PITX1_HUMAN - dbPTM
PITX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PITX1_HUMAN
UniProt AC P78337
Protein Name Pituitary homeobox 1
Gene Name PITX1
Organism Homo sapiens (Human).
Sequence Length 314
Subcellular Localization Nucleus.
Protein Description Sequence-specific transcription factor that binds gene promoters and activates their transcription. May play a role in the development of anterior structures, and in particular, the brain and facies and in specifying the identity or structure of hindlimb..
Protein Sequence MDAFKGGMSLERLPEGLRPPPPPPHDMGPAFHLARPADPREPLENSASESSDTELPEKERGGEPKGPEDSGAGGTGCGGADDPAKKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSMREEIAVWTNLTEPRVRVWFKNRRAKWRKRERNQQLDLCKGGYVPQFSGLVQPYEDVYAAGYSYNNWAAKSLAPAPLSTKSFTFFNSMSPLSSQSMFSAPSSISSMTMPSSMGPGAVPGMPNSGLNNINNLTGSSLNSAMSPGACPYGTPASPYSVYRDTCNSSLASLRLKSKQHSSFGYGGLQGPASGLNACQYNS
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
1Acetylation-------MDAFKGGM
-------CCCCCCCC		8.2822814378
46PhosphorylationPREPLENSASESSDT
CCCCCCCCCCCCCCC		24.6425463755
48PhosphorylationEPLENSASESSDTEL
CCCCCCCCCCCCCCC		37.5225463755
50PhosphorylationLENSASESSDTELPE
CCCCCCCCCCCCCCH		30.9022617229
51PhosphorylationENSASESSDTELPEK
CCCCCCCCCCCCCHH		44.4925463755
53PhosphorylationSASESSDTELPEKER
CCCCCCCCCCCHHHC		41.1721712546
70PhosphorylationEPKGPEDSGAGGTGC
CCCCCCCCCCCCCCC		28.9625159151
75PhosphorylationEDSGAGGTGCGGADD
CCCCCCCCCCCCCCC		28.5122210691
85AcetylationGGADDPAKKKKQRRQ
CCCCCHHHHHHHHHH		71.2026051181
98PhosphorylationRQRTHFTSQQLQELE
HHHHCCCHHHHHHHH		18.2628555341
160PhosphorylationLDLCKGGYVPQFSGL
CCCCCCCCCCCCCCC		20.02-
175PhosphorylationVQPYEDVYAAGYSYN
CCCHHHHHCCCCCCC		11.76-
179PhosphorylationEDVYAAGYSYNNWAA
HHHHCCCCCCCCCCH		11.85-
188O-linked_GlycosylationYNNWAAKSLAPAPLS
CCCCCHHHCCCCCCC		25.6630059200
188PhosphorylationYNNWAAKSLAPAPLS
CCCCCHHHCCCCCCC		25.6628555341
195PhosphorylationSLAPAPLSTKSFTFF
HCCCCCCCCCCEEEC		32.5028555341
196PhosphorylationLAPAPLSTKSFTFFN
CCCCCCCCCCEEECC		38.0928555341
281PhosphorylationYRDTCNSSLASLRLK
HHHCCCCCHHHHHHC		17.6023186163
284PhosphorylationTCNSSLASLRLKSKQ
CCCCCHHHHHHCCCC		21.2226434776
290UbiquitinationASLRLKSKQHSSFGY
HHHHHCCCCCCCCCC		50.90-
293PhosphorylationRLKSKQHSSFGYGGL
HHCCCCCCCCCCCCC		25.5220068231
294PhosphorylationLKSKQHSSFGYGGLQ
HCCCCCCCCCCCCCC		22.1420068231
297PhosphorylationKQHSSFGYGGLQGPA
CCCCCCCCCCCCCCC		13.1520068231
305PhosphorylationGGLQGPASGLNACQY
CCCCCCCCCCCCCCC		47.1220068231
312PhosphorylationSGLNACQYNS-----
CCCCCCCCCC-----		19.7720068231
314PhosphorylationLNACQYNS-------
CCCCCCCC-------		36.3420068231
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 PITX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PITX1_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 PITX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBPMS_HUMANRBPMSphysical
16189514
RHXF2_HUMANRHOXF2physical
16189514
PIT1_HUMANPOU1F1physical
8755540
SMCA2_HUMANSMARCA2physical
17043312
RBPMS_HUMANRBPMSphysical
24722188
ALG13_HUMANALG13physical
24722188
CA094_HUMANC1orf94physical
24722188
CDX4_HUMANCDX4physical
24722188
HGS_HUMANHGSphysical
24722188
IPO13_HUMANIPO13physical
24722188
LZTS2_HUMANLZTS2physical
24722188
MAGD1_HUMANMAGED1physical
24722188
MGT5B_HUMANMGAT5Bphysical
24722188
PLS1_HUMANPLSCR1physical
24722188
PR20E_HUMANPRR20Aphysical
24722188
PR20C_HUMANPRR20Aphysical
24722188
PR20D_HUMANPRR20Aphysical
24722188
PR20B_HUMANPRR20Aphysical
24722188
PR20A_HUMANPRR20Aphysical
24722188
RFX6_HUMANRFX6physical
24722188
RNF31_HUMANRNF31physical
24722188
SPAG8_HUMANSPAG8physical
24722188
TRI23_HUMANTRIM23physical
24722188
ZBT32_HUMANZBTB32physical
24722188
RBPMS_HUMANRBPMSphysical
25416956
TPC2A_HUMANTRAPPC2physical
20498720
TPC2B_HUMANTRAPPC2physical
20498720
FOXO1_HUMANFOXO1physical
24065703
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
119800Clubfoot, congenital, with or without deficiency of long bones and/or mirror-image polydactyly (CCF)
186550Liebenberg syndrome (LBNBG)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PITX1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-48 AND SER-50,AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-50; SER-51 ANDTHR-53, AND MASS SPECTROMETRY.

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