ADCY7_HUMAN - dbPTM
ADCY7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADCY7_HUMAN
UniProt AC P51828
Protein Name Adenylate cyclase type 7
Gene Name ADCY7
Organism Homo sapiens (Human).
Sequence Length 1080
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description This is a membrane-bound, calcium-inhibitable adenylyl cyclase..
Protein Sequence MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRASVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRSEDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACASLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISERVETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLPYYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKPNGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFETMENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
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
154PhosphorylationAVAVGAVSTASHLLV
CHHHHCCHHHHHHHH
20.0946159659
155PhosphorylationVAVGAVSTASHLLVL
HHHHCCHHHHHHHHH
26.1146159677
157PhosphorylationVGAVSTASHLLVLGS
HHCCHHHHHHHHHHH
18.1146159665
214UbiquitinationDLFTYTVKCIQIRRK
HHHHHHHHHHHHHHH
20.16-
273UbiquitinationNFHSLYVKRHQNVSI
CCCHHHHCCCCCCEE
30.52-
316UbiquitinationGKFDQIAKANECMRI
CCHHHHHHHHCCEEE
54.06-
324UbiquitinationANECMRIKILGDCYY
HHCCEEEEEECCCEE
22.86-
349UbiquitinationTHARNCVKMGLDMCQ
HHHHHHHHHCHHHHH
29.47-
359UbiquitinationLDMCQAIKQVREATG
HHHHHHHHHHHHHHC
45.84-
365PhosphorylationIKQVREATGVDINMR
HHHHHHHHCCCCEEE
32.7410486863
389UbiquitinationCGVIGLRKWQYDVWS
EEEEEEEECEEEECC
43.63-
422UbiquitinationHITEATLKHLDKAYE
EEEHHHHHHHHHHEE
37.4521890473
422AcetylationHITEATLKHLDKAYE
EEEHHHHHHHHHHEE
37.4520167786
426AcetylationATLKHLDKAYEVEDG
HHHHHHHHHEECCCC
60.2620167786
426UbiquitinationATLKHLDKAYEVEDG
HHHHHHHHHEECCCC
60.26-
443UbiquitinationQQRDPYLKEMNIRTY
CCCCHHHHHCCCCEE
49.4221890473
477UbiquitinationPKGDAALKMRASVRM
CCCCHHHHHHHHHHH
22.93-
490PhosphorylationRMTRYLESWGAARPF
HHHHHHHHCCCCCCC
28.37101661943
505PhosphorylationAHLNHRESVSSGETH
CCCCCCCCCCCCCCC
27.5382900321
507PhosphorylationLNHRESVSSGETHVP
CCCCCCCCCCCCCCC
41.7428450419
508PhosphorylationNHRESVSSGETHVPN
CCCCCCCCCCCCCCC
38.1928450419
511PhosphorylationESVSSGETHVPNGRR
CCCCCCCCCCCCCCC
31.5328450419
535PhosphorylationRTPDRSMSPKGRSED
CCCCCCCCCCCCCCC
25.38113310213
570PhosphorylationCSKSDDFYTFGSIFL
CCCCCCCEEECHHHH
14.2527642862
579UbiquitinationFGSIFLEKGFEREYR
ECHHHHHCCCCCEEE
71.67-
701N-linked_GlycosylationVPELPVGNETGLLAA
CCCCCCCCCCCCCCC
43.84UniProtKB CARBOHYD
776N-linked_GlycosylationCCGQGLGNLTKPNGT
CCCCCCCCCCCCCCC
49.97UniProtKB CARBOHYD
781N-linked_GlycosylationLGNLTKPNGTTSGTP
CCCCCCCCCCCCCCC
63.10UniProtKB CARBOHYD
783PhosphorylationNLTKPNGTTSGTPSC
CCCCCCCCCCCCCCC
25.1624043423
784PhosphorylationLTKPNGTTSGTPSCS
CCCCCCCCCCCCCCC
26.9324043423
785PhosphorylationTKPNGTTSGTPSCSW
CCCCCCCCCCCCCCH
40.2724043423
787PhosphorylationPNGTTSGTPSCSWKD
CCCCCCCCCCCCHHH
16.2824043423
789PhosphorylationGTTSGTPSCSWKDLK
CCCCCCCCCCHHHHH
22.1824043423
791PhosphorylationTSGTPSCSWKDLKTM
CCCCCCCCHHHHHHH
41.3124043423
797PhosphorylationCSWKDLKTMTNFYLV
CCHHHHHHHHHHHHH
36.2024043423
799PhosphorylationWKDLKTMTNFYLVLF
HHHHHHHHHHHHHHH
27.6624043423
802PhosphorylationLKTMTNFYLVLFYIT
HHHHHHHHHHHHHHH
9.6624043423
807PhosphorylationNFYLVLFYITLLTLS
HHHHHHHHHHHHHHH
6.7124043423
809PhosphorylationYLVLFYITLLTLSRQ
HHHHHHHHHHHHHHH
12.3424043423
812PhosphorylationLFYITLLTLSRQIDY
HHHHHHHHHHHHHHH
26.2924043423
814PhosphorylationYITLLTLSRQIDYYC
HHHHHHHHHHHHHHH
19.5346159671
832UbiquitinationCLWKKKFKKEHEEFE
HHHHHHHHHHHHHHH
67.16-
833UbiquitinationLWKKKFKKEHEEFET
HHHHHHHHHHHHHHH
68.39-
892PhosphorylationVPDFKVFYTECDVNK
CCCEEEEEEECCCCH
12.4825884760
899UbiquitinationYTECDVNKEGLECLR
EEECCCCHHHHHHHH
53.67-
925PhosphorylationLLLKPKFSGVEKIKT
HHHCCCCCCCCCCEE
48.3224719451
929UbiquitinationPKFSGVEKIKTIGST
CCCCCCCCCEECCHH
47.28-
982PhosphorylationLDGINRHSFNSFRLR
CCCCCCCCCCEEEEE
23.9230266825
985PhosphorylationINRHSFNSFRLRVGI
CCCCCCCEEEEEEEC
15.1030266825
1006UbiquitinationAGVIGARKPQYDIWG
EEEECCCCCCCCCCC
35.6221890473
1057UbiquitinationCRGLINVKGKGELRT
EECEEEECCCCEEEE
50.87-
1073UbiquitinationFVCTDTAKFQGLGLN
EEECCCHHHCCCCCC
40.07-

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

Oops, there are no upstream regulatory protein records of ADCY7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADCY7_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
443Ubiquitination439 (4)DErs78534766
  • Ulcerative colitis
28067908

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
21988832
PLS1_HUMANPLSCR1physical
21988832
BUD31_HUMANBUD31physical
21988832

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D01697 Colforsin daropate hydrochloride (JAN); Nkh 477; Adehl (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADCY7_HUMAN

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Related Literatures of Post-Translational Modification

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