PPIH_HUMAN - dbPTM
PPIH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIH_HUMAN
UniProt AC O43447
Protein Name Peptidyl-prolyl cis-trans isomerase H
Gene Name PPIH
Organism Homo sapiens (Human).
Sequence Length 177
Subcellular Localization Nucleus speckle . Cytoplasm . Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.
Protein Description PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. [PubMed: 20676357 Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone.]
Protein Sequence MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGVASIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVISQCGEM
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
2Acetylation------MAVANSSPV
------CCCCCCCCC		14.7725944712
6Phosphorylation--MAVANSSPVNPVV
--CCCCCCCCCCCEE		26.7028464451
7Phosphorylation-MAVANSSPVNPVVF
-CCCCCCCCCCCEEE		32.4528464451
10UbiquitinationVANSSPVNPVVFFDV
CCCCCCCCCEEEEEE		27.34-
18UbiquitinationPVVFFDVSIGGQEVG
CEEEEEEEECCEEEC		19.8421890473
27UbiquitinationGGQEVGRMKIELFAD
CCEEECCEEEEEEEE		4.16-
28UbiquitinationGQEVGRMKIELFADV
CEEECCEEEEEEEEE		31.50-
38AcetylationLFADVVPKTAENFRQ
EEEEECHHHHHHHHH		49.0825825284
38SuccinylationLFADVVPKTAENFRQ
EEEEECHHHHHHHHH		49.0827452117
38SumoylationLFADVVPKTAENFRQ
EEEEECHHHHHHHHH		49.08-
38UbiquitinationLFADVVPKTAENFRQ
EEEEECHHHHHHHHH		49.08-
38SumoylationLFADVVPKTAENFRQ
EEEEECHHHHHHHHH		49.08-
44MethylationPKTAENFRQFCTGEF
HHHHHHHHHHHCCCC		40.00115488339
52MethylationQFCTGEFRKDGVPIG
HHHCCCCCCCCCEEC		31.67115488333
53UbiquitinationFCTGEFRKDGVPIGY
HHCCCCCCCCCEECC		65.24-
58UbiquitinationFRKDGVPIGYKGSTF
CCCCCCEECCCCCHH		9.7721890473
58AcetylationFRKDGVPIGYKGSTF
CCCCCCEECCCCCHH		9.77-
60PhosphorylationKDGVPIGYKGSTFHR
CCCCEECCCCCHHHH		16.9420873877
61UbiquitinationDGVPIGYKGSTFHRV
CCCEECCCCCHHHHH		40.9721906983
61AcetylationDGVPIGYKGSTFHRV
CCCEECCCCCHHHHH		40.9725953088
63PhosphorylationVPIGYKGSTFHRVIK
CEECCCCCHHHHHHH		24.6120873877
64PhosphorylationPIGYKGSTFHRVIKD
EECCCCCHHHHHHHH		31.9320873877
70UbiquitinationSTFHRVIKDFMIQGG
CHHHHHHHHHEEECC		41.9021906983
85PhosphorylationDFVNGDGTGVASIYR
CCCCCCCCCEEEEEE		32.9722468782
89PhosphorylationGDGTGVASIYRGPFA
CCCCCEEEEEECCCC		20.1122468782
94UbiquitinationVASIYRGPFADENFK
EEEEEECCCCCCCCE		16.56-
100UbiquitinationGPFADENFKLRHSAP
CCCCCCCCEECCCCC		8.09-
101UbiquitinationPFADENFKLRHSAPG
CCCCCCCEECCCCCC		57.0821890473
101AcetylationPFADENFKLRHSAPG
CCCCCCCEECCCCCC		57.0823954790
110UbiquitinationRHSAPGLLSMANSGP
CCCCCCHHHHCCCCC		4.00-
118PhosphorylationSMANSGPSTNGCQFF
HHCCCCCCCCCCCEE		37.7222210691
119PhosphorylationMANSGPSTNGCQFFI
HCCCCCCCCCCCEEE		38.4722210691
121UbiquitinationNSGPSTNGCQFFITC
CCCCCCCCCCEEEEE		13.49-
131S-nitrosylationFFITCSKCDWLDGKH
EEEEECCCCCCCCCC		2.3319483679
131S-nitrosocysteineFFITCSKCDWLDGKH
EEEEECCCCCCCCCC		2.33-
137AcetylationKCDWLDGKHVVFGKI
CCCCCCCCCEEEEEE		32.6626051181
137UbiquitinationKCDWLDGKHVVFGKI
CCCCCCCCCEEEEEE		32.66-
143UbiquitinationGKHVVFGKIIDGLLV
CCCEEEEEEECCCEE		25.64-
153UbiquitinationDGLLVMRKIENVPTG
CCCEEEEEEECCCCC		35.9521906983
153AcetylationDGLLVMRKIENVPTG
CCCEEEEEEECCCCC		35.9526051181
159PhosphorylationRKIENVPTGPNNKPK
EEEECCCCCCCCCCC		62.0726657352
164UbiquitinationVPTGPNNKPKLPVVI
CCCCCCCCCCCCEEE		50.612190698
166AcetylationTGPNNKPKLPVVISQ
CCCCCCCCCCEEEEE		68.0126051181
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 PPIH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIH_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 PPIH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NH2L1_HUMANNHP2L1physical
16723661
PPIH_HUMANPPIHphysical
16723661
PRPF3_HUMANPRPF3physical
16723661
PRP4_HUMANPRPF4physical
16723661
PRP31_HUMANPRPF31physical
16723661
PRP4_HUMANPRPF4physical
22939629
PRP4_HUMANPRPF4physical
22365833
BAG2_HUMANBAG2physical
22365833
ITPA_HUMANITPAphysical
26344197
PRPF3_HUMANPRPF3physical
27173435
PRP4_HUMANPRPF4physical
27173435
LSM8_HUMANLSM8physical
27173435
THOC4_HUMANALYREFphysical
27173435
SART3_HUMANSART3physical
27173435
LSM4_HUMANLSM4physical
27173435
LSM6_HUMANLSM6physical
27173435
RL26L_HUMANRPL26L1physical
27173435
OLA1_HUMANOLA1physical
27173435
RL32_HUMANRPL32physical
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
DB00172L-Proline
Regulatory Network of PPIH_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-38, AND MASS SPECTROMETRY.

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