ZN268_HUMAN - dbPTM
ZN268_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN268_HUMAN
UniProt AC Q14587
Protein Name Zinc finger protein 268
Gene Name ZNF268
Organism Homo sapiens (Human).
Sequence Length 947
Subcellular Localization Isoform 1: Nucleus .
Isoform 2: Nucleus . Cytoplasm .
Protein Description Isoform 1: Acts as a transcriptional repressor. Inhibits erythroid differentiation and tumor cell proliferation. Plays a role during ovarian cancer development and progression.; Isoform 2: Contributes to cervical carcinogenesis in part through the TNF-alpha-induced NF-kappa-B signaling pathway by interacting with the I-kappa-B-kinase (IKK) core complex..
Protein Sequence MATRVRTASIWVPPLQERNSSWDRIRKLQGQESILGQGTPGLQPLPGTPRQKQKSRRIEKVLEWLFISQEQPKITKSWGPLSFMDVFVDFTWEEWQLLDPAQKCLYRSVMLENYSNLVSLGYQHTKPDIIFKLEQGEELCMVQAQVPNQTCPNTVWKIDDLMDWHQENKDKLGSTAKSFECTTFGKLCLLSTKYLSRQKPHKCGTHGKSLKYIDFTSDYARNNPNGFQVHGKSFFHSKHEQTVIGIKYCESIESGKTVNKKSQLMCQQMYMGEKPFGCSCCEKAFSSKSYLLVHQQTHAEEKPYGCNECGKDFSSKSYLIVHQRIHTGEKLHECSECRKTFSFHSQLVIHQRIHTGENPYECCECGKVFSRKDQLVSHQKTHSGQKPYVCNECGKAFGLKSQLIIHERIHTGEKPYECNECQKAFNTKSNLMVHQRTHTGEKPYVCSDCGKAFTFKSQLIVHQGIHTGVKPYGCIQCGKGFSLKSQLIVHQRSHTGMKPYVCNECGKAFRSKSYLIIHTRTHTGEKLHECNNCGKAFSFKSQLIIHQRIHTGENPYECHECGKAFSRKYQLISHQRTHAGEKPYECTDCGKAFGLKSQLIIHQRTHTGEKPFECSECQKAFNTKSNLIVHQRTHTGEKPYSCNECGKAFTFKSQLIVHKGVHTGVKPYGCSQCAKTFSLKSQLIVHQRSHTGVKPYGCSECGKAFRSKSYLIIHMRTHTGEKPHECRECGKSFSFNSQLIVHQRIHTGENPYECSECGKAFNRKDQLISHQRTHAGEKPYGCSECGKAFSSKSYLIIHMRTHSGEKPYECNECGKAFIWKSLLIVHERTHAGVNPYKCSQCEKSFSGKLRLLVHQRMHTREKPYECSECGKAFIRNSQLIVHQRTHSGEKPYGCNECGKTFSQKSILSAHQRTHTGEKPCKCTECGKAFCWKSQLIMHQRTHVDDKH
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
9PhosphorylationATRVRTASIWVPPLQ
CCEEEEEEEECCCHH
19.1728555341
33PhosphorylationRKLQGQESILGQGTP
HHHCCCCCCCCCCCC
18.4127732954
39PhosphorylationESILGQGTPGLQPLP
CCCCCCCCCCCCCCC
13.2928555341
48PhosphorylationGLQPLPGTPRQKQKS
CCCCCCCCCCHHHHH
17.2325850435
106PhosphorylationDPAQKCLYRSVMLEN
CHHHHHHHHHHHHHC
15.43-
114PhosphorylationRSVMLENYSNLVSLG
HHHHHHCHHHHHHCC
6.9122817900
115PhosphorylationSVMLENYSNLVSLGY
HHHHHCHHHHHHCCC
34.9622817900
174PhosphorylationENKDKLGSTAKSFEC
HCHHHCCCCCCCEEE
35.3126657352
175PhosphorylationNKDKLGSTAKSFECT
CHHHCCCCCCCEEEC
35.9826657352
178PhosphorylationKLGSTAKSFECTTFG
HCCCCCCCEEECHHH
24.6626657352
190PhosphorylationTFGKLCLLSTKYLSR
HHHHHHHHCHHHHHC
6.2827251275
191PhosphorylationFGKLCLLSTKYLSRQ
HHHHHHHCHHHHHCC
15.2024719451
251PhosphorylationIGIKYCESIESGKTV
EEEEEEEECCCCCCC
28.2629083192
254PhosphorylationKYCESIESGKTVNKK
EEEEECCCCCCCCHH
43.8729083192
257PhosphorylationESIESGKTVNKKSQL
EECCCCCCCCHHHHH
32.6029083192
262PhosphorylationGKTVNKKSQLMCQQM
CCCCCHHHHHHHHHH
30.1023401153
270PhosphorylationQLMCQQMYMGEKPFG
HHHHHHHHCCCCCCC
9.5324043423
335PhosphorylationGEKLHECSECRKTFS
CCCCEECCHHCCEEE
36.4227251275
340PhosphorylationECSECRKTFSFHSQL
ECCHHCCEEEEECEE
12.7427251275
342PhosphorylationSECRKTFSFHSQLVI
CHHCCEEEEECEEEE
27.5527251275
345PhosphorylationRKTFSFHSQLVIHQR
CCEEEEECEEEEEEE
24.1727251275
377PhosphorylationSRKDQLVSHQKTHSG
ECHHHHHCCCCCCCC
28.8829083192
411PhosphorylationIIHERIHTGEKPYEC
EEEEEECCCCCCCCC
44.6728655764
437PhosphorylationNLMVHQRTHTGEKPY
CEEEEECCCCCCCCE
19.74-
439PhosphorylationMVHQRTHTGEKPYVC
EEEECCCCCCCCEEE
46.56-
521PhosphorylationYLIIHTRTHTGEKLH
EEEEEECCCCCCCCE
25.58-
523PhosphorylationIIHTRTHTGEKLHEC
EEEECCCCCCCCEEC
46.56-
538PhosphorylationNNCGKAFSFKSQLII
CCCCCCEEEECEEEE
36.3024719451
540SumoylationCGKAFSFKSQLIIHQ
CCCCEEEECEEEEEE
35.77-
540SumoylationCGKAFSFKSQLIIHQ
CCCCEEEECEEEEEE
35.77-
584PhosphorylationTHAGEKPYECTDCGK
CCCCCCCEEECCHHH
34.40-
596SumoylationCGKAFGLKSQLIIHQ
HHHHHCCCCEEEEEE
36.21-
596SumoylationCGKAFGLKSQLIIHQ
HHHHHCCCCEEEEEE
36.21-
605PhosphorylationQLIIHQRTHTGEKPF
EEEEEECCCCCCCCC
19.74-
607PhosphorylationIIHQRTHTGEKPFEC
EEEECCCCCCCCCCC
46.56-
610AcetylationQRTHTGEKPFECSEC
ECCCCCCCCCCCHHH
57.2511566381
633PhosphorylationNLIVHQRTHTGEKPY
CEEEEECCCCCCCCC
19.74-
635PhosphorylationIVHQRTHTGEKPYSC
EEEECCCCCCCCCCC
46.56-
717PhosphorylationYLIIHMRTHTGEKPH
EEEEEEEECCCCCCC
19.06-
719PhosphorylationIIHMRTHTGEKPHEC
EEEEEECCCCCCCCC
46.56-
747PhosphorylationIVHQRIHTGENPYEC
EEEEEEECCCCCCCH
43.7628152594
752PhosphorylationIHTGENPYECSECGK
EECCCCCCCHHHHHH
40.9425839225
755PhosphorylationGENPYECSECGKAFN
CCCCCCHHHHHHHCC
24.7928152594
759SumoylationYECSECGKAFNRKDQ
CCHHHHHHHCCCHHH
62.56-
759SumoylationYECSECGKAFNRKDQ
CCHHHHHHHCCCHHH
62.56-
806UbiquitinationMRTHSGEKPYECNEC
EEECCCCCCEECCCC
57.32-
846PhosphorylationSQCEKSFSGKLRLLV
CCCCCCCCCCHHHHH
41.9524719451
871UbiquitinationYECSECGKAFIRNSQ
CCCCHHHHEEHHHCE
52.35-
913PhosphorylationILSAHQRTHTGEKPC
HHHHHHCCCCCCCCE
19.74-
915PhosphorylationSAHQRTHTGEKPCKC
HHHHCCCCCCCCEEC
46.56-

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 ZN268_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN268_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 ZN268_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN268_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN268_HUMAN

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Related Literatures of Post-Translational Modification

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