KDF1_HUMAN - dbPTM
KDF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDF1_HUMAN
UniProt AC Q8NAX2
Protein Name Keratinocyte differentiation factor 1
Gene Name KDF1
Organism Homo sapiens (Human).
Sequence Length 398
Subcellular Localization Cytoplasm . Cell junction . Localized at cell borders in single layered keratinocytes. Localized at cell borders in the basal and spinous layers but is more diffusely localized in the granular layer. Colocalized with actin near the cell membrane, esp
Protein Description Plays a role in the regulation of the epidermis formation during early development. Required both as an inhibitor of basal cell proliferation and a promoter of differentiation of basal progenitor cell progeny (By similarity)..
Protein Sequence MPRPGHPRPASGPPRLGPWERPTELCLETYDKPPQPPPSRRTRRPDPKDPGHHGPESITFISGSAEPALESPTCCLLWRPWVWEWCRAAFCFRRCRDCLQRCGACVRGCSPCLSTEDSTEGTAEANWAKEHNGVPPSPDRAPPSRRDGQRLKSTMGSSFSYPDVKLKGIPVYPYPRATSPAPDADSCCKEPLADPPPMRHSLPSTFASSPRGSEEYYSFHESDLDLPEMGSGSMSSREIDVLIFKKLTELFSVHQIDELAKCTSDTVFLEKTSKISDLISSITQDYHLDEQDAEGRLVRGIIRISTRKSRARPQTSEGRSTRAAAPTAAAPDSGHETMVGSGLSQDELTVQISQETTADAIARKLRPYGAPGYPASHDSSFQGTDTDSSGAPLLQVYC
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
11PhosphorylationPGHPRPASGPPRLGP
CCCCCCCCCCCCCCC
25394399
30PhosphorylationTELCLETYDKPPQPP
CHHHHHCCCCCCCCC
22817900
118PhosphorylationPCLSTEDSTEGTAEA
CCCCCCCCCCCCHHH
-
119PhosphorylationCLSTEDSTEGTAEAN
CCCCCCCCCCCHHHH
-
122PhosphorylationTEDSTEGTAEANWAK
CCCCCCCCHHHHHHH
-
137PhosphorylationEHNGVPPSPDRAPPS
HHCCCCCCCCCCCCC
25849741
144PhosphorylationSPDRAPPSRRDGQRL
CCCCCCCCCCCCHHH
27050516
153PhosphorylationRDGQRLKSTMGSSFS
CCCHHHHHHCCCCCC
28985074
154PhosphorylationDGQRLKSTMGSSFSY
CCHHHHHHCCCCCCC
28176443
157PhosphorylationRLKSTMGSSFSYPDV
HHHHHCCCCCCCCCC
29978859
158PhosphorylationLKSTMGSSFSYPDVK
HHHHCCCCCCCCCCE
28176443
160PhosphorylationSTMGSSFSYPDVKLK
HHCCCCCCCCCCEEC
28176443
161PhosphorylationTMGSSFSYPDVKLKG
HCCCCCCCCCCEECC
28176443
172PhosphorylationKLKGIPVYPYPRATS
EECCCCCCCCCCCCC
28152594
174PhosphorylationKGIPVYPYPRATSPA
CCCCCCCCCCCCCCC
28152594
178PhosphorylationVYPYPRATSPAPDAD
CCCCCCCCCCCCCHH
23090842
179PhosphorylationYPYPRATSPAPDADS
CCCCCCCCCCCCHHH
25849741
186PhosphorylationSPAPDADSCCKEPLA
CCCCCHHHCCCCCCC
25849741
201PhosphorylationDPPPMRHSLPSTFAS
CCCCCCCCCCCCCCC
25849741
204PhosphorylationPMRHSLPSTFASSPR
CCCCCCCCCCCCCCC
23927012
205PhosphorylationMRHSLPSTFASSPRG
CCCCCCCCCCCCCCC
23927012
208PhosphorylationSLPSTFASSPRGSEE
CCCCCCCCCCCCCCC
25849741
209PhosphorylationLPSTFASSPRGSEEY
CCCCCCCCCCCCCCC
25849741
213PhosphorylationFASSPRGSEEYYSFH
CCCCCCCCCCCEECC
21406692
216PhosphorylationSPRGSEEYYSFHESD
CCCCCCCCEECCHHH
21406692
217PhosphorylationPRGSEEYYSFHESDL
CCCCCCCEECCHHHC
21406692
218PhosphorylationRGSEEYYSFHESDLD
CCCCCCEECCHHHCC
26657352
222PhosphorylationEYYSFHESDLDLPEM
CCEECCHHHCCCCCC
26657352
231PhosphorylationLDLPEMGSGSMSSRE
CCCCCCCCCCCCHHH
27080861
233PhosphorylationLPEMGSGSMSSREID
CCCCCCCCCCHHHCE
27080861
235PhosphorylationEMGSGSMSSREIDVL
CCCCCCCCHHHCEEE
27080861
236PhosphorylationMGSGSMSSREIDVLI
CCCCCCCHHHCEEEH
27080861
286PhosphorylationISSITQDYHLDEQDA
HHHHHCCCCCCHHHC
27642862
305PhosphorylationVRGIIRISTRKSRAR
HHHEEEEECCCCCCC
23312004
306PhosphorylationRGIIRISTRKSRARP
HHEEEEECCCCCCCC
23312004
315PhosphorylationKSRARPQTSEGRSTR
CCCCCCCCCCCCCCC
28102081
316PhosphorylationSRARPQTSEGRSTRA
CCCCCCCCCCCCCCC
28102081
368PhosphorylationIARKLRPYGAPGYPA
HHHHHCCCCCCCCCC
27642862
373PhosphorylationRPYGAPGYPASHDSS
CCCCCCCCCCCCCCC
27642862
376PhosphorylationGAPGYPASHDSSFQG
CCCCCCCCCCCCCCC
23898821
379PhosphorylationGYPASHDSSFQGTDT
CCCCCCCCCCCCCCC
23898821
380PhosphorylationYPASHDSSFQGTDTD
CCCCCCCCCCCCCCC
28348404
397PhosphorylationGAPLLQVYC------
CCCEEEEEC------
27642862

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 KDF1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDF1_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 KDF1_HUMAN !!

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

Oops, there are no PPI records of KDF1_HUMAN !!

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 KDF1_HUMAN

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Related Literatures of Post-Translational Modification

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