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Q03154

- ACY1_HUMAN

UniProt

Q03154 - ACY1_HUMAN

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Protein

Aminoacylase-1

Gene
ACY1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).1 Publication

Catalytic activityi

An N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate.1 Publication
An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate.1 Publication

Cofactori

Binds 2 zinc ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Zinc 1
Active sitei82 – 821 By similarity
Metal bindingi113 – 1131Zinc 1
Metal bindingi113 – 1131Zinc 2
Active sitei147 – 1471Proton acceptor1 Publication
Metal bindingi148 – 1481Zinc 2
Metal bindingi175 – 1751Zinc 1
Metal bindingi373 – 3731Zinc 2

GO - Molecular functioni

  1. aminoacylase activity Source: ProtInc
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS03800-MONOMER.
BRENDAi3.5.1.14. 2681.
SABIO-RKQ03154.

Protein family/group databases

MEROPSiM20.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacylase-1 (EC:3.5.1.14)
Short name:
ACY-1
Alternative name(s):
N-acyl-L-amino-acid amidohydrolase
Gene namesi
Name:ACY1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:177. ACY1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: ProtInc
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Aminoacylase-1 deficiency (ACY1D) [MIM:609924]: An enzymatic deficiency resulting in encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature. All affected individuals exhibit markedly increased urinary excretion of several N-acetylated amino acids.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti197 – 1971R → W in ACY1D; loss of activity. 2 Publications
VAR_043113
Natural varianti233 – 2331E → D in ACY1D; loss of activity. 2 Publications
VAR_026104
Natural varianti353 – 3531R → C in ACY1D; loss of activity. 4 Publications
Corresponds to variant rs121912698 [ dbSNP | Ensembl ].
VAR_026105
Natural varianti378 – 3781R → Q in ACY1D. 1 Publication
VAR_065562
Natural varianti378 – 3781R → W in ACY1D; slightly reduced activity. 1 Publication
VAR_065563
Natural varianti386 – 3861R → C in ACY1D; loss of activity. 1 Publication
Corresponds to variant rs2229152 [ dbSNP | Ensembl ].
VAR_020452
Natural varianti393 – 3931R → H in ACY1D. 1 Publication
Corresponds to variant rs121912701 [ dbSNP | Ensembl ].
VAR_043114

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801H → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi113 – 1131D → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi147 – 1471E → A or Q: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi147 – 1471E → D: Decreased protein stability. Loss of enzyme activity. 1 Publication
Mutagenesisi148 – 1481E → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi175 – 1751E → A: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi206 – 2061H → N: Almost abolishes enzyme activity. 1 Publication
Mutagenesisi373 – 3731H → A: Almost abolishes enzyme activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi609924. phenotype.
Orphaneti137754. Neurological conditions associated with aminoacylase 1 deficiency.
PharmGKBiPA24497.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 408407Aminoacylase-1PRO_0000185236Add
BLAST

Proteomic databases

MaxQBiQ03154.
PaxDbiQ03154.
PeptideAtlasiQ03154.
PRIDEiQ03154.

2D gel databases

REPRODUCTION-2DPAGEIPI00009268.

PTM databases

PhosphoSiteiQ03154.

Expressioni

Tissue specificityi

Expression is highest in kidney, strong in brain and weaker in placenta and spleen.1 Publication

Gene expression databases

BgeeiQ03154.
CleanExiHS_ACY1.
GenevestigatoriQ03154.

Organism-specific databases

HPAiCAB003695.
HPA036174.
HPA036175.

Interactioni

Subunit structurei

Homodimer. Interacts with SPHK1 By similarity.1 Publication

Protein-protein interaction databases

BioGridi106610. 9 interactions.
IntActiQ03154. 5 interactions.
MINTiMINT-4999851.
STRINGi9606.ENSP00000232907.

Structurei

Secondary structure

1
408
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2010
Helixi31 – 4515
Beta strandi48 – 558
Beta strandi58 – 658
Beta strandi74 – 807
Helixi88 – 903
Turni95 – 973
Beta strandi104 – 1074
Turni109 – 1146
Helixi115 – 13016
Beta strandi139 – 1457
Helixi147 – 1493
Turni152 – 1543
Helixi155 – 1584
Helixi162 – 1654
Beta strandi169 – 1746
Beta strandi180 – 1889
Helixi194 – 1963
Helixi322 – 33312
Beta strandi338 – 3425
Helixi348 – 3547
Beta strandi359 – 3624
Beta strandi378 – 3803
Helixi381 – 39919
Helixi405 – 4073

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7LX-ray1.40A/C1-198[»]
B/D321-408[»]
ProteinModelPortaliQ03154.
SMRiQ03154. Positions 7-408.

Miscellaneous databases

EvolutionaryTraceiQ03154.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.

Phylogenomic databases

eggNOGiCOG0624.
HOGENOMiHOG000021196.
HOVERGENiHBG000982.
InParanoidiQ03154.
KOiK14677.
PhylomeDBiQ03154.
TreeFamiTF313693.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF036696. ACY-1. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q03154-1) [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

MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ    50
KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK 100
DSEGYIYARG AQDMKCVSIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG 150
GHQGMELFVQ RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS 200
TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS 250
VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG 300
VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR 350
YIRAVGVPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS 400
VPALPSDS 408
Length:408
Mass (Da):45,885
Last modified:February 1, 1994 - v1
Checksum:i293350CD7759826C
GO
Isoform 2 (identifier: Q03154-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     103-174: Missing.

Note: Gene prediction based on EST data.

Show »
Length:336
Mass (Da):37,597
Checksum:i68C1E4266A8CBE70
GO
Isoform 3 (identifier: Q03154-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     220-284: Missing.

Note: Gene prediction based on EST data.

Show »
Length:343
Mass (Da):38,629
Checksum:i75F9FBDC8348189E
GO
Isoform 4 (identifier: Q03154-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     32-66: Missing.

Note: Gene prediction based on EST data.

Show »
Length:373
Mass (Da):42,195
Checksum:i343DC089BDBDC22F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791N → S.
Corresponds to variant rs887540 [ dbSNP | Ensembl ].
VAR_051805
Natural varianti197 – 1971R → W in ACY1D; loss of activity. 2 Publications
VAR_043113
Natural varianti233 – 2331E → D in ACY1D; loss of activity. 2 Publications
VAR_026104
Natural varianti353 – 3531R → C in ACY1D; loss of activity. 4 Publications
Corresponds to variant rs121912698 [ dbSNP | Ensembl ].
VAR_026105
Natural varianti378 – 3781R → Q in ACY1D. 1 Publication
VAR_065562
Natural varianti378 – 3781R → W in ACY1D; slightly reduced activity. 1 Publication
VAR_065563
Natural varianti381 – 3811E → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036076
Natural varianti386 – 3861R → C in ACY1D; loss of activity. 1 Publication
Corresponds to variant rs2229152 [ dbSNP | Ensembl ].
VAR_020452
Natural varianti393 – 3931R → H in ACY1D. 1 Publication
Corresponds to variant rs121912701 [ dbSNP | Ensembl ].
VAR_043114

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 6635Missing in isoform 4. VSP_046876Add
BLAST
Alternative sequencei103 – 17472Missing in isoform 2. VSP_046877Add
BLAST
Alternative sequencei220 – 28465Missing in isoform 3. VSP_046878Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07548 mRNA. Translation: AAA02852.1.
D14524 mRNA. Translation: BAA03397.1.
D16307 mRNA. Translation: BAA03814.1.
AC115284 Genomic DNA. No translation available.
BC000545 mRNA. Translation: AAH00545.1.
BC003023 mRNA. Translation: AAH03023.1.
BC014112 mRNA. Translation: AAH14112.1.
CCDSiCCDS2844.1. [Q03154-1]
CCDS56261.1. [Q03154-2]
CCDS56262.1. [Q03154-3]
CCDS56263.1. [Q03154-4]
PIRiA47488.
RefSeqiNP_000657.1. NM_000666.2. [Q03154-1]
NP_001185824.1. NM_001198895.1. [Q03154-1]
NP_001185825.1. NM_001198896.1. [Q03154-2]
NP_001185826.1. NM_001198897.1. [Q03154-3]
NP_001185827.1. NM_001198898.1. [Q03154-4]
UniGeneiHs.334707.

Genome annotation databases

EnsembliENST00000404366; ENSP00000384296; ENSG00000243989. [Q03154-1]
ENST00000476351; ENSP00000417056; ENSG00000243989. [Q03154-4]
ENST00000476854; ENSP00000419262; ENSG00000243989. [Q03154-3]
ENST00000494103; ENSP00000417618; ENSG00000243989. [Q03154-2]
GeneIDi95.
KEGGihsa:95.
UCSCiuc003dcp.3. human. [Q03154-1]

Polymorphism databases

DMDMi461466.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07548 mRNA. Translation: AAA02852.1 .
D14524 mRNA. Translation: BAA03397.1 .
D16307 mRNA. Translation: BAA03814.1 .
AC115284 Genomic DNA. No translation available.
BC000545 mRNA. Translation: AAH00545.1 .
BC003023 mRNA. Translation: AAH03023.1 .
BC014112 mRNA. Translation: AAH14112.1 .
CCDSi CCDS2844.1. [Q03154-1 ]
CCDS56261.1. [Q03154-2 ]
CCDS56262.1. [Q03154-3 ]
CCDS56263.1. [Q03154-4 ]
PIRi A47488.
RefSeqi NP_000657.1. NM_000666.2. [Q03154-1 ]
NP_001185824.1. NM_001198895.1. [Q03154-1 ]
NP_001185825.1. NM_001198896.1. [Q03154-2 ]
NP_001185826.1. NM_001198897.1. [Q03154-3 ]
NP_001185827.1. NM_001198898.1. [Q03154-4 ]
UniGenei Hs.334707.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Q7L X-ray 1.40 A/C 1-198 [» ]
B/D 321-408 [» ]
ProteinModelPortali Q03154.
SMRi Q03154. Positions 7-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106610. 9 interactions.
IntActi Q03154. 5 interactions.
MINTi MINT-4999851.
STRINGi 9606.ENSP00000232907.

Chemistry

DrugBanki DB00128. L-Aspartic Acid.

Protein family/group databases

MEROPSi M20.973.

PTM databases

PhosphoSitei Q03154.

Polymorphism databases

DMDMi 461466.

2D gel databases

REPRODUCTION-2DPAGE IPI00009268.

Proteomic databases

MaxQBi Q03154.
PaxDbi Q03154.
PeptideAtlasi Q03154.
PRIDEi Q03154.

Protocols and materials databases

DNASUi 95.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000404366 ; ENSP00000384296 ; ENSG00000243989 . [Q03154-1 ]
ENST00000476351 ; ENSP00000417056 ; ENSG00000243989 . [Q03154-4 ]
ENST00000476854 ; ENSP00000419262 ; ENSG00000243989 . [Q03154-3 ]
ENST00000494103 ; ENSP00000417618 ; ENSG00000243989 . [Q03154-2 ]
GeneIDi 95.
KEGGi hsa:95.
UCSCi uc003dcp.3. human. [Q03154-1 ]

Organism-specific databases

CTDi 95.
GeneCardsi GC03P052017.
HGNCi HGNC:177. ACY1.
HPAi CAB003695.
HPA036174.
HPA036175.
MIMi 104620. gene.
609924. phenotype.
neXtProti NX_Q03154.
Orphaneti 137754. Neurological conditions associated with aminoacylase 1 deficiency.
PharmGKBi PA24497.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0624.
HOGENOMi HOG000021196.
HOVERGENi HBG000982.
InParanoidi Q03154.
KOi K14677.
PhylomeDBi Q03154.
TreeFami TF313693.

Enzyme and pathway databases

BioCyci MetaCyc:HS03800-MONOMER.
BRENDAi 3.5.1.14. 2681.
SABIO-RK Q03154.

Miscellaneous databases

ChiTaRSi ACY1. human.
EvolutionaryTracei Q03154.
GeneWikii ACY1.
GenomeRNAii 95.
NextBioi 361.
PROi Q03154.
SOURCEi Search...

Gene expression databases

Bgeei Q03154.
CleanExi HS_ACY1.
Genevestigatori Q03154.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036696. ACY-1. 1 hit.
SUPFAMi SSF55031. SSF55031. 1 hit.
TIGRFAMsi TIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEi PS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of human aminoacylase-1."
    Mitta M., Kato I., Tsunasawa S.
    Biochim. Biophys. Acta 1174:201-203(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer."
    Cook R.M., Burke B.J., Buchhagen D.L., Minna J.D., Miller Y.E.
    J. Biol. Chem. 268:17010-17017(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. Iwaki K., Tanaka Y., Ohta T., Fukuda S., Kurimoto M.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Brain, Lung and Skin.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family."
    Lindner H.A., Lunin V.V., Alary A., Hecker R., Cygler M., Menard R.
    J. Biol. Chem. 278:44496-44504(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-80; ASP-113; GLU-147; GLU-148; GLU-175; HIS-206 AND HIS-373.
  8. Cited for: VARIANT ACY1D CYS-353.
  9. Cited for: VARIANTS ACY1D ASP-233 AND CYS-353, TISSUE SPECIFICITY.
  10. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-381.
  11. Cited for: VARIANTS ACY1D TRP-197; CYS-353 AND HIS-393.
  12. Cited for: VARIANTS ACY1D GLN-378; TRP-378 AND CYS-386, CHARACTERIZATION OF VARIANTS ACY1D TRP-197; ASP-233; CYS-353; TRP-378 AND CYS-386.

Entry informationi

Entry nameiACY1_HUMAN
AccessioniPrimary (citable) accession number: Q03154
Secondary accession number(s): C9J6I6, C9J9D8, C9JWD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 145 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 3
    Human chromosome 3: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi