PITH1_HUMAN - dbPTM
PITH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PITH1_HUMAN
UniProt AC Q9GZP4
Protein Name PITH domain-containing protein 1
Gene Name PITHD1
Organism Homo sapiens (Human).
Sequence Length 211
Subcellular Localization
Protein Description
Protein Sequence MSHGHSHGGGGCRCAAEREEPPEQRGLAYGLYLRIDLERLQCLNESREGSGRGVFKPWEERTDRSKFVESDADEELLFNIPFTGNVKLKGIIIMGEDDDSHPSEMRLYKNIPQMSFDDTEREPDQTFSLNRDLTGELEYATKISRFSNVYHLSIHISKNFGADTTKVFYIGLRGEWTELRRHEVTICNYEASANPADHRVHQVTPQTHFIS
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
2Phosphorylation------MSHGHSHGG
------CCCCCCCCC
37.87-
6Phosphorylation--MSHGHSHGGGGCR
--CCCCCCCCCCCCC
28.55-
52MethylationESREGSGRGVFKPWE
CCCCCCCCCCCCCHH
39.54115487587
56UbiquitinationGSGRGVFKPWEERTD
CCCCCCCCCHHHCCC
46.98-
65 (in isoform 2)Ubiquitination-33.0021890473
66 (in isoform 1)Ubiquitination-55.0821890473
66UbiquitinationEERTDRSKFVESDAD
HHCCCHHHCCCCCCC
55.0821906983
87UbiquitinationIPFTGNVKLKGIIIM
CCCCCCEEEEEEEEE
48.78-
89AcetylationFTGNVKLKGIIIMGE
CCCCEEEEEEEEECC
42.2026051181
89UbiquitinationFTGNVKLKGIIIMGE
CCCCEEEEEEEEECC
42.20-
108 (in isoform 2)Ubiquitination-7.5121890473
109 (in isoform 1)Ubiquitination-53.6521890473
109UbiquitinationPSEMRLYKNIPQMSF
HHHHHHHHCCCCCCC
53.6521906983
141 (in isoform 2)Ubiquitination-28.1921890473
142UbiquitinationGELEYATKISRFSNV
CCHHHHHEEECCCCE
30.4321890473
142 (in isoform 1)Ubiquitination-30.4321890473
150PhosphorylationISRFSNVYHLSIHIS
EECCCCEEEEEEEEE
10.99-
169PhosphorylationADTTKVFYIGLRGEW
CCCEEEEEEEECCCC
9.32-
185PhosphorylationELRRHEVTICNYEAS
ECEEEEEEEECCCHH
19.4821945579
189PhosphorylationHEVTICNYEASANPA
EEEEEECCCHHCCCC
14.4121945579
192PhosphorylationTICNYEASANPADHR
EEECCCHHCCCCCCC
19.3521945579
192O-linked_GlycosylationTICNYEASANPADHR
EEECCCHHCCCCCCC
19.35OGP
204PhosphorylationDHRVHQVTPQTHFIS
CCCCEECCCCCCCCC
11.7826462736
204O-linked_GlycosylationDHRVHQVTPQTHFIS
CCCCEECCCCCCCCC
11.7854901545
207PhosphorylationVHQVTPQTHFIS---
CEECCCCCCCCC---
21.6920068231
207O-linked_GlycosylationVHQVTPQTHFIS---
CEECCCCCCCCC---
21.6955828789
211PhosphorylationTPQTHFIS-------
CCCCCCCC-------
32.9725159151
211O-linked_GlycosylationTPQTHFIS-------
CCCCCCCC-------
32.9772257159

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 PITH1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PITH1_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 PITH1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC73_HUMANCDC73physical
16169070
CETN2_HUMANCETN2physical
26344197
SLK_HUMANSLKphysical
26344197
1433B_HUMANYWHABphysical
26344197
WDR59_HUMANWDR59physical
28514442
DPYL1_HUMANCRMP1physical
28514442
EF1A2_HUMANEEF1A2physical
28514442
RPR1A_HUMANRPRD1Aphysical
28514442
RECQ5_HUMANRECQL5physical
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 PITH1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-189, AND MASSSPECTROMETRY.

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