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P30414 (NKTR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. 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:
NK-tumor recognition protein

Short name=NK-TR protein
Alternative name(s):
Natural-killer cells cyclophilin-related protein

Including the following 1 domains:

  1. Putative peptidyl-prolyl cis-trans isomerase
    Short name=PPIase
    EC=5.2.1.8
    Alternative name(s):
    Rotamase
Gene names
Name:NKTR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a putative tumor-recognition complex. Involved in the function of NK cells.

Catalytic activity

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

Subcellular location

Membrane; Peripheral membrane protein. Note: Attached to the membrane via its N-terminus.

Sequence similarities

Contains 1 PPIase cyclophilin-type domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandCyclosporin
   Molecular functionIsomerase
Rotamase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncyclosporin A binding

Traceable author statement Ref.1. Source: ProtInc

peptidyl-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 – 14621462NK-tumor recognition protein
PRO_0000064217

Regions

Domain10 – 175166PPIase cyclophilin-type
Region1311 – 134838Arg/Ser tandem repeat-rich
Compositional bias194 – 24451Arg/Ser-rich
Compositional bias219 – 24022Arg/Lys-rich (basic)
Compositional bias421 – 45737Arg/Lys-rich (basic)
Compositional bias466 – 574109Arg/Ser-rich
Compositional bias664 – 814151Arg/Ser-rich
Compositional bias970 – 101041Arg/Lys-rich (basic)

Amino acid modifications

Modified residue3791Phosphoserine Ref.4 Ref.8
Modified residue4631Phosphoserine Ref.5 Ref.7 Ref.8
Modified residue8871Phosphoserine Ref.5
Modified residue8891Phosphoserine Ref.5
Modified residue8911Phosphoserine Ref.5
Modified residue11461Phosphoserine Ref.7 Ref.8
Modified residue11551Phosphothreonine Ref.8
Cross-link1258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant2711V → G.
Corresponds to variant rs35726114 [ dbSNP | Ensembl ].
VAR_061765
Natural variant8611L → V.
Corresponds to variant rs33969824 [ dbSNP | Ensembl ].
VAR_051773
Natural variant9351S → L.
Corresponds to variant rs35770315 [ dbSNP | Ensembl ].
VAR_051774
Natural variant11821M → T.
Corresponds to variant rs34897686 [ dbSNP | Ensembl ].
VAR_061766

Secondary structure

................................... 1462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30414 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: D98A1147763EF527

FASTA1,462165,677
        10         20         30         40         50         60 
MGAQDRPQCH FDIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGLG KTTGKKLCYK 

        70         80         90        100        110        120 
GSTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI LKHDRAFLLS MANRGKHTNG 

       130        140        150        160        170        180 
SQFFITTKPA PHLDGVHVVF GLVISGFEVI EQIENLKTDA ASRPYADVRV IDCGVLATKS 

       190        200        210        220        230        240 
IKDVFEKKRK KPTHSEGSDS SSNSSSSSES SSESELEHER SRRRKHKRRP KVKRSKKRRK 

       250        260        270        280        290        300 
EASSSEEPRN KHAMNPKGHS ERSDTNEKRS VDSSAKREKP VVRPEEIPPV PENRFLLRRD 

       310        320        330        340        350        360 
MPVVTAEPEP KIPDVAPIVS DQKPSVSKSG RKIKGRGTIR YHTPPRSRSC SESDDDDSSE 

       370        380        390        400        410        420 
TPPHWKEEMQ RLRAYRPPSG EKWSKGDKLS DPCSSRWDER SLSQRSRSWS YNGYYSDLST 

       430        440        450        460        470        480 
ARHSGHHKKR RKEKKVKHKK KGKKQKHCRR HKQTKKRRIL IPSDIESSKS STRRMKSSCD 

       490        500        510        520        530        540 
RERSSRSSSL SSHHSSKRDW SKSDKDVQSS LTHSSRDSYR SKSHSQSYSR GSSRSRTASK 

       550        560        570        580        590        600 
SSSHSRSRSK SRSSSKSGHR KRASKSPRKT ASQLSENKPV KTEPLRATMA QNENVVVQPV 

       610        620        630        640        650        660 
VAENIPVIPL SDSPPPSRWK PGQKPWKPSY ERIQEMKAKT THLLPIQSTY SLANIKETGS 

       670        680        690        700        710        720 
SSSYHKREKN SESDQSTYSK YSDRSSESSP RSRSRSSRSR SYSRSYTRSR SLASSHSRSR 

       730        740        750        760        770        780 
SPSSRSHSRN KYSDHSQCSR SSSYTSISSD DGRRAKRRLR SSGKKNSVSH KKHSSSSEKT 

       790        800        810        820        830        840 
LHSKYVKGRD RSSCVRKYSE SRSSLDYSSD SEQSSVQATQ SAQEKEKQGQ MERTHNKQEK 

       850        860        870        880        890        900 
NRGEEKSKSE RECPHSKKRT LKENLSDHLR NGSKPKRKNY AGSKWDSESN SERDVTKNSK 

       910        920        930        940        950        960 
NDSHPSSDKE EGEATSDSES EVSEIHIKVK PTTKSSTNTS LPDDNGAWKS SKQRTSTSDS 

       970        980        990       1000       1010       1020 
EGSCSNSENN RGKPQKHKHG SKENLKREHT KKVKEKLKGK KDKKHKAPKR KQAFHWQPPL 

      1030       1040       1050       1060       1070       1080 
EFGEEEEEEI DDKQVTQESK EKKVSENNET IKDNILKTEK SSEEDLSGKH DTVTVSSDLD 

      1090       1100       1110       1120       1130       1140 
QFTKDDSKLS ISPTALNTEE NVACLQNIQH VEESVPNGVE DVLQTDDNME ICTPDRSSPA 

      1150       1160       1170       1180       1190       1200 
KVEETSPLGN ARLDTPDINI VLKQDMATEH PQAEVVKQES SMSESKVLGE VGKQDSSSAS 

      1210       1220       1230       1240       1250       1260 
LASAGESTGK KEVAEKSQIN LIDKKWKPLQ GVGNLAAPNA ATSSAVEVKV LTTVPEMKPQ 

      1270       1280       1290       1300       1310       1320 
GLRIEIKSKN KVRPGSLFDE VRKTARLNRR PRNQESSSDE QTPSRDDDSQ SRSPSRSRSK 

      1330       1340       1350       1360       1370       1380 
SETKSRHRTR SVSYSHSRSR SRSSTSSYRS RSYSRSRSRG WYSRGRTRSR SSSYRSYKSH 

      1390       1400       1410       1420       1430       1440 
RTSSRSRSRS SSYDPHSRSR SYTYDSYYSR SRSRSRSQRS DSYHRGRSYN RRSRSCRSYG 

      1450       1460 
SDSESDRSYS HHRSPSESSR YS 

« Hide

References

« Hide 'large scale' references
[1]"A cyclophilin-related protein involved in the function of natural killer cells."
Anderson S.K., Gallinger S., Roder J., Frey J., Young H.A., Ortaldo J.R.
Proc. Natl. Acad. Sci. U.S.A. 90:542-546(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[2]Anderson S.K.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Structure of the human NKTR gene."
Anderson S.K.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463; SER-887; SER-889 AND SER-891, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[7]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 AND SER-1146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-463; SER-1146 AND THR-1155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04288 mRNA. Translation: AAA35734.2.
AF184110 Genomic DNA. Translation: AAD56402.1.
PIRA47328.
RefSeqNP_005376.2. NM_005385.3.
UniGeneHs.529509.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HE9X-ray2.00A/B7-179[»]
ProteinModelPortalP30414.
SMRP30414. Positions 7-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110885. 6 interactions.
IntActP30414. 5 interactions.
STRING9606.ENSP00000232978.

PTM databases

PhosphoSiteP30414.

Polymorphism databases

DMDM8039798.

Proteomic databases

PaxDbP30414.
PeptideAtlasP30414.
PRIDEP30414.

Protocols and materials databases

DNASU4820.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000232978; ENSP00000232978; ENSG00000114857.
GeneID4820.
KEGGhsa:4820.
UCSCuc003clm.1. human.

Organism-specific databases

CTD4820.
GeneCardsGC03P042617.
HGNCHGNC:7833. NKTR.
HPAHPA022120.
HPA051576.
MIM161565. gene.
neXtProtNX_P30414.
PharmGKBPA31641.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0652.
HOGENOMHOG000113792.
HOVERGENHBG052631.
InParanoidP30414.
KOK12740.
OMAVSDQKPS.
OrthoDBEOG79GT7W.
PhylomeDBP30414.
TreeFamTF318563.

Gene expression databases

ArrayExpressP30414.
BgeeP30414.
CleanExHS_NKTR.
GenevestigatorP30414.

Family and domain databases

InterProIPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSPR00153. CSAPPISMRASE.
PROSITEPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNKTR. human.
EvolutionaryTraceP30414.
GeneWikiNKTR.
GenomeRNAi4820.
NextBio18572.
PMAP-CutDBP30414.
PROP30414.
SOURCESearch...

Entry information

Entry nameNKTR_HUMAN
AccessionPrimary (citable) accession number: P30414
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 117 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 3

Human chromosome 3: entries, gene names and cross-references to MIM