ID   BRK1_HUMAN              Reviewed;          75 AA.
AC   Q8WUW1; B2R5E2; Q9P082;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   26-FEB-2020, entry version 146.
DE   RecName: Full=Protein BRICK1;
DE            Short=BRK1;
GN   Name=BRK1; Synonyms=C3orf10; ORFNames=HSPC300, MDS027;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain, and Lung;
RA   Xu Q., Duan R., Huo Y., Fan B., Zhang K., Wu D.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Umbilical cord blood;
RA   Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA   Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT   "Human partial CDS from CD34+ stem cells.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH WASF2.
RX   PubMed=15070726; DOI=10.1073/pnas.0400628101;
RA   Gautreau A., Ho H.-Y., Li J., Steen H., Gygi S.P., Kirschner M.W.;
RT   "Purification and architecture of the ubiquitous Wave complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:4379-4383(2004).
RN   [7]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=18560548; DOI=10.1371/journal.pone.0002462;
RA   Derivery E., Fink J., Martin D., Houdusse A., Piel M., Stradal T.E.,
RA   Louvard D., Gautreau A.;
RT   "Free Brick1 is a trimeric precursor in the assembly of a functional wave
RT   complex.";
RL   PLoS ONE 3:E2462-E2462(2008).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, AND SUBUNIT.
RX   PubMed=21107423; DOI=10.1038/nature09623;
RA   Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M.,
RA   Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.;
RT   "Structure and control of the actin regulatory WAVE complex.";
RL   Nature 468:533-538(2010).
CC   -!- FUNCTION: Involved in regulation of actin and microtubule organization.
CC       Part of a WAVE complex that activates the Arp2/3 complex. As component
CC       of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and
CC       signaling from early endosomes (By similarity).
CC       {ECO:0000250|UniProtKB:Q91VR8, ECO:0000269|PubMed:18560548}.
CC   -!- SUBUNIT: Homotrimer when in free form. Directly interacts with WASF2.
CC       Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2,
CC       BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC       containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC       WAVE1, ABI2 and BRK1. {ECO:0000269|PubMed:15070726,
CC       ECO:0000269|PubMed:18560548, ECO:0000269|PubMed:21107423}.
CC   -!- INTERACTION:
CC       Q96EV8:DTNBP1; NbExp=3; IntAct=EBI-2837444, EBI-465804;
CC       O75506:HSBP1; NbExp=4; IntAct=EBI-2837444, EBI-748664;
CC       Q9GZM8:NDEL1; NbExp=3; IntAct=EBI-2837444, EBI-928842;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WUW1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WUW1-2; Sequence=VSP_024350;
CC   -!- SIMILARITY: Belongs to the BRK1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF28978.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY148219; AAN60161.1; -; mRNA.
DR   EMBL; AY148220; AAN60162.1; -; mRNA.
DR   EMBL; AF161418; AAF28978.1; ALT_INIT; mRNA.
DR   EMBL; AK312155; BAG35089.1; -; mRNA.
DR   EMBL; CH471055; EAW64061.1; -; Genomic_DNA.
DR   EMBL; BC001067; AAH01067.1; -; mRNA.
DR   EMBL; BC007929; AAH07929.1; -; mRNA.
DR   EMBL; BC019303; AAH19303.1; -; mRNA.
DR   CCDS; CCDS54553.1; -. [Q8WUW1-1]
DR   RefSeq; NP_060932.2; NM_018462.4. [Q8WUW1-1]
DR   PDB; 3P8C; X-ray; 2.29 A; E=1-75.
DR   PDB; 4N78; X-ray; 2.43 A; E=1-75.
DR   PDBsum; 3P8C; -.
DR   PDBsum; 4N78; -.
DR   SMR; Q8WUW1; -.
DR   BioGrid; 120947; 28.
DR   CORUM; Q8WUW1; -.
DR   DIP; DIP-41554N; -.
DR   IntAct; Q8WUW1; 40.
DR   MINT; Q8WUW1; -.
DR   STRING; 9606.ENSP00000432472; -.
DR   ChEMBL; CHEMBL3758062; -.
DR   iPTMnet; Q8WUW1; -.
DR   PhosphoSitePlus; Q8WUW1; -.
DR   BioMuta; BRK1; -.
DR   DMDM; 74730773; -.
DR   EPD; Q8WUW1; -.
DR   jPOST; Q8WUW1; -.
DR   MassIVE; Q8WUW1; -.
DR   MaxQB; Q8WUW1; -.
DR   PaxDb; Q8WUW1; -.
DR   PeptideAtlas; Q8WUW1; -.
DR   PRIDE; Q8WUW1; -.
DR   ProteomicsDB; 74714; -. [Q8WUW1-1]
DR   ProteomicsDB; 74715; -. [Q8WUW1-2]
DR   TopDownProteomics; Q8WUW1-1; -. [Q8WUW1-1]
DR   TopDownProteomics; Q8WUW1-2; -. [Q8WUW1-2]
DR   DNASU; 55845; -.
DR   Ensembl; ENST00000530758; ENSP00000432472; ENSG00000254999. [Q8WUW1-1]
DR   GeneID; 55845; -.
DR   KEGG; hsa:55845; -.
DR   UCSC; uc003bvb.4; human. [Q8WUW1-1]
DR   CTD; 55845; -.
DR   DisGeNET; 55845; -.
DR   GeneCards; BRK1; -.
DR   HGNC; HGNC:23057; BRK1.
DR   HPA; HPA060391; -.
DR   MIM; 611183; gene.
DR   neXtProt; NX_Q8WUW1; -.
DR   OpenTargets; ENSG00000254999; -.
DR   PharmGKB; PA134866423; -.
DR   eggNOG; ENOG410J0X8; Eukaryota.
DR   eggNOG; ENOG4111UHX; LUCA.
DR   GeneTree; ENSGT00390000011082; -.
DR   HOGENOM; CLU_175202_0_0_1; -.
DR   InParanoid; Q8WUW1; -.
DR   KO; K05752; -.
DR   OMA; ACVTQGE; -.
DR   OrthoDB; 1579787at2759; -.
DR   PhylomeDB; Q8WUW1; -.
DR   TreeFam; TF324876; -.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   SIGNOR; Q8WUW1; -.
DR   ChiTaRS; BRK1; human.
DR   EvolutionaryTrace; Q8WUW1; -.
DR   GeneWiki; C3orf10; -.
DR   GenomeRNAi; 55845; -.
DR   Pharos; Q8WUW1; Tbio.
DR   PRO; PR:Q8WUW1; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q8WUW1; protein.
DR   Bgee; ENSG00000254999; Expressed in sperm and 196 other tissues.
DR   Genevisible; Q8WUW1; HS.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0031209; C:SCAR complex; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:UniProtKB.
DR   GO; GO:0016601; P:Rac protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IBA:GO_Central.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   InterPro; IPR033378; BRICK1.
DR   PANTHER; PTHR33668; PTHR33668; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22814378"
FT   CHAIN           2..75
FT                   /note="Protein BRICK1"
FT                   /id="PRO_0000283646"
FT   COILED          41..72
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22814378"
FT   VAR_SEQ         75
FT                   /note="T -> TRTVPCCCWEVALHNTGHMGKAPAAFSSFLSP (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_024350"
FT   HELIX           11..68
FT                   /evidence="ECO:0000244|PDB:3P8C"
SQ   SEQUENCE   75 AA;  8745 MW;  637B5461A2D96587 CRC64;
     MAGQEDPVQR EIHQDWANRE YIEIITSSIK KIADFLNSFD MSCRSRLATL NEKLTALERR
     IEYIEARVTK GETLT
//