HMGA1_RAT - dbPTM
HMGA1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HMGA1_RAT
UniProt AC Q8K585
Protein Name High mobility group protein HMG-I/HMG-Y
Gene Name Hmga1
Organism Rattus norvegicus (Rat).
Sequence Length 107
Subcellular Localization Nucleus. Chromosome.
Protein Description HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions (By similarity)..
Protein Sequence MSESVSKSSQPLASKQEKDGTEKRGRGRPRKQPSVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGTAKTRKVTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ
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------MSESVSKSS
------CCCCCCCCC
38.2827097102
2Acetylation------MSESVSKSS
------CCCCCCCCC
38.28-
4Phosphorylation----MSESVSKSSQP
----CCCCCCCCCCC
25.1227097102
6Phosphorylation--MSESVSKSSQPLA
--CCCCCCCCCCCCC
35.7823984901
7Acetylation-MSESVSKSSQPLAS
-CCCCCCCCCCCCCC
52.5522902405
8ADP-ribosylationMSESVSKSSQPLASK
CCCCCCCCCCCCCCH
27.05-
8PhosphorylationMSESVSKSSQPLASK
CCCCCCCCCCCCCCH
27.0523984901
9PhosphorylationSESVSKSSQPLASKQ
CCCCCCCCCCCCCHH
39.2823984901
9ADP-ribosylationSESVSKSSQPLASKQ
CCCCCCCCCCCCCHH
39.28-
15AcetylationSSQPLASKQEKDGTE
CCCCCCCHHCCCCCC
57.7925786129
18AcetylationPLASKQEKDGTEKRG
CCCCHHCCCCCCCCC
59.9922902405
26MethylationDGTEKRGRGRPRKQP
CCCCCCCCCCCCCCC
41.82-
26Asymmetric dimethylarginineDGTEKRGRGRPRKQP
CCCCCCCCCCCCCCC
41.82-
34 (in isoform 2)Phosphorylation-32.5027097102
34PhosphorylationGRPRKQPSVSPGTAL
CCCCCCCCCCCCCCC
32.5027097102
35 (in isoform 2)Acetylation-11.58-
36PhosphorylationPRKQPSVSPGTALVG
CCCCCCCCCCCCCCC
23.1927097102
38 (in isoform 2)Phosphorylation-19.0023984901
39PhosphorylationQPSVSPGTALVGSQK
CCCCCCCCCCCCCCC
21.8727097102
42 (in isoform 2)Phosphorylation-6.8628432305
44PhosphorylationPGTALVGSQKEPSEV
CCCCCCCCCCCCCCC
30.5127097102
49PhosphorylationVGSQKEPSEVPTPKR
CCCCCCCCCCCCCCC
52.9328432305
53PhosphorylationKEPSEVPTPKRPRGR
CCCCCCCCCCCCCCC
46.7727097102
58MethylationVPTPKRPRGRPKGSK
CCCCCCCCCCCCCCC
58.76-
58Asymmetric dimethylarginineVPTPKRPRGRPKGSK
CCCCCCCCCCCCCCC
58.76-
60MethylationTPKRPRGRPKGSKNK
CCCCCCCCCCCCCCC
30.91-
60Asymmetric dimethylarginineTPKRPRGRPKGSKNK
CCCCCCCCCCCCCCC
30.91-
64PhosphorylationPRGRPKGSKNKGTAK
CCCCCCCCCCCCCCC
38.9022817900
78PhosphorylationKTRKVTTTPGRKPRG
CEEEEECCCCCCCCC
17.8722817900
99PhosphorylationKEEEEGISQESSEEE
HHHHCCCCCCCHHHC
38.4623712012
102PhosphorylationEEGISQESSEEEQ--
HCCCCCCCHHHCC--
35.1023712012
103PhosphorylationEGISQESSEEEQ---
CCCCCCCHHHCC---
48.5523712012

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
36SPhosphorylationKinaseCDC2P39951
Uniprot
36SPhosphorylationKinaseHIPK2-Uniprot
44SPhosphorylationKinasePRKCAP17252
GPS
44SPhosphorylationKinasePRKCBP05771
GPS
44SPhosphorylationKinasePRKCDQ05655
GPS
44SPhosphorylationKinasePRKCGP05129
GPS
53TPhosphorylationKinaseCDK1P06493
PSP
53TPhosphorylationKinaseCDC2P39951
Uniprot
53TPhosphorylationKinaseHIPK2-Uniprot
64SPhosphorylationKinasePRKCAP17252
GPS
64SPhosphorylationKinasePRKCBP05771
GPS
64SPhosphorylationKinasePRKCDQ05655
GPS
64SPhosphorylationKinasePRKCGP05129
GPS
78TPhosphorylationKinaseCDK1P06493
PSP
78TPhosphorylationKinaseCDC2P39951
Uniprot
78TPhosphorylationKinaseHIPK2-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
58RMethylation

-
60RMethylation

-

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 HMGA1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HMGA1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HMGA1_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, AND MASSSPECTROMETRY.

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