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Protein

Melanoma-associated antigen 2

Gene

MAGEA2

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

Functioni

Reduces p53/TP53 transactivation function through recruitment of HDAC3 to p53/TP53 transcription sites. Also represses p73/TP73 activity. Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination by TRIM28 potentially in presence of Ubl-conjugating enzyme UBE2H. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes. Negatively regulates acetylation and sumoylation of PML and represses PML-induced p53/TP53 acetylation and activation.4 Publications

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • repressing transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cellular protein catabolic process Source: UniProtKB
  • cellular senescence Source: UniProtKB
  • negative regulation of protein acetylation Source: UniProtKB
  • negative regulation of protein sumoylation Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
  • signal transduction by p53 class mediator Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Tumor antigen

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Melanoma-associated antigen 2
Alternative name(s):
Cancer/testis antigen 1.2
Short name:
CT1.2
MAGE-2 antigen
Gene namesi
Name:MAGEA2
Synonyms:MAGE2, MAGEA2A
AND
Name:MAGEA2B
Synonyms:MAGE2, MAGEA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:6800. MAGEA2.
HGNC:19340. MAGEA2B.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701V → D: Improves ability to bind to HLA-A1. 1 Publication

Organism-specific databases

PharmGKBiPA30546.

Polymorphism and mutation databases

BioMutaiMAGEA2.
DMDMi1170856.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Melanoma-associated antigen 2PRO_0000156702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP43356.
PRIDEiP43356.

PTM databases

iPTMnetiP43356.
PhosphoSiteiP43356.

Expressioni

Tissue specificityi

Expressed in many tumors of several types, such as melanoma, head and neck squamous cell carcinoma, lung carcinoma and breast carcinoma, but not in normal tissues except for testes.

Gene expression databases

BgeeiP43356.
CleanExiHS_MAGEA2.
ExpressionAtlasiP43356. baseline and differential.
GenevisibleiP43356. HS.

Interactioni

Subunit structurei

Interacts with TRIM28 and UBE2H. Interacts with HDAC3. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC3O153794EBI-5650739,EBI-607682
TP53P046376EBI-5650739,EBI-366083
TRIM28Q132636EBI-5650739,EBI-78139
UBE2HP622562EBI-5650739,EBI-2129909

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • repressing transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110275. 6 interactions.
129334. 10 interactions.
DIPiDIP-61231N.
IntActiP43356. 6 interactions.
STRINGi9606.ENSP00000359307.

Structurei

3D structure databases

ProteinModelPortaliP43356.
SMRiP43356. Positions 104-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 308200MAGEPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi40 – 434Poly-Ser

Sequence similaritiesi

Contains 1 MAGE domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4562. Eukaryota.
ENOG4111S70. LUCA.
GeneTreeiENSGT00760000118824.
HOGENOMiHOG000231161.
HOVERGENiHBG006315.
InParanoidiP43356.
OMAiEPHISYP.
OrthoDBiEOG75F4GM.
PhylomeDBiP43356.
TreeFamiTF328505.

Family and domain databases

InterProiIPR021072. MAGE_N.
IPR030103. MAGEA2.
IPR002190. MHD_dom.
[Graphical view]
PANTHERiPTHR11736:SF78. PTHR11736:SF78. 1 hit.
PfamiPF01454. MAGE. 1 hit.
PF12440. MAGE_N. 1 hit.
[Graphical view]
SMARTiSM01373. MAGE. 1 hit.
SM01392. MAGE_N. 1 hit.
[Graphical view]
PROSITEiPS50838. MAGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43356-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLEQRSQHC KPEEGLEARG EALGLVGAQA PATEEQQTAS SSSTLVEVTL
60 70 80 90 100
GEVPAADSPS PPHSPQGASS FSTTINYTLW RQSDEGSSNQ EEEGPRMFPD
110 120 130 140 150
LESEFQAAIS RKMVELVHFL LLKYRAREPV TKAEMLESVL RNCQDFFPVI
160 170 180 190 200
FSKASEYLQL VFGIEVVEVV PISHLYILVT CLGLSYDGLL GDNQVMPKTG
210 220 230 240 250
LLIIVLAIIA IEGDCAPEEK IWEELSMLEV FEGREDSVFA HPRKLLMQDL
260 270 280 290 300
VQENYLEYRQ VPGSDPACYE FLWGPRALIE TSYVKVLHHT LKIGGEPHIS
310
YPPLHERALR EGEE
Length:314
Mass (Da):35,055
Last modified:November 1, 1995 - v1
Checksum:i844F16335A2BECE7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18920 Genomic DNA. Translation: AAA17729.1.
AK290443 mRNA. Translation: BAF83132.1.
U82671 Genomic DNA. No translation available.
CH471169 Genomic DNA. Translation: EAW99429.1.
BC108720 mRNA. Translation: AAI08721.1.
BC112158 mRNA. Translation: AAI12159.1.
BC112160 mRNA. Translation: AAI12161.1.
CCDSiCCDS76046.1.
CCDS76049.1.
PIRiI68889.
RefSeqiNP_001269430.1. NM_001282501.1.
NP_001269431.1. NM_001282502.1.
NP_001269433.1. NM_001282504.1.
NP_001269434.1. NM_001282505.1.
NP_005352.1. NM_005361.3.
NP_705692.1. NM_153488.4.
NP_786884.1. NM_175742.2.
NP_786885.1. NM_175743.2.
XP_011529445.1. XM_011531143.1.
XP_011529461.1. XM_011531159.1.
UniGeneiHs.534597.
Hs.713061.
Hs.736992.

Genome annotation databases

EnsembliENST00000331220; ENSP00000333487; ENSG00000183305.
ENST00000370293; ENSP00000359316; ENSG00000183305.
ENST00000595583; ENSP00000470872; ENSG00000268606.
ENST00000598543; ENSP00000469919; ENSG00000268606.
ENST00000611557; ENSP00000480738; ENSG00000268606.
ENST00000611674; ENSP00000480491; ENSG00000268606.
ENST00000620710; ENSP00000484290; ENSG00000268606.
ENST00000623438; ENSP00000485391; ENSG00000268606.
ENST00000623806; ENSP00000485541; ENSG00000268606.
GeneIDi266740.
4101.
KEGGihsa:266740.
hsa:4101.
UCSCiuc004fgg.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18920 Genomic DNA. Translation: AAA17729.1.
AK290443 mRNA. Translation: BAF83132.1.
U82671 Genomic DNA. No translation available.
CH471169 Genomic DNA. Translation: EAW99429.1.
BC108720 mRNA. Translation: AAI08721.1.
BC112158 mRNA. Translation: AAI12159.1.
BC112160 mRNA. Translation: AAI12161.1.
CCDSiCCDS76046.1.
CCDS76049.1.
PIRiI68889.
RefSeqiNP_001269430.1. NM_001282501.1.
NP_001269431.1. NM_001282502.1.
NP_001269433.1. NM_001282504.1.
NP_001269434.1. NM_001282505.1.
NP_005352.1. NM_005361.3.
NP_705692.1. NM_153488.4.
NP_786884.1. NM_175742.2.
NP_786885.1. NM_175743.2.
XP_011529445.1. XM_011531143.1.
XP_011529461.1. XM_011531159.1.
UniGeneiHs.534597.
Hs.713061.
Hs.736992.

3D structure databases

ProteinModelPortaliP43356.
SMRiP43356. Positions 104-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110275. 6 interactions.
129334. 10 interactions.
DIPiDIP-61231N.
IntActiP43356. 6 interactions.
STRINGi9606.ENSP00000359307.

PTM databases

iPTMnetiP43356.
PhosphoSiteiP43356.

Polymorphism and mutation databases

BioMutaiMAGEA2.
DMDMi1170856.

Proteomic databases

PaxDbiP43356.
PRIDEiP43356.

Protocols and materials databases

DNASUi266740.
4101.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331220; ENSP00000333487; ENSG00000183305.
ENST00000370293; ENSP00000359316; ENSG00000183305.
ENST00000595583; ENSP00000470872; ENSG00000268606.
ENST00000598543; ENSP00000469919; ENSG00000268606.
ENST00000611557; ENSP00000480738; ENSG00000268606.
ENST00000611674; ENSP00000480491; ENSG00000268606.
ENST00000620710; ENSP00000484290; ENSG00000268606.
ENST00000623438; ENSP00000485391; ENSG00000268606.
ENST00000623806; ENSP00000485541; ENSG00000268606.
GeneIDi266740.
4101.
KEGGihsa:266740.
hsa:4101.
UCSCiuc004fgg.3. human.

Organism-specific databases

CTDi266740.
4101.
GeneCardsiMAGEA2.
MAGEA2B.
HGNCiHGNC:6800. MAGEA2.
HGNC:19340. MAGEA2B.
MIMi300173. gene.
300549. gene.
neXtProtiNX_P43356.
PharmGKBiPA30546.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4562. Eukaryota.
ENOG4111S70. LUCA.
GeneTreeiENSGT00760000118824.
HOGENOMiHOG000231161.
HOVERGENiHBG006315.
InParanoidiP43356.
OMAiEPHISYP.
OrthoDBiEOG75F4GM.
PhylomeDBiP43356.
TreeFamiTF328505.

Miscellaneous databases

GeneWikiiMAGEA2.
PROiP43356.
SOURCEiSearch...

Gene expression databases

BgeeiP43356.
CleanExiHS_MAGEA2.
ExpressionAtlasiP43356. baseline and differential.
GenevisibleiP43356. HS.

Family and domain databases

InterProiIPR021072. MAGE_N.
IPR030103. MAGEA2.
IPR002190. MHD_dom.
[Graphical view]
PANTHERiPTHR11736:SF78. PTHR11736:SF78. 1 hit.
PfamiPF01454. MAGE. 1 hit.
PF12440. MAGE_N. 1 hit.
[Graphical view]
SMARTiSM01373. MAGE. 1 hit.
SM01392. MAGE_N. 1 hit.
[Graphical view]
PROSITEiPS50838. MAGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Skin.
  7. "Human gene MAGE-3 codes for an antigen recognized on a melanoma by autologous cytolytic T lymphocytes."
    Gaugler B., van den Eynde B., van der Bruggen P., Romero P., Gaforio J.J., De Plaen E., Lethe B.G., Brasseur F., Boon T.
    J. Exp. Med. 179:921-930(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
    Tissue: Blood.
  8. "MAGE-A tumor antigens target p53 transactivation function through histone deacetylase recruitment and confer resistance to chemotherapeutic agents."
    Monte M., Simonatto M., Peche L.Y., Bublik D.R., Gobessi S., Pierotti M.A., Rodolfo M., Schneider C.
    Proc. Natl. Acad. Sci. U.S.A. 103:11160-11165(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53 AND HDAC3.
  9. "MAGE-A, mMage-b, and MAGE-C proteins form complexes with KAP1 and suppress p53-dependent apoptosis in MAGE-positive cell lines."
    Yang B., O'Herrin S.M., Wu J., Reagan-Shaw S., Ma Y., Bhat K.M., Gravekamp C., Setaluri V., Peters N., Hoffmann F.M., Peng H., Ivanov A.V., Simpson A.J., Longley B.J.
    Cancer Res. 67:9954-9962(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases."
    Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.
    Mol. Cell 39:963-974(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRIM28 AND UBE2H.
  11. "MageA2 restrains cellular senescence by targeting the function of PMLIV/p53 axis at the PML-NBs."
    Peche L.Y., Scolz M., Ladelfa M.F., Monte M., Schneider C.
    Cell Death Differ. 19:926-936(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.

Entry informationi

Entry nameiMAGA2_HUMAN
AccessioniPrimary (citable) accession number: P43356
Secondary accession number(s): A8K328, Q32NC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 140 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 X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.