BCR
entrez
613
canonical
uniprot
P11274
canonical
ensembl
ENSG00000186716
resolver
ensp
ENSP00000303507
resolver
ensp
ENSP00000352535
resolver
genesymbol
BCR
resolver
genesymbol_syn
BCR1
resolver
genesymbol_syn
D22S11
resolver
hgnc
HGNC:1014
resolver
uniprot
P78501
resolver
uniprot
Q12842
resolver
uniprot
Q4LE80
resolver
uniprot
Q6NZI3
resolver
uniprot_entry
BCR_HUMAN
resolver
uniprot_sec
P78501
resolver
uniprot_sec
Q12842
resolver
uniprot_sec
Q4LE80
resolver
uniprot_sec
Q6NZI3
resolver
amino_acid_sequence
MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV
uniprot
proteins
disease_involvement
DISEASE: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T-lymphoid cells, but not marrow fibroblasts. {ECO:0000269|PubMed:2407300, ECO:0000269|PubMed:3107980, ECO:0000269|PubMed:3540951}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Note=A chromosomal aberration involving BCR has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with ABL1. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL). {ECO:0000269|PubMed:3107980, ECO:0000269|PubMed:7665185}.
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form (PubMed:17116687, PubMed:1903516, PubMed:7479768). The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (PubMed:23940119, PubMed:7479768). The amino terminus contains an intrinsic kinase activity (PubMed:1657398). Functions as an important negative regulator of neuronal RAC1 activity (By similarity). Regulates macrophage functions such as CSF1-directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687). Plays a major role as a RHOA GEF in keratinocytes being involved in focal adhesion formation and keratinocyte differentiation (PubMed:23940119). {ECO:0000250|UniProtKB:Q6PAJ1, ECO:0000269|PubMed:1657398, ECO:0000269|PubMed:17116687, ECO:0000269|PubMed:1903516, ECO:0000269|PubMed:23940119, ECO:0000269|PubMed:7479768}.
uniprot
proteins
mass_dalton
142819
uniprot
proteins
mutagenesis
MUTAGEN 177; /note="Y->F: Abolishes interaction with FES and GRB2."; /evidence="ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:9407116"; MUTAGEN 689..690; /note="NE->AA: Loss of RHOAGEF activity."; /evidence="ECO:0000269|PubMed:23940119"; MUTAGEN 1090; /note="R->A: Loss of GAP activity. Loss of GAP activity; when associated with A-1202."; /evidence="ECO:0000269|PubMed:17116687"; MUTAGEN 1202; /note="N->A: Loss of GAP activity; when associated with A-1090."; /evidence="ECO:0000269|PubMed:17116687"; MUTAGEN 1269..1271; /note="Missing: Abolishes interaction with PDZK1."; /evidence="ECO:0000269|PubMed:15494376"; MUTAGEN 1271; /note="V->A: Reduces interaction with PDZK1. Abolishes interaction with DLG4. No effect on synaptic localization."; /evidence="ECO:0000269|PubMed:15494376, ECO:0000269|PubMed:20962234
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation at Tyr-177 by HCK is important for interaction with GRB2. {ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:9407116}.
uniprot
proteins
pubmed
10508479
uniprot
proteins
pubmed
11780146
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15302586
uniprot
proteins
pubmed
15494376
uniprot
proteins
pubmed
1657398
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17116687
uniprot
proteins
pubmed
1712671
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
1900918
uniprot
proteins
pubmed
1903516
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20962234
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
2263470
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23940119
uniprot
proteins
pubmed
2407300
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25331951
uniprot
proteins
pubmed
2825022
uniprot
proteins
pubmed
2915904
uniprot
proteins
pubmed
2989703
uniprot
proteins
pubmed
3107980
uniprot
proteins
pubmed
3285291
uniprot
proteins
pubmed
3540951
uniprot
proteins
pubmed
7479768
uniprot
proteins
pubmed
7665185
uniprot
proteins
pubmed
9407116
uniprot
proteins
sequence_length
1271
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PAJ1}. Synapse {ECO:0000250|UniProtKB:F1LXF1}.
uniprot
proteins