ATP7B_HUMAN - dbPTM
ATP7B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATP7B_HUMAN
UniProt AC P35670
Protein Name Copper-transporting ATPase 2
Gene Name ATP7B
Organism Homo sapiens (Human).
Sequence Length 1465
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Multi-pass membrane protein . Late endosome . Predominantly found in the trans-Golgi network (TGN). Localized in the trans-Golgi network under low copper conditions, redistributes to cytoplasmic vesicle
Protein Description Copper ion transmembrane transporter involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile..
Protein Sequence MPEQERQITAREGASRKILSKLSLPTRAWEPAMKKSFAFDNVGYEGGLDGLGPSSQVATSTVRILGMTCQSCVKSIEDRISNLKGIISMKVSLEQGSATVKYVPSVVCLQQVCHQIGDMGFEASIAEGKAASWPSRSLPAQEAVVKLRVEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAAIKSKVAPLSLGPIDIERLQSTNPKRPLSSANQNFNNSETLGHQGSHVVTLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEALPPGNFKVSLPDGAEGSGTDHRSSSSHSPGSPPRNQVQGTCSTTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSESCSTNPLGNHSAGNSMVQTTDGTPTSVQEVAPHTGRLPANHAPDILAKSPQSTRAVAPQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVMEDYAGSDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIEEIGFHASLAQRNPNAHHLDHKMEIKQWKKSFLCSLVFGIPVMALMIYMLIPSNEPHQSMVLDHNIIPGLSILNLIFFILCTFVQLLGGWYFYVQAYKSLRHRSANMDVLIVLATSIAYVYSLVILVVAVAEKAERSPVTFFDTPPMLFVFIALGRWLEHLAKSKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKAPIQQLADRFSGYFVPFIIIMSTLTLVVWIVIGFIDFGVVQRYFPNPNKHISQTEVIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCTDFQAVPGCGIGCKVSNVEGILAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIVLQPWMGSAAMAASSVSVVLSSLQLKCYKKPDLERYEAQAHGHMKPLTASQVSVHIGMDDRWRDSPRATPWDQVSYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQYI
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
9PhosphorylationPEQERQITAREGASR
CHHHHHHHHHCCHHH
16.01-
20PhosphorylationGASRKILSKLSLPTR
CHHHHHHHHCCCCCC
34.7223186163
23PhosphorylationRKILSKLSLPTRAWE
HHHHHHCCCCCCCCC
35.7229978859
26PhosphorylationLSKLSLPTRAWEPAM
HHHCCCCCCCCCCHH
38.0123186163
44PhosphorylationFAFDNVGYEGGLDGL
CCCCCCCCCCCCCCC
13.7127642862
132PhosphorylationIAEGKAASWPSRSLP
HHCCCCCCCCCCCCC
44.3623403867
135PhosphorylationGKAASWPSRSLPAQE
CCCCCCCCCCCCHHH
28.3923403867
137PhosphorylationAASWPSRSLPAQEAV
CCCCCCCCCCHHHHE
42.9423403867
177PhosphorylationGVVRVKVSLSNQEAV
CEEEEEEEECCCEEE
21.9924043423
179PhosphorylationVRVKVSLSNQEAVIT
EEEEEEECCCEEEEE
29.0324043423
186PhosphorylationSNQEAVITYQPYLIQ
CCCEEEEEEECEECC
14.9824043423
187PhosphorylationNQEAVITYQPYLIQP
CCEEEEEEECEECCH
9.0724043423
190PhosphorylationAVITYQPYLIQPEDL
EEEEEECEECCHHHH
10.8324043423
218PhosphorylationKSKVAPLSLGPIDIE
HCCCCCCCCCCCCHH
30.1630266825
229PhosphorylationIDIERLQSTNPKRPL
CCHHHHHCCCCCCCC
34.44-
301PhosphorylationNKTAQVKYDPSCTSP
CCCCEEECCCCCCCH
33.9429209046
304PhosphorylationAQVKYDPSCTSPVAL
CEEECCCCCCCHHHH
27.4229209046
306PhosphorylationVKYDPSCTSPVALQR
EECCCCCCCHHHHHH
40.1629209046
307PhosphorylationKYDPSCTSPVALQRA
ECCCCCCCHHHHHHH
23.0029209046
340PhosphorylationGSGTDHRSSSSHSPG
CCCCCCCCCCCCCCC
31.0223312004
341PhosphorylationSGTDHRSSSSHSPGS
CCCCCCCCCCCCCCC
35.5023312004
342PhosphorylationGTDHRSSSSHSPGSP
CCCCCCCCCCCCCCC
33.0625002506
343PhosphorylationTDHRSSSSHSPGSPP
CCCCCCCCCCCCCCC
29.9025002506
345PhosphorylationHRSSSSHSPGSPPRN
CCCCCCCCCCCCCCH
32.6723312004
348PhosphorylationSSSHSPGSPPRNQVQ
CCCCCCCCCCCHHCC
34.8128857561
378 (in isoform 3)Ubiquitination-45.8021890473
477UbiquitinationHAPDILAKSPQSTRA
CCCHHHHCCCCCCCC
60.26-
478PhosphorylationAPDILAKSPQSTRAV
CCHHHHCCCCCCCCC
23.6729978859
481PhosphorylationILAKSPQSTRAVAPQ
HHHCCCCCCCCCCCC
24.2029978859
482PhosphorylationLAKSPQSTRAVAPQK
HHCCCCCCCCCCCCC
19.8723186163
489 (in isoform 1)Ubiquitination-26.3721890473
489UbiquitinationTRAVAPQKCFLQIKG
CCCCCCCCEEEEECC
26.3721890473
489 (in isoform 2)Ubiquitination-26.3721890473
489 (in isoform 4)Ubiquitination-26.3721890473
496 (in isoform 3)Ubiquitination-20.4721890473
518PhosphorylationQKEAGVLSVLVALMA
HHHHHHHHHHHHHHH
15.82-
587PhosphorylationHNIESKLTRTNGITY
HHHHCHHHCCCCCCH
38.9028842319
589PhosphorylationIESKLTRTNGITYAS
HHCHHHCCCCCCHHH
32.3423312004
593PhosphorylationLTRTNGITYASVALA
HHCCCCCCHHHHHHH
17.9023312004
594PhosphorylationTRTNGITYASVALAT
HCCCCCCHHHHHHHH
8.5823312004
596PhosphorylationTNGITYASVALATSK
CCCCCHHHHHHHHCC
9.4823312004
607 (in isoform 2)Ubiquitination-44.9221890473
607 (in isoform 1)Ubiquitination-44.9221890473
607UbiquitinationATSKALVKFDPEIIG
HHCCHHHCCCHHHHC
44.9221890473
607 (in isoform 4)Ubiquitination-44.9221890473
787UbiquitinationLEHLAKSKTSEALAK
HHHHHCCCCHHHHHH
56.20-
788O-linked_GlycosylationEHLAKSKTSEALAKL
HHHHCCCCHHHHHHH
38.6030379171
821 (in isoform 2)Ubiquitination-15.3821890473
876PhosphorylationGSTVIAGSINAHGSV
CCEEEEEEECCCCCE
12.0323879269
882PhosphorylationGSINAHGSVLIKATH
EEECCCCCEEEEEEE
12.1323879269
910UbiquitinationVEEAQMSKAPIQQLA
HHHHHHCCCCHHHHH
53.49-
917 (in isoform 3)Ubiquitination-11.1221890473
1010 (in isoform 4)Ubiquitination-59.1621890473
1028 (in isoform 1)Ubiquitination-37.2721890473
1028UbiquitinationIKTVMFDKTGTITHG
CCEEEECCCCCCCCC
37.2721890473
1028AcetylationIKTVMFDKTGTITHG
CCEEEECCCCCCCCC
37.277307309
1050PhosphorylationLLLGDVATLPLRKVL
HHHCCCCCCCHHHHH
28.85-
1066PhosphorylationVVGTAEASSEHPLGV
HHCCCCCCCCCCCHH
27.9723532336
1076PhosphorylationHPLGVAVTKYCKEEL
CCCHHHHHHHHHHHH
13.42-
1078PhosphorylationLGVAVTKYCKEELGT
CHHHHHHHHHHHHCC
10.2123532336
1121PhosphorylationAHSERPLSAPASHLN
CCCCCCCCCCHHHCC
34.5822817900
1208PhosphorylationEAALAVHTLQSMGVD
HHHHHHHHHHHCCCC
21.64-
1211PhosphorylationLAVHTLQSMGVDVVL
HHHHHHHHCCCCEEE
22.18-
1220PhosphorylationGVDVVLITGDNRKTA
CCCEEEEECCCHHHH
34.03-
1258AcetylationKVQELQNKGKKVAMV
HHHHHHHCCCCEEEE
60.187668361
1260AcetylationQELQNKGKKVAMVGD
HHHHHCCCCEEEECC
45.767668371
1310PhosphorylationDLLDVVASIHLSKRT
CHHHHHHHHHCCHHH
10.0326270265
1314PhosphorylationVVASIHLSKRTVRRI
HHHHHHCCHHHHHHH
13.1126270265
1398PhosphorylationHMKPLTASQVSVHIG
CCCCCCHHHEEEEEC
26.3620363803
1401PhosphorylationPLTASQVSVHIGMDD
CCCHHHEEEEECCCC
10.5920363803
1413PhosphorylationMDDRWRDSPRATPWD
CCCCCCCCCCCCCHH
14.01-
1423PhosphorylationATPWDQVSYVSQVSL
CCCHHHHHEEEEEEH
17.74-
1424PhosphorylationTPWDQVSYVSQVSLS
CCHHHHHEEEEEEHH
12.7927642862
1426PhosphorylationWDQVSYVSQVSLSSL
HHHHHEEEEEEHHHC
19.3427251275
1429PhosphorylationVSYVSQVSLSSLTSD
HHEEEEEEHHHCCCC
18.2024719451
1442PhosphorylationSDKPSRHSAAADDDG
CCCCCCCCCCCCCCC
20.6326471730
1453PhosphorylationDDDGDKWSLLLNGRD
CCCCCCEEEEECCCC
18.1922817900

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
478SPhosphorylationKinasePRKD1Q15139
PSP
481SPhosphorylationKinasePRKD1Q15139
PSP
1121SPhosphorylationKinasePRKD1Q15139
PSP
1453SPhosphorylationKinasePRKD1Q15139
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATP7B_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 ATP7B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLRX1_HUMANGLRXphysical
16884690
ATOX1_HUMANATOX1physical
10497213
ATOX1_HUMANATOX1physical
10557326
DCTN4_HUMANDCTN4physical
16554302
COMD1_HUMANCOMMD1physical
12968035
ATOX1_HUMANATOX1physical
16573520
ZBT16_HUMANZBTB16physical
16676348
HPT_HUMANHPphysical
16676348
CLUS_HUMANCLUphysical
21242307
CLUS_HUMANCLUphysical
22130675
COMD1_HUMANCOMMD1physical
22130675

Drug and Disease Associations
Kegg Disease
H00210 Wilson disease; Hepatolenticular degeneration
OMIM Disease
277900Wilson disease (WD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00958Carboplatin
DB00515Cisplatin
DB00526Oxaliplatin
Regulatory Network of ATP7B_HUMAN

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Related Literatures of Post-Translational Modification

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