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Q9Y536 (PAL4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Peptidyl-prolyl cis-trans isomerase A-like 4A/B/C

Short name=PPIase A-like 4A
EC=5.2.1.8
Alternative name(s):
Chromosome 1-amplified sequence 2
Short name=COAS-2
Cyclophilin homolog overexpressed in liver cancer
Gene names
Name:PPIAL4A
Synonyms:COAS2
AND
Name:PPIAL4B
AND
Name:PPIAL4C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in brain, ovary and mammary gland. Moderately expressed in lung, salivary gland, kidney, skin, adipose tissue, intestine and spleen. Weakly expressed in skeletal muscle, liver and stomach. Expressed in pleiomorphic and undifferentiated liposarcomas, osteosarcomas and breast carcinomas. Ref.3

Miscellaneous

It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 1.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Peptidyl-prolyl cis-trans isomerase A-like 4A/B/C
PRO_0000324640

Regions

Domain7 – 163157PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
Q9Y536 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 99D50A72B0896C4C

FASTA16418,182
        10         20         30         40         50         60 
MVNSVVFFDI TVDGKPLGRI SIKLFADKIL KTAENFRALS TGEKGFRYKG SCFHRIIPGF 

        70         80         90        100        110        120 
MCQGGDFTRH NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICAAKTE 

       130        140        150        160 
WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF 

« Hide

References

« Hide 'large scale' references
[1]"Cyclophilin homologue overexpressed in liver cancer."
Tanaka S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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].
[3]"Positional cloning identifies a novel cyclophilin as a candidate amplified oncogene in 1q21."
Meza-Zepeda L.A., Forus A., Lygren B., Dahlberg A.B., Godager L.H., South A.P., Marenholz I., Lioumi M., Florenes V.A., Maelandsmo G.M., Serra M., Mischke D., Nizetic D., Ragoussis J., Tarkkanen M., Nesland J.M., Knuutila S., Myklebost O.
Oncogene 21:2261-2269(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB084917 mRNA. Translation: BAB92073.1.
AL022240 Genomic DNA. Translation: CAB46877.1.
AL451058 Genomic DNA. Translation: CAH71953.1.
BX248398 Genomic DNA. Translation: CAI18814.1.
CCDSCCDS44205.1.
RefSeqNP_001137355.1. NM_001143883.2.
UniGeneHs.573713.
Hs.631792.

3D structure databases

ProteinModelPortalQ9Y536.
SMRQ9Y536. Positions 2-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127884. 1 interaction.
STRING9606.ENSP00000358224.

PTM databases

PhosphoSiteQ9Y536.

Proteomic databases

MaxQBQ9Y536.
PaxDbQ9Y536.
PRIDEQ9Y536.

Protocols and materials databases

DNASU164022.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369222; ENSP00000358224; ENSG00000198161.
ENST00000539781; ENSP00000439146; ENSG00000255963.
ENST00000540273; ENSP00000443989; ENSG00000255854.
GeneID653505.
KEGGhsa:100996725.
hsa:164022.
hsa:653505.
hsa:653598.
UCSCuc001ekw.3. human.

Organism-specific databases

CTD653505.
653598.
GeneCardsGC01M144360.
GC01M147954.
GC01P149552.
H-InvDBHIX0028837.
HIX0159741.
HGNCHGNC:24369. PPIAL4A.
HGNC:33994. PPIAL4B.
HGNC:33995. PPIAL4C.
MIM608608. gene.
neXtProtNX_Q9Y536.
PharmGKBPA164724917.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
HOVERGENHBG001065.
InParanoidQ9Y536.
KOK12738.
OMAFPSAMVN.
OrthoDBEOG79GT7W.
PhylomeDBQ9Y536.
TreeFamTF316719.

Gene expression databases

BgeeQ9Y536.
GenevestigatorQ9Y536.

Family and domain databases

Gene3D2.40.100.10. 1 hit.
InterProIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSPR00153. CSAPPISMRASE.
SUPFAMSSF50891. SSF50891. 1 hit.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio88425.
SOURCESearch...

Entry information

Entry namePAL4A_HUMAN
AccessionPrimary (citable) accession number: Q9Y536
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 114 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

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM