TIPRL_HUMAN - dbPTM
TIPRL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TIPRL_HUMAN
UniProt AC O75663
Protein Name TIP41-like protein
Gene Name TIPRL
Organism Homo sapiens (Human).
Sequence Length 272
Subcellular Localization Cytoplasm .
Protein Description May be a allosteric regulator of serine/threonine-protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. Acts as negative regulator of serine/threonine-protein phosphatase 4 probably by inhibiting the formation of the active PPP4C:PPP4R2 complex; the function is proposed to implicate it in DNA damage response by promoting H2AFX phosphorylated on Ser-140 (gamma-H2AFX). May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair..
Protein Sequence MMIHGFQSSHRDFCFGPWKLTASKTHIMKSADVEKLADELHMPSLPEMMFGDNVLRIQHGSGFGIEFNATDALRCVNNYQGMLKVACAEEWQESRTEGEHSKEVIKPYDWTYTTDYKGTLLGESLKLKVVPTTDHIDTEKLKAREQIKFFEEVLLFEDELHDHGVSSLSVKIRVMPSSFFLLLRFFLRIDGVLIRMNDTRLYHEADKTYMLREYTSRESKISSLMHVPPSLFTEPNEISQYLPIKEAVCEKLIFPERIDPNPADSQKSTQVE
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
8PhosphorylationMMIHGFQSSHRDFCF
CCCCCCCCCCCCCCC
26.3324719451
9PhosphorylationMIHGFQSSHRDFCFG
CCCCCCCCCCCCCCC
16.2626853621
19AcetylationDFCFGPWKLTASKTH
CCCCCCCEEEECCCE
38.8123749302
19UbiquitinationDFCFGPWKLTASKTH
CCCCCCCEEEECCCE
38.81-
24UbiquitinationPWKLTASKTHIMKSA
CCEEEECCCEEHHHC
41.4829967540
29UbiquitinationASKTHIMKSADVEKL
ECCCEEHHHCCHHHH
41.7229967540
29AcetylationASKTHIMKSADVEKL
ECCCEEHHHCCHHHH
41.7225953088
44PhosphorylationADELHMPSLPEMMFG
HHHHCCCCCCHHHHC
49.3224043423
79PhosphorylationALRCVNNYQGMLKVA
HHHHHHHHCHHHHHH
10.97-
84UbiquitinationNNYQGMLKVACAEEW
HHHCHHHHHHHHHHH
20.9232015554
87GlutathionylationQGMLKVACAEEWQES
CHHHHHHHHHHHHHH
5.6922555962
101PhosphorylationSRTEGEHSKEVIKPY
HCCCCCCCCCCCCCC
26.64-
102UbiquitinationRTEGEHSKEVIKPYD
CCCCCCCCCCCCCCC
58.8923000965
106 (in isoform 2)Ubiquitination-42.5821890473
106 (in isoform 1)Ubiquitination-42.5821890473
106UbiquitinationEHSKEVIKPYDWTYT
CCCCCCCCCCCCEEE
42.5823000965
106AcetylationEHSKEVIKPYDWTYT
CCCCCCCCCCCCEEE
42.5819608861
108PhosphorylationSKEVIKPYDWTYTTD
CCCCCCCCCCEEECC
21.0727642862
111PhosphorylationVIKPYDWTYTTDYKG
CCCCCCCEEECCCCC
14.2127642862
112PhosphorylationIKPYDWTYTTDYKGT
CCCCCCEEECCCCCE
11.9127642862
113PhosphorylationKPYDWTYTTDYKGTL
CCCCCEEECCCCCEE
13.0527642862
114PhosphorylationPYDWTYTTDYKGTLL
CCCCEEECCCCCEEE
27.2427642862
117AcetylationWTYTTDYKGTLLGES
CEEECCCCCEEECCE
48.5161253
117 (in isoform 1)Ubiquitination-48.5121890473
117UbiquitinationWTYTTDYKGTLLGES
CEEECCCCCEEECCE
48.5121963094
117 (in isoform 2)Ubiquitination-48.5121890473
117SumoylationWTYTTDYKGTLLGES
CEEECCCCCEEECCE
48.51-
124PhosphorylationKGTLLGESLKLKVVP
CCEEECCEEEEEEEE
29.0727067055
126UbiquitinationTLLGESLKLKVVPTT
EEECCEEEEEEEECC
56.3821963094
126AcetylationTLLGESLKLKVVPTT
EEECCEEEEEEEECC
56.3825953088
126 (in isoform 2)Ubiquitination-56.38-
128UbiquitinationLGESLKLKVVPTTDH
ECCEEEEEEEECCCC
39.3321906983
128 (in isoform 1)Ubiquitination-39.3321890473
128 (in isoform 2)Ubiquitination-39.3321890473
132PhosphorylationLKLKVVPTTDHIDTE
EEEEEEECCCCCCHH
32.9929759185
133PhosphorylationKLKVVPTTDHIDTEK
EEEEEECCCCCCHHH
21.3629759185
138PhosphorylationPTTDHIDTEKLKARE
ECCCCCCHHHHHHHH
34.1229759185
140UbiquitinationTDHIDTEKLKAREQI
CCCCCHHHHHHHHHH
58.3333845483
142UbiquitinationHIDTEKLKAREQIKF
CCCHHHHHHHHHHHH
57.37-
167PhosphorylationLHDHGVSSLSVKIRV
HHHCCCCEEEEEEEE
23.4324719451
202PhosphorylationRMNDTRLYHEADKTY
EECCCEEEECCCCCC
8.3629496907
207 (in isoform 1)Ubiquitination-48.9121890473
2072-HydroxyisobutyrylationRLYHEADKTYMLREY
EEEECCCCCCCCHHH
48.91-
207AcetylationRLYHEADKTYMLREY
EEEECCCCCCCCHHH
48.9119608861
207UbiquitinationRLYHEADKTYMLREY
EEEECCCCCCCCHHH
48.9122817900
208PhosphorylationLYHEADKTYMLREYT
EEECCCCCCCCHHHC
18.0828064214
209PhosphorylationYHEADKTYMLREYTS
EECCCCCCCCHHHCC
10.4125839225
245UbiquitinationISQYLPIKEAVCEKL
HHHCCCCCHHHHHHH
37.3729967540
251AcetylationIKEAVCEKLIFPERI
CCHHHHHHHCCCCCC
41.5823749302
251UbiquitinationIKEAVCEKLIFPERI
CCHHHHHHHCCCCCC
41.5829967540
265PhosphorylationIDPNPADSQKSTQVE
CCCCCCCCCCCCCCC
41.4317525332
267UbiquitinationPNPADSQKSTQVE--
CCCCCCCCCCCCC--
60.4627667366
267 (in isoform 1)Ubiquitination-60.4621890473
268PhosphorylationNPADSQKSTQVE---
CCCCCCCCCCCC---
19.2122817901
269PhosphorylationPADSQKSTQVE----
CCCCCCCCCCC----
43.6023312004

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 TIPRL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TIPRL_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 TIPRL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2AB_HUMANPPP2CBphysical
16085932
PP4C_HUMANPPP4Cphysical
16085932
PPP6_HUMANPPP6Cphysical
16085932
A4_HUMANAPPphysical
21832049
XPP1_HUMANXPNPEP1physical
22939629
VATA_HUMANATP6V1Aphysical
22939629
IGBP1_HUMANIGBP1physical
23892082
PP2AA_RATPpp2caphysical
23892082
RHG44_HUMANARHGAP44physical
26344197
MCMBP_HUMANMCMBPphysical
26344197
PEPL1_HUMANNPEPL1physical
26344197
3BP1_HUMANSH3BP1physical
26344197
DYLT1_HUMANDYNLT1physical
27173435
TC1D2_HUMANTCTEX1D2physical
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 TIPRL_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106 AND LYS-207, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209, AND MASSSPECTROMETRY.

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