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Protein

Amine oxidase [flavin-containing] A

Gene

MAOA

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

Functioni

Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.

Catalytic activityi

RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.

Cofactori

FAD2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei335Important for substrate specificityBy similarity1
Sitei374Important for catalytic activity1

GO - Molecular functioni

GO - Biological processi

  • cellular biogenic amine metabolic process Source: ProtInc
  • dopamine catabolic process Source: ParkinsonsUK-UCL
  • neurotransmitter catabolic process Source: UniProtKB-KW
  • neurotransmitter metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Catecholamine metabolism, Neurotransmitter degradation

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS01798-MONOMER.
ZFISH:HS01798-MONOMER.
BRENDAi1.4.3.4. 2681.
ReactomeiR-HSA-141333. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
R-HSA-181430. Norepinephrine Neurotransmitter Release Cycle.
R-HSA-379397. Enzymatic degradation of dopamine by COMT.
R-HSA-379398. Enzymatic degradation of Dopamine by monoamine oxidase.
R-HSA-380612. Metabolism of serotonin.
SABIO-RKP21397.

Names & Taxonomyi

Protein namesi
Recommended name:
Amine oxidase [flavin-containing] A (EC:1.4.3.4)
Alternative name(s):
Monoamine oxidase type A
Short name:
MAO-A
Gene namesi
Name:MAOA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:6833. MAOA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 497Cytoplasmic1 PublicationAdd BLAST497
Transmembranei498 – 518Helical; Anchor for type IV membrane proteinAdd BLAST21
Topological domaini519 – 527Mitochondrial intermembrane1 Publication9

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: ParkinsonsUK-UCL
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Brunner syndrome (BRNRS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of X-linked non-dysmorphic mild mental retardation. Male patients are affected by borderline mental retardation and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior.
See also OMIM:300615

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi165C → S: No loss of activity. 1 Publication1
Mutagenesisi266C → S: No loss of activity. 1 Publication1
Mutagenesisi306C → S: No loss of activity. 1 Publication1
Mutagenesisi321C → S: No loss of activity. 1 Publication1
Mutagenesisi323C → S: No loss of activity. 1 Publication1
Mutagenesisi374C → S: Complete loss of activity. 1 Publication1
Mutagenesisi398C → S: No loss of activity. 1 Publication1
Mutagenesisi406C → S: Complete loss of activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi4128.
MalaCardsiMAOA.
MIMi300615. phenotype.
OpenTargetsiENSG00000189221.
Orphaneti3057. Monoamine oxidase A deficiency.
PharmGKBiPA236.

Chemistry databases

ChEMBLiCHEMBL1951.
DrugBankiDB00918. Almotriptan.
DB06774. Capsaicin.
DB00988. Dopamine.
DB01363. Ephedra.
DB03147. Flavin adenine dinucleotide.
DB00614. Furazolidone.
DB01247. Isocarboxazid.
DB00601. Linezolid.
DB01577. Methamphetamine.
DB00805. Minaprine.
DB01171. Moclobemide.
DB08804. Nandrolone decanoate.
DB00952. Naratriptan.
DB00184. Nicotine.
DB06412. Oxymetholone.
DB01626. Pargyline.
DB00780. Phenelzine.
DB00191. Phentermine.
DB00388. Phenylephrine.
DB00397. Phenylpropanolamine.
DB00721. Procaine.
DB00852. Pseudoephedrine.
DB00140. Riboflavin.
DB00953. Rizatriptan.
DB01037. Selegiline.
DB01104. Sertraline.
DB00669. Sumatriptan.
DB00624. Testosterone.
DB00752. Tranylcypromine.
DB00315. Zolmitriptan.
DB00909. Zonisamide.
GuidetoPHARMACOLOGYi2489.

Polymorphism and mutation databases

BioMutaiMAOA.
DMDMi113978.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000998501 – 527Amine oxidase [flavin-containing] AAdd BLAST527

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei383PhosphoserineBy similarity1
Modified residuei406S-8alpha-FAD cysteine1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP21397.
PaxDbiP21397.
PeptideAtlasiP21397.
PRIDEiP21397.

PTM databases

iPTMnetiP21397.
PhosphoSitePlusiP21397.
SwissPalmiP21397.

Expressioni

Tissue specificityi

Heart, liver, duodenum, blood vessels and kidney.

Gene expression databases

BgeeiENSG00000189221.
CleanExiHS_MAOA.
ExpressionAtlasiP21397. baseline and differential.
GenevisibleiP21397. HS.

Organism-specific databases

HPAiCAB009437.
HPA054807.
HPA059299.

Interactioni

Subunit structurei

Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer.2 Publications

Protein-protein interaction databases

BioGridi110301. 4 interactors.
IntActiP21397. 2 interactors.
MINTiMINT-4054607.
STRINGi9606.ENSP00000340684.

Chemistry databases

BindingDBiP21397.

Structurei

Secondary structure

1527
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 19Combined sources5
Helixi23 – 34Combined sources12
Beta strandi39 – 42Combined sources4
Beta strandi44 – 49Combined sources6
Beta strandi54 – 57Combined sources4
Turni58 – 60Combined sources3
Beta strandi61 – 66Combined sources6
Helixi75 – 83Combined sources9
Beta strandi88 – 90Combined sources3
Beta strandi94 – 101Combined sources8
Beta strandi104 – 108Combined sources5
Beta strandi110 – 112Combined sources3
Helixi118 – 136Combined sources19
Helixi143 – 145Combined sources3
Helixi149 – 154Combined sources6
Helixi157 – 164Combined sources8
Helixi168 – 182Combined sources15
Turni186 – 188Combined sources3
Helixi191 – 199Combined sources9
Turni200 – 202Combined sources3
Helixi204 – 208Combined sources5
Beta strandi211 – 213Combined sources3
Beta strandi216 – 219Combined sources4
Helixi224 – 234Combined sources11
Helixi235 – 237Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi244 – 248Combined sources5
Beta strandi250 – 258Combined sources9
Beta strandi263 – 271Combined sources9
Helixi275 – 278Combined sources4
Beta strandi281 – 285Combined sources5
Helixi289 – 295Combined sources7
Beta strandi303 – 309Combined sources7
Helixi314 – 317Combined sources4
Beta strandi320 – 327Combined sources8
Beta strandi334 – 338Combined sources5
Beta strandi348 – 354Combined sources7
Helixi355 – 361Combined sources7
Helixi366 – 381Combined sources16
Helixi385 – 387Combined sources3
Beta strandi390 – 397Combined sources8
Turni401 – 403Combined sources3
Beta strandi405 – 407Combined sources3
Helixi415 – 418Combined sources4
Helixi420 – 422Combined sources3
Beta strandi430 – 432Combined sources3
Helixi435 – 437Combined sources3
Beta strandi439 – 441Combined sources3
Helixi445 – 462Combined sources18
Beta strandi464 – 466Combined sources3
Helixi469 – 471Combined sources3
Beta strandi479 – 481Combined sources3
Helixi490 – 494Combined sources5
Helixi498 – 520Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H8Qmodel-A14-468[»]
2BXRX-ray3.00A/B1-527[»]
2BXSX-ray3.15A/B1-527[»]
2Z5XX-ray2.20A12-524[»]
2Z5YX-ray2.17A12-524[»]
ProteinModelPortaliP21397.
SMRiP21397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21397.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni520 – 522Interaction with membrane phospholipid headgroupsCurated3

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0029. Eukaryota.
ENOG410XSNC. LUCA.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21397.
KOiK00274.
OMAiDAPWEAP.
OrthoDBiEOG091G0G7P.
PhylomeDBiP21397.
TreeFamiTF313314.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P21397-1) [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
MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG
60 70 80 90 100
RTYTIRNEHV DYVDVGGAYV GPTQNRILRL SKELGIETYK VNVSERLVQY
110 120 130 140 150
VKGKTYPFRG AFPPVWNPIA YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD
160 170 180 190 200
KWDKMTMKEL IDKICWTKTA RRFAYLFVNI NVTSEPHEVS ALWFLWYVKQ
210 220 230 240 250
CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL NHPVTHVDQS
260 270 280 290 300
SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM
310 320 330 340 350
GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM
360 370 380 390 400
GFILARKADR LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE
410 420 430 440 450
QYSGGCYTAY FPPGIMTQYG RVIRQPVGRI FFAGTETATK WSGYMEGAVE
460 470 480 490 500
AGERAAREVL NGLGKVTEKD IWVQEPESKD VPAVEITHTF WERNLPSVSG
510 520
LLKIIGFSTS VTALGFVLYK YKLLPRS
Length:527
Mass (Da):59,682
Last modified:May 1, 1991 - v1
Checksum:i4270E346928AE832
GO
Isoform 2 (identifier: P21397-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Show »
Length:394
Mass (Da):44,848
Checksum:iCA2429F72CD7F231
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti397W → M AA sequence (PubMed:3178846).Curated1

Mass spectrometryi

Molecular mass is 60512±6 Da from positions 1 - 527. Determined by ESI. 1 Publication

Polymorphismi

A polymorphism 1.2 kb upstream of the MAOA coding sequences consists of a 30-bp repeated sequence present in 3, 3.5, 4, or 5 copies. The polymorphism affect transcriptional activity of the MAOA gene promoter. Alleles with 3.5 or 4 copies of the repeat sequence are transcribed 2 to 10 times more efficiently than those with 3 or 5 copies of the repeat.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03654515D → E in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_064573188E → K.1 PublicationCorresponds to variant rs77698881dbSNPEnsembl.1
Natural variantiVAR_071963266C → F Probable disease-associated mutation found in a family with Brunner syndrome-like behavioral disturbances; reduced activity. 1 PublicationCorresponds to variant rs587777457dbSNPEnsembl.1
Natural variantiVAR_014795314F → V.Corresponds to variant rs1799835dbSNPEnsembl.1
Natural variantiVAR_014796520K → R.Corresponds to variant rs1800466dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0451731 – 133Missing in isoform 2. 1 PublicationAdd BLAST133

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69226 mRNA. Translation: AAA59549.1.
M68840 mRNA. Translation: AAA59548.1.
X60806 Genomic DNA. No translation available.
X60807 Genomic DNA. No translation available.
X60808 Genomic DNA. No translation available.
X60809 Genomic DNA. No translation available.
X60810 Genomic DNA. No translation available.
X60811 Genomic DNA. No translation available.
X60812 Genomic DNA. No translation available.
X60813 Genomic DNA. No translation available.
X60814 Genomic DNA. No translation available.
X60815 Genomic DNA. No translation available.
X60816 Genomic DNA. No translation available.
X60817 Genomic DNA. No translation available.
X60818 Genomic DNA. No translation available.
X60819 Genomic DNA. No translation available.
M68857
, M68843, M68844, M68845, M68846, M68847, M68848, M68849, M68850, M68851, M68852, M68853, M68854, M68855, M68856 Genomic DNA. Translation: AAA59547.1.
AK293926 mRNA. Translation: BAG57307.1.
AL109855 Genomic DNA. No translation available.
BX530072 Genomic DNA. No translation available.
BX537147 Genomic DNA. No translation available.
BX537148 Genomic DNA. No translation available.
BC008064 mRNA. Translation: AAH08064.1.
M89636 Genomic DNA. Translation: AAB46385.1.
S81371 Genomic DNA. Translation: AAD14361.1.
S72704 Genomic DNA. Translation: AAD14113.1.
CCDSiCCDS14260.1. [P21397-1]
CCDS59163.1. [P21397-2]
PIRiA36175.
RefSeqiNP_000231.1. NM_000240.3. [P21397-1]
NP_001257387.1. NM_001270458.1. [P21397-2]
UniGeneiHs.183109.

Genome annotation databases

EnsembliENST00000338702; ENSP00000340684; ENSG00000189221. [P21397-1]
ENST00000542639; ENSP00000440846; ENSG00000189221. [P21397-2]
GeneIDi4128.
KEGGihsa:4128.
UCSCiuc011mkw.3. human. [P21397-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Monoamine oxidase entry

Protein Spotlight

Approaching happiness - Issue 172 of August 2015

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69226 mRNA. Translation: AAA59549.1.
M68840 mRNA. Translation: AAA59548.1.
X60806 Genomic DNA. No translation available.
X60807 Genomic DNA. No translation available.
X60808 Genomic DNA. No translation available.
X60809 Genomic DNA. No translation available.
X60810 Genomic DNA. No translation available.
X60811 Genomic DNA. No translation available.
X60812 Genomic DNA. No translation available.
X60813 Genomic DNA. No translation available.
X60814 Genomic DNA. No translation available.
X60815 Genomic DNA. No translation available.
X60816 Genomic DNA. No translation available.
X60817 Genomic DNA. No translation available.
X60818 Genomic DNA. No translation available.
X60819 Genomic DNA. No translation available.
M68857
, M68843, M68844, M68845, M68846, M68847, M68848, M68849, M68850, M68851, M68852, M68853, M68854, M68855, M68856 Genomic DNA. Translation: AAA59547.1.
AK293926 mRNA. Translation: BAG57307.1.
AL109855 Genomic DNA. No translation available.
BX530072 Genomic DNA. No translation available.
BX537147 Genomic DNA. No translation available.
BX537148 Genomic DNA. No translation available.
BC008064 mRNA. Translation: AAH08064.1.
M89636 Genomic DNA. Translation: AAB46385.1.
S81371 Genomic DNA. Translation: AAD14361.1.
S72704 Genomic DNA. Translation: AAD14113.1.
CCDSiCCDS14260.1. [P21397-1]
CCDS59163.1. [P21397-2]
PIRiA36175.
RefSeqiNP_000231.1. NM_000240.3. [P21397-1]
NP_001257387.1. NM_001270458.1. [P21397-2]
UniGeneiHs.183109.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H8Qmodel-A14-468[»]
2BXRX-ray3.00A/B1-527[»]
2BXSX-ray3.15A/B1-527[»]
2Z5XX-ray2.20A12-524[»]
2Z5YX-ray2.17A12-524[»]
ProteinModelPortaliP21397.
SMRiP21397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110301. 4 interactors.
IntActiP21397. 2 interactors.
MINTiMINT-4054607.
STRINGi9606.ENSP00000340684.

Chemistry databases

BindingDBiP21397.
ChEMBLiCHEMBL1951.
DrugBankiDB00918. Almotriptan.
DB06774. Capsaicin.
DB00988. Dopamine.
DB01363. Ephedra.
DB03147. Flavin adenine dinucleotide.
DB00614. Furazolidone.
DB01247. Isocarboxazid.
DB00601. Linezolid.
DB01577. Methamphetamine.
DB00805. Minaprine.
DB01171. Moclobemide.
DB08804. Nandrolone decanoate.
DB00952. Naratriptan.
DB00184. Nicotine.
DB06412. Oxymetholone.
DB01626. Pargyline.
DB00780. Phenelzine.
DB00191. Phentermine.
DB00388. Phenylephrine.
DB00397. Phenylpropanolamine.
DB00721. Procaine.
DB00852. Pseudoephedrine.
DB00140. Riboflavin.
DB00953. Rizatriptan.
DB01037. Selegiline.
DB01104. Sertraline.
DB00669. Sumatriptan.
DB00624. Testosterone.
DB00752. Tranylcypromine.
DB00315. Zolmitriptan.
DB00909. Zonisamide.
GuidetoPHARMACOLOGYi2489.

PTM databases

iPTMnetiP21397.
PhosphoSitePlusiP21397.
SwissPalmiP21397.

Polymorphism and mutation databases

BioMutaiMAOA.
DMDMi113978.

Proteomic databases

EPDiP21397.
PaxDbiP21397.
PeptideAtlasiP21397.
PRIDEiP21397.

Protocols and materials databases

DNASUi4128.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338702; ENSP00000340684; ENSG00000189221. [P21397-1]
ENST00000542639; ENSP00000440846; ENSG00000189221. [P21397-2]
GeneIDi4128.
KEGGihsa:4128.
UCSCiuc011mkw.3. human. [P21397-1]

Organism-specific databases

CTDi4128.
DisGeNETi4128.
GeneCardsiMAOA.
HGNCiHGNC:6833. MAOA.
HPAiCAB009437.
HPA054807.
HPA059299.
MalaCardsiMAOA.
MIMi300615. phenotype.
309850. gene.
neXtProtiNX_P21397.
OpenTargetsiENSG00000189221.
Orphaneti3057. Monoamine oxidase A deficiency.
PharmGKBiPA236.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0029. Eukaryota.
ENOG410XSNC. LUCA.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21397.
KOiK00274.
OMAiDAPWEAP.
OrthoDBiEOG091G0G7P.
PhylomeDBiP21397.
TreeFamiTF313314.

Enzyme and pathway databases

BioCyciMetaCyc:HS01798-MONOMER.
ZFISH:HS01798-MONOMER.
BRENDAi1.4.3.4. 2681.
ReactomeiR-HSA-141333. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
R-HSA-181430. Norepinephrine Neurotransmitter Release Cycle.
R-HSA-379397. Enzymatic degradation of dopamine by COMT.
R-HSA-379398. Enzymatic degradation of Dopamine by monoamine oxidase.
R-HSA-380612. Metabolism of serotonin.
SABIO-RKP21397.

Miscellaneous databases

ChiTaRSiMAOA. human.
EvolutionaryTraceiP21397.
GeneWikiiMonoamine_oxidase_A.
GenomeRNAii4128.
PROiP21397.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000189221.
CleanExiHS_MAOA.
ExpressionAtlasiP21397. baseline and differential.
GenevisibleiP21397. HS.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiAOFA_HUMAN
AccessioniPrimary (citable) accession number: P21397
Secondary accession number(s): B4DF46, Q16426
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 30, 2016
This is version 192 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  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.