P30414 (NKTR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Putative peptidyl-prolyl cis-trans isomerase
   Short name=PPIase
   EC=5.2.1.8
   Alternative name(s):
   Rotamase

Gene names

Name:

NKTR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1462 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Cyclosporin
Molecular function	Isomerase Rotamase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cyclosporin 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1462

1462

NK-tumor recognition protein

PRO_0000064217

Regions

Domain

10 – 175

166

PPIase cyclophilin-type

Region

1311 – 1348

38

Arg/Ser tandem repeat-rich

Compositional bias

194 – 244

51

Arg/Ser-rich

Compositional bias

219 – 240

22

Arg/Lys-rich (basic)

Compositional bias

421 – 457

37

Arg/Lys-rich (basic)

Compositional bias

466 – 574

109

Arg/Ser-rich

Compositional bias

664 – 814

151

Arg/Ser-rich

Compositional bias

970 – 1010

41

Arg/Lys-rich (basic)

Amino acid modifications

Modified residue

379

1

Phosphoserine Ref.4 Ref.8

Modified residue

463

1

Phosphoserine Ref.5 Ref.7 Ref.8

Modified residue

887

1

Phosphoserine Ref.5

Modified residue

889

1

Phosphoserine Ref.5

Modified residue

891

1

Phosphoserine Ref.5

Modified residue

1146

1

Phosphoserine Ref.7 Ref.8

Modified residue

1155

1

Phosphothreonine Ref.8

Cross-link

1258

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Natural variant

271

1

V → G.
Corresponds to variant rs35726114 [ dbSNP | Ensembl ].

VAR_061765

Natural variant

861

1

L → V.
Corresponds to variant rs33969824 [ dbSNP | Ensembl ].

VAR_051773

Natural variant

935

1

S → L.
Corresponds to variant rs35770315 [ dbSNP | Ensembl ].

VAR_051774

Natural variant

1182

1

M → T.
Corresponds to variant rs34897686 [ dbSNP | Ensembl ].

VAR_061766

Secondary structure

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1462

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Beta strand

18 – 27

10

Turn

29 – 31

3

Helix

33 – 44

12

Turn

51 – 53

3

Beta strand

55 – 57

3

Beta strand

63 – 68

6

Turn

69 – 71

3

Beta strand

72 – 75

4

Turn

78 – 80

3

Beta strand

81 – 84

4

Beta strand

108 – 111

4

Beta strand

123 – 128

6

Helix

131 – 133

3

Turn

134 – 136

3

Beta strand

139 – 145

7

Helix

147 – 154

8

Beta strand

164 – 166

3

Beta strand

168 – 175

8

Sequences

	Sequence		Length	Mass (Da)
	P30414 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: D98A1147763EF527	FASTA	1,462	165,677
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L04288 mRNA. Translation: AAA35734.2.
AF184110 Genomic DNA. Translation: AAD56402.1.

IPI

IPI00295022.

PIR

A47328.

RefSeq

NP_005376.2. NM_005385.3.

UniGene

Hs.529509.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HE9	X-ray	2.00	A/B	7-179	[»]

ProteinModelPortal

P30414.

ModBase

Search...

Protein-protein interaction databases

IntAct

P30414. 5 interactions.

STRING

9606.ENSP00000232978.

PTM databases

PhosphoSite

P30414.

Polymorphism databases

DMDM

8039798.

Proteomic databases

PaxDb

P30414.

PeptideAtlas

P30414.

PRIDE

P30414.

Protocols and materials databases

DNASU

4820.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000232978; ENSP00000232978; ENSG00000114857.

GeneID

4820.

KEGG

hsa:4820.

UCSC

uc003clm.1. human.

Organism-specific databases

CTD

4820.

GeneCards

GC03P042617.

HGNC

HGNC:7833. NKTR.

HPA

HPA022120.

MIM

161565. gene.

neXtProt

NX_P30414.

PharmGKB

PA31641.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0652.

HOGENOM

HOG000113792.

HOVERGEN

HBG052631.

InParanoid

P30414.

KO

K12740.

OMA

SWSYNGY.

OrthoDB

EOG47SSD2.

PhylomeDB

P30414.

Gene expression databases

ArrayExpress

P30414.

Bgee

P30414.

CleanEx

HS_NKTR.

Genevestigator

P30414.

GermOnline

ENSG00000114857. Homo sapiens.

Family and domain databases

InterPro

IPR002130. Cyclophilin-like_PPIase_dom.
IPR020892. Cyclophilin-type_PPIase_CS.
[Graphical view]

Pfam

PF00160. Pro_isomerase. 1 hit.
[Graphical view]

PRINTS

PR00153. CSAPPISMRASE.

SUPFAM

SSF50891. CSA_PPIase. 1 hit.

PROSITE

PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NKTR. human.

EvolutionaryTrace

P30414.

GenomeRNAi

4820.

NextBio

18572.

PMAP-CutDB

P30414.

SOURCE

Search...

Entry information

Entry name

NKTR_HUMAN

Accession

Primary (citable) accession number: P30414

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.