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P30414

- NKTR_HUMAN

UniProt

P30414 - NKTR_HUMAN

Protein

NK-tumor recognition protein

Gene

NKTR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31641.

    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 – 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

    1
    1462
    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.
    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.
    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

    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: October 1, 2014
    This is version 122 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