| General information | | DisProt: | DP00091 | | Name: | DNA repair protein complementing XP-A cells homolog | | Synonym(s): | XPA_XENLA
Xeroderma pigmentosum group A-complementing protein homolog
DNA repair protein XPAC
| | First appeared in release: | Release 2.0 (02/14/2005) | | UniProt: | P27088 | | UniGene: | Xl.902 | | SwissProt: | XPA_XENLA | | TrEMBL: | | | NCBI (GI): | 139817 | | Source organism: | Xenopus laevis (African clawed frog) | | Sequence length: | 267 | | Percent disordered: | 63% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MEPEPEPEQE ANKEEEKILS AAVRAKIERN RQRALMLRQA RLACRPYPTG EGISTVKAPP - 60
KVIDSGGGFF IEEEEAEEQH VENVVRQPGP VLECDYLICE ECGKDFMDSY LSNHFDLAVC - 120
DSCRDAEEKH KLITRTEAKQ EYLLKDCDID KREPVLKFIL KKNPHNTHWG DMKLYLKAQV - 180
IKRSLEVWGS EEALEEAKEV RKDNRDKMKQ KKFDKKVKEL RRTVRSSLWK KEASGHQHEY - 240
GPEEHVEEDS YKKTCITCGY EMNYEKM
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| Functional narrative |
This protein is involved in DNA- excision repair by recognizing large abnormalities during DNA repair. It is a member of the XPA family and is located in the nuclear region of cells.
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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 - Extended | | Name: | | | Location: | 1 - 84 | | Length: | 84 | | Region sequence: |
MEPEPEPEQEANKEEEKILSAAVRAKIERNRQRALMLRQARLACRPYPTGEGISTVKAPP
KVIDSGGGFFIEEEEAEEQHVENV | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Sensitivity to proteolysis (310 K; pH: 7.5; Hepes-KOH 25 mM; KCl 100 mM; trypsin (Second Concentration) 0.05 %; trypsin (First Concentration) 0.5 %)
- ESI-FTICR mass spectrometry (433 K; )
| References:
- Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ. "Identification of intrinsic order and disorder in the DNA repair protein XPA." Protein Sci. 2001; 10(3): 560-71. PubMed: 11344324
| Comments:The results from the laboratory experiments were compared to PONDR predictions and found to be identical.
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| Region 2 | | Type: | Disordered - Extended | | Name: | | | Location: | 181 - 265 | | Length: | 85 | | Region sequence: |
IKRSLEVWGSEEALEEAKEVRKDNRDKMKQKKFDKKVKELRRTVRSSLWKKEASGHQHEY
GPEEHVEEDSYKKTCITCGYEMNYE | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Sensitivity to proteolysis (310 K; pH: 7.5; Hepes-KOH 25 mM; KCl 100 mM; trypsin (First Concentration) 0.5 %; trypsin (Second Concentration) 0.05 %)
- ESI-FTICR mass spectrometry (433 K; )
| References:
- Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ. "Identification of intrinsic order and disorder in the DNA repair protein XPA." Protein Sci. 2001; 10(3): 560-71. PubMed: 11344324
| Comments:The results from the laboratory experiments were compared to PONDR predictions and found to be identical.
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