Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase A-like 4G

Gene

PPIAL4G

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: GO_Central

GO - Biological processi

  1. protein folding Source: InterPro
  2. protein peptidyl-prolyl isomerization Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase A-like 4G (EC:5.2.1.8)
Short name:
PPIase A-like 4G
Alternative name(s):
Peptidylprolyl cis-trans isomerase A-like 4
Gene namesi
Name:PPIAL4G
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:33996. PPIAL4G.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164724931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164Peptidyl-prolyl cis-trans isomerase A-like 4GPRO_0000324639Add
BLAST

Proteomic databases

PaxDbiA2BFH1.
PRIDEiA2BFH1.

PTM databases

PhosphoSiteiA2BFH1.

Expressioni

Gene expression databases

BgeeiA2BFH1.
CleanExiHS_PPIAL4A.
GenevestigatoriA2BFH1.

Organism-specific databases

HPAiHPA058345.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000393845.

Structurei

3D structure databases

ProteinModelPortaliA2BFH1.
SMRiA2BFH1. Positions 2-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 163157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiA2BFH1.
KOiK12738.
OrthoDBiEOG79GT7W.
PhylomeDBiA2BFH1.
TreeFamiTF316719.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2BFH1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNSVIFFDI TVDGKPLGRI SIKQFADKIP KTAENFRALS TGEKGFRYKG
60 70 80 90 100
SCFHRIIPGF MCQGGDFTHP NGTGDKSIYG EKFDDENLIR KHTGSGILSM
110 120 130 140 150
ANAGPNTNGS QFFICTAKTE WLDGKHVAFG KVKERVNIVE AMEHFGYRNS
160
KTSKKITIAD CGQF
Length:164
Mass (Da):18,166
Last modified:February 20, 2007 - v1
Checksum:iCEAFE5FE3D858213
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61I → V in AAI30379 (PubMed:15489334).Curated
Sequence conflicti6 – 61I → V in AAI30377 (PubMed:15489334).Curated
Sequence conflicti24 – 241Q → L in AAI30379 (PubMed:15489334).Curated
Sequence conflicti24 – 241Q → L in AAI30377 (PubMed:15489334).Curated
Sequence conflicti69 – 691H → R in AAI30379 (PubMed:15489334).Curated
Sequence conflicti69 – 691H → R in AAI30377 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284650 Genomic DNA. Translation: CAM26887.1.
BC130376 mRNA. Translation: AAI30377.1.
BC130378 mRNA. Translation: AAI30379.1.
CCDSiCCDS41375.2.
RefSeqiNP_001116540.1. NM_001123068.1.
NP_001129261.2. NM_001135789.3.
UniGeneiHs.534674.

Genome annotation databases

EnsembliENST00000419275; ENSP00000393845; ENSG00000236334.
GeneIDi644591.
653598.
KEGGihsa:644591.
hsa:653598.
UCSCiuc001ejt.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284650 Genomic DNA. Translation: CAM26887.1.
BC130376 mRNA. Translation: AAI30377.1.
BC130378 mRNA. Translation: AAI30379.1.
CCDSiCCDS41375.2.
RefSeqiNP_001116540.1. NM_001123068.1.
NP_001129261.2. NM_001135789.3.
UniGeneiHs.534674.

3D structure databases

ProteinModelPortaliA2BFH1.
SMRiA2BFH1. Positions 2-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000393845.

PTM databases

PhosphoSiteiA2BFH1.

Proteomic databases

PaxDbiA2BFH1.
PRIDEiA2BFH1.

Protocols and materials databases

DNASUi644591.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000419275; ENSP00000393845; ENSG00000236334.
GeneIDi644591.
653598.
KEGGihsa:644591.
hsa:653598.
UCSCiuc001ejt.3. human.

Organism-specific databases

CTDi644591.
653598.
GeneCardsiGC01M143767.
HGNCiHGNC:33996. PPIAL4G.
HPAiHPA058345.
neXtProtiNX_A2BFH1.
PharmGKBiPA164724931.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiA2BFH1.
KOiK12738.
OrthoDBiEOG79GT7W.
PhylomeDBiA2BFH1.
TreeFamiTF316719.

Miscellaneous databases

NextBioi116407.
PROiA2BFH1.

Gene expression databases

BgeeiA2BFH1.
CleanExiHS_PPIAL4A.
GenevestigatoriA2BFH1.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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].

Entry informationi

Entry nameiPAL4G_HUMAN
AccessioniPrimary (citable) accession number: A2BFH1
Secondary accession number(s): A1L431
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: February 20, 2007
Last modified: March 4, 2015
This is version 77 of the entry and version 1 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

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.