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Protein

E3 ubiquitin-protein ligase MARCH8

Gene

MARCH8

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

Functioni

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.5 Publications

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 fingeri72 – 13362RING-CH-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Adaptive immunity, Immunity, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MARCH8 (EC:6.3.2.-)
Alternative name(s):
Cellular modulator of immune recognition
Short name:
c-MIR
Membrane-associated RING finger protein 8
Membrane-associated RING-CH protein VIII
Short name:
MARCH-VIII
RING finger protein 178
Gene namesi
Name:MARCH8
Synonyms:MIR, RNF178
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:23356. MARCH8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei157 – 17721HelicalSequence analysisAdd
BLAST
Transmembranei197 – 21721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • early endosome membrane Source: UniProtKB-SubCell
  • endosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB-SubCell
  • lysosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37370.

Polymorphism and mutation databases

BioMutaiMARK8.
DMDMi74744352.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291E3 ubiquitin-protein ligase MARCH8PRO_0000274370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5T0T0.
MaxQBiQ5T0T0.
PaxDbiQ5T0T0.
PeptideAtlasiQ5T0T0.
PRIDEiQ5T0T0.

PTM databases

iPTMnetiQ5T0T0.
PhosphoSiteiQ5T0T0.

Expressioni

Tissue specificityi

Broadly expressed. Present in immature dendritic cells (at protein level).2 Publications

Gene expression databases

BgeeiQ5T0T0.
CleanExiHS_MARCH8.
ExpressionAtlasiQ5T0T0. baseline and differential.
GenevisibleiQ5T0T0. HS.

Organism-specific databases

HPAiHPA014597.

Interactioni

Subunit structurei

Interacts with CD86.1 Publication

Protein-protein interaction databases

BioGridi128666. 8 interactions.
STRINGi9606.ENSP00000317087.

Structurei

Secondary structure

1
291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi81 – 833Combined sources
Beta strandi89 – 913Combined sources
Beta strandi96 – 983Combined sources
Beta strandi101 – 1033Combined sources
Helixi110 – 1189Combined sources
Beta strandi124 – 1263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8SNMR-A70-136[»]
ProteinModelPortaliQ5T0T0.
SMRiQ5T0T0. Positions 72-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5T0T0.

Family & Domainsi

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 fingeri72 – 13362RING-CH-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000113483.
HOVERGENiHBG081957.
InParanoidiQ5T0T0.
KOiK10656.
OMAiSGDTCRI.
OrthoDBiEOG7W6WKW.
PhylomeDBiQ5T0T0.
TreeFamiTF319557.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
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: Q5T0T0-1) [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
MSMPLHQISA IPSQDAISAR VYRSKTKEKE REEQNEKTLG HFMSHSSNIS
60 70 80 90 100
KAGSPPSASA PAPVSSFSRT SITPSSQDIC RICHCEGDDE SPLITPCHCT
110 120 130 140 150
GSLHFVHQAC LQQWIKSSDT RCCELCKYEF IMETKLKPLR KWEKLQMTSS
160 170 180 190 200
ERRKIMCSVT FHVIAITCVV WSLYVLIDRT AEEIKQGQAT GILEWPFWTK
210 220 230 240 250
LVVVAIGFTG GLLFMYVQCK VYVQLWKRLK AYNRVIYVQN CPETSKKNIF
260 270 280 290
EKSPLTEPNF ENKHGYGICH SDTNSSCCTE PEDTGAEIIH V
Length:291
Mass (Da):32,965
Last modified:April 12, 2005 - v1
Checksum:iF45D9BFAA3889BB3
GO
Isoform 2 (identifier: Q5T0T0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     79-79: I → ICSSSAVFSE...ISPVSTSGDV

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:573
Mass (Da):63,319
Checksum:i8B7E5DF14206565E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921P → S.
Corresponds to variant rs3764990 [ dbSNP | Ensembl ].
VAR_030266
Natural varianti266 – 2661Y → H.1 Publication
Corresponds to variant rs7908745 [ dbSNP | Ensembl ].
VAR_030267

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei79 – 791I → ICSSSAVFSECCHHSSVQSA VVSKAPHCQSSLTQGLTVTV ICKDTLQASKRNSFGSEWAQ ALKPAKNTKARRTLKFSRSL NDVGEKAQDTSESFAYVERT CSEGKLILPQDTCLRTNRFH HKEKRTLNHKPLGNSKHSCV SCLSAGRSTASEVEAGKGGR PGLLLEEKADGEATSRSRQL LQYLFSLSHGLSASSLHRFH ELESCAARLHTAKSSSGLAG SMGFCSDEMGDDDVFEDSTS AKLKSRVLRAPLCSTEKDSD LDCPSPFSEKLPPISPVSTS GDV in isoform 2. CuratedVSP_055697

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313340 mRNA. Translation: BAG36144.1.
AL445201 Genomic DNA. No translation available.
AL512595 Genomic DNA. No translation available.
AL731567 Genomic DNA. No translation available.
CH471160 Genomic DNA. Translation: EAW86647.1.
CH471160 Genomic DNA. Translation: EAW86648.1.
BC025394 mRNA. Translation: AAH25394.1.
BC066988 mRNA. Translation: AAH66988.1.
CCDSiCCDS60519.1. [Q5T0T0-2]
CCDS7213.1. [Q5T0T0-1]
RefSeqiNP_001002266.1. NM_001002266.2. [Q5T0T0-1]
NP_001269795.1. NM_001282866.1. [Q5T0T0-2]
NP_659458.2. NM_145021.5. [Q5T0T0-1]
XP_005271861.1. XM_005271804.1. [Q5T0T0-2]
XP_006717767.1. XM_006717704.2. [Q5T0T0-2]
XP_006717768.1. XM_006717705.1. [Q5T0T0-2]
XP_011537794.1. XM_011539492.1. [Q5T0T0-2]
XP_011537795.1. XM_011539493.1. [Q5T0T0-2]
XP_011537796.1. XM_011539494.1. [Q5T0T0-2]
XP_011537797.1. XM_011539495.1. [Q5T0T0-1]
UniGeneiHs.499489.

Genome annotation databases

EnsembliENST00000319836; ENSP00000317087; ENSG00000165406. [Q5T0T0-1]
ENST00000395769; ENSP00000379116; ENSG00000165406. [Q5T0T0-1]
ENST00000395771; ENSP00000379118; ENSG00000278545.
ENST00000453424; ENSP00000411848; ENSG00000165406. [Q5T0T0-2]
GeneIDi220972.
KEGGihsa:220972.
UCSCiuc001jcf.5. human. [Q5T0T0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313340 mRNA. Translation: BAG36144.1.
AL445201 Genomic DNA. No translation available.
AL512595 Genomic DNA. No translation available.
AL731567 Genomic DNA. No translation available.
CH471160 Genomic DNA. Translation: EAW86647.1.
CH471160 Genomic DNA. Translation: EAW86648.1.
BC025394 mRNA. Translation: AAH25394.1.
BC066988 mRNA. Translation: AAH66988.1.
CCDSiCCDS60519.1. [Q5T0T0-2]
CCDS7213.1. [Q5T0T0-1]
RefSeqiNP_001002266.1. NM_001002266.2. [Q5T0T0-1]
NP_001269795.1. NM_001282866.1. [Q5T0T0-2]
NP_659458.2. NM_145021.5. [Q5T0T0-1]
XP_005271861.1. XM_005271804.1. [Q5T0T0-2]
XP_006717767.1. XM_006717704.2. [Q5T0T0-2]
XP_006717768.1. XM_006717705.1. [Q5T0T0-2]
XP_011537794.1. XM_011539492.1. [Q5T0T0-2]
XP_011537795.1. XM_011539493.1. [Q5T0T0-2]
XP_011537796.1. XM_011539494.1. [Q5T0T0-2]
XP_011537797.1. XM_011539495.1. [Q5T0T0-1]
UniGeneiHs.499489.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8SNMR-A70-136[»]
ProteinModelPortaliQ5T0T0.
SMRiQ5T0T0. Positions 72-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128666. 8 interactions.
STRINGi9606.ENSP00000317087.

PTM databases

iPTMnetiQ5T0T0.
PhosphoSiteiQ5T0T0.

Polymorphism and mutation databases

BioMutaiMARK8.
DMDMi74744352.

Proteomic databases

EPDiQ5T0T0.
MaxQBiQ5T0T0.
PaxDbiQ5T0T0.
PeptideAtlasiQ5T0T0.
PRIDEiQ5T0T0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000319836; ENSP00000317087; ENSG00000165406. [Q5T0T0-1]
ENST00000395769; ENSP00000379116; ENSG00000165406. [Q5T0T0-1]
ENST00000395771; ENSP00000379118; ENSG00000278545.
ENST00000453424; ENSP00000411848; ENSG00000165406. [Q5T0T0-2]
GeneIDi220972.
KEGGihsa:220972.
UCSCiuc001jcf.5. human. [Q5T0T0-1]

Organism-specific databases

CTDi220972.
GeneCardsiMARCH8.
H-InvDBHIX0008790.
HGNCiHGNC:23356. MARCH8.
HPAiHPA014597.
MIMi613335. gene.
neXtProtiNX_Q5T0T0.
PharmGKBiPA37370.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1609. Eukaryota.
COG5183. LUCA.
GeneTreeiENSGT00730000110355.
HOGENOMiHOG000113483.
HOVERGENiHBG081957.
InParanoidiQ5T0T0.
KOiK10656.
OMAiSGDTCRI.
OrthoDBiEOG7W6WKW.
PhylomeDBiQ5T0T0.
TreeFamiTF319557.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

EvolutionaryTraceiQ5T0T0.
GenomeRNAii220972.
PROiQ5T0T0.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T0T0.
CleanExiHS_MARCH8.
ExpressionAtlasiQ5T0T0. baseline and differential.
GenevisibleiQ5T0T0. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR033275. MARCH-like.
IPR011016. Znf_RING-CH.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR23012. PTHR23012. 1 hit.
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. "c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity."
    Goto E., Ishido S., Sato Y., Ohgimoto S., Ohgimoto K., Nagano-Fujii M., Hotta H.
    J. Biol. Chem. 278:14657-14668(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CD86, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. "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].
    Tissue: Testis.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    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.
    Nature 429:375-381(2004) [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], VARIANT HIS-266.
    Tissue: Testis.
  6. "Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins."
    Bartee E., Mansouri M., Hovey Nerenberg B.T., Gouveia K., Frueh K.
    J. Virol. 78:1109-1120(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR BETA.
  8. "The HLA-DRalpha chain is modified by polyubiquitination."
    Lapaque N., Jahnke M., Trowsdale J., Kelly A.P.
    J. Biol. Chem. 284:7007-7016(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR ALPHA AND BETA, SUBCELLULAR LOCATION.
  9. "Sorting of MHC class II molecules into exosomes through a ubiquitin-independent pathway."
    Gauvreau M.E., Cote M.H., Bourgeois-Daigneault M.C., Rivard L.D., Xiu F., Brunet A., Shaw A., Steimle V., Thibodeau J.
    Traffic 10:1518-1527(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR.
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  11. "Solution structure of the RING domain of the human cellular modulator of immune recognition protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 65-136.

Entry informationi

Entry nameiMARH8_HUMAN
AccessioniPrimary (citable) accession number: Q5T0T0
Secondary accession number(s): B2R8E7
, H0Y7C6, Q5T0S8, Q8TC72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: April 12, 2005
Last modified: July 6, 2016
This is version 107 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.