TINAL_HUMAN - dbPTM
TINAL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TINAL_HUMAN
UniProt AC Q9GZM7
Protein Name Tubulointerstitial nephritis antigen-like
Gene Name TINAGL1
Organism Homo sapiens (Human).
Sequence Length 467
Subcellular Localization Secreted .
Protein Description May be implicated in the adrenocortical zonation and in mechanisms for repressing the CYP11B1 gene expression in adrenocortical cells. This is a non catalytic peptidase C1 family protein (By similarity)..
Protein Sequence MWRCPLGLLLLLPLAGHLALGAQQGRGRRELAPGLHLRGIRDAGGRYCQEQDLCCRGRADDCALPYLGAICYCDLFCNRTVSDCCPDFWDFCLGVPPPFPPIQGCMHGGRIYPVLGTYWDNCNRCTCQENRQWQCDQEPCLVDPDMIKAINQGNYGWQAGNHSAFWGMTLDEGIRYRLGTIRPSSSVMNMHEIYTVLNPGEVLPTAFEASEKWPNLIHEPLDQGNCAGSWAFSTAAVASDRVSIHSLGHMTPVLSPQNLLSCDTHQQQGCRGGRLDGAWWFLRRRGVVSDHCYPFSGRERDEAGPAPPCMMHSRAMGRGKRQATAHCPNSYVNNNDIYQVTPVYRLGSNDKEIMKELMENGPVQALMEVHEDFFLYKGGIYSHTPVSLGRPERYRRHGTHSVKITGWGEETLPDGRTLKYWTAANSWGPAWGERGHFRIVRGVNECDIESFVLGVWGRVGMEDMGHH
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
78N-linked_GlycosylationCYCDLFCNRTVSDCC
HHHHHHCCCCHHHHC
35.0119159218
161N-linked_GlycosylationNYGWQAGNHSAFWGM
CCCEECCCCCCCCCC
29.0219159218
387PhosphorylationIYSHTPVSLGRPERY
EECCCCCCCCCCHHH
26.7224719451

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 TINAL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TINAL_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 TINAL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED31_HUMANMED31physical
16169070
UT14A_HUMANUTP14Aphysical
16169070
KRA42_HUMANKRTAP4-2physical
25416956
KR122_HUMANKRTAP12-2physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
ANM5_HUMANPRMT5physical
26186194
GBB2_HUMANGNB2physical
26186194
CD59_HUMANCD59physical
26186194
RIOK1_HUMANRIOK1physical
26186194
PGBM_HUMANHSPG2physical
26186194
LOXL2_HUMANLOXL2physical
26186194
PGBM_HUMANHSPG2physical
28514442
RIOK1_HUMANRIOK1physical
28514442
ANM5_HUMANPRMT5physical
28514442
CD59_HUMANCD59physical
28514442
LOXL2_HUMANLOXL2physical
28514442
GBB2_HUMANGNB2physical
28514442

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 TINAL_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78 AND ASN-161, AND MASSSPECTROMETRY.

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