CHN2
entrez
1124
canonical
uniprot
P52757
canonical
ensembl
ENSG00000106069
resolver
ensp
ENSP00000222792
resolver
ensp
ENSP00000386849
resolver
ensp
ENSP00000386968
resolver
ensp
ENSP00000387425
resolver
ensp
ENSP00000394284
resolver
ensp
ENSP00000406337
resolver
ensp
ENSP00000486515
resolver
ensp
ENSP00000516239
resolver
ensp
ENSP00000516243
resolver
enst
ENST00000409041
resolver
enst
ENST00000409350
resolver
enst
ENST00000424025
resolver
enst
ENST00000439711
resolver
enst
ENST00000706161
resolver
genesymbol
CHN2
resolver
genesymbol_syn
ARHGAP3
resolver
genesymbol_syn
BCH
resolver
hgnc
HGNC:1944
resolver
uniprot
A0A0A0MSG1
resolver
uniprot
A0A0A0MSG7
resolver
uniprot
A0A0A0MSX8
resolver
uniprot
A0A994J7L4
resolver
uniprot
A0ACM8QIG5
resolver
uniprot
A4D1A2
resolver
uniprot
B3VCF1
resolver
uniprot
B3VCF2
resolver
uniprot
B3VCF3
resolver
uniprot
B3VCF4
resolver
uniprot
B3VCF5
resolver
uniprot
B3VCF6
resolver
uniprot
B3VCF7
resolver
uniprot
B3VCF9
resolver
uniprot
B3VCG1
resolver
uniprot
B7Z1V0
resolver
uniprot
B7Z1W9
resolver
uniprot
B7Z215
resolver
uniprot
B8ZZU1
resolver
uniprot
C9J7B0
resolver
uniprot
E9PGE0
resolver
uniprot
F8QPL9
resolver
uniprot
Q2M203
resolver
uniprot
Q75MM2
resolver
uniprot_entry
A0A0A0MSG1_HUMAN
resolver
uniprot_entry
A0A0A0MSG7_HUMAN
resolver
uniprot_entry
A0A0A0MSX8_HUMAN
resolver
uniprot_entry
A0A994J7L4_HUMAN
resolver
uniprot_entry
A0ACM8QIG5_HUMAN
resolver
uniprot_entry
B3VCF4_HUMAN
resolver
uniprot_entry
B3VCF5_HUMAN
resolver
uniprot_entry
B3VCF6_HUMAN
resolver
uniprot_entry
B3VCF9_HUMAN
resolver
uniprot_entry
B7Z1V0_HUMAN
resolver
uniprot_entry
B7Z1W9_HUMAN
resolver
uniprot_entry
B7Z215_HUMAN
resolver
uniprot_entry
CHIO_HUMAN
resolver
uniprot_sec
A4D1A2
resolver
uniprot_sec
B3VCF1
resolver
uniprot_sec
B3VCF2
resolver
uniprot_sec
B3VCF3
resolver
uniprot_sec
B3VCF7
resolver
uniprot_sec
B3VCG1
resolver
uniprot_sec
B8ZZU1
resolver
uniprot_sec
C9J7B0
resolver
uniprot_sec
E9PGE0
resolver
uniprot_sec
F8QPL9
resolver
uniprot_sec
Q2M203
resolver
uniprot_sec
Q75MM2
resolver
activity_regulation
ACTIVITY REGULATION: In the inactive state, the N terminus protrudes into the active site of the Rho-GAP domain, sterically blocking Rac binding. Phospholipid binding to the Phorbol-ester/DAG-type zinc-finger/C1 domain triggers the cooperative dissociation of these interactions, allowing the N-terminus to move out of the active site and thereby activating the enzyme. {ECO:0000269|PubMed:15507211}.
uniprot
proteins
amino_acid_sequence
MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQEAPRPKRIICPREVENRPKYYGREFHGIISREQADELLGGVEGAYILRESQRQPGCYTLALRFGNQTLNYRLFHDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYISKMTTNPIYEHIGYATLLREKVSRRLSRSKNEPRKTNVTHEEHTAVEKISSLVRRAALTHNDNHFNYEKTHNFKVHTFRGPHWCEYCANFMWGLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKRIKKVYCCDLTTLVKAHNTQRPMVVDICIREIEARGLKSEGLYRVSGFTEHIEDVKMAFDRDGEKADISANVYPDINIITGALKLYFRDLPIPVITYDTYSKFIDAAKISNADERLEAVHEVLMLLPPAHYETLRYLMIHLKKVTMNEKDNFMNAENLGIVFGPTLMRPPEDSTLTTLHDMRYQKLIVQILIENEDVLF
uniprot
proteins
function
FUNCTION: GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors.
uniprot
proteins
mass_dalton
53924
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15507211
uniprot
proteins
pubmed
7614486
uniprot
proteins
pubmed
8175705
uniprot
proteins
sequence_length
468
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
uniprot
proteins