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O75844

- FACE1_HUMAN

UniProt

O75844 - FACE1_HUMAN

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
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (27 Apr 2001)
      Previous versions | rss
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    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

    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

    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

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB
    5. nuclear inner membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiO75844.
    BgeeiO75844.
    CleanExiHS_ZMPSTE24.
    GenevestigatoriO75844.

    Organism-specific databases

    HPAiHPA006988.

    Interactioni

    Protein-protein interaction databases

    BioGridi115560. 23 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 – 133
    Helixi16 – 4732
    Helixi54 – 563
    Helixi61 – 9535
    Helixi97 – 1048
    Helixi117 – 14731
    Helixi149 – 1524
    Helixi160 – 19132
    Helixi196 – 21520
    Turni216 – 2194
    Helixi220 – 2234
    Beta strandi226 – 2283
    Helixi233 – 24412
    Beta strandi249 – 2557
    Helixi257 – 2593
    Beta strandi266 – 2738
    Beta strandi275 – 2806
    Helixi281 – 2844
    Helixi326 – 34116
    Helixi344 – 36623
    Helixi371 – 3755
    Helixi384 – 39310
    Helixi397 – 42428
    Turni425 – 4273
    Helixi428 – 44114
    Helixi450 – 4556
    Helixi462 – 47110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1818LumenalSequence AnalysisAdd
    BLAST
    Topological domaini40 – 8142NuclearSequence AnalysisAdd
    BLAST
    Topological domaini103 – 12321LumenalSequence AnalysisAdd
    BLAST
    Topological domaini145 – 17026NuclearSequence AnalysisAdd
    BLAST
    Topological domaini192 – 1954LumenalSequence Analysis
    Topological domaini217 – 347131NuclearSequence AnalysisAdd
    BLAST
    Topological domaini369 – 38214LumenalSequence AnalysisAdd
    BLAST
    Topological domaini406 – 47570NuclearSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei19 – 3921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei82 – 10221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei124 – 14421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei171 – 19121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei196 – 21621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei348 – 36821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei383 – 40523HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MGMWASLDAL WEMPAEKRIF GAVLLFSWTV YLWETFLAQR QRRIYKTTTH    50
    VPPELGQIMD SETFEKSRLY QLDKSTFSFW SGLYSETEGT LILLFGGIPY 100
    LWRLSGRFCG YAGFGPEYEI TQSLVFLLLA TLFSALTGLP WSLYNTFVIE 150
    EKHGFNQQTL GFFMKDAIKK FVVTQCILLP VSSLLLYIIK IGGDYFFIYA 200
    WLFTLVVSLV LVTIYADYIA PLFDKFTPLP EGKLKEEIEV MAKSIDFPLT 250
    KVYVVEGSKR SSHSNAYFYG FFKNKRIVLF DTLLEEYSVL NKDIQEDSGM 300
    EPRNEEEGNS EEIKAKVKNK KQGCKNEEVL AVLGHELGHW KLGHTVKNII 350
    ISQMNSFLCF FLFAVLIGRK ELFAAFGFYD SQPTLIGLLI IFQFIFSPYN 400
    EVLSFCLTVL SRRFEFQADA FAKKLGKAKD LYSALIKLNK DNLGFPVSDW 450
    LFSMWHYSHP PLLERLQALK TMKQH 475
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 23 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.
    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

    ArrayExpressi O75844.
    Bgeei O75844.
    CleanExi HS_ZMPSTE24.
    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

    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: October 1, 2014
    This is version 138 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