CFTR_HUMAN - dbPTM
CFTR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CFTR_HUMAN
UniProt AC P13569
Protein Name Cystic fibrosis transmembrane conductance regulator
Gene Name CFTR
Organism Homo sapiens (Human).
Sequence Length 1480
Subcellular Localization Apical cell membrane
Multi-pass membrane protein . Early endosome membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein . Recycling endosome membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-p
Protein Description Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. [PubMed: 26823428 Mediates the transport of chloride ions across the cell membrane]
Protein Sequence MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MQRSPLEKASV
----CCCCHHHHHHH
33.2824719451
45PhosphorylationYQIPSVDSADNLSEK
CCCCCCCCCCCHHHH
35.05-
50PhosphorylationVDSADNLSEKLEREW
CCCCCCHHHHHHHHH
38.65-
94PhosphorylationFLYLGEVTKAVQPLL
HHHHHHHHHHHHHHH
14.69-
256PhosphorylationDQRAGKISERLVITS
HHCCCCCCCEEEECH
21.83-
291PhosphorylationMIENLRQTELKLTRK
HHHHHHHHHHHHHHH
36.5320068231
420UbiquitinationKQNNNNRKTSNGDDS
HHCCCCCCCCCCCCC
59.43-
421PhosphorylationQNNNNRKTSNGDDSL
HCCCCCCCCCCCCCC
24.9624719451
422PhosphorylationNNNNRKTSNGDDSLF
CCCCCCCCCCCCCCC
41.6821930781
427PhosphorylationKTSNGDDSLFFSNFS
CCCCCCCCCCCCCCC
31.64-
447SumoylationVLKDINFKIERGQLL
CCCCCCEEEECCCEE
38.89-
447SumoylationVLKDINFKIERGQLL
CCCCCCEEEECCCEE
38.89-
466PhosphorylationSTGAGKTSLLMVIMG
CCCCCHHHEEEEEEC
24.0026657352
489PhosphorylationIKHSGRISFCSQFSW
CCCCCCEEEEECCCC
20.8830631047
492PhosphorylationSGRISFCSQFSWIMP
CCCEEEEECCCCCCC
32.0530631047
501PhosphorylationFSWIMPGTIKENIIF
CCCCCCCCCCCCEEE
24.0130631047
511PhosphorylationENIIFGVSYDEYRYR
CCEEEEECCCHHHHH
27.5221930781
512PhosphorylationNIIFGVSYDEYRYRS
CEEEEECCCHHHHHH
15.4721807898
515PhosphorylationFGVSYDEYRYRSVIK
EEECCCHHHHHHHHH
15.2817053785
524S-palmitoylationYRSVIKACQLEEDIS
HHHHHHHHCCHHHHH
3.9422119790
547PhosphorylationVLGEGGITLSGGQRA
EEECCCEECCCHHHH
20.3925278378
549PhosphorylationGEGGITLSGGQRARI
ECCCEECCCHHHHHH
32.0220068231
582PhosphorylationFGYLDVLTEKEIFES
CCCCCCCCHHHHHHH
44.8822817900
604PhosphorylationNKTRILVTSKMEHLK
CCCEEEEECCHHHHH
21.1322817900
605PhosphorylationKTRILVTSKMEHLKK
CCEEEEECCHHHHHH
23.64-
641PhosphorylationQNLQPDFSSKLMGCD
HHCCCCCCHHHCCCC
33.6622817900
660PhosphorylationFSAERRNSILTETLH
CCHHHHHHHHHHHHH
19.701716180
670PhosphorylationTETLHRFSLEGDAPV
HHHHHHHCCCCCCCC
26.0125330774
682PhosphorylationAPVSWTETKKQSFKQ
CCCCCCHHCCHHHHC
35.8522817900
686PhosphorylationWTETKKQSFKQTGEF
CCHHCCHHHHCCCCC
43.2022817900
688UbiquitinationETKKQSFKQTGEFGE
HHCCHHHHCCCCCCH
52.8022119790
700PhosphorylationFGEKRKNSILNPINS
CCHHHCCCCCCHHHH
31.3322817900
707PhosphorylationSILNPINSIRKFSIV
CCCCHHHHHHCCEEE
25.2122817900
712PhosphorylationINSIRKFSIVQKTPL
HHHHHCCEEEECCCC
25.5322817900
717PhosphorylationKFSIVQKTPLQMNGI
CCEEEECCCCCCCCC
16.4922119790
728PhosphorylationMNGIEEDSDEPLERR
CCCCCCCCCCCHHHH
47.3423879269
737PhosphorylationEPLERRLSLVPDSEQ
CCHHHHHCCCCCHHH
26.0521455600
753PhosphorylationEAILPRISVISTGPT
CEECCCEEEEECCCC
18.0622817900
768PhosphorylationLQARRRQSVLNLMTH
HHHHHHHHHHHHHHC
27.1021455600
774PhosphorylationQSVLNLMTHSVNQGQ
HHHHHHHHCCCCCCC
17.7323312004
776PhosphorylationVLNLMTHSVNQGQNI
HHHHHHCCCCCCCCC
17.3823312004
790PhosphorylationIHRKTTASTRKVSLA
CCCCCCCCCCCCCCC
27.0122817900
795PhosphorylationTASTRKVSLAPQANL
CCCCCCCCCCCCCCC
23.111716180
803PhosphorylationLAPQANLTELDIYSR
CCCCCCCCHHHHHHH
34.0224719451
808PhosphorylationNLTELDIYSRRLSQE
CCCHHHHHHHHHHHH
8.8728442448
809PhosphorylationLTELDIYSRRLSQET
CCHHHHHHHHHHHHH
15.9722817900
813PhosphorylationDIYSRRLSQETGLEI
HHHHHHHHHHHCCCC
24.9421455600
816PhosphorylationSRRLSQETGLEISEE
HHHHHHHHCCCCCHH
39.16-
894N-linked_GlycosylationTPLQDKGNSTHSRNN
CCCCCCCCCCCCCCC
49.857518437
900N-linked_GlycosylationGNSTHSRNNSYAVII
CCCCCCCCCEEEEEE
44.837518437
1014PhosphorylationVVAVLQPYIFVATVP
HHHHHHCCHHHHHHH
8.27-
1019PhosphorylationQPYIFVATVPVIVAF
HCCHHHHHHHHHHHH
21.75-
1045PhosphorylationQQLKQLESEGRSPIF
HHHHHHHHCCCCHHH
54.68-
1171PhosphorylationFKFIDMPTEGKPTKS
HHHCCCCCCCCCCCC
51.2128509920
1176PhosphorylationMPTEGKPTKSTKPYK
CCCCCCCCCCCCCCC
40.9019413330
1246PhosphorylationRVGLLGRTGSGKSTL
EEEEECCCCCCHHHH
33.6228258704
1248PhosphorylationGLLGRTGSGKSTLLS
EEECCCCCCHHHHHH
42.2928258704
1255PhosphorylationSGKSTLLSAFLRLLN
CCHHHHHHHHHHHHC
21.7822210691
1344GlutathionylationFVLVDGGCVLSHGHK
EEEEECCEEECCHHH
3.2122833525
1359PhosphorylationQLMCLARSVLSKAKI
HHHHHHHHHHHHCEE
23.0820068231
1362PhosphorylationCLARSVLSKAKILLL
HHHHHHHHHCEEHHH
28.5420068231
1395S-palmitoylationLKQAFADCTVILCEH
HHHHHCCCEEEEECH
2.6922119790
1424PhosphorylationEENKVRQYDSIQKLL
ECCCHHCHHHHHHHH
10.9026270265
1426PhosphorylationNKVRQYDSIQKLLNE
CCHHCHHHHHHHHHH
23.2226270265
1444PhosphorylationFRQAISPSDRVKLFP
HHHCCCHHHHCCCCC
31.1222119790
1455PhosphorylationKLFPHRNSSKCKSKP
CCCCCCCCHHCCCCH
31.0024670416
1456PhosphorylationLFPHRNSSKCKSKPQ
CCCCCCCHHCCCCHH
45.697680525
1471PhosphorylationIAALKEETEEEVQDT
HHHHHHHHHHHHHHH
50.1921930781

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
421TPhosphorylationKinaseCK2A1P68400
PSP
422SPhosphorylationKinaseCK2A1P68400
PSP
422SPhosphorylationKinasePKA-FAMILY-GPS
427SPhosphorylationKinaseCK2A1P68400
PSP
511SPhosphorylationKinaseCSNK2A1P68400
GPS
511SPhosphorylationKinaseCK2-FAMILY-GPS
512YPhosphorylationKinaseSYKP43405
PSP
604TPhosphorylationKinasePRKCAP05696
GPS
641SPhosphorylationKinasePRKCAP05696
GPS
641SPhosphorylationKinasePKCAP17252
PSP
660SPhosphorylationKinasePKG-FAMILY-GPS
660SPhosphorylationKinasePRKCAP17252
GPS
660SPhosphorylationKinasePKA-FAMILY-GPS
660SPhosphorylationKinasePRKG1P00516
GPS
660SPhosphorylationKinasePKA_GROUP-PhosphoELM
660SPhosphorylationKinasePKG/CGK_GROUP-PhosphoELM
660SPhosphorylationKinasePKA-Uniprot
660SPhosphorylationKinasePKACAP17612
PSP
660SPhosphorylationKinasePRKACAP00517
GPS
670SPhosphorylationKinasePKA-Uniprot
670SPhosphorylationKinasePKACAP17612
PSP
682TPhosphorylationKinasePKCAP17252
PSP
682TPhosphorylationKinasePRKCAP05696
GPS
686SPhosphorylationKinasePKC_GROUP-PhosphoELM
686SPhosphorylationKinasePKC-FAMILY-GPS
686SPhosphorylationKinasePKC-Uniprot
686SPhosphorylationKinaseKPCAP17252
PhosphoELM
686SPhosphorylationKinasePRKCAP05696
GPS
700SPhosphorylationKinasePKA-Uniprot
700SPhosphorylationKinasePKA-FAMILY-GPS
700SPhosphorylationKinasePKG/CGK_GROUP-PhosphoELM
700SPhosphorylationKinasePKG-FAMILY-GPS
700SPhosphorylationKinasePRKACAP00517
GPS
700SPhosphorylationKinasePKACAP17612
PSP
700SPhosphorylationKinasePKA_GROUP-PhosphoELM
700SPhosphorylationKinasePRKG1P00516
GPS
707SPhosphorylationKinasePRKCAP05696
GPS
712SPhosphorylationKinasePKA-Uniprot
712SPhosphorylationKinasePKA-FAMILY-GPS
712SPhosphorylationKinasePRKACAP17612
GPS
737SPhosphorylationKinasePKG-FAMILY-GPS
737SPhosphorylationKinasePRKAA1Q13131
GPS
737SPhosphorylationKinasePKG/CGK_GROUP-PhosphoELM
737SPhosphorylationKinasePKA_GROUP-PhosphoELM
737SPhosphorylationKinasePKA-Uniprot
737SPhosphorylationKinasePRKACAP17612
GPS
737SPhosphorylationKinaseLMTK2Q8IWU2
GPS
737SPhosphorylationKinasePRKCAP17252
GPS
737SPhosphorylationKinasePKA-FAMILY-GPS
753SPhosphorylationKinasePKA_GROUP-PhosphoELM
753SPhosphorylationKinasePKA-FAMILY-GPS
753SPhosphorylationKinasePKA-Uniprot
753SPhosphorylationKinasePRKACAP17612
GPS
768SPhosphorylationKinasePKA-FAMILY-GPS
768SPhosphorylationKinaseAMPK-FAMILY-GPS
768SPhosphorylationKinasePKG/CGK_GROUP-PhosphoELM
768SPhosphorylationKinasePKA_GROUP-PhosphoELM
768SPhosphorylationKinasePKA-Uniprot
768SPhosphorylationKinasePRKAA1Q13131
GPS
768SPhosphorylationKinasePRKACAP17612
GPS
768SPhosphorylationKinasePKG-FAMILY-GPS
790SPhosphorylationKinasePKC-Uniprot
790SPhosphorylationKinasePKC_GROUP-PhosphoELM
790SPhosphorylationKinasePRKCAP05696
GPS
790SPhosphorylationKinasePKC-FAMILY-GPS
795SPhosphorylationKinasePKA-FAMILY-GPS
795SPhosphorylationKinasePRKCAP17252
GPS
795SPhosphorylationKinasePKA-Uniprot
795SPhosphorylationKinasePRKACAP17612
GPS
795SPhosphorylationKinasePKG/CGK_GROUP-PhosphoELM
795SPhosphorylationKinasePKA_GROUP-PhosphoELM
795SPhosphorylationKinasePKG-FAMILY-GPS
813SPhosphorylationKinasePKA-FAMILY-GPS
813SPhosphorylationKinasePKG/CGK_GROUP-PhosphoELM
813SPhosphorylationKinasePKA_GROUP-PhosphoELM
813SPhosphorylationKinasePKA-Uniprot
813SPhosphorylationKinasePKG-FAMILY-GPS
813SPhosphorylationKinasePRKCAP17252
GPS
813SPhosphorylationKinasePRKACAP17612
GPS
813SPhosphorylationKinasePRKAA1Q13131
GPS
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:11146634
-KUbiquitinationE3 ubiquitin ligaseAMFRQ9UKV5
PMID:18216283
-KUbiquitinationE3 ubiquitin ligaseRNF5Q99942
PMID:21148293
-KUbiquitinationE3 ubiquitin ligaseRNF185Q96GF1
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:22467879
-KUbiquitinationE3 ubiquitin ligaseMARCHF2Q9P0N8
PMID:23818989

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CFTR_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CFTR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GOPC_HUMANGOPCphysical
11707463
KCNJ1_HUMANKCNJ1physical
14604981
NHRF4_HUMANPDZD3physical
12615054
NHRF1_HUMANSLC9A3R1physical
12615054
NHRF1_HUMANSLC9A3R1physical
9613608
HSP7C_HUMANHSPA8physical
10075921
DNJB1_HUMANDNAJB1physical
10075921
DNJA1_HUMANDNAJA1physical
10075921
KPCE_HUMANPRKCEphysical
11956211
SNP23_HUMANSNAP23physical
12209004
STX1A_HUMANSTX1Aphysical
12209004
CLCN3_HUMANCLCN3physical
12471024
NHRF1_HUMANSLC9A3R1physical
9671706
NHRF2_HUMANSLC9A3R2physical
10893422
EZRI_HUMANEZRphysical
10893422
NHRF1_HUMANSLC9A3R1physical
9677412
NHRF1_HUMANSLC9A3R1physical
12403779
NHRF3_MOUSEPdzk1physical
11051556
CFTR_HUMANCFTRphysical
11051556
DNJC5_HUMANDNAJC5physical
12039948
AMFR_HUMANAMFRphysical
18216283
TERA_HUMANVCPphysical
16621797
HSP7C_HUMANHSPA8physical
15611333
COMD1_HUMANCOMMD1physical
21483833
CBL_HUMANCBLphysical
20525683
NEDD4_HUMANNEDD4physical
19617352
JKAMP_HUMANJKAMPphysical
19269966
RNF5_HUMANRNF5physical
19269966
TERA_HUMANVCPphysical
19828134
AMFR_HUMANAMFRphysical
19828134
RAB5A_HUMANRAB5Aphysical
19398555
RB11A_HUMANRAB11Aphysical
19398555
XPO2_DANREcse1lphysical
20933420
HSP74_HUMANHSPA4physical
17272822
HSP7C_HUMANHSPA8physical
17272822
HS90A_HUMANHSP90AA1physical
17272822
TERA_HUMANVCPphysical
17272822
DERL1_HUMANDERL1physical
16954204
TERA_HUMANVCPphysical
16954204
HSP74_HUMANHSPA4physical
18556464
HS90A_HUMANHSP90AA1physical
18556464
AHSA1_HUMANAHSA1physical
18556464
HSP74_HUMANHSPA4physical
19098309
CHIP_HUMANSTUB1physical
19098309
NHS_HUMANNHSphysical
14595111
CALX_HUMANCANXphysical
18716059
HSP74_HUMANHSPA4physical
18716059
BAG1_HUMANBAG1physical
23178238
HSPB1_HUMANHSPB1physical
23155000
HSPB2_HUMANHSPB2physical
23155000
UBP19_HUMANUSP19physical
19465887
CFTR_HUMANCFTRphysical
17110338
IMB1_HUMANKPNB1physical
17110338
HSP7C_HUMANHSPA8physical
17110338
DNJA1_HUMANDNAJA1physical
17110338
IPO7_HUMANIPO7physical
17110338
AHSA1_HUMANAHSA1physical
17110338
COF1_HUMANCFL1physical
17110338
DNJA2_HUMANDNAJA2physical
17110338
PP2AA_HUMANPPP2CAphysical
17110338
XPO2_HUMANCSE1Lphysical
17110338
2ABA_HUMANPPP2R2Aphysical
17110338
RCN1_HUMANRCN1physical
17110338
RACK1_HUMANGNB2L1physical
17110338
RCN2_HUMANRCN2physical
17110338
SEP11_HUMANSEPT11physical
17110338
RANG_HUMANRANBP1physical
17110338
XPO1_HUMANXPO1physical
17110338
2AAB_HUMANPPP2R1Bphysical
17110338
AT2A2_HUMANATP2A2physical
17110338
TCPG_HUMANCCT3physical
17110338
S61A1_HUMANSEC61A1physical
17110338
BAG2_HUMANBAG2physical
17110338
CALX_HUMANCANXphysical
17110338
TNPO3_HUMANTNPO3physical
17110338
NRIP3_HUMANNRIP3physical
17110338
MIRO1_HUMANRHOT1physical
17110338
HSP72_HUMANHSPA2physical
17110338
CALU_HUMANCALUphysical
17110338
TCPD_HUMANCCT4physical
17110338
PSA_HUMANNPEPPSphysical
17110338
RAN_HUMANRANphysical
17110338
HS90A_HUMANHSP90AA1physical
17110338
SYFA_HUMANFARSAphysical
17110338
P4HA1_HUMANP4HA1physical
17110338
KIF5C_HUMANKIF5Cphysical
17110338
HSP76_HUMANHSPA6physical
17110338
SNX4_HUMANSNX4physical
17110338
B3GN9_HUMANB3GNT9physical
17110338
IPO11_HUMANIPO11physical
17110338
KINH_HUMANKIF5Bphysical
17110338
KIF3A_HUMANKIF3Aphysical
17110338
DTL_HUMANDTLphysical
17110338
APC_HUMANAPCphysical
17110338
VIPR1_HUMANVIPR1physical
17110338
USP9X_HUMANUSP9Xphysical
17110338
PKD1_HUMANPKD1physical
17110338
CYTB_HUMANCSTBphysical
17110338
ELOB_HUMANTCEB2physical
17110338
S10A9_HUMANS100A9physical
17110338
HS90B_HUMANHSP90AB1physical
17110338
PSME2_HUMANPSME2physical
17110338
LEG3_HUMANLGALS3physical
17110338
S10A7_HUMANS100A7physical
17110338
TFG_HUMANTFGphysical
17110338
THEM6_HUMANTHEM6physical
17110338
SQOR_HUMANSQRDLphysical
17110338
NHRF2_HUMANSLC9A3R2physical
17110338
CH60_HUMANHSPD1physical
17110338
HS71L_HUMANHSPA1Lphysical
17110338
2AAA_HUMANPPP2R1Aphysical
17110338
SPTC1_HUMANSPTLC1physical
17110338
AIFM1_HUMANAIFM1physical
17110338
UBE3A_HUMANUBE3Aphysical
17110338
PSMD2_HUMANPSMD2physical
17110338
TMM43_HUMANTMEM43physical
17110338
BCR_HUMANBCRphysical
17110338
RYR2_HUMANRYR2physical
17110338
ELOC_HUMANTCEB1physical
17110338
PIMT_HUMANPCMT1physical
17110338
PDCD6_HUMANPDCD6physical
17110338
EMD_HUMANEMDphysical
17110338
S61A2_HUMANSEC61A2physical
17110338
TERA_HUMANVCPphysical
17110338
SFXN3_HUMANSFXN3physical
17110338
LEG4_HUMANLGALS4physical
17110338
F120A_HUMANFAM120Aphysical
17110338
COPB_HUMANCOPB1physical
17110338
LMO7_HUMANLMO7physical
17110338
VPS4A_HUMANVPS4Aphysical
17110338
ATX2L_HUMANATXN2Lphysical
17110338
TRIPC_HUMANTRIP12physical
17110338
PRKDC_HUMANPRKDCphysical
17110338
HSPB1_HUMANHSPB1physical
17110338
CD59_HUMANCD59physical
17110338
SH3L2_HUMANSH3BGRL2physical
17110338
MRP_HUMANMARCKSL1physical
17110338
LIN7C_HUMANLIN7Cphysical
17110338
HAX1_HUMANHAX1physical
17110338
EPN4_HUMANCLINT1physical
17110338
MS4A5_HUMANMS4A5physical
17110338
GNA11_HUMANGNA11physical
17110338
CLCA_HUMANCLTAphysical
17110338
EPCAM_HUMANEPCAMphysical
17110338
ATD3A_HUMANATAD3Aphysical
17110338
LRRF2_HUMANLRRFIP2physical
17110338
EPS8_HUMANEPS8physical
17110338
GNAI2_HUMANGNAI2physical
17110338
CLH2_HUMANCLTCL1physical
17110338
GRN_HUMANGRNphysical
17110338
SAP_HUMANPSAPphysical
17110338
CADH1_HUMANCDH1physical
17110338
REPS1_HUMANREPS1physical
17110338
PKHA6_HUMANPLEKHA6physical
17110338
XPP3_HUMANXPNPEP3physical
17110338
DAB2_HUMANDAB2physical
17110338
FLOT2_HUMANFLOT2physical
17110338
SNX9_HUMANSNX9physical
17110338
IRPL1_HUMANIL1RAPL1physical
17110338
CE170_HUMANCEP170physical
17110338
RYK_HUMANRYKphysical
17110338
ZO3_HUMANTJP3physical
17110338
MUC13_HUMANMUC13physical
17110338
ADCY8_HUMANADCY8physical
17110338
CLCA1_HUMANCLCA1physical
17110338
TIAM1_HUMANTIAM1physical
17110338
SVIL_HUMANSVILphysical
17110338
SORL_HUMANSORL1physical
17110338
IMB1_MOUSEKpnb1physical
17110338
RCN1_MOUSERcn1physical
17110338
GRP78_MOUSEHspa5physical
17110338
RCN2_MOUSERcn2physical
17110338
HS90B_MOUSEHsp90ab1physical
17110338
NHRF1_MOUSESlc9a3r1physical
17110338
S10A6_MOUSES100a6physical
17110338
TPP1_MOUSETpp1physical
17110338
ARF4_MOUSEArf4physical
17110338
TCPE_MOUSECct5physical
17110338
UBB_MOUSEUbbphysical
17110338
MMS19_MOUSEMms19physical
17110338
SRA1_MOUSESra1physical
17110338
TCPA_MOUSETcp1physical
17110338
FCN1_MOUSEFcnaphysical
17110338
RUVB1_MOUSERuvbl1physical
17110338
SEPT6_MOUSESept6physical
17110338
VATA_MOUSEAtp6v1aphysical
17110338
TRIM2_MOUSETrim2physical
17110338
DPYL2_MOUSEDpysl2physical
17110338
MAP4_MOUSEMap4physical
17110338
PCD15_MOUSEPcdh15physical
17110338
RACK1_MOUSEGnb2l1physical
17110338
LMNA_MOUSELmnaphysical
17110338
GRP75_MOUSEHspa9physical
17110338
CPNS1_MOUSECapns1physical
17110338
TPM3_MOUSETpm3physical
17110338
CAPR1_MOUSECaprin1physical
17110338
APOA2_MOUSEApoa2physical
17110338
TMOD3_MOUSETmod3physical
17110338
WSB1_MOUSEWsb1physical
17110338
ZO1_MOUSETjp1physical
17110338
LIMA1_MOUSELima1physical
17110338
AT2A3_MOUSEAtp2a3physical
17110338
AP1B1_MOUSEAp1b1physical
17110338
SHRM3_MOUSEShroom3physical
17110338
NHRF1_RATSlc9a3r1physical
17110338
TMM33_RATTmem33physical
17110338
UBC_RATUbcphysical
17110338
GRIP1_RATGrip1physical
17110338
FAT2_RATFat2physical
17110338
COF1_RATCfl1physical
17110338
DNJA1_RATDnaja1physical
17110338
HSP72_RATHspa2physical
17110338
GNA11_RATGna11physical
17110338
PLD2_RATPld2physical
17110338
ERLN2_HUMANERLIN2physical
17110338
PSB3_HUMANPSMB3physical
17110338
SGMR1_HUMANSIGMAR1physical
17110338
PSB1_HUMANPSMB1physical
17110338
ERLN1_HUMANERLIN1physical
17110338
CCD51_HUMANCCDC51physical
17110338
PSB4_HUMANPSMB4physical
17110338
TEBP_HUMANPTGES3physical
17110338
PPIB_HUMANPPIBphysical
17110338
PRS6B_HUMANPSMC4physical
17110338
SARAF_HUMANSARAFphysical
17110338
EMC2_HUMANEMC2physical
17110338
IPO9_HUMANIPO9physical
17110338
CAND1_HUMANCAND1physical
17110338
IPO5_HUMANIPO5physical
17110338
2ABB_HUMANPPP2R2Bphysical
17110338
SEPT6_HUMANSEPT6physical
17110338
HACD3_HUMANPTPLAD1physical
17110338
ESYT1_HUMANESYT1physical
17110338
PSD11_HUMANPSMD11physical
17110338
ERBIN_HUMANERBB2IPphysical
17110338
DCLK1_HUMANDCLK1physical
17110338
SEPT9_HUMANSEPT9physical
17110338
AT2A1_HUMANATP2A1physical
17110338
A2MG_HUMANA2Mphysical
17110338
PCDB8_HUMANPCDHB8physical
17110338
AKAP6_HUMANAKAP6physical
17110338
MED12_HUMANMED12physical
17110338
RYR3_HUMANRYR3physical
17110338
XPO2_MOUSECse1lphysical
17110338
CALU_MOUSECaluphysical
17110338
PSB1_MOUSEPsmb1physical
17110338
PSA5_MOUSEPsma5physical
17110338
PSA2_MOUSEPsma2physical
17110338
COF2_MOUSECfl2physical
17110338
FKBP8_MOUSEFkbp8physical
17110338
PSB3_MOUSEPsmb3physical
17110338
TEBP_MOUSEPtges3physical
17110338
EMC2_MOUSEEmc2physical
17110338
BAG3_MOUSEBag3physical
17110338
STIP1_MOUSEStip1physical
17110338
HS105_MOUSEHsph1physical
17110338
PP2AB_MOUSEPpp2cbphysical
17110338
SEPT3_MOUSESept3physical
17110338
CDC37_MOUSECdc37physical
17110338
PRS6A_MOUSEPsmc3physical
17110338
RUVB2_MOUSERuvbl2physical
17110338
CADH1_MOUSECdh1physical
17110338
PDE8A_MOUSEPde8aphysical
17110338
GRIK5_RATGrik5physical
17110338
ESYT1_RATEsyt1physical
17110338
DYHC1_RATDync1h1physical
17110338
TERA_HUMANVCPphysical
18216283
MRP4_HUMANABCC4physical
18045536
NHRF3_HUMANPDZK1physical
18045536
NHRF1_HUMANSLC9A3R1physical
17110338
S61A1_MOUSESec61a1physical
17110338
ELOC_RATTceb1physical
17110338
HS105_HUMANHSPH1physical
17110338
DNJA3_MOUSEDnaja3physical
17110338
TCPA_RATTcp1physical
17110338
SQSTM_HUMANSQSTM1physical
20711182
SQSTM_HUMANSQSTM1physical
23686137
EEA1_HUMANEEA1physical
23686137
NEDD4_HUMANNEDD4physical
25384981
S4A7_HUMANSLC4A7physical
12403779
HSPB1_HUMANHSPB1physical
26627832
AP2A_HUMANTFAP2Aphysical
20351096
DAB2_HUMANDAB2physical
20351096
MYO6_HUMANMYO6physical
20351096
UBP10_HUMANUSP10physical
22904170
RN185_HUMANRNF185physical
24019521
DNJC5_HUMANDNAJC5physical
16857740
HSP7C_HUMANHSPA8physical
16857740
JAK1_HUMANJAK1physical
27261451
CBL_HUMANCBLphysical
27261451
MARH2_HUMANMARCH2physical
27308891

Drug and Disease Associations
Kegg Disease
H00218 Cystic fibrosis (CF)
H00933 Hereditary pancreatitis; Hereditary chronic pancreatitis
H01033 Congenital bilateral absence of vas deferens
OMIM Disease
219700Cystic fibrosis (CF)
277180Congenital bilateral absence of the vas deferens (CBAVD)
Kegg Drug
D00808 Suramin hexasodium (USAN); Bayer 205 (TN)
D09916 Ivacaftor (USAN/INN); Kalydeco (TN)
D10134 Lumacaftor (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CFTR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mapping of cystic fibrosis transmembrane conductance regulatormembrane topology by glycosylation site insertion.";
Chang X.-B., Hou Y.-X., Jensen T.J., Riordan J.R.;
J. Biol. Chem. 269:18572-18575(1994).
Cited for: GLYCOSYLATION AT ASN-894 AND ASN-900, AND TOPOLOGY.
Palmitoylation
ReferencePubMed
"Purification of CFTR for mass spectrometry analysis: identificationof palmitoylation and other post-translational modifications.";
McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q.,Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.;
Protein Eng. Des. Sel. 25:7-14(2012).
Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717;SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688,PALMITOYLATION AT CYS-524 AND CYS-1395, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Purification of CFTR for mass spectrometry analysis: identificationof palmitoylation and other post-translational modifications.";
McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q.,Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.;
Protein Eng. Des. Sel. 25:7-14(2012).
Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717;SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688,PALMITOYLATION AT CYS-524 AND CYS-1395, AND MASS SPECTROMETRY.
"Evidence for phosphorylation of serine 753 in CFTR using a novelmetal-ion affinity resin and matrix-assisted laser desorption massspectrometry.";
Neville D.C.A., Rozanas C.R., Rice E.M., Gruis D.B., Verkman A.S.,Townsend R.R.;
Protein Sci. 6:2436-2445(1997).
Cited for: PHOSPHORYLATION AT SER-660; SER-700; SER-712; SER-737; SER-753;SER-768; SER-795 AND SER-813.
"Phosphorylation of the cystic fibrosis transmembrane conductanceregulator.";
Picciotto M.R., Cohn J.A., Bertuzzi G., Greenguard P., Nairn A.C.;
J. Biol. Chem. 267:12742-12752(1992).
Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-737; SER-768;SER-790; SER-795 AND SER-813.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1176, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-515, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Purification of CFTR for mass spectrometry analysis: identificationof palmitoylation and other post-translational modifications.";
McClure M., Delucas L.J., Wilson L., Ray M., Rowe S.M., Wu X., Dai Q.,Hong J.S., Sorscher E.J., Kappes J.C., Barnes S.;
Protein Eng. Des. Sel. 25:7-14(2012).
Cited for: PHOSPHORYLATION AT SER-660; SER-686; SER-700; SER-712; THR-717;SER-737; SER-795; SER-1444 AND SER-1456, UBIQUITINATION AT LYS-688,PALMITOYLATION AT CYS-524 AND CYS-1395, AND MASS SPECTROMETRY.

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