DP00153: GTPase HRasFASTA viewXML view

General information
DisProt:DP00153
Name:GTPase HRas
Synonym(s):RASH_HUMAN
Transforming protein p21
p21ras
H-Ras-1
c-H-ras
Ha-Ras
GTPase HRas, N-terminally processed [cleavage product 1]
First appeared in release:Release 1.1 (12/01/2003)
UniProt:P01112
UniGene:Hs.37003
SwissProt: RASH_HUMAN
TrEMBL:  
NCBI (GI): 131869
Source organism:Homo sapiens (Human)
Sequence length:189
Percent disordered:33%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG - 60
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL - 120
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG - 180
CMSCKCVLS



Functional narrative    

Hras, a member of the ras GTPase family, is a regulator of the RAS protein signal transduction pathway. It functions as a switch that contributes the regulation of cellular growth and differentiation by interacting with and hydrolyzing GTP. Once bound to a molecule of GTP, Hras is indirectly influenced by GTPase activating proteins (GAPS), and GTPase, which hydrolyzes GTP. GDP is then released by Hras due to its interaction with guanine nucleotide exchange factors (GEFs). When inactive, Hras can be found in the cytosol. However, when activated, Hras will migrate toward the golgi apparatus or plasma membrane of the cell. The disordered regions of Hras each interact with various proteins, including GTP, by altering their conformation in order to accommodate the interacting molecule.

Region 1: 10-13 Region 2: 10-16 Region 3: 21-21 Region 4: 27-32 Region 5: 30-38 Region 7: 32-38 Region 6: 31-39 Region 8: 32-40 Region 9: 57-61 Region 10: 57-64 Region 13: 60-64 Region 15: 61-65 Region 16: 62-65 Region 11: 58-66 Region 14: 60-68 Region 17: 71-71 Region 12: 59-72 Region 18: 107-109 Region 19: 168-189 Region 20: 172-189

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.


Region 1
Type:Disordered - Extended
Name: 
Location:10 - 13
Length:4
Region sequence:

GAGG

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM; MgCl2 10 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 2
Type:Disordered - Extended
Name: 
Location:10 - 16
Length:7
Region sequence:

GAGGVGK

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 3
Type:Disordered
Name: 
Location:21 - 21
Length:1
Region sequence:

I

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM; MgCl2 10 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 4
Type:Disordered
Name: 
Location:27 - 32
Length:6
Region sequence:

HFVDEY

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM; MgCl2 10 mM)

  2. Nuclear magnetic resonance (NMR) (303 K; D2O 10 %; DTT 5 mM; GDP 30 µM; H2O 90 %; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 (pH 6.5) 20 mM)

  3. Nuclear magnetic resonance (NMR) (303 K; D2O 100 %; DTT 5 mM; GDP 30 µM; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 (pH 6.5) 20 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043

  2. Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED. "Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy." Biochemistry. 1994; 33(12): 3515-3531. PubMed: 8142349
Comments:
 



Region 5
Type:Disordered
Name: 
Location:30 - 38
Length:9
Region sequence:

DEYDPTIED

Modification type: Complex
Engineered
Fragment
PDB: 1CRP:A, 1CRQ:A, 1CRR:A, 1Q21:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Nuclear magnetic resonance (NMR) (303 K; pH: 6.5; D2O 10 %; DTT 5 mM; GDP 30 µM; H2O 90 %; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 20 mM)

  2. Nuclear magnetic resonance (NMR) (303 K; pH: 6.5; D2O 100 %; DTT 5 mM; GDP 30 µM; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 20 mM)

  3. X-ray crystallography
References:
  1. Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED. "Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy." Biochemistry. 1994; 33(12): 3515-3531. PubMed: 8142349

  2. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Region 6
Type:Disordered
Name: 
Location:31 - 39
Length:9
Region sequence:

EYDPTIEDS

Modification type: Complex
Engineered
Fragment
PDB: 1AA9:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 7
Type:Disordered
Name: 
Location:32 - 38
Length:7
Region sequence:

YDPTIED

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (298 K; 1,6-hexanediol 60 %; 2,2,2-trifluoroethanol 50 %; isopropanol 50 %)
References:
  1. Buhrman G, de Serrano V, Mattos C. "Organic solvents order the dynamic switch II in Ras crystals." Structure. 2003; 11(7): 747-51. PubMed: 12842038
Comments:
 



Region 8
Type:Disordered
Name: 
Location:32 - 40
Length:9
Region sequence:

YDPTIEDSY

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 9
Type:Disordered
Name: 
Location:57 - 61
Length:5
Region sequence:

DTAGQ

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 10
Type:Disordered
Name: 
Location:57 - 64
Length:8
Region sequence:

DTAGQEEY

Modification type: Complex
Engineered
Fragment
PDB: 1AA9:A, 1IOZ:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 11
Type:Disordered
Name: 
Location:58 - 66
Length:9
Region sequence:

TAGQEEYSA

Modification type: Complex
Engineered
Fragment
PDB: 1AA9:A, 1CRP:A, 1CRQ:A, 1CRR:A, 1IOZ:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (303 K; D2O 10 %; DTT 5 mM; GDP 30 µM; H2O 90 %; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 (pH 6.5) 20 mM)

  2. Nuclear magnetic resonance (NMR) (303 K; pH: 5.5; D2O 100 %; DTT 5 mM; GDP 30 µM; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 (pH 6.5) 20 mM)

  3. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2-HPO4-NaH2PO4 20 mM; NaCl 150 mM)

  4. X-ray crystallography
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043

  2. Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED. "Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy." Biochemistry. 1994; 33(12): 3515-3531. PubMed: 8142349

  3. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Region 12
Type:Disordered
Name: 
Location:59 - 72
Length:14
Region sequence:

AGQEEYSAMRDQYM

Modification type: Complex
Engineered
Fragment
PDB: 121P:A, 1P2U:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (298 K; 1,6-hexanediol 60 %; 2,2,2-trifluoroethanol 50 %; isopropanol 50 %)
References:
  1. Buhrman G, de Serrano V, Mattos C. "Organic solvents order the dynamic switch II in Ras crystals." Structure. 2003; 11(7): 747-51. PubMed: 12842038
Comments:
 



Region 13
Type:Disordered
Name: 
Location:60 - 64
Length:5
Region sequence:

GQEEY

Modification type: Complex
Engineered
Fragment
PDB: 4Q21:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography
References:
  1. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Region 14
Type:Disordered
Name: 
Location:60 - 68
Length:9
Region sequence:

GQEEYSAMR

Modification type: Complex
Engineered
Fragment
PDB: 1Q21:A, 6Q21:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography
References:
  1. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Region 15
Type:Disordered
Name: 
Location:61 - 65
Length:5
Region sequence:

QEEYS

Modification type: Complex
Engineered
Fragment
PDB: 1Q21:A, 6Q21:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography
References:
  1. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Region 16
Type:Disordered
Name: 
Location:62 - 65
Length:4
Region sequence:

EEYS

Modification type: Complex
Engineered
Fragment
PDB: 1Q21:A, 6Q21:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography
References:
  1. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Region 17
Type:Disordered
Name: 
Location:71 - 71
Length:1
Region sequence:

Y

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2HPO4-NaH2PO4 20 mM; NaCl 150 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043
Comments:
 



Region 18
Type:Disordered
Name: 
Location:107 - 109
Length:3
Region sequence:

DDV

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (303 K; pH: 6.5; D2O 10 %; DTT 5 mM; GDP 30 µM; H2O 90 %; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 20 mM)

  2. Nuclear magnetic resonance (NMR) (303 K; pH: 6.5; D2O 100 %; DTT 5 mM; GDP 30 µM; MgCl2 5 mM; NaCl 40 mM; sodium azide 0.01 %; Tris-maleate-d15 20 mM)

  3. Nuclear magnetic resonance (NMR) (pH: 5.5; 1H2O 90 %; 2H2O 10 %; MgCl2 10 mM; Na2-HPO4-NaH2PO4 20 mM; NaCl 150 mM)
References:
  1. Ito Y, Yamasaki K, Iwahara J, Terada T, Kamiya A, Shirouzu M, Muto Y, Kawai G, Yokoyama S, Laue ED, Walchli M, Shibata T, Nishimura S, Miyazawa T. "Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein." Biochemistry. 1997; 36(30): 9109-9119. PubMed: 9230043

  2. Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED. "Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy." Biochemistry. 1994; 33(12): 3515-3531. PubMed: 8142349
Comments:
 



Region 19
Type:Disordered
Name: 
Location:168 - 189
Length:22
Region sequence:

LRKLNPPDESGPGCMSCKCVLS

Modification type: Complex
Engineered
Fragment
PDB: 4Q21:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography
References:
  1. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Region 20
Type:Disordered
Name: 
Location:172 - 189
Length:18
Region sequence:

NPPDESGPGCMSCKCVLS

Modification type: Complex
Engineered
Fragment
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography
References:
  1. Milburn MV, Tong L, deVos AM, Brunger A, Yamaizumi Z, Nishimura S, Kim SH. "Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins." Science. 1990; 247(4945): 939-945. PubMed: 2406906
Comments:
 



Comments


Disordered residues lie within the region corresponding to cleavage product 1, however, there is no indication that the cleavage product was discussed in the references provided. The N-terminally processed cleavage product differs from the full-length protein by a single methionine removed at the N-terminus.


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