CAN7_HUMAN - dbPTM
CAN7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAN7_HUMAN
UniProt AC Q9Y6W3
Protein Name Calpain-7
Gene Name CAPN7
Organism Homo sapiens (Human).
Sequence Length 813
Subcellular Localization Nucleus.
Protein Description Calcium-regulated non-lysosomal thiol-protease..
Protein Sequence MDATALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQSKSADPLKSKHQLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLTKPVGKISSTSVKPKPPPVRAHFPLGANPFLERPQSFISPQSCDAQGQRYTAEEIEVLRTTSKINGIEYVPFMNVDLRERFAYPMPFCDRWGKLPLSPKQKTTFSKWVRPEDLTNNPTMIYTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKKLITGIIYPQNKDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHKGELLCSYSNNKSELWVSLIEKAYMKVMGGYDFPGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYQRFHKGDVLITASTGMMTEAEGEKWGLVPTHAYAVLDIREFKGLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQKYLNFDPRTAQKIDNGIFWISWDDLCQYYDVIYLSWNPGLFKESTCIHSTWDAKQGPVKDAYSLANNPQYKLEVQCPQGGAAVWVLLSRHITDKDDFANNREFITMVVYKTDGKKVYYPADPPPYIDGIRINSPHYLTKIKLTTPGTHTFTLVVSQYEKQNTIHYTVRVYSACSFTFSKIPSPYTLSKRINGKWSGQSAGGCGNFQETHKNNPIYQFHIEKTGPLLIELRGPRQYSVGFEVVTVSTLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQLQ
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
1Acetylation-------MDATALER
-------CCCHHHHH
7.7422814378
33PhosphorylationYSEAVFYYKEAAQAL
CEEEEEEHHHHHHHH
7.2924719451
42PhosphorylationEAAQALIYAEMAGSS
HHHHHHHHHHHCCCC
9.43-
74UbiquitinationLHSAVQSKSADPLKS
HHHHHHCCCCCCCCC
32.3521890473
75PhosphorylationHSAVQSKSADPLKSK
HHHHHCCCCCCCCCH
43.0524719451
80UbiquitinationSKSADPLKSKHQLDL
CCCCCCCCCHHHHHH
63.95-
82UbiquitinationSADPLKSKHQLDLER
CCCCCCCHHHHHHHH
33.51-
95PhosphorylationERAHFLVTQAFDEDE
HHHHHHHEECCCHHH
19.1422817900
124PhosphorylationVDLCLKTSYETADKV
HHHHHHCCHHHHHHH
21.2728796482
125PhosphorylationDLCLKTSYETADKVL
HHHHHCCHHHHHHHH
23.6428796482
127PhosphorylationCLKTSYETADKVLQN
HHHCCHHHHHHHHHH
31.7428796482
130UbiquitinationTSYETADKVLQNKLK
CCHHHHHHHHHHHHH
42.2421890473
135UbiquitinationADKVLQNKLKQLARQ
HHHHHHHHHHHHHHH
44.06-
137UbiquitinationKVLQNKLKQLARQAL
HHHHHHHHHHHHHHH
44.89-
156AcetylationALSEPLTKPVGKISS
HHCCCCCCCCCCCCC
45.4423236377
156UbiquitinationALSEPLTKPVGKISS
HHCCCCCCCCCCCCC
45.4421890473
162O-linked_GlycosylationTKPVGKISSTSVKPK
CCCCCCCCCCCCCCC
30.9229351928
162PhosphorylationTKPVGKISSTSVKPK
CCCCCCCCCCCCCCC
30.9223312004
163PhosphorylationKPVGKISSTSVKPKP
CCCCCCCCCCCCCCC
28.3326270265
164PhosphorylationPVGKISSTSVKPKPP
CCCCCCCCCCCCCCC
30.6528857561
165PhosphorylationVGKISSTSVKPKPPP
CCCCCCCCCCCCCCC
30.0528857561
167UbiquitinationKISSTSVKPKPPPVR
CCCCCCCCCCCCCCC
47.28-
190PhosphorylationPFLERPQSFISPQSC
CCCCCCCHHCCCCCC
27.5120873877
193PhosphorylationERPQSFISPQSCDAQ
CCCCHHCCCCCCCCC
18.1820873877
214PhosphorylationEEIEVLRTTSKINGI
HHHHHHEECCCCCCE
31.1224719451
216PhosphorylationIEVLRTTSKINGIEY
HHHHEECCCCCCEEE
30.8124719451
217UbiquitinationEVLRTTSKINGIEYV
HHHEECCCCCCEEEE
37.79-
247UbiquitinationPFCDRWGKLPLSPKQ
CCCCCCCCCCCCCCC
39.7221890473
251PhosphorylationRWGKLPLSPKQKTTF
CCCCCCCCCCCCCCC
28.2823312004
253UbiquitinationGKLPLSPKQKTTFSK
CCCCCCCCCCCCCCC
62.14-
279PhosphorylationTMIYTVSSFSIKQTI
EEEEEEEECCCCEEE
20.7624719451
281PhosphorylationIYTVSSFSIKQTIVS
EEEEEECCCCEEECC
30.7224719451
309UbiquitinationYERRFNKKLITGIIY
HHHHHCCCEEEEEEC
46.34-
320UbiquitinationGIIYPQNKDGEPEYN
EEECCCCCCCCCCCC
62.96-
331UbiquitinationPEYNPCGKYMVKLHL
CCCCCCCCEEEEEEC
36.57-
335UbiquitinationPCGKYMVKLHLNGVP
CCCCEEEEEECCCCC
17.41-
344UbiquitinationHLNGVPRKVIIDDQL
ECCCCCCEEEECCCC
31.54-
356UbiquitinationDQLPVDHKGELLCSY
CCCCCCCCCCEEEEE
50.01-
362PhosphorylationHKGELLCSYSNNKSE
CCCCEEEEECCCCCH
31.4023401153
363PhosphorylationKGELLCSYSNNKSEL
CCCEEEEECCCCCHH
17.8920873877
364PhosphorylationGELLCSYSNNKSELW
CCEEEEECCCCCHHH
20.0320873877
373PhosphorylationNKSELWVSLIEKAYM
CCCHHHHHHHHHHHH
16.4324719451
412PhosphorylationPERIAMHSDSQTFSK
CHHEECCCCCCCCCC
26.35-
414PhosphorylationRIAMHSDSQTFSKDN
HEECCCCCCCCCCCC
33.85-
416PhosphorylationAMHSDSQTFSKDNSF
ECCCCCCCCCCCCHH
33.55-
419UbiquitinationSDSQTFSKDNSFRML
CCCCCCCCCCHHHHH
57.6521890473
477UbiquitinationGLRFIQLKNPWSHLR
CCEEEEECCCCHHHC
44.59-
489PhosphorylationHLRWKGRYSENDVKN
HHCCCCCCCCCHHHH
29.07-
490PhosphorylationLRWKGRYSENDVKNW
HCCCCCCCCCHHHHC
28.67-
495UbiquitinationRYSENDVKNWTPELQ
CCCCCHHHHCCHHHH
50.0221890473
498PhosphorylationENDVKNWTPELQKYL
CCHHHHCCHHHHHHH
19.1129396449
503UbiquitinationNWTPELQKYLNFDPR
HCCHHHHHHHCCCHH
65.4121890473
556UbiquitinationIHSTWDAKQGPVKDA
EEEECCCCCCCCCCH
54.00-
561UbiquitinationDAKQGPVKDAYSLAN
CCCCCCCCCHHHHHC
39.51-
596UbiquitinationLSRHITDKDDFANNR
EECCCCCHHHCCCCC
51.0121890473
617UbiquitinationVYKTDGKKVYYPADP
EEEECCCEEEECCCC
40.78-
619PhosphorylationKTDGKKVYYPADPPP
EECCCEEEECCCCCC
16.7722817900
620PhosphorylationTDGKKVYYPADPPPY
ECCCEEEECCCCCCC
8.5722817900
627PhosphorylationYPADPPPYIDGIRIN
ECCCCCCCCCCEEEC
19.8822817900
635PhosphorylationIDGIRINSPHYLTKI
CCCEEECCCCEEEEE
15.64-
641UbiquitinationNSPHYLTKIKLTTPG
CCCCEEEEEEEECCC
34.94-
659PhosphorylationFTLVVSQYEKQNTIH
EEEEEEEECCCCCEE
20.00-
667PhosphorylationEKQNTIHYTVRVYSA
CCCCCEEEEEEEEEE
11.77-
695UbiquitinationLSKRINGKWSGQSAG
ECCCCCCEECCCCCC
33.43-
697PhosphorylationKRINGKWSGQSAGGC
CCCCCEECCCCCCCC
30.36-
700PhosphorylationNGKWSGQSAGGCGNF
CCEECCCCCCCCCCC
32.19-
712UbiquitinationGNFQETHKNNPIYQF
CCCHHHHCCCCEEEE
66.88-
723UbiquitinationIYQFHIEKTGPLLIE
EEEEEEEECCCEEEE
59.17-

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 CAN7_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAN7_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 CAN7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANCHR_HUMANZFYVE19physical
25416956
UBL7_HUMANUBL7physical
25416956
ZBTB9_HUMANZBTB9physical
25416956

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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAN7_HUMAN

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Related Literatures of Post-Translational Modification

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