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P30414

- NKTR_HUMAN

UniProt

P30414 - NKTR_HUMAN

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Protein
NK-tumor recognition protein
Gene
NKTR
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. cyclosporin A binding Source: ProtInc
  2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: UniProtKB-KW
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: Chromosome 3

Organism-specific databases

HGNCiHGNC:7833. NKTR.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31641.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14621462NK-tumor recognition protein
PRO_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 – 11551Phosphothreonine1 Publication
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

ArrayExpressiP30414.
BgeeiP30414.
CleanExiHS_NKTR.
GenevestigatoriP30414.

Organism-specific databases

HPAiHPA022120.
HPA051576.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HE9X-ray2.00A/B7-179[»]
ProteinModelPortaliP30414.
SMRiP30414. Positions 7-177.

Miscellaneous databases

EvolutionaryTraceiP30414.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 175166PPIase cyclophilin-type
Add
BLAST

Region

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

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0652.
HOGENOMiHOG000113792.
HOVERGENiHBG052631.
InParanoidiP30414.
KOiK12740.
OMAiVSDQKPS.
OrthoDBiEOG79GT7W.
PhylomeDBiP30414.
TreeFamiTF318563.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
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

MGAQDRPQCH FDIEINREPV GRIMFQLFSD ICPKTCKNFL CLCSGEKGLG     50
KTTGKKLCYK GSTFHRVVKN FMIQGGDFSE GNGKGGESIY GGYFKDENFI 100
LKHDRAFLLS MANRGKHTNG SQFFITTKPA PHLDGVHVVF GLVISGFEVI 150
EQIENLKTDA ASRPYADVRV IDCGVLATKS IKDVFEKKRK KPTHSEGSDS 200
SSNSSSSSES SSESELEHER SRRRKHKRRP KVKRSKKRRK EASSSEEPRN 250
KHAMNPKGHS ERSDTNEKRS VDSSAKREKP VVRPEEIPPV PENRFLLRRD 300
MPVVTAEPEP KIPDVAPIVS DQKPSVSKSG RKIKGRGTIR YHTPPRSRSC 350
SESDDDDSSE TPPHWKEEMQ RLRAYRPPSG EKWSKGDKLS DPCSSRWDER 400
SLSQRSRSWS YNGYYSDLST ARHSGHHKKR RKEKKVKHKK KGKKQKHCRR 450
HKQTKKRRIL IPSDIESSKS STRRMKSSCD RERSSRSSSL SSHHSSKRDW 500
SKSDKDVQSS LTHSSRDSYR SKSHSQSYSR GSSRSRTASK SSSHSRSRSK 550
SRSSSKSGHR KRASKSPRKT ASQLSENKPV KTEPLRATMA QNENVVVQPV 600
VAENIPVIPL SDSPPPSRWK PGQKPWKPSY ERIQEMKAKT THLLPIQSTY 650
SLANIKETGS SSSYHKREKN SESDQSTYSK YSDRSSESSP RSRSRSSRSR 700
SYSRSYTRSR SLASSHSRSR SPSSRSHSRN KYSDHSQCSR SSSYTSISSD 750
DGRRAKRRLR SSGKKNSVSH KKHSSSSEKT LHSKYVKGRD RSSCVRKYSE 800
SRSSLDYSSD SEQSSVQATQ SAQEKEKQGQ MERTHNKQEK NRGEEKSKSE 850
RECPHSKKRT LKENLSDHLR NGSKPKRKNY AGSKWDSESN SERDVTKNSK 900
NDSHPSSDKE EGEATSDSES EVSEIHIKVK PTTKSSTNTS LPDDNGAWKS 950
SKQRTSTSDS EGSCSNSENN RGKPQKHKHG SKENLKREHT KKVKEKLKGK 1000
KDKKHKAPKR KQAFHWQPPL EFGEEEEEEI DDKQVTQESK EKKVSENNET 1050
IKDNILKTEK SSEEDLSGKH DTVTVSSDLD QFTKDDSKLS ISPTALNTEE 1100
NVACLQNIQH VEESVPNGVE DVLQTDDNME ICTPDRSSPA KVEETSPLGN 1150
ARLDTPDINI VLKQDMATEH PQAEVVKQES SMSESKVLGE VGKQDSSSAS 1200
LASAGESTGK KEVAEKSQIN LIDKKWKPLQ GVGNLAAPNA ATSSAVEVKV 1250
LTTVPEMKPQ GLRIEIKSKN KVRPGSLFDE VRKTARLNRR PRNQESSSDE 1300
QTPSRDDDSQ SRSPSRSRSK SETKSRHRTR SVSYSHSRSR SRSSTSSYRS 1350
RSYSRSRSRG WYSRGRTRSR SSSYRSYKSH RTSSRSRSRS SSYDPHSRSR 1400
SYTYDSYYSR SRSRSRSQRS DSYHRGRSYN RRSRSCRSYG SDSESDRSYS 1450
HHRSPSESSR YS 1462
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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi8039798.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04288 mRNA. Translation: AAA35734.2 .
AF184110 Genomic DNA. Translation: AAD56402.1 .
CCDSi CCDS2702.1.
PIRi A47328.
RefSeqi NP_005376.2. NM_005385.3.
UniGenei Hs.529509.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HE9 X-ray 2.00 A/B 7-179 [» ]
ProteinModelPortali P30414.
SMRi P30414. Positions 7-177.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110885. 5 interactions.
IntActi P30414. 5 interactions.
STRINGi 9606.ENSP00000232978.

PTM databases

PhosphoSitei P30414.

Polymorphism databases

DMDMi 8039798.

Proteomic databases

MaxQBi P30414.
PaxDbi P30414.
PeptideAtlasi P30414.
PRIDEi P30414.

Protocols and materials databases

DNASUi 4820.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000232978 ; ENSP00000232978 ; ENSG00000114857 .
GeneIDi 4820.
KEGGi hsa:4820.
UCSCi uc003clm.1. human.

Organism-specific databases

CTDi 4820.
GeneCardsi GC03P042617.
HGNCi HGNC:7833. NKTR.
HPAi HPA022120.
HPA051576.
MIMi 161565. gene.
neXtProti NX_P30414.
PharmGKBi PA31641.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0652.
HOGENOMi HOG000113792.
HOVERGENi HBG052631.
InParanoidi P30414.
KOi K12740.
OMAi VSDQKPS.
OrthoDBi EOG79GT7W.
PhylomeDBi P30414.
TreeFami TF318563.

Miscellaneous databases

ChiTaRSi NKTR. human.
EvolutionaryTracei P30414.
GeneWikii NKTR.
GenomeRNAii 4820.
NextBioi 18572.
PMAP-CutDB P30414.
PROi P30414.
SOURCEi Search...

Gene expression databases

ArrayExpressi P30414.
Bgeei P30414.
CleanExi HS_NKTR.
Genevestigatori P30414.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 121 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

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