PEAK3_HUMAN
ID PEAK3_HUMAN Reviewed; 473 AA.
AC Q6ZS72;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein PEAK3 {ECO:0000305};
GN Name=PEAK3 {ECO:0000312|HGNC:HGNC:24793}; Synonyms=C19orf35;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neutrophil;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP FUNCTION, INTERACTION WITH CRK, MUTAGENESIS OF 56-PRO--PRO-60; LEU-146;
RP ASP-330; ALA-436 AND CYS-453, AND SUBUNIT.
RX PubMed=31311869; DOI=10.1073/pnas.1906360116;
RA Lopez M.L., Lo M., Kung J.E., Dudkiewicz M., Jang G.M., Von Dollen J.,
RA Johnson J.R., Krogan N.J., Pawlowski K., Jura N.;
RT "PEAK3/C19orf35 pseudokinase, a new NFK3 kinase family member, inhibits
RT CrkII through dimerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:15495-15504(2019).
CC -!- FUNCTION: Probable catalytically inactive kinase (Probable). Interacts
CC with CRK-II and antagonizes CRK-II-signaling. Prevents the formation of
CC CRK-II-dependent membrane ruffling and lamellipodia-like extensions
CC (PubMed:31311869). {ECO:0000269|PubMed:31311869,
CC ECO:0000305|PubMed:31311869}.
CC -!- SUBUNIT: Homodimerizes (PubMed:31311869). Interacts with CRK isoform
CC CRK-II; the interaction requires PEAK3 homodimerization
CC (PubMed:31311869). {ECO:0000269|PubMed:31311869}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AK127680; BAC87082.1; -; mRNA.
DR EMBL; AC004152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS12087.1; -.
DR RefSeq; NP_940934.1; NM_198532.2.
DR AlphaFoldDB; Q6ZS72; -.
DR SMR; Q6ZS72; -.
DR STRING; 9606.ENSP00000345102; -.
DR iPTMnet; Q6ZS72; -.
DR PhosphoSitePlus; Q6ZS72; -.
DR BioMuta; PEAK3; -.
DR DMDM; 74749631; -.
DR MassIVE; Q6ZS72; -.
DR PaxDb; Q6ZS72; -.
DR PeptideAtlas; Q6ZS72; -.
DR PRIDE; Q6ZS72; -.
DR ProteomicsDB; 68194; -.
DR Antibodypedia; 53710; 17 antibodies from 8 providers.
DR DNASU; 374872; -.
DR Ensembl; ENST00000342063.5; ENSP00000345102.3; ENSG00000188305.6.
DR GeneID; 374872; -.
DR KEGG; hsa:374872; -.
DR MANE-Select; ENST00000342063.5; ENSP00000345102.3; NM_198532.3; NP_940934.1.
DR UCSC; uc002lvn.3; human.
DR CTD; 374872; -.
DR GeneCards; PEAK3; -.
DR HGNC; HGNC:24793; PEAK3.
DR HPA; ENSG00000188305; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 618526; gene.
DR neXtProt; NX_Q6ZS72; -.
DR OpenTargets; ENSG00000188305; -.
DR PharmGKB; PA134922698; -.
DR VEuPathDB; HostDB:ENSG00000188305; -.
DR eggNOG; ENOG502R3B9; Eukaryota.
DR GeneTree; ENSGT00940000163597; -.
DR HOGENOM; CLU_032877_0_0_1; -.
DR InParanoid; Q6ZS72; -.
DR OMA; TWSTQPT; -.
DR OrthoDB; 1077871at2759; -.
DR PhylomeDB; Q6ZS72; -.
DR TreeFam; TF341835; -.
DR PathwayCommons; Q6ZS72; -.
DR SignaLink; Q6ZS72; -.
DR BioGRID-ORCS; 374872; 13 hits in 1037 CRISPR screens.
DR GenomeRNAi; 374872; -.
DR Pharos; Q6ZS72; Tdark.
DR PRO; PR:Q6ZS72; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6ZS72; protein.
DR Bgee; ENSG00000188305; Expressed in blood and 83 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..473
FT /note="Protein PEAK3"
FT /id="PRO_0000277808"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 56..60
FT /note="PPPLP->APPAA: Abolishes interaction with CRK isoform
FT CRK-II. Abolishes inhibition of CRK-II-dependent membrane
FT ruffling."
FT /evidence="ECO:0000269|PubMed:31311869"
FT MUTAGEN 146
FT /note="L->E: Abolishes homodimerization and interaction
FT with CRK isoform CRK-II."
FT /evidence="ECO:0000269|PubMed:31311869"
FT MUTAGEN 330
FT /note="D->N: Strongly decreases homodimerization and
FT interaction with CRK isoform CRK-II."
FT /evidence="ECO:0000269|PubMed:31311869"
FT MUTAGEN 436
FT /note="A->E: Abolishes homodimerization and interaction
FT with CRK isoform CRK-II."
FT /evidence="ECO:0000269|PubMed:31311869"
FT MUTAGEN 453
FT /note="C->E: Abolishes homodimerization and interaction
FT with CRK isoform CRK-II."
FT /evidence="ECO:0000269|PubMed:31311869"
SQ SEQUENCE 473 AA; 50509 MW; 2389CA1E429679F3 CRC64;
MSSPEPPTEP PEPDNPTWST QPTYSNLGQI RAHLLPSKAC RLRTPGSLST NPEPLPPPLP
KKILTRTQSL PTRRTLHPSS IQVQPPRRPF LGSHSVDKSQ AAVGPACLPA ELTFGPADAP
LGLSLRDLHS PEAVHTALAA RQLQGLRTIY ARLRARLMGG HPGPCHPGHS FRLLDSSPCA
ESGDALYYRV VRAHEDAWHI LVAKVPKPGA DVPHPWGLEL QASLSPHFNL QGLCGLVPEG
TLPGAPWRGA VALAAEVPER TVAQWLAEAC TQPPEEFVWA VALLLLQLSA ALKFLEAWGA
ALVELRPENL LLVAPRGCAT TGPPRLLLTD FGRVCLQPPG PPGSPGPHAP QLGSLLRALL
SLAAPSTTPL AAGLELLAAQ LTRLRPSASR TRGALQALLW GPGPELRGRG APLGPWLRAL
GPWLRVRRGL LVLRLAERAA GGEAPSLEDW LCCEYLAEAT ESSMGQALAL LWD
