| General information | | DisProt: | DP00574 | | Name: | Serum response factor | | Synonym(s): | SRF_HUMAN
SRF
| | First appeared in release: | Release 4.5 (07/17/2008) | | UniProt: | P11831 | | UniGene: | Hs.520140 | | SwissProt: | SRF_HUMAN | | TrEMBL: | | | NCBI (GI): | 134876 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 508 | | Percent disordered: | 9% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MLPTQAGAAA ALGRGSALGG SLNRTPTGRP GGGGGTRGAN GGRVPGNGAG LGPGRLEREA - 60
AAAAATTPAP TAGALYSGSE GDSESGEEEE LGAERRGLKR SLSEMEIGMV VGGPEASAAA - 120
TGGYGPVSGA VSGAKPGKKT RGRVKIKMEF IDNKLRRYTT FSKRKTGIMK KAYELSTLTG - 180
TQVLLLVASE TGHVYTFATR KLQPMITSET GKALIQTCLN SPDSPPRSDP TTDQRMSATG - 240
FEETDLTYQV SESDSSGETK DTLKPAFTVT NLPGTTSTIQ TAPSTSTTMQ VSSGPSFPIT - 300
NYLAPVSASV SPSAVSSANG TVLKSTGSGP VSSGGLMQLP TSFTLMPGGA VAQQVPVQAI - 360
QVHQAPQQAS PSRDSSTDLT QTSSSGTVTL PATIMTSSVP TTVGGHMMYP SPHAVMYAPT - 420
SGLGDGSLTV LNAFSQAPST MQVSHSQVQE PGGVPQVFLT ASSGTVQIPV SAVQLHQMAV - 480
IGQQAGSSSN LTELQVVNLD TAHSTKSE
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| Functional narrative |
SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Required for cardiac differentiation and maturation.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 93 - 137 | | Length: | 45 | | Region sequence: |
AERRGLKRSLSEMEIGMVVGGPEASAAATGGYGPVSGAVSGAKPG | | Modification type: | Native
| | PDB: | 1HBX:A, 1K6O:A, 1SRS:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Modification site
Molecular assembly
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
| References:
There are no documents referencing this region. | Comments:
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| References |
- Hassler M, Richmond TJ. "The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex." Embo J. 2001; 20(12): 3018-28. PubMed: 11406578
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