Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Cystic fibrosis transmembrane conductance regulator  

UniProtKB / Swiss-Prot ID :  CFTR_HUMAN

Gene Name (Synonyms) : 
CFTR, ABCC7  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Early endosome membrane; Multi-pass membrane protein. 

Protein Function :  Involved in the transport of chloride ions. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the SLC4A7 transporter. 

Transmembrane Topology (topPTM) : CFTR_HUMAN 

Protein Sequence MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLI...
Predicted Secondary Structure CCCCCCCCCCCHHHHHHHHHHHHHHHCCCCCCCHHCCCCCCHHHHHHHHHHHHHHHHHHHCCCCCCCHHH...
Protein Variant
LocationDescription
13S -> F (in CF). VAR_000101
31R -> C (in dbSNP:rs1800073). VAR_000102
31R -> L (in CF). VAR_000103
42S -> F (in CF). VAR_000104
44D -> G (in CF). VAR_000105
44D -> V (in dbSNP:rs1800074). VAR_000106
50S -> Y (in CBAVD). VAR_000107
57W -> G (in CF). VAR_000108
67P -> L (in CF). VAR_000109
74R -> W (in CF). VAR_000110
75R -> Q (in dbSNP:rs1800076). VAR_000111
85G -> E (in CF). VAR_000112
87F -> L (in CF). VAR_000113
91G -> R (in CF). VAR_000114
92E -> K (in CF). VAR_000115
98Q -> R (in CF). VAR_000116
105I -> S (in CF). VAR_000117
109Y -> C (in CF). VAR_000118
110D -> H (in CF). VAR_000119
111P -> L (in CBAVD). VAR_000120
117R -> C (in CF). VAR_000121
117R -> H (in CF and CBAVD). VAR_000122
117R -> L (in CF). VAR_000123
117R -> P (in CF). VAR_000124
120A -> T (in CF). VAR_000125
138L -> P (in dbSNP:rs1800078). VAR_009895
139H -> R (in CF). VAR_000126
141A -> D (in CF). VAR_000127
148I -> T (in CF; dbSNP:rs35516286). VAR_000128
149G -> R (in CBAVD). VAR_000129
170R -> H (in dbSNP:rs1800079). VAR_009896
178G -> R (in CF). VAR_000130
182S -> G (in dbSNP:rs1800080). VAR_009897
192Missing (in CF). VAR_000131
193E -> K (in CBAVD and CF). VAR_000132
199H -> Q (in CF). VAR_000133
199H -> Y (in CF). VAR_000134
205P -> S (in CF). VAR_000135
206L -> W (in CF). VAR_000136
225C -> R (in CF). VAR_000137
244M -> K (in CBAVD). VAR_000138
258R -> G (in CBAVD). VAR_000139
287N -> Y (in CF). VAR_000140
297R -> Q (in CF). VAR_000141
301Y -> C (in CF). VAR_000142
307S -> N (in CF). VAR_000143
311F -> L (in CF). VAR_000144
311Missing (in CF). VAR_000145
314G -> E (in CF). VAR_000146
314G -> R (in CF). VAR_000147
322V -> M (in dbSNP:rs1800085). VAR_009898
334R -> W (in CF; mild). VAR_000148
336I -> K (in CF). VAR_000150
338T -> I (in CF; mild; isolated hypotonicdehydration).
346L -> P (in CF; dominant mutation but mildphenotype).
347R -> H (in CF). VAR_000153
347R -> L (in CF). VAR_000154
347R -> P (in CF; MILD). VAR_000155
351T -> S (in dbSNP:rs1800086). VAR_009899
352R -> Q (in CF). VAR_000156
353Q -> H (in dbSNP:rs1800087). VAR_009900
359QT -> KK (in CF). VAR_000158
359Q -> K (in CF). VAR_000157
370K -> KNK (in CF). VAR_000159
455A -> E (in CF). VAR_000160
456V -> F (in CF). VAR_000161
458G -> V (in CF). VAR_000162
467L -> F (in dbSNP:rs1800089). VAR_000163
470V -> M (in dbSNP:rs213950). VAR_000164
480G -> C (in CF). VAR_000165
492S -> F (in CF). VAR_000166
504E -> Q (in CF). VAR_000167
506I -> M (in dbSNP:rs1800092). VAR_009901
506I -> V. VAR_000168
507I -> V (in dbSNP:rs1800091). VAR_000169
507Missing (in CF). VAR_000170
508F -> C (in dbSNP:rs1800093). VAR_000172
508Missing (in CF and CBAVD; most commonmutation; 72% of the population; CFTR
513D -> G (in CBAVD). VAR_000173
520V -> F (in CF). VAR_000174
532K -> E (in dbSNP:rs35032490). VAR_048150
544G -> V (in CBAVD). VAR_000175
549S -> I (in CF). VAR_000177
549S -> N (in CF). VAR_000176
549S -> R (in CF). VAR_000178
551G -> D (in CF). VAR_000179
551G -> S (in CF). VAR_000180
553R -> Q (in CF). VAR_000181
558L -> S (in CF). VAR_000182
559A -> T (in CF). VAR_000183
560R -> K (in CF). VAR_000184
560R -> S (in CF). VAR_000185
560R -> T (in CF). VAR_000186
562V -> I (in dbSNP:rs1800097). VAR_000187
562V -> L (in CF). VAR_000188
563Y -> N (in CF). VAR_000189
569Y -> C (in CF). VAR_000190
569Y -> D (in CF). VAR_000191
569Y -> H (in CF). VAR_000192
571L -> S (in CF). VAR_000193
572D -> N (in CF). VAR_000194
574P -> H (in CF). VAR_000195
576G -> A (in dbSNP:rs1800098). VAR_000196
579D -> G (in CF). VAR_000197
601I -> F (in CF). VAR_000198
605S -> F (in dbSNP:rs766874). VAR_048151
610L -> S (in CF). VAR_000199
613A -> T (in CF). VAR_000200
614D -> G (in CF). VAR_000201
618I -> T (in CF). VAR_000202
619L -> S (in CF). VAR_000203
620H -> P (in CF). VAR_000204
620H -> Q (in CF). VAR_000205
622G -> D (in oligospermia). VAR_000206
628G -> R (in CF). VAR_000207
633L -> P (in CF). VAR_000208
648D -> V (in CF). VAR_000209
651D -> N (in CF). VAR_000210
654S -> G (in dbSNP:rs1800099). VAR_009902
665T -> S (in CF). VAR_000211
668R -> C (in dbSNP:rs1800100). VAR_000212
693F -> L (in dbSNP:rs1800101). VAR_000213
754V -> M (in CF). VAR_000214
766R -> M (in CBAVD). VAR_000215
792R -> G (in CBAVD). VAR_000216
800A -> G (in CBAVD). VAR_000217
807I -> M (in CBAVD; dbSNP:rs1800103). VAR_000218
822E -> K (in CF). VAR_000219
826E -> K (in thoracic sarcoidosis). VAR_000220
866C -> Y (in CF). VAR_000221
903Y -> H (in dbSNP:rs1800106). VAR_009903
909S -> I (in dbSNP:rs1800107). VAR_009904
912S -> L. VAR_000222
913Y -> C (in CF). VAR_000223
917Y -> C (in CF). VAR_000224
949H -> Y (in CF). VAR_000225
952M -> I (in CF). VAR_000226
967L -> S (in dbSNP:rs1800110). VAR_009905
997L -> F (in CF; dbSNP:rs1800111). VAR_000227
1005I -> R (in CF). VAR_000228
1006A -> E (in CF). VAR_000229
1013P -> L (in CF). VAR_000230
1028M -> I (in CF). VAR_000231
1052F -> V (in CF). VAR_000232
1061G -> R (in CF). VAR_000233
1065L -> P (in CF). VAR_000234
1065L -> R (in CF). VAR_000235
1066R -> C (in CF). VAR_000236
1066R -> H (in CF). VAR_000237
1066R -> L (in CF). VAR_000238
1067A -> T (in CF). VAR_000239
1067A -> V (in dbSNP:rs1800114). VAR_000240
1070R -> P (in CF). VAR_000242
1070R -> Q (in CF). VAR_000241
1070R -> W (in CBAVD). VAR_011564
1071Q -> P (in CF). VAR_000243
1072P -> L (in CF). VAR_000244
1077L -> P (in CF). VAR_000245
1085H -> R (in CF). VAR_000246
1098W -> R (in CF). VAR_000247
1101M -> K (in CF; dbSNP:rs36210737). VAR_000248
1101M -> R (in CF). VAR_011565
1137M -> V (in CF). VAR_000249
1140Missing (in CF). VAR_000250
1152D -> H (in CF). VAR_000251
1162R -> L (in dbSNP:rs1800120). VAR_000252
1220T -> I (in dbSNP:rs1800123). VAR_000253
1234I -> V (in CF). VAR_000254
1235S -> R (in CF). VAR_000255
1244G -> E (in CF). VAR_000256
1249G -> E (in CF). VAR_000257
1251S -> N (in CF). VAR_000258
1255S -> P (in CF). VAR_000259
1270D -> N (in CF; dbSNP:rs11971167). VAR_000260
1282W -> R (in CF). VAR_000261
1283R -> M (in CF). VAR_000262
1286F -> S (in CF). VAR_000263
1291Q -> H (in CF). VAR_000264
1291Q -> R (in CF). VAR_000265
1303N -> H (in CF). VAR_000266
1303N -> K (in CF). VAR_000267
1349G -> D (in CF). VAR_000268
1364A -> V (in CBAVD). VAR_000269
1397V -> E (in CF). VAR_000270
1453R -> W (in dbSNP:rs4148725). VAR_048152
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
291PhosphothreonineNLRQTELKL
HHHHHHHHH
36.53HPRD
Link-
291PhosphothreonineNLRQTELKL
HHHHHHHHH
36.53Phosphositeplus
Link-
422PhosphoserineNRKTSNGDD
CCCCCCCEE
41.68Phosphositeplus
Link-
511PhosphoserineIFGVSYDEY
CCCCCCCCH
27.52Phosphositeplus
Link
512PhosphotyrosineFGVSYDEYR
CCCCCCCHH
15.47Phosphositeplus
Link
515PhosphotyrosineSYDEYRYRS
CCCCHHHHH
15.28Phosphositeplus
Link
515Phosphotyrosine.SYDEYRYRS
CCCCHHHHH
15.28UniProtKB
Link
524S-palmitoyl cysteine.VIKACQLEE
HHHHHHHHH
3.94UniProtKB
Link
549PhosphoserineGITLSGGQR
CCCCCHHHH
32.02HPRD
Link
549PhosphoserineGITLSGGQR
CCCCCHHHH
32.02Phosphositeplus
Link
582PhosphothreonineLDVLTEKEI
CCHHHHHHH
44.88Phosphositeplus
Link
604PhosphothreonineRILVTSKME
EEEEECCHH
21.13Phosphositeplus
Link
641PhosphoserineQPDFSSKLM
CCHHHHHHH
33.66Phosphositeplus
Link
660PhosphoserineERRNSILTE
HHHCCCCCC
19.70Phosphositeplus
Link
660Phosphoserine (PKA_group;PKG/cGK_group)ERRNSILTE
HHHCCCCCC
19.70PhosphoELM
Link
660Phosphoserine (PRKG1)ERRNSILTE
HHHCCCCCC
19.70HPRD
Link
660Phosphoserine; by PKA.ERRNSILTE
HHHCCCCCC
19.70UniProtKB
Link
682PhosphothreonineSWTETKKQS
HHHHHHHHH
35.85Phosphositeplus
Link-
686PhosphoserineTKKQSFKQT
HHHHHHCCC
43.20Phosphositeplus
Link-
686Phosphoserine (PKC_group;PKC_group;PKC_alpha;PKC_alpha)TKKQSFKQT
HHHHHHCCC
43.20PhosphoELM
Link-
686Phosphoserine (PRKCA)TKKQSFKQT
HHHHHHCCC
43.20HPRD
Link-
686Phosphoserine; by PKC.TKKQSFKQT
HHHHHHCCC
43.20UniProtKB
Link-
688Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).KQSFKQTGE
HHHHCCCCC
52.80UniProtKB
Link-
700PhosphoserineKRKNSILNP
CCCCCCCCC
31.33Phosphositeplus
Link-
700Phosphoserine (PKA_group;PKG/cGK_group)KRKNSILNP
CCCCCCCCC
31.33PhosphoELM
Link-
700Phosphoserine (PRKACA)KRKNSILNP
CCCCCCCCC
31.33HPRD
Link-
700Phosphoserine (PRKG1)KRKNSILNP
CCCCCCCCC
31.33HPRD
Link-
700Phosphoserine; by PKA.KRKNSILNP
CCCCCCCCC
31.33UniProtKB
Link-
707PhosphoserineNPINSIRKF
CCCHHHHHH
25.21Phosphositeplus
Link-
712PhosphoserineIRKFSIVQK
HHHHEEECC
25.53PhosphoELM
Link-
712PhosphoserineIRKFSIVQK
HHHHEEECC
25.53Phosphositeplus
Link-
712Phosphoserine; by PKA.IRKFSIVQK
HHHHEEECC
25.53UniProtKB
Link-
717Phosphothreonine.IVQKTPLQM
EECCCCCCH
16.49UniProtKB
Link-
737PhosphoserineERRLSLVPD
CCEEEECCC
26.05Phosphositeplus
Link-
737Phosphoserine (PKA_group;PKG/cGK_group)ERRLSLVPD
CCEEEECCC
26.05PhosphoELM
Link-
737Phosphoserine (PRKACA)ERRLSLVPD
CCEEEECCC
26.05HPRD
Link-
737Phosphoserine (PRKG1)ERRLSLVPD
CCEEEECCC
26.05HPRD
Link-
737Phosphoserine; by PKA.ERRLSLVPD
CCEEEECCC
26.05UniProtKB
Link-
753PhosphoserineLPRISVIST
CCCCCCCCC
18.06Phosphositeplus
Link-
753Phosphoserine (PKA_group)LPRISVIST
CCCCCCCCC
18.06PhosphoELM
Link-
753Phosphoserine; by PKA.LPRISVIST
CCCCCCCCC
18.06UniProtKB
Link-
768PhosphoserineRRRQSVLNL
HHHHHHHHH
27.10Phosphositeplus
Link-
768Phosphoserine (PKA_group;PKG/cGK_group)RRRQSVLNL
HHHHHHHHH
27.10PhosphoELM
Link-
768Phosphoserine (PRKACA)RRRQSVLNL
HHHHHHHHH
27.10HPRD
Link-
768Phosphoserine (PRKG1)RRRQSVLNL
HHHHHHHHH
27.10HPRD
Link-
768Phosphoserine; by PKA.RRRQSVLNL
HHHHHHHHH
27.10UniProtKB
Link-
790PhosphoserineKTTASTRKV
CCCCCCCEE
27.01Phosphositeplus
Link-
790Phosphoserine (PKC_group)KTTASTRKV
CCCCCCCEE
27.01PhosphoELM
Link-
790Phosphoserine (PRKCA)KTTASTRKV
CCCCCCCEE
27.01HPRD
Link-
790Phosphoserine; by PKC.KTTASTRKV
CCCCCCCEE
27.01UniProtKB
Link-
795PhosphoserineTRKVSLAPQ
CCEEECCCC
23.11Phosphositeplus
Link-
795Phosphoserine (PKA_group;PKG/cGK_group)TRKVSLAPQ
CCEEECCCC
23.11PhosphoELM
Link-
795Phosphoserine (PRKACA)TRKVSLAPQ
CCEEECCCC
23.11HPRD
Link-
795Phosphoserine (PRKG1)TRKVSLAPQ
CCEEECCCC
23.11HPRD
Link-
795Phosphoserine; by PKA.TRKVSLAPQ
CCEEECCCC
23.11UniProtKB
Link-
809PhosphoserineLDIYSRRLS
CCCCCCCCC
15.97Phosphositeplus
Link-
813PhosphoserineSRRLSQETG
CCCCCCHHH
24.94Phosphositeplus
Link-
813Phosphoserine (PKA_group;PKG/cGK_group)SRRLSQETG
CCCCCCHHH
24.94PhosphoELM
Link-
813Phosphoserine (PRKACA)SRRLSQETG
CCCCCCHHH
24.94HPRD
Link-
813Phosphoserine (PRKG1)SRRLSQETG
CCCCCCHHH
24.94HPRD
Link-
813Phosphoserine; by PKA.SRRLSQETG
CCCCCCHHH
24.94UniProtKB
Link-
894N-linked (GlcNAc...).QDKGNSTHS
CCCCCCCCC
49.85UniProtKB
Link-
900N-linked (GlcNAc...).THSRNNSYA
CCCCCCCCC
44.83UniProtKB
Link-
1176PhosphothreonineEGKPTKSTK
CCCCCCCCC
40.90HPRD
Link-
1176Phosphothreonine.EGKPTKSTK
CCCCCCCCC
40.90UniProtKB
Link-
1362PhosphoserineRSVLSKAKI
HHHHHCCCE
28.54HPRD
Link-
1362PhosphoserineRSVLSKAKI
HHHHHCCCE
28.54Phosphositeplus
Link-
1395S-palmitoyl cysteine.AFADCTVIL
HHCCCEEEE
2.69UniProtKB
Link-
1444Phosphoserine.AISPSDRVK
HHHHHHHHH
31.12UniProtKB
Link-
1456Phosphoserine.HRNSSKCKS
HHHHCCCCC
45.69UniProtKB
Link-
1471PhosphothreonineLKEETEEEV
HHHHHHHHH
50.19Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NHERF_HUMANphysical interactionMINT-13968MINT11158634
NHERF_HUMANphysical interactionMINT-13969MINT11158634
NHERF_HUMANdirect interactionMINT-1796681MINT9671706
NHERF_HUMANdirect interactionMINT-1796707MINT9671706
NHERF_HUMANphysical interactionMINT-1783564MINT12471024
CFTR_HUMANphysical interactionMINT-73264MINT11051556
CALX_HUMANphysical interactionMINT-1794969MINT16546175
CALX_HUMANphysical interactionMINT-1794992MINT16546175
CALX_HUMANphysical interactionMINT-14845MINT12208510
2AAA_HUMANphysical interactionMINT-62221MINT15936019
2AAA_HUMANphysical interactionMINT-62222MINT15936019
2AAA_HUMANphysical interactionMINT-62219MINT15936019
2AAA_HUMANphysical interactionMINT-62218MINT15936019
PDZD1_HUMANphysical interactionMINT-73265MINT11051556
PDZD1_HUMANphysical interactionMINT-73266MINT11051556
PDZD1_HUMANphysical interactionMINT-1783789MINT12471024
PDZD1_HUMANphysical interactionMINT-1783586MINT12471024
PDZD1_HUMANphysical interactionMINT-1790139MINT12471024
GOPC_HUMANcolocalizationMINT-1783772MINT12471024
GOPC_HUMANphysical interactionMINT-1783657MINT12471024
SL9A2_HUMANphysical interaction
physical interaction
EBI-1108003
EBI-1107976
intact16203867
16203867
EDG4_HUMANphysical interaction
physical interaction
physical interaction
EBI-1108003
EBI-1149539
EBI-1
intact16203867
16203867
16203867
RNF5_HUMANcolocalization
physical interaction
physical interaction
EBI-988724
EBI-988819
EBI-988
intact16901789
16901789
16901789
XPO1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1170380
EBI-1
intact17110338
17110338
17110338
17110338
17110338
SNX4_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1170380
EBI-1
intact17110338
17110338
17110338
XPO2_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1170380
EBI-1
intact17110338
17110338
17110338
HSP77_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1170380
EBI-1
intact17110338
17110338
17110338
17110338
S10A7_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1170380
EBI-1
intact17110338
17110338
17110338
TFG_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1170380
intact17110338
17110338
2AAA_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1170380
intact17110338
17110338
SQRD_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1170380
EBI-1
intact17110338
17110338
17110338
17110338
TMM43_HUMANphysical interactionEBI-1171566
intact17110338
AIFM1_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1170380
intact17110338
17110338
DNJA1_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1171876
intact17110338
17110338
HS71L_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1170380
EBI-1
intact17110338
17110338
17110338
CH60_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1170380
intact17110338
17110338
UBE3A_HUMANphysical interactionEBI-1171566
intact17110338
PSMD2_HUMANphysical interactionEBI-1171566
intact17110338
SPTC1_HUMANphysical interactionEBI-1171566
intact17110338
LMNA_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1171876
EBI-1
intact17110338
17110338
17110338
CYTB_HUMANphysical interactionEBI-1171566
intact17110338
DNJB1_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1171876
intact17110338
17110338
RCN1_HUMANphysical interactionEBI-1171566
intact17110338
S10A9_HUMANphysical interactionEBI-1171566
intact17110338
GRP78_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1171716
intact17110338
17110338
IPO7_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1171876
intact17110338
17110338
RCN2_HUMANphysical interaction
physical interaction
EBI-1171566
EBI-1171716
intact17110338
17110338
IMB1_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171566
EBI-1171360
EBI-1
intact17110338
17110338
17110338
CALU_HUMANphysical interactionEBI-1171566
intact17110338
UBIQ_HUMANphysical interactionEBI-1170380
intact17110338
Q6UX72_HUMANphysical interactionEBI-1170380
intact17110338
AHSA1_HUMANphysical interactionEBI-1170380
intact17110338
G8_HUMANphysical interaction
physical interaction
physical interaction
EBI-1170380
EBI-1171360
EBI-1
intact17110338
17110338
17110338
LEG3_HUMANphysical interactionEBI-1170380
intact17110338
ELOB_HUMANphysical interaction
physical interaction
EBI-1170380
EBI-1171360
intact17110338
17110338
PSME2_HUMANphysical interactionEBI-1170380
intact17110338
GBLP_HUMANphysical interactionEBI-1170380
intact17110338
HS90B_HUMANphysical interaction
physical interaction
physical interaction
EBI-1170380
EBI-1171876
EBI-1
intact17110338
17110338
17110338
CH055_HUMANphysical interaction
physical interaction
EBI-1170380
EBI-1171716
intact17110338
17110338
BCR_HUMANphysical interactionEBI-1170380
intact17110338
RYR2_HUMANphysical interactionEBI-1170380
intact17110338
HSP72_HUMANphysical interaction
physical interaction
EBI-1170380
EBI-1171716
intact17110338
17110338
HCLS1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1171098
EBI-1171360
EBI-1
intact17110338
17110338
17110338
17110338
CD59_HUMANphysical interactionEBI-1171098
intact17110338
Q9UMI9_HUMANphysical interactionEBI-1171098
intact17110338
LEG4_HUMANphysical interaction
physical interaction
EBI-1171098
EBI-1171876
intact17110338
17110338
GRP75_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171098
EBI-1171360
EBI-1
intact17110338
17110338
17110338
SH3L2_HUMANphysical interactionEBI-1171098
intact17110338
EPN4_HUMANphysical interaction
physical interaction
EBI-1171098
EBI-1171360
intact17110338
17110338
TPM3_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171098
EBI-1171360
EBI-1
intact17110338
17110338
17110338
LRRF2_HUMANphysical interactionEBI-1171098
intact17110338
CLCA_HUMANphysical interactionEBI-1171098
intact17110338
EPS8_HUMANphysical interactionEBI-1171098
intact17110338
TMOD3_HUMANphysical interaction
physical interaction
EBI-1171098
EBI-1171360
intact17110338
17110338
MS4A5_HUMANphysical interactionEBI-1171098
intact17110338
REPS1_HUMANphysical interactionEBI-1171098
intact17110338
TACD1_HUMANphysical interactionEBI-1171098
intact17110338
ATD3A_HUMANphysical interactionEBI-1171098
intact17110338
GNAI2_HUMANphysical interactionEBI-1171098
intact17110338
GNA11_HUMANphysical interaction
physical interaction
EBI-1171098
EBI-1171360
intact17110338
17110338
CADH1_HUMANphysical interaction
physical interaction
EBI-1171098
EBI-1171360
intact17110338
17110338
PKHA6_HUMANphysical interactionEBI-1171098
intact17110338
DAB2_HUMANphysical interactionEBI-1171098
intact17110338
FLOT2_HUMANphysical interactionEBI-1171098
intact17110338
SNX9_HUMANphysical interactionEBI-1171098
intact17110338
CE170_HUMANphysical interactionEBI-1171098
intact17110338
PLD2_HUMANphysical interactionEBI-1171098
intact17110338
IRPL1_HUMANphysical interactionEBI-1171098
intact17110338
AT2A3_HUMANphysical interactionEBI-1171098
intact17110338
AP1B1_HUMANphysical interactionEBI-1171098
intact17110338
MUC13_HUMANphysical interactionEBI-1171098
intact17110338
SORL_HUMANphysical interactionEBI-1171098
intact17110338
SVIL_HUMANphysical interactionEBI-1171098
intact17110338
HSP71_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171360
EBI-1171876
EBI-1
intact17110338
17110338
17110338
TIAM1_HUMANphysical interactionEBI-1171360
intact17110338
EXO1_HUMANphysical interactionEBI-1171360
intact17110338
Q5TDF4_HUMANphysical interactionEBI-1171360
intact17110338
ZO3_HUMANphysical interactionEBI-1171360
intact17110338
LIMA1_HUMANphysical interactionEBI-1171360
intact17110338
ADCY8_HUMANphysical interactionEBI-1171360
intact17110338
WFS1_HUMANphysical interactionEBI-1171360
intact17110338
XPP3_HUMANphysical interactionEBI-1171360
intact17110338
RYK_HUMANphysical interactionEBI-1171360
intact17110338
SAP_HUMANphysical interactionEBI-1171360
intact17110338
ZO1_HUMANphysical interactionEBI-1171360
intact17110338
CLH2_HUMANphysical interactionEBI-1171360
intact17110338
GRN_HUMANphysical interactionEBI-1171360
intact17110338
WSB1_HUMANphysical interactionEBI-1171360
intact17110338
PRKDC_HUMANphysical interaction
physical interaction
EBI-1171360
EBI-1171716
intact17110338
17110338
APOA2_HUMANphysical interactionEBI-1171360
intact17110338
HAX1_HUMANphysical interactionEBI-1171360
intact17110338
LIN7C_HUMANphysical interactionEBI-1171360
intact17110338
HSPB1_HUMANphysical interactionEBI-1171360
intact17110338
PIMT_HUMANphysical interaction
physical interaction
physical interaction
EBI-1171360
EBI-1171876
EBI-1
intact17110338
17110338
17110338
CPNS1_HUMANphysical interaction
physical interaction
EBI-1171360
EBI-1171876
intact17110338
17110338
AT2A2_HUMANphysical interactionEBI-1171360
intact17110338
S61A1_HUMANphysical interaction
physical interaction
EBI-1171360
EBI-1171876
intact17110338
17110338
CALX_HUMANphysical interactionEBI-1171360
intact17110338
TERA_HUMANphysical interactionEBI-1171876
intact17110338
S61A2_HUMANphysical interactionEBI-1171876
intact17110338
FATH_HUMANphysical interactionEBI-1171876
intact17110338
VPS4A_HUMANphysical interactionEBI-1171876
intact17110338
SFXN3_HUMANphysical interactionEBI-1171876
intact17110338
TRIPC_HUMANphysical interactionEBI-1171876
intact17110338
F120A_HUMANphysical interactionEBI-1171876
intact17110338
COPB_HUMANphysical interaction
physical interaction
EBI-1171876
EBI-1171716
intact17110338
17110338
CAPR1_HUMANphysical interactionEBI-1171716
intact17110338
ATX2L_HUMANphysical interactionEBI-1171716
intact17110338
PDCD6_HUMANphysical interactionEBI-1171716
intact17110338
EMD_HUMANphysical interactionEBI-1171716
intact17110338
LMO7_HUMANphysical interactionEBI-1171716
intact17110338
NHERF_HUMANphysical interaction
physical interaction
EBI-1171716
EBI-349895
intact17110338
12471024
DNJA2_HUMANphysical interactionEBI-1171716
intact17110338
ELOC_HUMANphysical interactionEBI-1171716
intact17110338
CALX_HUMANin vitroHPRD:03883HPRD12208510
EZRI_HUMANin vivoHPRD:03883HPRD10893422
KPCE_HUMANin vivoHPRD:03883HPRD11956211
STX1A_HUMANin vitro
in vivo
HPRD:03883HPRD9384384
SL9A6_HUMANin vivoHPRD:03883HPRD11707463
CFTR_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03883HPRD11707463
11051556
10893422
12471024
KAP2_HUMANin vivoHPRD:03883HPRD10799517
NHRF2_HUMANENSP00000003084STRING
STX1A_HUMANENSP00000003084STRING
CALX_HUMANENSP00000003084STRING
DERL1_HUMANENSP00000003084STRING
S12A2_HUMANENSP00000003084STRING
NHERF_HUMANENSP00000003084STRING
KGP2_HUMANENSP00000003084STRING
SL9A3_HUMANENSP00000003084STRING
CCL5_HUMANENSP00000003084STRING
PDZD1_HUMANENSP00000003084STRING
S26A3_HUMANENSP00000003084STRING
CLCN3_HUMANENSP00000003084STRING
DNJC5_HUMANENSP00000003084STRING
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Disease Reference
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)
Drug Reference
Kegg drug
D00808 Suramin hexasodium (USAN); Bayer 205 (TN)
D09916 Ivacaftor (USAN/INN); Kalydeco (TN)
D10134 Lumacaftor (USAN)
There are no disease associations of PTM sites.
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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
"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.
"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.
"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 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.
"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.
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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures