PINX1_HUMAN - dbPTM
PINX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PINX1_HUMAN
UniProt AC Q96BK5
Protein Name PIN2/TERF1-interacting telomerase inhibitor 1
Gene Name PINX1
Organism Homo sapiens (Human).
Sequence Length 328
Subcellular Localization Nucleus. Nucleus, nucleolus. Chromosome, telomere. Chromosome, centromere, kinetochore. Localizes in nucleoli, at telomere speckles and to the outer plate of kinetochores. Localization to the kinetochore is mediated by its central region and depends
Protein Description Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor..
Protein Sequence MSMLAERRRKQKWAVDPQNTAWSNDDSKFGQRMLEKMGWSKGKGLGAQEQGATDHIKVQVKNNHLGLGATINNEDNWIAHQDDFNQLLAELNTCHGQETTDSSDKKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSKTDLDCIFGKRQSKKTPEGDASPSTPEENETTTTSAFTIQEYFAKRMAALKNKPQVPVPGSDISETQVERKRGKKRNKEATGKDVESYLQPKAKRHTEGKPERAEAQERVAKKKSAPAEEQLRGPCWDQSSKASAQDAGDHVQPPEGRDFTLKPKKRRGKKKLQKPVEIAEDATLEETLVKKKKKKDSK
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
7Methylation-MSMLAERRRKQKWA
-CCHHHHHHHHHCCC		37.79115487571
12UbiquitinationAERRRKQKWAVDPQN
HHHHHHHCCCCCCCC		39.9129967540
20PhosphorylationWAVDPQNTAWSNDDS
CCCCCCCCCCCCCCC		25.0228509920
23PhosphorylationDPQNTAWSNDDSKFG
CCCCCCCCCCCCHHH		28.1128509920
40PhosphorylationMLEKMGWSKGKGLGA
HHHHHCCCCCCCCCC		26.2924505115
41AcetylationLEKMGWSKGKGLGAQ
HHHHCCCCCCCCCCH		59.1225953088
110PhosphorylationSDKKEKKSFSLEEKS
CCHHHHHCCCHHHHH		31.0021815630
112PhosphorylationKKEKKSFSLEEKSKI
HHHHHCCCHHHHHHH		41.8021815630
117PhosphorylationSFSLEEKSKISKNRV
CCCHHHHHHHCCCCC		38.2025056879
126PhosphorylationISKNRVHYMKFTKGK
HCCCCCEEEEECCCC		10.11-
137O-linked_GlycosylationTKGKDLSSRSKTDLD
CCCCCCCCCCCCHHH		48.1230379171
140AcetylationKDLSSRSKTDLDCIF
CCCCCCCCCHHHHHH		44.9727452117
141PhosphorylationDLSSRSKTDLDCIFG
CCCCCCCCHHHHHHC		42.9428555341
149AcetylationDLDCIFGKRQSKKTP
HHHHHHCCCCCCCCC		36.1925953088
1492-HydroxyisobutyrylationDLDCIFGKRQSKKTP
HHHHHHCCCCCCCCC		36.19-
155PhosphorylationGKRQSKKTPEGDASP
CCCCCCCCCCCCCCC		30.2430576142
161PhosphorylationKTPEGDASPSTPEEN
CCCCCCCCCCCCCCC		24.9125159151
163PhosphorylationPEGDASPSTPEENET
CCCCCCCCCCCCCCC		54.8425159151
164PhosphorylationEGDASPSTPEENETT
CCCCCCCCCCCCCCC		37.8025159151
170PhosphorylationSTPEENETTTTSAFT
CCCCCCCCCCCCCHH		40.8128176443
171PhosphorylationTPEENETTTTSAFTI
CCCCCCCCCCCCHHH		23.1528176443
172PhosphorylationPEENETTTTSAFTIQ
CCCCCCCCCCCHHHH		26.6028464451
173PhosphorylationEENETTTTSAFTIQE
CCCCCCCCCCHHHHH		18.9019690332
174PhosphorylationENETTTTSAFTIQEY
CCCCCCCCCHHHHHH		21.2028450419
177PhosphorylationTTTTSAFTIQEYFAK
CCCCCCHHHHHHHHH		22.8228450419
181PhosphorylationSAFTIQEYFAKRMAA
CCHHHHHHHHHHHHH		7.7728176443
192AcetylationRMAALKNKPQVPVPG
HHHHHCCCCCCCCCC		34.9326051181
192UbiquitinationRMAALKNKPQVPVPG
HHHHHCCCCCCCCCC		34.9324816145
200PhosphorylationPQVPVPGSDISETQV
CCCCCCCCCCCHHHH		26.2120068231
203PhosphorylationPVPGSDISETQVERK
CCCCCCCCHHHHHHH		39.3120873877
205PhosphorylationPGSDISETQVERKRG
CCCCCCHHHHHHHHC		30.9924626860
222AcetylationRNKEATGKDVESYLQ
CCHHHCCCCHHHHHC		55.0026051181
226PhosphorylationATGKDVESYLQPKAK
HCCCCHHHHHCHHHH		30.8720573420
227PhosphorylationTGKDVESYLQPKAKR
CCCCHHHHHCHHHHH		8.8927642862
231SumoylationVESYLQPKAKRHTEG
HHHHHCHHHHHHCCC		54.29-
231SumoylationVESYLQPKAKRHTEG
HHHHHCHHHHHHCCC		54.29-
252UbiquitinationAQERVAKKKSAPAEE
HHHHHHHHCCCCHHH		42.0724816145
252MethylationAQERVAKKKSAPAEE
HHHHHHHHCCCCHHH		42.07116253397
270PhosphorylationGPCWDQSSKASAQDA
CCCCCCCHHCCHHHC		26.97-
273PhosphorylationWDQSSKASAQDAGDH
CCCCHHCCHHHCCCC		30.14-
290PhosphorylationPPEGRDFTLKPKKRR
CCCCCCCCCCCCCCC		37.85-
292UbiquitinationEGRDFTLKPKKRRGK
CCCCCCCCCCCCCCC		52.3024816145
292AcetylationEGRDFTLKPKKRRGK
CCCCCCCCCCCCCCC		52.3026051181
2942-HydroxyisobutyrylationRDFTLKPKKRRGKKK
CCCCCCCCCCCCCCC		58.27-
304AcetylationRGKKKLQKPVEIAED
CCCCCCCCCCHHHCC		62.5626051181
317PhosphorylationEDATLEETLVKKKKK
CCCCHHHHHHHHHCC		27.7220573420
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
110SPhosphorylationKinasePLK1P53350
PSP
117SPhosphorylationKinasePLK1P53350
PSP
141TPhosphorylationKinasePLK1P53350
PSP
226SPhosphorylationKinasePLK1P53350
PSP
317TPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PINX1_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 PINX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCRS1_HUMANMCRS1physical
15044100
PKHJ1_HUMANPLEKHJ1physical
17353931
PABP1_HUMANPABPC1physical
17353931
THIO_HUMANTXNphysical
17353931
RS10_HUMANRPS10physical
17353931
HORN_HUMANHRNRphysical
17353931
RL31_HUMANRPL31physical
17353931
RS3A_HUMANRPS3Aphysical
17353931
RS19_HUMANRPS19physical
17353931
RL23A_HUMANRPL23Aphysical
17353931
NOG1_HUMANGTPBP4physical
17353931
RS28_HUMANRPS28physical
17353931
PABP4_HUMANPABPC4physical
17353931
RS16_HUMANRPS16physical
17353931
SAHH_HUMANAHCYphysical
17353931
CAPR1_HUMANCAPRIN1physical
17353931
TERF1_HUMANTERF1physical
11701125
TERT_HUMANTERTphysical
11701125
AIDA_HUMANAIDAphysical
21900206
DHX15_HUMANDHX15physical
21900206
TERF1_HUMANTERF1physical
19164295
P63_HUMANTP63physical
21988832
ALBU_HUMANALBphysical
26186194
FXR1_HUMANFXR1physical
26186194
FA98A_HUMANFAM98Aphysical
26186194
2ABD_HUMANPPP2R2Dphysical
26186194
TERF1_HUMANTERF1physical
26186194
DHX15_HUMANDHX15physical
24823796
TERF1_HUMANTERF1physical
28514442
FXR1_HUMANFXR1physical
28514442
FA98A_HUMANFAM98Aphysical
28514442
RL8_HUMANRPL8physical
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 PINX1_HUMAN

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Related Literatures of Post-Translational Modification

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