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Reviewed, UniProtKB/Swiss-Prot Q9Y536 (PAL4B_HUMAN)

Last modified November 4, 2008. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidylprolyl cis-trans isomerase A-like 4B
      Short name=PPIase A-like 4B
    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: PPIAL4B
Synonyms: COAS2
AND
Name: PPIAL4C
AND
Name: PPIAL4D
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

CytoplasmBy 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 pleomorphic and undifferentiated liposarcomas, osteosarcomas and breast carcinomas.

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.

Caution

Expression studies do not distinguish between PPIAL4B and PPIAL4 (Ref.3).

Ontologies

Keywords

   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase

Gene Ontology (GO)

   Biological processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Peptidylprolyl cis-trans isomerase A-like 4B
PRO_0000324640

Regions

Domain7 – 163157PPIase cyclophilin-type

Sequences

Sequence LengthMass (Da)Tools
Q9Y536-1 [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: 16710414] [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: 11948409] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

AB084917 mRNA. Translation: BAB92073.1.
AL022240 Genomic DNA. Translation: CAB46877.1.
AL451058 Genomic DNA. Translation: CAH71953.1.
BX248398 Genomic DNA. Translation: CAI18814.1.
RefSeqNP_839944.1.
XP_932860.1.
XP_933431.1.
UniGeneHs.573713

3D structure databases

HSSPHSSP built from PDB template 1E3B based on UniProtKB P52011.
SMRQ9Y536. Positions 1-164.
ModBaseSearch...

Genome annotation databases

EnsemblENSG00000198161. Homo sapiens. [Contig view]
GeneID164022.
653505.
653598.
KEGGhsa:164022.
hsa:653505.
hsa:653598.

Organism-specific databases

MIM608608. gene.
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ9Y536.
HOVERGENQ9Y536.

Family and domain databases

InterProIPR002130. PPIase_cyclophilin.
[Graphical view]
Gene3DG3DSA:2.40.100.10. PPIase_cyclophilin. 1 hit.
PANTHERPTHR11071. PPIase_cyclophilin. 1 hit.
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

LinkHubQ9Y536.
NextBio88425.
SOURCESearch...

Entry information

Entry namePAL4B_HUMAN
AccessionPrimary (citable) accession number: Q9Y536
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 1, 1999
Last modified: November 4, 2008
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents