Search Results

Overview

Uniprot IDP30414
Protein NameNK-tumor recognition protein
Gene NameNKTR
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1224 SQINLIDKKWKPLQG
1225 QINLIDKKWKPLQGV
328 DQKPSVSKSGRKIKG
637 YERIQEMKAKTTHLL
784 SEKTLHSKYVKGRDR

Function

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Component of a putative tumor-recognition complex involved in the function of NK cells (PubMed:8421688)

Protein Sequence

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

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0016018 cyclosporin A binding
Molecular Function GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Biological Process GO:0006457 protein folding

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.