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Protein

NK-tumor recognition protein

Gene

NKTR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  • cyclosporin A binding Source: ProtInc
  • peptidyl-prolyl cis-trans isomerase activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
NK-tumor recognition protein
Short name:
NK-TR protein
Alternative name(s):
Natural-killer cells cyclophilin-related protein
Including the following 1 domains:
Putative peptidyl-prolyl cis-trans isomerase (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Rotamase
Gene namesi
Name:NKTR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:7833. NKTR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31641.

Polymorphism and mutation databases

BioMutaiNKTR.
DMDMi8039798.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14621462NK-tumor recognition proteinPRO_0000064217Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei379 – 3791Phosphoserine2 Publications
Modified residuei463 – 4631Phosphoserine3 Publications
Modified residuei887 – 8871Phosphoserine1 Publication
Modified residuei889 – 8891Phosphoserine1 Publication
Modified residuei891 – 8911Phosphoserine1 Publication
Modified residuei1146 – 11461Phosphoserine2 Publications
Modified residuei1155 – 11551Phosphothreonine2 Publications
Cross-linki1258 – 1258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP30414.
PaxDbiP30414.
PeptideAtlasiP30414.
PRIDEiP30414.

PTM databases

PhosphoSiteiP30414.

Miscellaneous databases

PMAP-CutDBP30414.

Expressioni

Gene expression databases

BgeeiP30414.
CleanExiHS_NKTR.
ExpressionAtlasiP30414. baseline and differential.
GenevisibleiP30414. HS.

Organism-specific databases

HPAiHPA022120.
HPA051576.

Interactioni

Protein-protein interaction databases

BioGridi110885. 12 interactions.
IntActiP30414. 5 interactions.
STRINGi9606.ENSP00000232978.

Structurei

Secondary structure

1
1462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158Combined sources
Beta strandi18 – 2710Combined sources
Turni29 – 313Combined sources
Helixi33 – 4412Combined sources
Turni51 – 533Combined sources
Beta strandi55 – 573Combined sources
Beta strandi63 – 686Combined sources
Turni69 – 713Combined sources
Beta strandi72 – 754Combined sources
Turni78 – 803Combined sources
Beta strandi81 – 844Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi123 – 1286Combined sources
Helixi131 – 1333Combined sources
Turni134 – 1363Combined sources
Beta strandi139 – 1457Combined sources
Helixi147 – 1548Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1758Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HE9X-ray2.00A/B7-179[»]
ProteinModelPortaliP30414.
SMRiP30414. Positions 7-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 175166PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1311 – 134838Arg/Ser tandem repeat-richAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi194 – 24451Arg/Ser-richAdd
BLAST
Compositional biasi219 – 24022Arg/Lys-rich (basic)Add
BLAST
Compositional biasi421 – 45737Arg/Lys-rich (basic)Add
BLAST
Compositional biasi466 – 574109Arg/Ser-richAdd
BLAST
Compositional biasi664 – 814151Arg/Ser-richAdd
BLAST
Compositional biasi970 – 101041Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00550000074595.
HOGENOMiHOG000113792.
HOVERGENiHBG052631.
InParanoidiP30414.
KOiK12740.
OMAiINEKQVT.
OrthoDBiEOG79GT7W.
PhylomeDBiP30414.
TreeFamiTF318563.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30414-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQDRPQCH FDIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGLG
60 70 80 90 100
KTTGKKLCYK GSTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI
110 120 130 140 150
LKHDRAFLLS MANRGKHTNG SQFFITTKPA PHLDGVHVVF GLVISGFEVI
160 170 180 190 200
EQIENLKTDA ASRPYADVRV IDCGVLATKS IKDVFEKKRK KPTHSEGSDS
210 220 230 240 250
SSNSSSSSES SSESELEHER SRRRKHKRRP KVKRSKKRRK EASSSEEPRN
260 270 280 290 300
KHAMNPKGHS ERSDTNEKRS VDSSAKREKP VVRPEEIPPV PENRFLLRRD
310 320 330 340 350
MPVVTAEPEP KIPDVAPIVS DQKPSVSKSG RKIKGRGTIR YHTPPRSRSC
360 370 380 390 400
SESDDDDSSE TPPHWKEEMQ RLRAYRPPSG EKWSKGDKLS DPCSSRWDER
410 420 430 440 450
SLSQRSRSWS YNGYYSDLST ARHSGHHKKR RKEKKVKHKK KGKKQKHCRR
460 470 480 490 500
HKQTKKRRIL IPSDIESSKS STRRMKSSCD RERSSRSSSL SSHHSSKRDW
510 520 530 540 550
SKSDKDVQSS LTHSSRDSYR SKSHSQSYSR GSSRSRTASK SSSHSRSRSK
560 570 580 590 600
SRSSSKSGHR KRASKSPRKT ASQLSENKPV KTEPLRATMA QNENVVVQPV
610 620 630 640 650
VAENIPVIPL SDSPPPSRWK PGQKPWKPSY ERIQEMKAKT THLLPIQSTY
660 670 680 690 700
SLANIKETGS SSSYHKREKN SESDQSTYSK YSDRSSESSP RSRSRSSRSR
710 720 730 740 750
SYSRSYTRSR SLASSHSRSR SPSSRSHSRN KYSDHSQCSR SSSYTSISSD
760 770 780 790 800
DGRRAKRRLR SSGKKNSVSH KKHSSSSEKT LHSKYVKGRD RSSCVRKYSE
810 820 830 840 850
SRSSLDYSSD SEQSSVQATQ SAQEKEKQGQ MERTHNKQEK NRGEEKSKSE
860 870 880 890 900
RECPHSKKRT LKENLSDHLR NGSKPKRKNY AGSKWDSESN SERDVTKNSK
910 920 930 940 950
NDSHPSSDKE EGEATSDSES EVSEIHIKVK PTTKSSTNTS LPDDNGAWKS
960 970 980 990 1000
SKQRTSTSDS EGSCSNSENN RGKPQKHKHG SKENLKREHT KKVKEKLKGK
1010 1020 1030 1040 1050
KDKKHKAPKR KQAFHWQPPL EFGEEEEEEI DDKQVTQESK EKKVSENNET
1060 1070 1080 1090 1100
IKDNILKTEK SSEEDLSGKH DTVTVSSDLD QFTKDDSKLS ISPTALNTEE
1110 1120 1130 1140 1150
NVACLQNIQH VEESVPNGVE DVLQTDDNME ICTPDRSSPA KVEETSPLGN
1160 1170 1180 1190 1200
ARLDTPDINI VLKQDMATEH PQAEVVKQES SMSESKVLGE VGKQDSSSAS
1210 1220 1230 1240 1250
LASAGESTGK KEVAEKSQIN LIDKKWKPLQ GVGNLAAPNA ATSSAVEVKV
1260 1270 1280 1290 1300
LTTVPEMKPQ GLRIEIKSKN KVRPGSLFDE VRKTARLNRR PRNQESSSDE
1310 1320 1330 1340 1350
QTPSRDDDSQ SRSPSRSRSK SETKSRHRTR SVSYSHSRSR SRSSTSSYRS
1360 1370 1380 1390 1400
RSYSRSRSRG WYSRGRTRSR SSSYRSYKSH RTSSRSRSRS SSYDPHSRSR
1410 1420 1430 1440 1450
SYTYDSYYSR SRSRSRSQRS DSYHRGRSYN RRSRSCRSYG SDSESDRSYS
1460
HHRSPSESSR YS
Length:1,462
Mass (Da):165,677
Last modified:May 30, 2000 - v2
Checksum:iD98A1147763EF527
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti271 – 2711V → G.
Corresponds to variant rs35726114 [ dbSNP | Ensembl ].
VAR_061765
Natural varianti861 – 8611L → V.
Corresponds to variant rs33969824 [ dbSNP | Ensembl ].
VAR_051773
Natural varianti935 – 9351S → L.
Corresponds to variant rs35770315 [ dbSNP | Ensembl ].
VAR_051774
Natural varianti1182 – 11821M → T.
Corresponds to variant rs34897686 [ dbSNP | Ensembl ].
VAR_061766

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04288 mRNA. Translation: AAA35734.2.
AF184110 Genomic DNA. Translation: AAD56402.1.
CCDSiCCDS2702.1.
PIRiA47328.
RefSeqiNP_005376.2. NM_005385.3.
UniGeneiHs.529509.

Genome annotation databases

EnsembliENST00000232978; ENSP00000232978; ENSG00000114857.
GeneIDi4820.
KEGGihsa:4820.
UCSCiuc003clm.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04288 mRNA. Translation: AAA35734.2.
AF184110 Genomic DNA. Translation: AAD56402.1.
CCDSiCCDS2702.1.
PIRiA47328.
RefSeqiNP_005376.2. NM_005385.3.
UniGeneiHs.529509.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HE9X-ray2.00A/B7-179[»]
ProteinModelPortaliP30414.
SMRiP30414. Positions 7-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110885. 12 interactions.
IntActiP30414. 5 interactions.
STRINGi9606.ENSP00000232978.

PTM databases

PhosphoSiteiP30414.

Polymorphism and mutation databases

BioMutaiNKTR.
DMDMi8039798.

Proteomic databases

MaxQBiP30414.
PaxDbiP30414.
PeptideAtlasiP30414.
PRIDEiP30414.

Protocols and materials databases

DNASUi4820.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000232978; ENSP00000232978; ENSG00000114857.
GeneIDi4820.
KEGGihsa:4820.
UCSCiuc003clm.1. human.

Organism-specific databases

CTDi4820.
GeneCardsiGC03P042643.
HGNCiHGNC:7833. NKTR.
HPAiHPA022120.
HPA051576.
MIMi161565. gene.
neXtProtiNX_P30414.
PharmGKBiPA31641.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0652.
GeneTreeiENSGT00550000074595.
HOGENOMiHOG000113792.
HOVERGENiHBG052631.
InParanoidiP30414.
KOiK12740.
OMAiINEKQVT.
OrthoDBiEOG79GT7W.
PhylomeDBiP30414.
TreeFamiTF318563.

Miscellaneous databases

ChiTaRSiNKTR. human.
EvolutionaryTraceiP30414.
GeneWikiiNKTR.
GenomeRNAii4820.
NextBioi18572.
PMAP-CutDBP30414.
PROiP30414.
SOURCEiSearch...

Gene expression databases

BgeeiP30414.
CleanExiHS_NKTR.
ExpressionAtlasiP30414. baseline and differential.
GenevisibleiP30414. HS.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNKTR_HUMAN
AccessioniPrimary (citable) accession number: P30414
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 30, 2000
Last modified: June 24, 2015
This is version 130 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.