767.1; XM_006717704.2. [Q5T0T0-2]
RefSeq; XP_011537794.1; XM_011539492.2. [Q5T0T0-2]
RefSeq; XP_011537795.1; XM_011539493.2. [Q5T0T0-2]
RefSeq; XP_011537796.1; XM_011539494.2. [Q5T0T0-2]
RefSeq; XP_011537797.1; XM_011539495.1. [Q5T0T0-1]
RefSeq; XP_016871383.1; XM_017015894.1. [Q5T0T0-1]
UniGene; Hs.499489; -.
PDB; 2D8S; NMR; -; A=70-136.
PDBsum; 2D8S; -.
ProteinModelPortal; Q5T0T0; -.
SMR; Q5T0T0; -.
BioGrid; 128666; 9.
IntAct; Q5T0T0; 1.
STRING; 9606.ENSP00000317087; -.
iPTMnet; Q5T0T0; -.
PhosphoSitePlus; Q5T0T0; -.
BioMuta; MARK8; -.
DMDM; 74744352; -.
MaxQB; Q5T0T0; -.
PaxDb; Q5T0T0; -.
PeptideAtlas; Q5T0T0; -.
PRIDE; Q5T0T0; -.
Ensembl; ENST00000319836; ENSP00000317087; ENSG00000165406. [Q5T0T0-1]
Ensembl; ENST00000395769; ENSP00000379116; ENSG00000165406. [Q5T0T0-1]
Ensembl; ENST00000395771; ENSP00000379118; ENSG00000278545.
Ensembl; ENST00000453424; ENSP00000411848; ENSG00000165406. [Q5T0T0-2]
GeneID; 220972; -.
KEGG; hsa:220972; -.
UCSC; uc001jcf.5; human. [Q5T0T0-1]
CTD; 220972; -.
DisGeNET; 220972; -.
GeneCards; MARCH8; -.
H-InvDB; HIX0008790; -.
HGNC; HGNC:23356; MARCH8.
HPA; HPA014597; -.
MIM; 613335; gene.
neXtProt; NX_Q5T0T0; -.
OpenTargets; ENSG00000165406; -.
PharmGKB; PA37370; -.
eggNOG; KOG1609; Eukaryota.
eggNOG; COG5183; LUCA.
GeneTree; ENSGT00730000110355; -.
HOGENOM; HOG000113483; -.
HOVERGEN; HBG081957; -.
InParanoid; Q5T0T0; -.
KO; K10656; -.
OMA; SGDTCRI; -.
OrthoDB; EOG091G0WJX; -.
PhylomeDB; Q5T0T0; -.
TreeFam; TF319557; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q5T0T0; -.
GenomeRNAi; 220972; -.
PRO; PR:Q5T0T0; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000165406; -.
CleanEx; HS_MARCH8; -.
ExpressionAtlas; Q5T0T0; baseline and differential.
Genevisible; Q5T0T0; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR033275; MARCH-like.
InterPro; IPR011016; Znf_RING-CH.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR23012; PTHR23012; 1.
Pfam; PF12906; RINGv; 1.
SMART; SM00744; RINGv; 1.
PROSITE; PS51292; ZF_RING_CH; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing;
Complete proteome; Cytoplasmic vesicle; Endosome; Immunity; Lysosome;
Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 291 E3 ubiquitin-protein ligase MARCH8.
/FTId=PRO_0000274370.
TRANSMEM 157 177 Helical. {ECO:0000255}.
TRANSMEM 197 217 Helical. {ECO:0000255}.
ZN_FING 72 133 RING-CH-type. {ECO:0000255|PROSITE-
ProRule:PRU00623}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 79 79 I -> ICSSSAVFSECCHHSSVQSAVVSKAPHCQSSLTQGL
TVTVICKDTLQASKRNSFGSEWAQALKPAKNTKARRTLKFS
RSLNDVGEKAQDTSESFAYVERTCSEGKLILPQDTCLRTNR
FHHKEKRTLNHKPLGNSKHSCVSCLSAGRSTASEVEAGKGG
RPGLLLEEKADGEATSRSRQLLQYLFSLSHGLSASSLHRFH
ELESCAARLHTAKSSSGLAGSMGFCSDEMGDDDVFEDSTSA
KLKSRVLRAPLCSTEKDSDLDCPSPFSEKLPPISPVSTSGD
V (in isoform 2). {ECO:0000305}.
/FTId=VSP_055697.
VARIANT 92 92 P -> S (in dbSNP:rs3764990).
/FTId=VAR_030266.
VARIANT 266 266 Y -> H (in dbSNP:rs7908745).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030267.
STRAND 81 83 {ECO:0000244|PDB:2D8S}.
STRAND 89 91 {ECO:0000244|PDB:2D8S}.
STRAND 96 98 {ECO:0000244|PDB:2D8S}.
STRAND 101 103 {ECO:0000244|PDB:2D8S}.
HELIX 110 118 {ECO:0000244|PDB:2D8S}.
STRAND 124 126 {ECO:0000244|PDB:2D8S}.
SEQUENCE 291 AA; 32965 MW; F45D9BFAA3889BB3 CRC64;
MSMPLHQISA IPSQDAISAR VYRSKTKEKE REEQNEKTLG HFMSHSSNIS KAGSPPSASA
PAPVSSFSRT SITPSSQDIC RICHCEGDDE SPLITPCHCT GSLHFVHQAC LQQWIKSSDT
RCCELCKYEF IMETKLKPLR KWEKLQMTSS ERRKIMCSVT FHVIAITCVV WSLYVLIDRT
AEEIKQGQAT GILEWPFWTK LVVVAIGFTG GLLFMYVQCK VYVQLWKRLK AYNRVIYVQN
CPETSKKNIF EKSPLTEPNF ENKHGYGICH SDTNSSCCTE PEDTGAEIIH V


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EIAAB43861 E3 ubiquitin-protein ligase TRIM17,Homo sapiens,Human,RBCC,RING finger protein 16,RNF16,TERF,Testis RING finger protein,TRIM17,Tripartite motif-containing protein 17
EIAAB33374 E3 ubiquitin-protein ligase RNF144B,Homo sapiens,Human,IBR domain-containing protein 2,IBRDC2,p53-inducible RING finger protein,P53RFP,RING finger protein 144B,RNF144B
EIAAB43778 E3 ubiquitin-protein ligase TRAF7,Homo sapiens,Human,RFWD1,RING finger and WD repeat-containing protein 1,RING finger protein 119,RNF119,TNF receptor-associated factor 7,TRAF7
EIAAB07154 Checkpoint with forkhead and RING finger domains protein,CHFR,E3 ubiquitin-protein ligase CHFR,Homo sapiens,Human,RING finger protein 196,RNF196
EIAAB34425 E3 ubiquitin-protein ligase RFWD3,Homo sapiens,Human,RFWD3,RING finger and WD repeat domain-containing protein 3,RING finger protein 201,RNF201
EIAAB34369 E3 ubiquitin-protein ligase rififylin,FYVE-RING finger protein Sakura,Rat,Rattus norvegicus,Rffl,RING finger and FYVE-like domain-containing protein 1
EIAAB35481 Dorfin,Double ring-finger protein,E3 ubiquitin-protein ligase RNF19A,Homo sapiens,Human,p38,RING finger protein 19A,RNF19,RNF19A


 

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