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A2BFH1 (PAL4G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 4G

Short name=PPIase A-like 4G
EC=5.2.1.8
Alternative name(s):
Peptidylprolyl cis-trans isomerase A-like 4
Gene names
Name:PPIAL4G
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.

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

protein peptidyl-prolyl isomerization

Inferred from electronic annotation. Source: GOC

   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 4G
PRO_0000324639

Regions

Domain7 – 163157PPIase cyclophilin-type

Experimental info

Sequence conflict61I → V in AAI30379. Ref.2
Sequence conflict61I → V in AAI30377. Ref.2
Sequence conflict241Q → L in AAI30379. Ref.2
Sequence conflict241Q → L in AAI30377. Ref.2
Sequence conflict691H → R in AAI30379. Ref.2
Sequence conflict691H → R in AAI30377. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A2BFH1 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: CEAFE5FE3D858213

FASTA16418,166
        10         20         30         40         50         60 
MVNSVIFFDI TVDGKPLGRI SIKQFADKIP KTAENFRALS TGEKGFRYKG SCFHRIIPGF 

        70         80         90        100        110        120 
MCQGGDFTHP NGTGDKSIYG EKFDDENLIR KHTGSGILSM ANAGPNTNGS QFFICTAKTE 

       130        140        150        160 
WLDGKHVAFG KVKERVNIVE AMEHFGYRNS KTSKKITIAD CGQF 

« Hide

References

[1]"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].
[2]"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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX284650 Genomic DNA. Translation: CAM26887.1.
BC130376 mRNA. Translation: AAI30377.1.
BC130378 mRNA. Translation: AAI30379.1.
RefSeqNP_001116540.1. NM_001123068.1.
UniGeneHs.534674.
Hs.573713.

3D structure databases

ProteinModelPortalA2BFH1.
SMRA2BFH1. Positions 2-164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000393845.

PTM databases

PhosphoSiteA2BFH1.

Proteomic databases

PaxDbA2BFH1.
PRIDEA2BFH1.

Protocols and materials databases

DNASU644591.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000419275; ENSP00000393845; ENSG00000236334.
GeneID644591.
KEGGhsa:644591.
UCSCuc001ejt.3. human.

Organism-specific databases

CTD644591.
GeneCardsGC01M143767.
HGNCHGNC:33996. PPIAL4G.
neXtProtNX_A2BFH1.
PharmGKBPA164724931.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000065981.
HOVERGENHBG001065.
InParanoidA2BFH1.
KOK12738.
OrthoDBEOG79GT7W.
TreeFamTF316719.

Gene expression databases

BgeeA2BFH1.
CleanExHS_PPIAL4A.
GenevestigatorA2BFH1.

Family and domain databases

InterProIPR024936. 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.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi644591.
NextBio116407.
PROA2BFH1.

Entry information

Entry namePAL4G_HUMAN
AccessionPrimary (citable) accession number: A2BFH1
Secondary accession number(s): A1L431
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: February 20, 2007
Last modified: March 19, 2014
This is version 67 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

Human chromosome 1

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