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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSESVSKSS ------CCCCCCCCC | 38.28 | 27097102 | |
2 | Acetylation | ------MSESVSKSS ------CCCCCCCCC | 38.28 | - | |
4 | Phosphorylation | ----MSESVSKSSQP ----CCCCCCCCCCC | 25.12 | 27097102 | |
6 | Phosphorylation | --MSESVSKSSQPLA --CCCCCCCCCCCCC | 35.78 | 23984901 | |
7 | Acetylation | -MSESVSKSSQPLAS -CCCCCCCCCCCCCC | 52.55 | 22902405 | |
8 | ADP-ribosylation | MSESVSKSSQPLASK CCCCCCCCCCCCCCH | 27.05 | - | |
8 | Phosphorylation | MSESVSKSSQPLASK CCCCCCCCCCCCCCH | 27.05 | 23984901 | |
9 | Phosphorylation | SESVSKSSQPLASKQ CCCCCCCCCCCCCHH | 39.28 | 23984901 | |
9 | ADP-ribosylation | SESVSKSSQPLASKQ CCCCCCCCCCCCCHH | 39.28 | - | |
15 | Acetylation | SSQPLASKQEKDGTE CCCCCCCHHCCCCCC | 57.79 | 25786129 | |
18 | Acetylation | PLASKQEKDGTEKRG CCCCHHCCCCCCCCC | 59.99 | 22902405 | |
26 | Methylation | DGTEKRGRGRPRKQP CCCCCCCCCCCCCCC | 41.82 | - | |
26 | Asymmetric dimethylarginine | DGTEKRGRGRPRKQP CCCCCCCCCCCCCCC | 41.82 | - | |
34 (in isoform 2) | Phosphorylation | - | 32.50 | 27097102 | |
34 | Phosphorylation | GRPRKQPSVSPGTAL CCCCCCCCCCCCCCC | 32.50 | 27097102 | |
35 (in isoform 2) | Acetylation | - | 11.58 | - | |
36 | Phosphorylation | PRKQPSVSPGTALVG CCCCCCCCCCCCCCC | 23.19 | 27097102 | |
38 (in isoform 2) | Phosphorylation | - | 19.00 | 23984901 | |
39 | Phosphorylation | QPSVSPGTALVGSQK CCCCCCCCCCCCCCC | 21.87 | 27097102 | |
42 (in isoform 2) | Phosphorylation | - | 6.86 | 28432305 | |
44 | Phosphorylation | PGTALVGSQKEPSEV CCCCCCCCCCCCCCC | 30.51 | 27097102 | |
49 | Phosphorylation | VGSQKEPSEVPTPKR CCCCCCCCCCCCCCC | 52.93 | 28432305 | |
53 | Phosphorylation | KEPSEVPTPKRPRGR CCCCCCCCCCCCCCC | 46.77 | 27097102 | |
58 | Methylation | VPTPKRPRGRPKGSK CCCCCCCCCCCCCCC | 58.76 | - | |
58 | Asymmetric dimethylarginine | VPTPKRPRGRPKGSK CCCCCCCCCCCCCCC | 58.76 | - | |
60 | Methylation | TPKRPRGRPKGSKNK CCCCCCCCCCCCCCC | 30.91 | - | |
60 | Asymmetric dimethylarginine | TPKRPRGRPKGSKNK CCCCCCCCCCCCCCC | 30.91 | - | |
64 | Phosphorylation | PRGRPKGSKNKGTAK CCCCCCCCCCCCCCC | 38.90 | 22817900 | |
78 | Phosphorylation | KTRKVTTTPGRKPRG CEEEEECCCCCCCCC | 17.87 | 22817900 | |
99 | Phosphorylation | KEEEEGISQESSEEE HHHHCCCCCCCHHHC | 38.46 | 23712012 | |
102 | Phosphorylation | EEGISQESSEEEQ-- HCCCCCCCHHHCC-- | 35.10 | 23712012 | |
103 | Phosphorylation | EGISQESSEEEQ--- CCCCCCCHHHCC--- | 48.55 | 23712012 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
36 | S | Phosphorylation | Kinase | CDC2 | P39951 | Uniprot |
36 | S | Phosphorylation | Kinase | HIPK2 | - | Uniprot |
44 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
44 | S | Phosphorylation | Kinase | PRKCB | P05771 | GPS |
44 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
44 | S | Phosphorylation | Kinase | PRKCG | P05129 | GPS |
53 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
53 | T | Phosphorylation | Kinase | CDC2 | P39951 | Uniprot |
53 | T | Phosphorylation | Kinase | HIPK2 | - | Uniprot |
64 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
64 | S | Phosphorylation | Kinase | PRKCB | P05771 | GPS |
64 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
64 | S | Phosphorylation | Kinase | PRKCG | P05129 | GPS |
78 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
78 | T | Phosphorylation | Kinase | CDC2 | P39951 | Uniprot |
78 | T | Phosphorylation | Kinase | HIPK2 | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
58 | R | Methylation |
| - |
60 | R | Methylation |
| - |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of HMGA1_RAT !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |