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O75844

- FACE1_HUMAN

UniProt

O75844 - FACE1_HUMAN

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Protein

CAAX prenyl protease 1 homolog

Gene

ZMPSTE24

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

Functioni

Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C.

Catalytic activityi

The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi335 – 3351Zinc; catalytic
Active sitei336 – 33611 Publication
Metal bindingi339 – 3391Zinc; catalytic
Metal bindingi415 – 4151Zinc; catalytic
Active sitei419 – 4191Proton donorBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: Ensembl
  3. metalloexopeptidase activity Source: ProtInc

GO - Biological processi

  1. CAAX-box protein processing Source: InterPro
  2. nuclear envelope organization Source: Ensembl
  3. prenylated protein catabolic process Source: Ensembl
  4. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.84. 2681.

Protein family/group databases

MEROPSiM48.003.
TCDBi9.B.1.1.1. the integral membrane caax protease (caax protease) family.

Names & Taxonomyi

Protein namesi
Recommended name:
CAAX prenyl protease 1 homolog (EC:3.4.24.84)
Alternative name(s):
Farnesylated proteins-converting enzyme 1
Short name:
FACE-1
Prenyl protein-specific endoprotease 1
Zinc metalloproteinase Ste24 homolog
Gene namesi
Name:ZMPSTE24
Synonyms:FACE1, STE24
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:12877. ZMPSTE24.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Nucleus inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818LumenalSequence AnalysisAdd
BLAST
Transmembranei19 – 3921HelicalSequence AnalysisAdd
BLAST
Topological domaini40 – 8142NuclearSequence AnalysisAdd
BLAST
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Topological domaini103 – 12321LumenalSequence AnalysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence AnalysisAdd
BLAST
Topological domaini145 – 17026NuclearSequence AnalysisAdd
BLAST
Transmembranei171 – 19121HelicalSequence AnalysisAdd
BLAST
Topological domaini192 – 1954LumenalSequence Analysis
Transmembranei196 – 21621HelicalSequence AnalysisAdd
BLAST
Topological domaini217 – 347131NuclearSequence AnalysisAdd
BLAST
Transmembranei348 – 36821HelicalSequence AnalysisAdd
BLAST
Topological domaini369 – 38214LumenalSequence AnalysisAdd
BLAST
Transmembranei383 – 40523HelicalSequence AnalysisAdd
BLAST
Topological domaini406 – 47570NuclearSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Mandibuloacral dysplasia with type B lipodystrophy (MADB) [MIM:608612]: A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, joint contractures, and generalized lipodystrophy with loss of subcutaneous fat from the extremities, face, neck and trunk.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti248 – 2481P → L in MADB; found in compound heterozygotes carrying a null allele; does not affect enzyme activity. 2 Publications
VAR_064501
Natural varianti265 – 2651N → S in MADB. 1 Publication
VAR_064502
Natural varianti340 – 3401W → R in MADB. 1 Publication
VAR_019308
Lethal tight skin contracture syndrome (LTSCS) [MIM:275210]: Rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi275210. phenotype.
608612. phenotype.
Orphaneti740. Hutchinson-Gilford progeria syndrome.
1662. Lethal restrictive dermopathy.
90154. Mandibuloacral dysplasia with type B lipodystrophy.
PharmGKBiPA37466.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 475475CAAX prenyl protease 1 homologPRO_0000138844Add
BLAST

Proteomic databases

MaxQBiO75844.
PaxDbiO75844.
PeptideAtlasiO75844.
PRIDEiO75844.

PTM databases

PhosphoSiteiO75844.

Expressioni

Tissue specificityi

Widely expressed. High levels in kidney, prostate, testis and ovary.

Gene expression databases

BgeeiO75844.
CleanExiHS_ZMPSTE24.
ExpressionAtlasiO75844. baseline and differential.
GenevestigatoriO75844.

Organism-specific databases

HPAiHPA006988.

Interactioni

Protein-protein interaction databases

BioGridi115560. 26 interactions.
IntActiO75844. 2 interactions.
STRINGi9606.ENSP00000361845.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133Combined sources
Helixi16 – 4732Combined sources
Helixi54 – 563Combined sources
Helixi61 – 9535Combined sources
Helixi97 – 1048Combined sources
Helixi117 – 14731Combined sources
Helixi149 – 1524Combined sources
Helixi160 – 19132Combined sources
Helixi196 – 21520Combined sources
Turni216 – 2194Combined sources
Helixi220 – 2234Combined sources
Beta strandi226 – 2283Combined sources
Helixi233 – 24412Combined sources
Beta strandi249 – 2557Combined sources
Helixi257 – 2593Combined sources
Beta strandi266 – 2738Combined sources
Beta strandi275 – 2806Combined sources
Helixi281 – 2844Combined sources
Helixi326 – 34116Combined sources
Helixi344 – 36623Combined sources
Helixi371 – 3755Combined sources
Helixi384 – 39310Combined sources
Helixi397 – 42428Combined sources
Turni425 – 4273Combined sources
Helixi428 – 44114Combined sources
Helixi450 – 4556Combined sources
Helixi462 – 47110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YPTX-ray3.80A/B/D/E1-475[»]
4AW6X-ray3.40A/B/D/E1-475[»]
ProteinModelPortaliO75844.
SMRiO75844. Positions 2-472.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The metalloprotease domain is constituted by the two C-terminal nuclear regions.

Sequence similaritiesi

Belongs to the peptidase M48A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0501.
GeneTreeiENSGT00390000002053.
HOGENOMiHOG000257874.
HOVERGENiHBG051541.
InParanoidiO75844.
KOiK06013.
OMAiSEVEGTM.
OrthoDBiEOG7RRF70.
PhylomeDBiO75844.
TreeFamiTF105972.

Family and domain databases

InterProiIPR027057. CAXX_Prtase_1.
IPR001915. Peptidase_M48.
[Graphical view]
PANTHERiPTHR10120:SF24. PTHR10120:SF24. 1 hit.
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75844-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGMWASLDAL WEMPAEKRIF GAVLLFSWTV YLWETFLAQR QRRIYKTTTH
60 70 80 90 100
VPPELGQIMD SETFEKSRLY QLDKSTFSFW SGLYSETEGT LILLFGGIPY
110 120 130 140 150
LWRLSGRFCG YAGFGPEYEI TQSLVFLLLA TLFSALTGLP WSLYNTFVIE
160 170 180 190 200
EKHGFNQQTL GFFMKDAIKK FVVTQCILLP VSSLLLYIIK IGGDYFFIYA
210 220 230 240 250
WLFTLVVSLV LVTIYADYIA PLFDKFTPLP EGKLKEEIEV MAKSIDFPLT
260 270 280 290 300
KVYVVEGSKR SSHSNAYFYG FFKNKRIVLF DTLLEEYSVL NKDIQEDSGM
310 320 330 340 350
EPRNEEEGNS EEIKAKVKNK KQGCKNEEVL AVLGHELGHW KLGHTVKNII
360 370 380 390 400
ISQMNSFLCF FLFAVLIGRK ELFAAFGFYD SQPTLIGLLI IFQFIFSPYN
410 420 430 440 450
EVLSFCLTVL SRRFEFQADA FAKKLGKAKD LYSALIKLNK DNLGFPVSDW
460 470
LFSMWHYSHP PLLERLQALK TMKQH
Length:475
Mass (Da):54,813
Last modified:April 27, 2001 - v2
Checksum:i6C49179DEB0C8F7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161E → K in BAA33727. (PubMed:10076063)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371T → A.1 Publication
Corresponds to variant rs17853725 [ dbSNP | Ensembl ].
VAR_034711
Natural varianti248 – 2481P → L in MADB; found in compound heterozygotes carrying a null allele; does not affect enzyme activity. 2 Publications
VAR_064501
Natural varianti265 – 2651N → S in MADB. 1 Publication
VAR_064502
Natural varianti340 – 3401W → R in MADB. 1 Publication
VAR_019308

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016068 mRNA. Translation: BAA33727.1.
AF064867 mRNA. Translation: AAC68866.1.
Y13834 mRNA. Translation: CAB46277.1.
AK075007 mRNA. Translation: BAG52049.1.
AL050341 Genomic DNA. Translation: CAB81610.1.
CH471059 Genomic DNA. Translation: EAX07233.1.
CH471059 Genomic DNA. Translation: EAX07234.1.
BC037283 mRNA. Translation: AAH37283.1.
CCDSiCCDS449.1.
RefSeqiNP_005848.2. NM_005857.4.
UniGeneiHs.132642.
Hs.721062.

Genome annotation databases

EnsembliENST00000372759; ENSP00000361845; ENSG00000084073.
GeneIDi10269.
KEGGihsa:10269.
UCSCiuc001cfg.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016068 mRNA. Translation: BAA33727.1 .
AF064867 mRNA. Translation: AAC68866.1 .
Y13834 mRNA. Translation: CAB46277.1 .
AK075007 mRNA. Translation: BAG52049.1 .
AL050341 Genomic DNA. Translation: CAB81610.1 .
CH471059 Genomic DNA. Translation: EAX07233.1 .
CH471059 Genomic DNA. Translation: EAX07234.1 .
BC037283 mRNA. Translation: AAH37283.1 .
CCDSi CCDS449.1.
RefSeqi NP_005848.2. NM_005857.4.
UniGenei Hs.132642.
Hs.721062.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YPT X-ray 3.80 A/B/D/E 1-475 [» ]
4AW6 X-ray 3.40 A/B/D/E 1-475 [» ]
ProteinModelPortali O75844.
SMRi O75844. Positions 2-472.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115560. 26 interactions.
IntActi O75844. 2 interactions.
STRINGi 9606.ENSP00000361845.

Protein family/group databases

MEROPSi M48.003.
TCDBi 9.B.1.1.1. the integral membrane caax protease (caax protease) family.

PTM databases

PhosphoSitei O75844.

Proteomic databases

MaxQBi O75844.
PaxDbi O75844.
PeptideAtlasi O75844.
PRIDEi O75844.

Protocols and materials databases

DNASUi 10269.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372759 ; ENSP00000361845 ; ENSG00000084073 .
GeneIDi 10269.
KEGGi hsa:10269.
UCSCi uc001cfg.4. human.

Organism-specific databases

CTDi 10269.
GeneCardsi GC01P040723.
HGNCi HGNC:12877. ZMPSTE24.
HPAi HPA006988.
MIMi 275210. phenotype.
606480. gene.
608612. phenotype.
neXtProti NX_O75844.
Orphaneti 740. Hutchinson-Gilford progeria syndrome.
1662. Lethal restrictive dermopathy.
90154. Mandibuloacral dysplasia with type B lipodystrophy.
PharmGKBi PA37466.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0501.
GeneTreei ENSGT00390000002053.
HOGENOMi HOG000257874.
HOVERGENi HBG051541.
InParanoidi O75844.
KOi K06013.
OMAi SEVEGTM.
OrthoDBi EOG7RRF70.
PhylomeDBi O75844.
TreeFami TF105972.

Enzyme and pathway databases

BRENDAi 3.4.24.84. 2681.

Miscellaneous databases

GenomeRNAii 10269.
NextBioi 38906.
PROi O75844.
SOURCEi Search...

Gene expression databases

Bgeei O75844.
CleanExi HS_ZMPSTE24.
ExpressionAtlasi O75844. baseline and differential.
Genevestigatori O75844.

Family and domain databases

InterProi IPR027057. CAXX_Prtase_1.
IPR001915. Peptidase_M48.
[Graphical view ]
PANTHERi PTHR10120:SF24. PTHR10120:SF24. 1 hit.
Pfami PF01435. Peptidase_M48. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a human cDNA encoding a novel protein structurally related to the yeast membrane-associated metalloprotease, Ste24p."
    Kumagai H., Kawamura Y., Yanagisawa K., Komano H.
    Biochim. Biophys. Acta 1426:468-474(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing."
    Tam A., Nouvet F.J., Fujimura-Kamada K., Slunt H., Sisodia S.S., Michaelis S.
    J. Cell Biol. 142:635-649(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: B-cell and Fetal brain.
  3. "Identification and chromosomal location of two human genes encoding enzymes potentially involved in proteolytic maturation of farnesylated proteins."
    Freije J.M.P., Blay P., Pendas A.M., Cadinanos J., Crespo P., Lopez-Otin C.
    Genomics 58:270-280(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  4. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 ALA-137.
    Tissue: Testis.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH TETRAPEPTIDE, ACTIVE SITE, COFACTOR, METALLOPROTEASE DOMAIN, TOPOLOGY, ZINC-BINDING SITES, SUBCELLULAR LOCATION.
  11. "Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia."
    Agarwal A.K., Fryns J.-P., Auchus R.J., Garg A.
    Hum. Mol. Genet. 12:1995-2001(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MADB ARG-340.
  12. Cited for: INVOLVEMENT IN LTSCS.
  13. "Focal segmental glomerulosclerosis in patients with mandibuloacral dysplasia owing to ZMPSTE24 deficiency."
    Agarwal A.K., Zhou X.J., Hall R.K., Nicholls K., Bankier A., Van Esch H., Fryns J.P., Garg A.
    J. Invest. Med. 54:208-213(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MADB SER-265.
  14. "Severe mandibuloacral dysplasia caused by novel compound heterozygous ZMPSTE24 mutations in two Japanese siblings."
    Miyoshi Y., Akagi M., Agarwal A.K., Namba N., Kato-Nishimura K., Mohri I., Yamagata M., Nakajima S., Mushiake S., Shima M., Auchus R.J., Taniike M., Garg A., Ozono K.
    Clin. Genet. 73:535-544(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MADB LEU-248, CHARACTERIZATION OF VARIANT MADB.
  15. "Early onset mandibuloacral dysplasia due to compound heterozygous mutations in ZMPSTE24."
    Ahmad Z., Zackai E., Medne L., Garg A.
    Am. J. Med. Genet. A 152:2703-2710(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MADB LEU-248.

Entry informationi

Entry nameiFACE1_HUMAN
AccessioniPrimary (citable) accession number: O75844
Secondary accession number(s): B3KQI7
, D3DPU7, Q8NDZ8, Q9UBQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 27, 2001
Last modified: November 26, 2014
This is version 140 of the entry and version 2 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 1
    Human chromosome 1: 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