ZN587_HUMAN - dbPTM
ZN587_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN587_HUMAN
UniProt AC Q96SQ5
Protein Name Zinc finger protein 587
Gene Name ZNF587
Organism Homo sapiens (Human).
Sequence Length 575
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MAAAVPRRPTQQGTVTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLGCWCGSKDEEAPCKQRISVQRESQSRTPRAGVSPKKAHPCEMCGLILEDVFHFADHQETHHKQKLNRSGACGKNLDDTAYLHQHQKQHIGEKFYRKSVREASFVKKRKLRVSQEPFVFREFGKDVLPSSGLCQEEAAVEKTDSETMHGPPFQEGKTNYSCGKRTKAFSTKHSVIPHQKLFTRDGCYVCSDCGKSFSRYVSFSNHQRDHTAKGPYDCGECGKSYSRKSSLIQHQRVHTGQTAYPCEECGKSFSQKGSLISHQLVHTGEGPYECRECGKSFGQKGNLIQHQQGHTGERAYHCGECGKSFRQKFCFINHQRVHTGERPYKCGECGKSFGQKGNLVHHQRGHTGERPYECKECGKSFRYRSHLTEHQRLHTGERPYNCRECGKLFNRKYHLLVHERVHTGERPYACEVCGKLFGNKHSVTIHQRIHTGERPYECSECGKSFLSSSALHVHKRVHSGQKPYKCSECGKSFSECSSLIKHRRIHTGERPYECTKCGKTFQRSSTLLHHQSSHRRKAL
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
77PhosphorylationRISVQRESQSRTPRA
CEEEHHHHHCCCCCC
35.3328555341
81PhosphorylationQRESQSRTPRAGVSP
HHHHHCCCCCCCCCC
23.5228555341
126UbiquitinationLNRSGACGKNLDDTA
CCCCCCCCCCCCCHH
22.7329967540
127UbiquitinationNRSGACGKNLDDTAY
CCCCCCCCCCCCHHH
54.9729967540
132PhosphorylationCGKNLDDTAYLHQHQ
CCCCCCCHHHHHHHH
19.5028555341
139UbiquitinationTAYLHQHQKQHIGEK
HHHHHHHHHHHHHHH
40.3029967540
140UbiquitinationAYLHQHQKQHIGEKF
HHHHHHHHHHHHHHH
41.5429967540
159AcetylationVREASFVKKRKLRVS
HHHHHHEECCCCCCC
44.8730593819
160AcetylationREASFVKKRKLRVSQ
HHHHHEECCCCCCCC
49.847366075
166PhosphorylationKKRKLRVSQEPFVFR
ECCCCCCCCCCCHHH
23.5328555341
176UbiquitinationPFVFREFGKDVLPSS
CCHHHHCCCCCCCCC
22.0929967540
177UbiquitinationFVFREFGKDVLPSSG
CHHHHCCCCCCCCCC
50.4029967540
209AcetylationGPPFQEGKTNYSCGK
CCCCCCCCCCCCCCC
32.617406617
216AcetylationKTNYSCGKRTKAFST
CCCCCCCCCCCCCCC
62.317406625
223UbiquitinationKRTKAFSTKHSVIPH
CCCCCCCCCCCCCCC
26.7329967540
224UbiquitinationRTKAFSTKHSVIPHQ
CCCCCCCCCCCCCCC
32.4629967540
231UbiquitinationKHSVIPHQKLFTRDG
CCCCCCCCCCCCCCC
38.5029967540
232UbiquitinationHSVIPHQKLFTRDGC
CCCCCCCCCCCCCCE
42.4029967540
232SumoylationHSVIPHQKLFTRDGC
CCCCCCCCCCCCCCE
42.40-
232SumoylationHSVIPHQKLFTRDGC
CCCCCCCCCCCCCCE
42.40-
250PhosphorylationSDCGKSFSRYVSFSN
CCCCCCHHHEEECCC
29.7717081983
254PhosphorylationKSFSRYVSFSNHQRD
CCHHHEEECCCCCCC
17.6427251275
280SumoylationCGKSYSRKSSLIQHQ
CCCCCCCCCCCCCCC
38.16-
280UbiquitinationCGKSYSRKSSLIQHQ
CCCCCCCCCCCCCCC
38.16-
280SumoylationCGKSYSRKSSLIQHQ
CCCCCCCCCCCCCCC
38.16-
281PhosphorylationGKSYSRKSSLIQHQR
CCCCCCCCCCCCCCC
29.3028555341
291PhosphorylationIQHQRVHTGQTAYPC
CCCCCCCCCCCCEEC
28.2928555341
319PhosphorylationISHQLVHTGEGPYEC
EEEEEEECCCCCCCH
29.4625159151
336SumoylationCGKSFGQKGNLIQHQ
CHHHHCCCCCCCCCC
50.58-
336SumoylationCGKSFGQKGNLIQHQ
CHHHHCCCCCCCCCC
50.58-
336UbiquitinationCGKSFGQKGNLIQHQ
CHHHHCCCCCCCCCC
50.58-
347PhosphorylationIQHQQGHTGERAYHC
CCCCCCCCCCCCEEC
47.7825159151
364SumoylationCGKSFRQKFCFINHQ
CCHHHHHEEEEEECC
39.58-
364SumoylationCGKSFRQKFCFINHQ
CCHHHHHEEEEEECC
39.58-
375PhosphorylationINHQRVHTGERPYKC
EECCCCCCCCCCEEC
37.5727251275
381SumoylationHTGERPYKCGECGKS
CCCCCCEECCCCCCC
38.15-
381SumoylationHTGERPYKCGECGKS
CCCCCCEECCCCCCC
38.15-
392SumoylationCGKSFGQKGNLVHHQ
CCCCCCCCCCCCCCC
50.58-
392SumoylationCGKSFGQKGNLVHHQ
CCCCCCCCCCCCCCC
50.58-
403PhosphorylationVHHQRGHTGERPYEC
CCCCCCCCCCCCEEC
43.4925159151
411SumoylationGERPYECKECGKSFR
CCCCEECCCCCCCEE
44.06-
411SumoylationGERPYECKECGKSFR
CCCCEECCCCCCCEE
44.06-
419PhosphorylationECGKSFRYRSHLTEH
CCCCCEECCCCCCCC
17.9223532336
421PhosphorylationGKSFRYRSHLTEHQR
CCCEECCCCCCCCCC
17.5723532336
431PhosphorylationTEHQRLHTGERPYNC
CCCCCCCCCCCCCCH
45.3829759185
436PhosphorylationLHTGERPYNCRECGK
CCCCCCCCCHHHHHH
32.8729759185
459PhosphorylationLVHERVHTGERPYAC
EEEECCCCCCCCEEE
37.5721712546
480PhosphorylationFGNKHSVTIHQRIHT
HCCCCEEEEEEEEEC
18.7622817900
487PhosphorylationTIHQRIHTGERPYEC
EEEEEEECCCCCEEC
38.06-
504PhosphorylationCGKSFLSSSALHVHK
HHHCHHCCCCEEHHH
23.0628555341
505PhosphorylationGKSFLSSSALHVHKR
HHCHHCCCCEEHHHH
31.3228555341
511SumoylationSSALHVHKRVHSGQK
CCCEEHHHHHHCCCC
55.84-
511SumoylationSSALHVHKRVHSGQK
CCCEEHHHHHHCCCC
55.84-
528PhosphorylationKCSECGKSFSECSSL
ECCCCCCCHHHHHHH
21.2028555341
534PhosphorylationKSFSECSSLIKHRRI
CCHHHHHHHHHHCCC
45.8624719451
543PhosphorylationIKHRRIHTGERPYEC
HHHCCCCCCCCCEEC
38.0625159151
561PhosphorylationGKTFQRSSTLLHHQS
CCEEEHHHHHHHHCH
25.8428555341

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 ZN587_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN587_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 ZN587_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRA23_HUMANKRTAP2-4physical
25416956
KRA24_HUMANKRTAP2-4physical
25416956
TRI41_HUMANTRIM41physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
FSD2_HUMANFSD2physical
25416956
K1C40_HUMANKRT40physical
25416956
ZN417_HUMANZNF417physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR101_HUMANKRTAP10-1physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
ZBT8A_HUMANZBTB8Aphysical
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 ZN587_HUMAN

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Related Literatures of Post-Translational Modification

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