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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei335 – 3351Important for substrate specificityBy similarity
Sitei374 – 3741Important for catalytic activity

GO - Molecular functioni

GO - Biological processi

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.
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.
R-HSA-5579012. Defective MAOA causes Brunner syndrome (BRUNS).
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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 497497Cytoplasmic1 PublicationAdd
BLAST
Transmembranei498 – 51821Helical; Anchor for type IV membrane proteinAdd
BLAST
Topological domaini519 – 5279Mitochondrial intermembrane1 Publication

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 (BRUNS)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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651C → S: No loss of activity. 1 Publication
Mutagenesisi266 – 2661C → S: No loss of activity. 1 Publication
Mutagenesisi306 – 3061C → S: No loss of activity. 1 Publication
Mutagenesisi321 – 3211C → S: No loss of activity. 1 Publication
Mutagenesisi323 – 3231C → S: No loss of activity. 1 Publication
Mutagenesisi374 – 3741C → S: Complete loss of activity. 1 Publication
Mutagenesisi398 – 3981C → S: No loss of activity. 1 Publication
Mutagenesisi406 – 4061C → S: Complete loss of activity. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiMAOA.
MIMi300615. phenotype.
309850. gene+phenotype.
Orphaneti3057. Monoamine oxidase A deficiency.
PharmGKBiPA236.

Chemistry

ChEMBLiCHEMBL2095205.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527Amine oxidase [flavin-containing] APRO_0000099850Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei383 – 3831PhosphoserineBy similarity
Modified residuei406 – 4061S-8alpha-FAD cysteine

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP21397.
PaxDbiP21397.
PeptideAtlasiP21397.
PRIDEiP21397.

PTM databases

iPTMnetiP21397.
PhosphoSiteiP21397.
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. 3 interactions.
IntActiP21397. 2 interactions.
MINTiMINT-4054607.
STRINGi9606.ENSP00000340684.

Chemistry

BindingDBiP21397.

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 195Combined sources
Helixi23 – 3412Combined sources
Beta strandi39 – 424Combined sources
Beta strandi44 – 496Combined sources
Beta strandi54 – 574Combined sources
Turni58 – 603Combined sources
Beta strandi61 – 666Combined sources
Helixi75 – 839Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 1018Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi110 – 1123Combined sources
Helixi118 – 13619Combined sources
Helixi143 – 1453Combined sources
Helixi149 – 1546Combined sources
Helixi157 – 1648Combined sources
Helixi168 – 18215Combined sources
Turni186 – 1883Combined sources
Helixi191 – 1999Combined sources
Turni200 – 2023Combined sources
Helixi204 – 2085Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi216 – 2194Combined sources
Helixi224 – 23411Combined sources
Helixi235 – 2373Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi250 – 2589Combined sources
Beta strandi263 – 2719Combined sources
Helixi275 – 2784Combined sources
Beta strandi281 – 2855Combined sources
Helixi289 – 2957Combined sources
Beta strandi303 – 3097Combined sources
Helixi314 – 3174Combined sources
Beta strandi320 – 3278Combined sources
Beta strandi334 – 3385Combined sources
Beta strandi348 – 3547Combined sources
Helixi355 – 3617Combined sources
Helixi366 – 38116Combined sources
Helixi385 – 3873Combined sources
Beta strandi390 – 3978Combined sources
Turni401 – 4033Combined sources
Beta strandi405 – 4073Combined sources
Helixi415 – 4184Combined sources
Helixi420 – 4223Combined sources
Beta strandi430 – 4323Combined sources
Helixi435 – 4373Combined sources
Beta strandi439 – 4413Combined sources
Helixi445 – 46218Combined sources
Beta strandi464 – 4663Combined sources
Helixi469 – 4713Combined sources
Beta strandi479 – 4813Combined sources
Helixi490 – 4945Combined sources
Helixi498 – 52023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 12-524.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21397.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni520 – 5223Interaction with membrane phospholipid headgroupsCurated

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971W → M AA sequence (PubMed:3178846).Curated

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151D → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_036545
Natural varianti188 – 1881E → K.1 Publication
Corresponds to variant rs77698881 [ dbSNP | Ensembl ].
VAR_064573
Natural varianti266 – 2661C → F Probable disease-associated mutation found in a family with Brunner syndrome-like behavioral disturbances; reduced activity. 1 Publication
Corresponds to variant rs587777457 [ dbSNP | Ensembl ].
VAR_071963
Natural varianti314 – 3141F → V.
Corresponds to variant rs1799835 [ dbSNP | Ensembl ].
VAR_014795
Natural varianti520 – 5201K → R.
Corresponds to variant rs1800466 [ dbSNP | Ensembl ].
VAR_014796

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 2. 1 PublicationVSP_045173Add
BLAST

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
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. Positions 12-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110301. 3 interactions.
IntActiP21397. 2 interactions.
MINTiMINT-4054607.
STRINGi9606.ENSP00000340684.

Chemistry

BindingDBiP21397.
ChEMBLiCHEMBL2095205.
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.
PhosphoSiteiP21397.
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.
GeneCardsiMAOA.
HGNCiHGNC:6833. MAOA.
HPAiCAB009437.
HPA054807.
HPA059299.
MalaCardsiMAOA.
MIMi300615. phenotype.
309850. gene+phenotype.
neXtProtiNX_P21397.
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.
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.
R-HSA-5579012. Defective MAOA causes Brunner syndrome (BRUNS).
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: September 7, 2016
This is version 189 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.