IFIX_HUMAN - dbPTM
IFIX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFIX_HUMAN
UniProt AC Q6K0P9
Protein Name Pyrin and HIN domain-containing protein 1
Gene Name PYHIN1
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Isoform 1: Nucleus, nucleoplasm.
Isoform 3: Nucleus, nucleoplasm.
Isoform 5: Nucleus. Nucleus speckle.
Protein Description Major mediator of the tumor suppressor activity of IFN in breast cancer cells. Promotes ubiquitination and subsequent degradation of MDM2, which leads to p53/TP53 stabilization. Promotes ubiquitination and subsequent degradation of HDAC1, which in turn enhances maspin expression, and impairs invasive activity of cancer cells..
Protein Sequence MANNYKKIVLLKGLEVINDYHFRIVKSLLSNDLKLNPKMKEEYDKIQIADLMEEKFPGDAGLGKLIEFFKEIPTLGDLAETLKREKLKVANKIESIPVKGIIPSKKTKQKEVYPATPACTPSNRLTAKGAEETLGPQKRKKPSEEETGTKRSKMSKEQTRPSCSAGASTSTAMGRSPPPQTSSSAPPNTSSTESLKPLANRHATASKNIFREDPIIAMVLNATKVFKYESSENEQRRMFHATVATQTQFFHVKVLNINLKRKFIKKRIIIISNYSKRNSLLEVNEASSVSEAGPDQTFEVPKDIIRRAKKIPKINILHKQTSGYIVYGLFMLHTKIVNRKTTIYEIQDKTGSMAVVGKGECHNIPCEKGDKLRLFCFRLRKRENMSKLMSEMHSFIQIQKNTNQRSHDSRSMALPQEQSQHPKPSEASTTLPESHLKTPQMPPTTPSSSSFTKKDETHPGAQSSPANFRITSPTVAPPLSSDTSTNRHPAVP
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
5Phosphorylation---MANNYKKIVLLK
---CCCCCCEEEEEE
17.2919835603
20PhosphorylationGLEVINDYHFRIVKS
CCEEECHHHHHHHHH
9.81-
40AcetylationLKLNPKMKEEYDKIQ
CCCCHHHHHHHHHHC
54.2220167786
45AcetylationKMKEEYDKIQIADLM
HHHHHHHHHCHHHHH
35.2920167786
104PhosphorylationPVKGIIPSKKTKQKE
CCCCCCCCCCCCCCC
36.0524719451
143PhosphorylationPQKRKKPSEEETGTK
CCCCCCCCHHHHCCC
67.5328060719
176PhosphorylationTSTAMGRSPPPQTSS
CCCCCCCCCCCCCCC
35.7130108239
181PhosphorylationGRSPPPQTSSSAPPN
CCCCCCCCCCCCCCC
36.0330108239
198UbiquitinationSTESLKPLANRHATA
CCCCHHHHHHCCCCC
6.7029967540
207UbiquitinationNRHATASKNIFREDP
HCCCCCCCCCCCCCC
52.1529967540
228PhosphorylationNATKVFKYESSENEQ
CCEEEEEECCCHHHH
15.02-
247PhosphorylationHATVATQTQFFHVKV
EEEECCCCCEEEEEE
24.00-
321PhosphorylationINILHKQTSGYIVYG
CCEEECCCCCCCEEE
28.9924719451
386PhosphorylationLRKRENMSKLMSEMH
HHHHHCHHHHHHHHH
33.93-
390PhosphorylationENMSKLMSEMHSFIQ
HCHHHHHHHHHHHHH
42.05-
425PhosphorylationQSQHPKPSEASTTLP
HHCCCCCCCCCCCCC
52.5022673903
428PhosphorylationHPKPSEASTTLPESH
CCCCCCCCCCCCHHH
20.2022673903
429PhosphorylationPKPSEASTTLPESHL
CCCCCCCCCCCHHHC
39.1222673903
430PhosphorylationKPSEASTTLPESHLK
CCCCCCCCCCHHHCC
37.5122673903
434PhosphorylationASTTLPESHLKTPQM
CCCCCCHHHCCCCCC
31.9822673903
438 (in isoform 4)Phosphorylation-25.72-
447 (in isoform 3)Phosphorylation-40.54-
450PhosphorylationPTTPSSSSFTKKDET
CCCCCCCCCCCCCCC
38.5924719451
453UbiquitinationPSSSSFTKKDETHPG
CCCCCCCCCCCCCCC
57.10-
454UbiquitinationSSSSFTKKDETHPGA
CCCCCCCCCCCCCCC
58.71-
463PhosphorylationETHPGAQSSPANFRI
CCCCCCCCCCCEEEE
37.4429978859
464PhosphorylationTHPGAQSSPANFRIT
CCCCCCCCCCEEEEC
18.8929978859

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 IFIX_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFIX_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 IFIX_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDM2_HUMANMDM2physical
16479015
TRI26_HUMANTRIM26physical
26186194
SPB5_HUMANSERPINB5physical
26186194
CALL3_HUMANCALML3physical
26186194
DCAF1_HUMANVPRBPphysical
26186194
LYG2_HUMANLYG2physical
26186194
S10A3_HUMANS100A3physical
26186194
PLCD1_HUMANPLCD1physical
26186194
LRC15_HUMANLRRC15physical
26186194
HPHL1_HUMANHEPHL1physical
26186194
LEG3_HUMANLGALS3physical
26186194
DSG4_HUMANDSG4physical
26186194
NEUR2_HUMANNEU2physical
26186194
CRBG1_HUMANAIM1physical
26186194
FA26D_HUMANFAM26Dphysical
26186194
PADI3_HUMANPADI3physical
26186194
MDM2_HUMANMDM2physical
26186194
TRI26_HUMANTRIM26physical
28514442
PADI3_HUMANPADI3physical
28514442
FA26D_HUMANFAM26Dphysical
28514442
LYG2_HUMANLYG2physical
28514442
CRBG1_HUMANAIM1physical
28514442
DSG4_HUMANDSG4physical
28514442
HPHL1_HUMANHEPHL1physical
28514442
PLCD1_HUMANPLCD1physical
28514442
S10A3_HUMANS100A3physical
28514442
LRC15_HUMANLRRC15physical
28514442
NEUR2_HUMANNEU2physical
28514442
CALL3_HUMANCALML3physical
28514442
DCAF1_HUMANVPRBPphysical
28514442
DUS14_HUMANDUSP14physical
28514442
LEG3_HUMANLGALS3physical
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 IFIX_HUMAN

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Related Literatures of Post-Translational Modification

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