PEAK1
entrez
79834
canonical
uniprot
Q9H792
canonical
ensembl
ENSG00000173517
resolver
ensp
ENSP00000309230
resolver
ensp
ENSP00000452796
resolver
ensp
ENSP00000507603
resolver
ensp
ENSP00000529417
resolver
ensp
ENSP00000593630
resolver
ensp
ENSP00000593631
resolver
ensp
ENSP00000593632
resolver
ensp
ENSP00000593633
resolver
ensp
ENSP00000638085
resolver
ensp
ENSP00000638086
resolver
ensp
ENSP00000638087
resolver
enst
ENST00000312493
resolver
enst
ENST00000560626
resolver
enst
ENST00000682557
resolver
enst
ENST00000859358
resolver
enst
ENST00000923571
resolver
enst
ENST00000923572
resolver
enst
ENST00000923573
resolver
enst
ENST00000923574
resolver
enst
ENST00000968026
resolver
enst
ENST00000968027
resolver
enst
ENST00000968028
resolver
genesymbol
PEAK1
resolver
genesymbol_syn
KIAA2002
resolver
hgnc
HGNC:29431
resolver
uniprot
Q6ZS78
resolver
uniprot
Q8NAZ4
resolver
uniprot
Q8NCM3
resolver
uniprot
Q8TEG7
resolver
uniprot_entry
PEAK1_HUMAN
resolver
uniprot_sec
Q6ZS78
resolver
uniprot_sec
Q8NAZ4
resolver
uniprot_sec
Q8NCM3
resolver
uniprot_sec
Q8TEG7
resolver
amino_acid_sequence
MSACNTFTEHVWKPGECKNCFKPKSLHQLPPDPEKAPITHGNVKTNANHSNNHRIRNTGNFRPPVAKKPTIAVKPTMIVADGQSICGELSIQEHCENKPVIIGWNRNRAALSQKPLNNNNEDDEGISHVPKPYGNNDSAKKMSDNNNGLTEVLKEIAGLDTAPQIRGNETNSRETFLGRINDCYKRSLERKLPPSCMIGGIKETQGKHVILSGSTEVISNEGGRFCYPEFSSGEESEEDVLFSNMEEEHESWDESDEELLAMEIRMRGQPRFANFRANTLSPVRFFVDKKWNTIPLRNKSLQRICAVDYDDSYDEILNGYEENSVVSYGQGSIQSMVSSDSTSPDSSLTEESRSETASSLSQKICNGGLSPGNPGDSKDMKEIEPNYESPSSNNQDKDSSQASKSSIKVPETHKAVLALRLEEKDGKIAVQTEKEESKASTDVAGQAVTINLVPTEEQAKPYRVVNLEQPLCKPYTVVDVSAAMASEHLEGPVNSPKTKSSSSTPNSPVTSSSLTPGQISAHFQKSSAIRYQEVWTSSTSPRQKIPKVELITSGTGPNVPPRKNCHKSAPTSPTATNISSKTIPVKSPNLSEIKFNSYNNAGMPPFPIIIHDEPTYARSSKNAIKVPIVINPNAYDNLAIYKSFLGTSGELSVKEKTTSVISHTYEEIETESKVPDNTTSKTTDCLQTKGFSNSTEHKRGSVAQKVQEFNNCLNRGQSSPQRSYSSSHSSPAKIQRATQEPVAKIEGTQESQMVGSSSTREKASTVLSQIVASIQPPQSPPETPQSGPKACSVEELYAIPPDADVAKSTPKSTPVRPKSLFTSQPSGEAEAPQTTDSPTTKVQKDPSIKPVTPSPSKLVTSPQSEPPAPFPPPRSTSSPYHAGNLLQRHFTNWTKPTSPTRSTEAESVLHSEGSRRAADAKPKRWISFKSFFRRRKTDEEDDKEKEREKGKLVGLDGTVIHMLPPPPVQRHHWFTEAKGESSEKPAIVFMYRCDPAQGQLSVDQSKARTDQAAVMEKGRAENALLQDSEKKRSHSSPSQIPKKILSHMTHEVTEDFSPRDPRTVVGKQDGRGCTSVTTALSLPELEREDGKEDISDPMDPNPCSATYSNLGQSRAAMIPPKQPRQPKGAVDDAIAFGGKTDQEAPNASQPTPPPLPKKMIIRANTEPISKDLQKSMESSLCVMANPTYDIDPNWDASSAGSSISYELKGLDIESYDSLERPLRKERPVPSAANSISSLTTLSIKDRFSNSMESLSSRRGPSCRQGRGIQKPQRQALYRGLENREEVVGKIRSLHTDALKKLAVKCEDLFMAGQKDQLRFGVDSWSDFRLTSDKPCCEAGDAVYYTASYAKDPLNNYAVKICKSKAKESQQYYHSLAVRQSLAVHFNIQQDCGHFLAEVPNRLLPWEDPDDPEKDEDDMEETEEDAKGETDGKNPKPCSEAASSQKENQGVMSKKQRSHVVVITREVPCLTVADFVRDSLAQHGKSPDLYERQVCLLLLQLCSGLEHLKPYHVTHCDLRLENLLLVHYQPGGTAQGFGPAEPSPTSSYPTRLIVSNFSQAKQKSHLVDPEILRDQSRLAPEIITATQYKKCDEFQTGILIYEMLHLPNPFDENPELKEREYTRADLPRIPFRSPYSRGLQQLASCLLNPNPSERILISDAKGILQCLLWGPREDLFQTFTACPSLVQRNTLLQNWLDIKRTLLMIKFAEKSLDREGGISLEDWLCAQYLAFATTDSLSCIVKILQHR
uniprot
proteins
function
FUNCTION: Probable catalytically inactive kinase. Scaffolding protein that regulates the cytoskeleton to control cell spreading and migration by modulating focal adhesion dynamics (PubMed:20534451, PubMed:23105102, PubMed:35687021). Acts as a scaffold for mediating EGFR signaling (PubMed:23846654). {ECO:0000269|PubMed:20534451, ECO:0000269|PubMed:23105102, ECO:0000269|PubMed:23846654, ECO:0000269|PubMed:35687021}.
uniprot
proteins
mass_dalton
193106
uniprot
proteins
mutagenesis
MUTAGEN 635; /note="Y->E: 50% reduction in interaction with GRB2. No effect on interaction with SHC1."; MUTAGEN 635; /note="Y->F: Impairs interaction with tensin TNS3 and association with integrin ITGB1. 50% reduction in interaction with GRB2. No effect on interaction with unphosphorylated SHC1 but reduces interaction with tyrosine-phosphorylated SHC1. Reduces focal adhesion localization. Reduces cell migration."; /evidence="ECO:0000269|PubMed:35687021"; MUTAGEN 665; /note="Y->E: No effect on localization with actin. Decreases localization in focal adhesion. Fails to regulate focal adhesion dynamics. Decreases cell migration."; /evidence="ECO:0000269|PubMed:23105102"; MUTAGEN 665; /note="Y->F: No effect on focal adhesion subcellular localization. Does not affect colocalization with F-actin."; /evidence="ECO:0000269|PubMed:23105102"; MUTAGEN 1188; /note="Y->F: Fails to bind SHC1. Reduced recruitment of SHC1 to focal adhesions. Slightly reduces interaction with GRB2. Does not affect interaction with RASAL2. Does not affect association with integrin ITGB1."; /evidence="ECO:0000269|PubMed:23846654, ECO:0000269|PubMed:35687021"; MUTAGEN 1609; /note="F->A: No effect on interaction with PRAG1."; /evidence="ECO:0000269|PubMed:29079850"; MUTAGEN 1707; /note="A->D: Disrupts homodimerization."; /evidence="ECO:0000269|PubMed:29212708
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine in a CSK-dependent manner in response to adhesion to fibronectin and to EGF stimulation (PubMed:20534451). Phosphorylation at Tyr-665 by a Src family kinase controls subcellular localization to focal adhesion and focal adhesion dynamics (PubMed:20534451). Phosphorylation at Tyr-1188 is essential for binding to SHC1 (PubMed:23846654). Phosphorylation at Tyr-635 promotes interaction with tensin TNS3 (PubMed:35687021). {ECO:0000269|PubMed:20534451, ECO:0000269|PubMed:23846654, ECO:0000269|PubMed:35687021}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
12056414
uniprot
proteins
pubmed
12471243
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20534451
uniprot
proteins
pubmed
23105102
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23846654
uniprot
proteins
pubmed
24107129
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29079850
uniprot
proteins
pubmed
29212708
uniprot
proteins
pubmed
35687021
uniprot
proteins
sequence_length
1746
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20534451, ECO:0000269|PubMed:23105102}. Cell junction, focal adhesion {ECO:0000269|PubMed:20534451, ECO:0000269|PubMed:23105102, ECO:0000269|PubMed:35687021}. Note=Colocalizes with F-actin in serum-rich medium (PubMed:20534451). Actin colocalization is reduced during serum starvation (PubMed:20534451). {ECO:0000269|PubMed:20534451}.
uniprot
proteins