TINAG_HUMAN - dbPTM
TINAG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TINAG_HUMAN
UniProt AC Q9UJW2
Protein Name Tubulointerstitial nephritis antigen
Gene Name TINAG
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization Secreted, extracellular space, extracellular matrix, basement membrane .
Protein Description Mediates adhesion of proximal tubule epithelial cells via integrins alpha3-beta1 and alphaV-beta3. This is a non catalytic peptidase C1 family protein..
Protein Sequence MWTGYKILIFSYLTTEIWMEKQYLSQREVDLEAYFTRNHTVLQGTRFKRAIFQGQYCRNFGCCEDRDDGCVTEFYAANALCYCDKFCDRENSDCCPDYKSFCREEKEWPPHTQPWYPEGCFKDGQHYEEGSVIKENCNSCTCSGQQWKCSQHVCLVRSELIEQVNKGDYGWTAQNYSQFWGMTLEDGFKFRLGTLPPSPMLLSMNEMTASLPATTDLPEFFVASYKWPGWTHGPLDQKNCAASWAFSTASVAADRIAIQSKGRYTANLSPQNLISCCAKNRHGCNSGSIDRAWWYLRKRGLVSHACYPLFKDQNATNNGCAMASRSDGRGKRHATKPCPNNVEKSNRIYQCSPPYRVSSNETEIMKEIMQNGPVQAIMQVREDFFHYKTGIYRHVTSTNKESEKYRKLQTHAVKLTGWGTLRGAQGQKEKFWIAANSWGKSWGENGYFRILRGVNESDIEKLIIAAWGQLTSSDEP
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
3Phosphorylation-----MWTGYKILIF
-----CCCCCEEEEE
29.3623663014
5Phosphorylation---MWTGYKILIFSY
---CCCCCEEEEEHH
6.3623663014
11PhosphorylationGYKILIFSYLTTEIW
CCEEEEEHHHHHHHH
16.5523663014
12PhosphorylationYKILIFSYLTTEIWM
CEEEEEHHHHHHHHH
9.4123663014
14PhosphorylationILIFSYLTTEIWMEK
EEEEHHHHHHHHHHH
17.7223663014
15PhosphorylationLIFSYLTTEIWMEKQ
EEEHHHHHHHHHHHH
23.9123663014
38N-linked_GlycosylationLEAYFTRNHTVLQGT
HHHHHCCCCCEECCC
31.93UniProtKB CARBOHYD
112O-linked_GlycosylationEKEWPPHTQPWYPEG
CCCCCCCCCCCCCCC
41.94OGP
175N-linked_GlycosylationDYGWTAQNYSQFWGM
CCCEECCCHHHHCCC
35.64UniProtKB CARBOHYD
286PhosphorylationKNRHGCNSGSIDRAW
HCCCCCCCCCHHHHH
37.6829759185
314N-linked_GlycosylationYPLFKDQNATNNGCA
HHHHCCCCCCCCCEE
59.89UniProtKB CARBOHYD
345PhosphorylationCPNNVEKSNRIYQCS
CCCCHHHCCCEEECC
20.17-
352PhosphorylationSNRIYQCSPPYRVSS
CCCEEECCCCCCCCC
17.24-
360N-linked_GlycosylationPPYRVSSNETEIMKE
CCCCCCCCHHHHHHH
53.34UniProtKB CARBOHYD
389PhosphorylationEDFFHYKTGIYRHVT
HHHHHHHHCCCCCCC
22.9629083192
392PhosphorylationFHYKTGIYRHVTSTN
HHHHHCCCCCCCCCC
8.9429083192
420PhosphorylationVKLTGWGTLRGAQGQ
HHHHCHHHHCCCCCC
13.5324114839
455N-linked_GlycosylationFRILRGVNESDIEKL
EEEEECCCHHHHHHH
45.97UniProtKB CARBOHYD

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 TINAG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TINAG_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 TINAG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM45B_HUMANTMEM45Bphysical
21988832
TYW3_HUMANTYW3physical
28514442
NUDT6_HUMANNUDT6physical
28514442
EPDR1_HUMANEPDR1physical
28514442
ACD11_HUMANACAD11physical
28514442
MOCS1_HUMANMOCS1physical
28514442
CTU2_HUMANCTU2physical
28514442
STK40_HUMANSTK40physical
28514442
RFWD2_HUMANRFWD2physical
28514442
ZN696_HUMANZNF696physical
28514442
IDE_HUMANIDEphysical
28514442
CTU1_HUMANCTU1physical
28514442
ZN579_HUMANZNF579physical
28514442
PP2AA_HUMANPPP2CAphysical
28514442
VP26A_HUMANVPS26Aphysical
28514442
CUL1_HUMANCUL1physical
28514442
CO4A1_HUMANCOL4A1physical
28514442
ALR_HUMANGFERphysical
28514442
ZN460_HUMANZNF460physical
28514442
TRAF7_HUMANTRAF7physical
28514442
GRP78_HUMANHSPA5physical
28514442

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

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Related Literatures of Post-Translational Modification

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