TUFT1_HUMAN - dbPTM
TUFT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TUFT1_HUMAN
UniProt AC Q9NNX1
Protein Name Tuftelin
Gene Name TUFT1
Organism Homo sapiens (Human).
Sequence Length 390
Subcellular Localization Secreted . Secreted at a very early stage of enamel formation, concentrated at the dentin-enamel junction and tightly bound to the surface of the growing crystallites.
Protein Description Involved in the mineralization and structural organization of enamel..
Protein Sequence MNGTRNWCTLVDVHPEDQAAGSVDILRLTLQGELTGDELEHIAQKAGRKTYAMVSSHSAGHSLASELVESHDGHEEIIKVYLKGRSGDKMIHEKNINQLKSEVQYIQEARNCLQKLREDISSKLDRNLGDSLHRQEIQVVLEKPNGFSQSPTALYSSPPEVDTCINEDVESLRKTVQDLLAKLQEAKRQHQSDCVAFEVTLSRYQREAEQSNVALQREEDRVEQKEAEVGELQRRLLGMETEHQALLAKVREGEVALEELRSNNADCQAEREKAATLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKAVIQSKDATIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFSTQARAKTENPGSIRISKPPSPKPMPVIRVVET
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
4 (in isoform 2)Phosphorylation-18.8022210691
9 (in isoform 2)Phosphorylation-22.7922210691
50PhosphorylationAQKAGRKTYAMVSSH
HHHCCCCCEEEECCC
18.36-
55PhosphorylationRKTYAMVSSHSAGHS
CCCEEEECCCHHCCH
14.8428348404
56PhosphorylationKTYAMVSSHSAGHSL
CCEEEECCCHHCCHH
15.2827251275
58PhosphorylationYAMVSSHSAGHSLAS
EEEECCCHHCCHHHH
37.5828348404
62PhosphorylationSSHSAGHSLASELVE
CCCHHCCHHHHHHHH
25.39-
94UbiquitinationGDKMIHEKNINQLKS
CCCCHHHHCHHHHHH
49.30-
100UbiquitinationEKNINQLKSEVQYIQ
HHCHHHHHHHHHHHH
34.50-
115UbiquitinationEARNCLQKLREDISS
HHHHHHHHHHHHHHH
36.24-
123UbiquitinationLREDISSKLDRNLGD
HHHHHHHHHHHHHHH
47.84-
131PhosphorylationLDRNLGDSLHRQEIQ
HHHHHHHHHHHHHHE
25.0320873877
148PhosphorylationLEKPNGFSQSPTALY
EECCCCCCCCCCCCC
31.0228348404
150PhosphorylationKPNGFSQSPTALYSS
CCCCCCCCCCCCCCC
24.0327251275
152PhosphorylationNGFSQSPTALYSSPP
CCCCCCCCCCCCCCC
34.2428348404
157PhosphorylationSPTALYSSPPEVDTC
CCCCCCCCCCCCCHH
30.80-
171PhosphorylationCINEDVESLRKTVQD
HCCCCHHHHHHHHHH
33.0724719451
182UbiquitinationTVQDLLAKLQEAKRQ
HHHHHHHHHHHHHHH
51.15-
192PhosphorylationEAKRQHQSDCVAFEV
HHHHHCHHCCEEEEH
30.7425002506
200PhosphorylationDCVAFEVTLSRYQRE
CCEEEEHHHHHHHHH
16.3025002506
225UbiquitinationEEDRVEQKEAEVGEL
HHHHHHHHHHHHHHH
45.44-
276PhosphorylationAEREKAATLEKEVAG
HHHHHHHHHHHHHHH
40.0724719451
2792-HydroxyisobutyrylationEKAATLEKEVAGLRE
HHHHHHHHHHHHHHH
61.68-
312PhosphorylationMIEQLQNSKAVIQSK
HHHHHHCCCHHHCCC
14.7224043423
319UbiquitinationSKAVIQSKDATIQEL
CCHHHCCCCHHHHHH
34.70-
370PhosphorylationAKTENPGSIRISKPP
CCCCCCCCCEECCCC
15.2224719451
374PhosphorylationNPGSIRISKPPSPKP
CCCCCEECCCCCCCC
29.3030619164
378PhosphorylationIRISKPPSPKPMPVI
CEECCCCCCCCCCEE
54.8325159151

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 TUFT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TUFT1_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 TUFT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TFP11_HUMANTFIP11physical
10806191
KAT5_HUMANKAT5physical
25416956
CEP76_HUMANCEP76physical
25416956
CCD33_HUMANCCDC33physical
25416956
SMC6_HUMANSMC6physical
26186194
RBGP1_HUMANRABGAP1physical
26186194
RBG10_HUMANRABGAP1Lphysical
26186194
RBG1L_HUMANRABGAP1Lphysical
26186194
ZYX_HUMANZYXphysical
26186194
CREB1_HUMANCREB1physical
26186194
ATF1_HUMANATF1physical
26186194
NSE4A_HUMANNSMCE4Aphysical
26186194
ZYX_HUMANZYXphysical
21516116
RBGP1_HUMANRABGAP1physical
28514442
ATF1_HUMANATF1physical
28514442
ZYX_HUMANZYXphysical
28514442
SMC6_HUMANSMC6physical
28514442
RBG10_HUMANRABGAP1Lphysical
28514442
RBG1L_HUMANRABGAP1Lphysical
28514442
CREB1_HUMANCREB1physical
28514442
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
YETS4_HUMANYEATS4physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS53_HUMANVPS53physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
RCOR1_HUMANRCOR1physical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
BMAL1_HUMANARNTLphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
NUF2_HUMANNUF2physical
27173435
VPS51_HUMANVPS51physical
27173435
EIPR1_HUMANTSSC1physical
27173435
RABE1_HUMANRABEP1physical
27173435
STRN_HUMANSTRNphysical
27173435

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 TUFT1_HUMAN

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Related Literatures of Post-Translational Modification

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