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Q9Y256 (FACE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CAAX prenyl protease 2

EC=3.4.22.-
Alternative name(s):
Farnesylated proteins-converting enzyme 2
Short name=FACE-2
Prenyl protein-specific endoprotease 2
RCE1 homolog
Short name=hRCE1
Gene names
Name:RCE1
Synonyms:FACE2, RCE1A, RCE1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1.

Enzyme regulation

Deubiquitination by USP17L2/USP17 negatively regulates the proteolytic activity toward Ras GTPases. Ref.5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.5.

Tissue specificity

Ubiquitous.

Post-translational modification

Ubiquitinated. Undergoes 'Lys-48'-and 'Lys-63'-linked ubiquitination. 'Lys-48' ubiquitination induces its degradation. Deubiquitinated by USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains. Ref.5

Sequence similarities

Belongs to the peptidase U48 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 329328CAAX prenyl protease 2
PRO_0000194830

Regions

Transmembrane25 – 4521Helical; Potential
Transmembrane75 – 9521Helical; Potential
Transmembrane112 – 13221Helical; Potential
Transmembrane186 – 20621Helical; Potential
Transmembrane229 – 24921Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane283 – 30321Helical; Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.6

Natural variations

Natural variant3261P → A in a breast cancer sample; somatic mutation. Ref.7
VAR_036407

Sequences

Sequence LengthMass (Da)Tools
Q9Y256 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: BA8F764651172BFA

FASTA32935,833
        10         20         30         40         50         60 
MAALGGDGLR LLSVSRPERP PESAALGGLG PGLCCWVSVF SCLSLACSYV GSLYVWKSEL 

        70         80         90        100        110        120 
PRDHPAVIKR RFTSVLVVSS LSPLCVLLWR ELTGIQPGTS LLTLMGFRLE GIFPAALLPL 

       130        140        150        160        170        180 
LLTMILFLGP LMQLSMDCPC DLADGLKVVL APRSWARCLT DMRWLRNQVI APLTEELVFR 

       190        200        210        220        230        240 
ACMLPMLAPC MGLGPAVFTC PLFFGVAHFH HIIEQLRFRQ SSVGNIFLSA AFQFSYTAVF 

       250        260        270        280        290        300 
GAYTAFLFIR TGHLIGPVLC HSFCNYMGFP AVCAALEHPQ RRPLLAGYAL GVGLFLLLLQ 

       310        320 
PLTDPKLYGS LPLCVLLERA GDSEAPLCS 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"Cloning and characterization of a mammalian prenyl protein-specific protease."
Otto J.C., Kim E., Young S.G., Casey P.J.
J. Biol. Chem. 274:8379-8382(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]"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].
Tissue: Brain.
[4]"Human ras-converting enzyme (hRCE1) endoproteolytic activity on K-ras-derived peptides."
Hollander I., Frommer E., Mallon R.
Anal. Biochem. 286:129-137(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[5]"USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity."
Burrows J.F., Kelvin A.A., McFarlane C., Burden R.E., McGrattan M.J., De la Vega M., Govender U., Quinn D.J., Dib K., Gadina M., Scott C.J., Johnston J.A.
J. Biol. Chem. 284:9587-9595(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP17L2, SUBCELLULAR LOCATION, ENZYME REGULATION.
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-326.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13835 mRNA. Translation: CAB46278.1.
AF121951 mRNA. Translation: AAD22632.1.
BC093726 mRNA. Translation: AAH93726.1.
BC093728 mRNA. Translation: AAH93728.1.
RefSeqNP_001027450.1. NM_001032279.1.
NP_005124.1. NM_005133.2.
UniGeneHs.292088.
Hs.654972.

3D structure databases

ProteinModelPortalQ9Y256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115307. 1 interaction.
STRING9606.ENSP00000309163.

Chemistry

BindingDBQ9Y256.
ChEMBLCHEMBL3411.

Protein family/group databases

MEROPSM79.002.

PTM databases

PhosphoSiteQ9Y256.

Polymorphism databases

DMDM13431529.

Proteomic databases

PaxDbQ9Y256.
PRIDEQ9Y256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309657; ENSP00000309163; ENSG00000173653.
GeneID9986.
KEGGhsa:79703.
hsa:9986.
UCSCuc001ojk.1. human.

Organism-specific databases

CTD79703.
9986.
GeneCardsGC11P066611.
HGNCHGNC:13721. RCE1.
MIM605385. gene.
neXtProtNX_Q9Y256.
PharmGKBPA34302.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264307.
HOGENOMHOG000006037.
HOVERGENHBG002541.
InParanoidQ9Y256.
KOK08658.
OMAYSAFLFA.
OrthoDBEOG7F24TC.
PhylomeDBQ9Y256.
TreeFamTF313800.

Enzyme and pathway databases

BRENDA3.4.22.22. 2681.

Gene expression databases

ArrayExpressQ9Y256.
BgeeQ9Y256.
CleanExHS_RCE1.
GenevestigatorQ9Y256.

Family and domain databases

InterProIPR003675. CAAX_protease.
[Graphical view]
PfamPF02517. Abi. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRCE1.
NextBio37706.
PROQ9Y256.
SOURCESearch...

Entry information

Entry nameFACE2_HUMAN
AccessionPrimary (citable) accession number: Q9Y256
Secondary accession number(s): Q52LZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM