Full text data of FOCAD
FOCAD
(KIAA1797)
[Confidence: low (only semi-automatic identification from reviews)]
Focadhesin
Focadhesin
UniProt
Q5VW36
ID FOCAD_HUMAN Reviewed; 1801 AA.
AC Q5VW36; D3DRJ9; Q6ZME1; Q8IZG0; Q96JM8; Q96MS9; Q9BVF3; Q9NX87;
read moreDT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=Focadhesin;
GN Name=FOCAD; Synonyms=KIAA1797;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-718 AND
RP GLU-1668.
RC TISSUE=Brain;
RA Guo J.H., Chen L., Yu L.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-718.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-915 AND 1305-1801, AND
RP VARIANTS SER-718; ALA-1373 AND GLU-1668.
RC TISSUE=Endothelial cell, Hepatoma, and Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 521-1801, AND VARIANTS
RP SER-718 AND GLU-1668.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1300-1801, AND VARIANT
RP GLU-1668.
RC TISSUE=Choriocarcinoma;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16877819; DOI=10.1155/JBB/2006/71753;
RA Matlik K., Redik K., Speek M.;
RT "L1 antisense promoter drives tissue-specific transcription of human
RT genes.";
RL J. Biomed. Biotechnol. 2006:71753-71753(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-819, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(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.,
RA Buerckstuemmer T., 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 TISSUE SPECIFICITY, INTERACTION WITH VCL, AND FUNCTION.
RX PubMed=22427331; DOI=10.1093/brain/aws045;
RA Brockschmidt A., Trost D., Peterziel H., Zimmermann K., Ehrler M.,
RA Grassmann H., Pfenning P.N., Waha A., Wohlleber D., Brockschmidt F.F.,
RA Jugold M., Hoischen A., Kalla C., Waha A., Seifert G., Knolle P.A.,
RA Latz E., Hans V.H., Wick W., Pfeifer A., Angel P., Weber R.G.;
RT "KIAA1797/FOCAD encodes a novel focal adhesion protein with tumour
RT suppressor function in gliomas.";
RL Brain 135:1027-1041(2012).
CC -!- FUNCTION: Potential tumor suppressor in gliomas (By similarity).
CC -!- SUBUNIT: Interacts with VCL.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential). Cell junction, focal adhesion. Note=Colocalizes with
CC VCL in astrocytes.
CC -!- TISSUE SPECIFICITY: Ubiquitous. High expression in brain followed
CC by testis, muscle, pancreas, heart, ovary, small intestine,
CC placenta, prostate, thymus, kidney, colon, liver, lung, spleen and
CC leukocytes. Expression is reduced in most glioblastomas and all
CC glioblastoma cell lines.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91129.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA91129.1; Type=Frameshift; Positions=261;
CC Sequence=BAD18787.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AY139834; AAN17740.1; -; mRNA.
DR EMBL; AL392163; CAH73851.1; -; Genomic_DNA.
DR EMBL; AL445624; CAH73851.1; JOINED; Genomic_DNA.
DR EMBL; AL662879; CAH73851.1; JOINED; Genomic_DNA.
DR EMBL; AK000382; BAA91129.1; ALT_FRAME; mRNA.
DR EMBL; AK056522; BAB71203.1; -; mRNA.
DR EMBL; AK172818; BAD18787.1; ALT_INIT; mRNA.
DR EMBL; AB058700; BAB47426.1; -; mRNA.
DR EMBL; CH471071; EAW58627.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58628.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58629.1; -; Genomic_DNA.
DR EMBL; BC001246; AAH01246.2; -; mRNA.
DR RefSeq; NP_060264.3; NM_017794.3.
DR RefSeq; XP_005251551.1; XM_005251494.1.
DR UniGene; Hs.136247; -.
DR ProteinModelPortal; Q5VW36; -.
DR SMR; Q5VW36; 690-716.
DR IntAct; Q5VW36; 1.
DR MINT; MINT-8247615; -.
DR PhosphoSite; Q5VW36; -.
DR DMDM; 74747342; -.
DR PaxDb; Q5VW36; -.
DR PRIDE; Q5VW36; -.
DR Ensembl; ENST00000338382; ENSP00000344307; ENSG00000188352.
DR Ensembl; ENST00000380249; ENSP00000369599; ENSG00000188352.
DR GeneID; 54914; -.
DR KEGG; hsa:54914; -.
DR UCSC; uc003zog.1; human.
DR CTD; 54914; -.
DR GeneCards; GC09P020659; -.
DR HGNC; HGNC:23377; FOCAD.
DR HPA; HPA055015; -.
DR MIM; 614606; gene.
DR neXtProt; NX_Q5VW36; -.
DR PharmGKB; PA134934777; -.
DR eggNOG; NOG27815; -.
DR HOVERGEN; HBG095600; -.
DR InParanoid; Q5VW36; -.
DR OMA; SPKLSCD; -.
DR OrthoDB; EOG7N0C3T; -.
DR GeneWiki; KIAA1797; -.
DR GenomeRNAi; 54914; -.
DR NextBio; 57970; -.
DR PRO; PR:Q5VW36; -.
DR Bgee; Q5VW36; -.
DR CleanEx; HS_KIAA1797; -.
DR Genevestigator; Q5VW36; -.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021392; DUF3028.
DR InterPro; IPR022542; DUF3730.
DR Pfam; PF11229; DUF3028; 1.
DR Pfam; PF12530; DUF3730; 2.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Complete proteome; Membrane; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 1801 Focadhesin.
FT /FTId=PRO_0000314457.
FT TRANSMEM 404 424 Helical; (Potential).
FT TRANSMEM 441 461 Helical; (Potential).
FT TRANSMEM 1036 1056 Helical; (Potential).
FT MOD_RES 819 819 N6-acetyllysine.
FT VARIANT 166 166 L -> S (in dbSNP:rs10511687).
FT /FTId=VAR_037877.
FT VARIANT 234 234 V -> I (in dbSNP:rs10441706).
FT /FTId=VAR_037878.
FT VARIANT 523 523 I -> V (in dbSNP:rs17832431).
FT /FTId=VAR_037879.
FT VARIANT 718 718 T -> S (in dbSNP:rs7875872).
FT /FTId=VAR_037880.
FT VARIANT 721 721 E -> K (in dbSNP:rs10964742).
FT /FTId=VAR_049528.
FT VARIANT 1373 1373 T -> A (in dbSNP:rs3206852).
FT /FTId=VAR_061251.
FT VARIANT 1373 1373 T -> P (in dbSNP:rs3206852).
FT /FTId=VAR_037881.
FT VARIANT 1373 1373 T -> S (in dbSNP:rs3206852).
FT /FTId=VAR_061252.
FT VARIANT 1668 1668 K -> E (in dbSNP:rs4977881).
FT /FTId=VAR_037882.
FT CONFLICT 481 481 A -> V (in Ref. 1; AAN17740 and 4;
FT BAB71203).
FT CONFLICT 1430 1430 E -> D (in Ref. 6; AAH01246).
SQ SEQUENCE 1801 AA; 200072 MW; D9E96037C621FB80 CRC64;
MSDDIRKRFE FPNSLIQSQA VGHLIAAVLK ENGFSEKIHQ STNQTPALNL LWEKCCSDNV
VVRTACCEGL VALVAQDHAE FSYVLNGILN LIPSTRNTHG LIKAIMHLLQ MQALKEGQGG
EKNIQSIYTI RNHPHPLITV LEHRPDCWPV FLQQLTAFFQ QCPERLEVSC IQIMAPFLWY
LYCEPSQLQE YAKLRLALLK VLLQPQVLCD KDQPSILEQQ ILQLCCDIVP CLQVKDLIQT
TEAMMFIEEV CLSLLRHPVF WKIQLTQMSL QLLCVSEVSL KITGECSSSI HLLEHSVELL
KEDFPVELVI IGIALLLLQT PASQQKPILN LALKLLSVTE DQKIPKSSLL LVMPILQILS
STALEDCISV DEEGPSRQQL ALNLLEMIQQ ECYRDDHQKL SYKLVCPVTS MYGTIFTAWR
ILEVMTDSSA ASDWLASVES LLPITAVIPA PAFLLLAHLL VEDKGQNLHQ ILKVTTELAQ
ADSSQVPNLI PVLMFKLGRP LEPILYNDIL YTLPKLGVHK VCIGQILRII QLLGTTPRLR
AVTLRLLTSL WEKQDRVYPE LQRFMAVSDV PSLSVGKEVQ WEKLIAKAAS IRDICKQRPY
QHGADMLAAI SQVLNECTKP DQATPAALVL QGLHALCQAE VVCIRSTWNA LSPKLSCDTR
PLILKTLSEL FSLVPSLTVN TTEYENFKVQ VLSFLWTHTQ NKDPIVANAA YRSLANFTAG
EHTILHLPEK IRPEIPIPEE LDDDEDVEDV DLSVPGSCYL KLLSLTPPLV LPALEEFFTS
LVKQEMVNMP RGIYHSALKG GARSDQGKTV AGIPNFILKM YETNKQPGLK PGLAGGMLFC
YDVSMYQSKD GKPLNRLMAS RGRSFKQTSL ALVHEVHIQL SEWHRAIFLP QAWLAYMNRA
YHAILQGRLG ELELQLKHGK EEPEEVQYKK STAWLWVRDM LTDEITKAAA KESPVVKGNA
LLALSSLAVV VSRHEASLSS DSDGLLEVQP NFLSMKEWVS MVLDTLLVIV DSHYQPRGQL
LSWFYYKSYS GENTASAIAR SAAATALSLL VPVFIISCKE KVEEILNMLT ARLPGKPSAD
ESQAVQIHMG LALGMFLSRL CEEKLSDISG QEMNLLLMKS LDALENCCFD TSLEYNTGCI
LGVGLVLSLM SHSSQMQSRV HVAALLRKLS AHVDDSGSQS RTFQEVLAYT LSCVCTSAFS
AGIIEATEAE DVMNKLRLLV ENSQQTSGFA LALGNIVHGL SVCGHGKAED LGSKLLPAWI
RIVLTEGTPT MLCLAALHGM VALVGSEGDV MQLKSEAIQT SHFQGRLNEV IRTLTQVISV
SGVIGLQSNA VWLLGHLHLS TLSSSQSRAS VPTDYSYLPE SSFIGAAIGF FITGGKKGPE
SVPPSLLKVV MKPIATVGES YQYPPVNWAA LLSPLMRLNF GEEIQQLCLE IMVTQAQSSQ
NAAALLGLWV TPPLIHSLSL NTKRYLLISA PLWIKHISDE QILGFVENLM VAVFKAASPL
GSPELCPSAL HGLSQAMKLP SPAHHLWSLL SEATGKIFDL LPNKIRRKDL ELYISIAKCL
LEMTDDDANR IAQVTKSNIE KAAFVKLYLV SQGRFPLVNL TDMLSVAVQH REKEVLAWMI
LHSLYQARIV SHANTGVLKR MEWLLELMGY IRNVAYQSTS FHNTALDKAL DFFLLIFATA
VVAWADHTAP LLLGLSASWL PWHQENGPAG PVPSFLGRSP MHRVTLQEVL TLLPNSMALL
LQKEPWKEQT QKFIDWLFSI MESPKEALSA QSRDLLKATL LSLRVLPEFK KKAVWTRAYG
W
//
ID FOCAD_HUMAN Reviewed; 1801 AA.
AC Q5VW36; D3DRJ9; Q6ZME1; Q8IZG0; Q96JM8; Q96MS9; Q9BVF3; Q9NX87;
read moreDT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 80.
DE RecName: Full=Focadhesin;
GN Name=FOCAD; Synonyms=KIAA1797;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-718 AND
RP GLU-1668.
RC TISSUE=Brain;
RA Guo J.H., Chen L., Yu L.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-718.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-915 AND 1305-1801, AND
RP VARIANTS SER-718; ALA-1373 AND GLU-1668.
RC TISSUE=Endothelial cell, Hepatoma, and Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 521-1801, AND VARIANTS
RP SER-718 AND GLU-1668.
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1300-1801, AND VARIANT
RP GLU-1668.
RC TISSUE=Choriocarcinoma;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16877819; DOI=10.1155/JBB/2006/71753;
RA Matlik K., Redik K., Speek M.;
RT "L1 antisense promoter drives tissue-specific transcription of human
RT genes.";
RL J. Biomed. Biotechnol. 2006:71753-71753(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-819, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(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.,
RA Buerckstuemmer T., 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 TISSUE SPECIFICITY, INTERACTION WITH VCL, AND FUNCTION.
RX PubMed=22427331; DOI=10.1093/brain/aws045;
RA Brockschmidt A., Trost D., Peterziel H., Zimmermann K., Ehrler M.,
RA Grassmann H., Pfenning P.N., Waha A., Wohlleber D., Brockschmidt F.F.,
RA Jugold M., Hoischen A., Kalla C., Waha A., Seifert G., Knolle P.A.,
RA Latz E., Hans V.H., Wick W., Pfeifer A., Angel P., Weber R.G.;
RT "KIAA1797/FOCAD encodes a novel focal adhesion protein with tumour
RT suppressor function in gliomas.";
RL Brain 135:1027-1041(2012).
CC -!- FUNCTION: Potential tumor suppressor in gliomas (By similarity).
CC -!- SUBUNIT: Interacts with VCL.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential). Cell junction, focal adhesion. Note=Colocalizes with
CC VCL in astrocytes.
CC -!- TISSUE SPECIFICITY: Ubiquitous. High expression in brain followed
CC by testis, muscle, pancreas, heart, ovary, small intestine,
CC placenta, prostate, thymus, kidney, colon, liver, lung, spleen and
CC leukocytes. Expression is reduced in most glioblastomas and all
CC glioblastoma cell lines.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91129.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAA91129.1; Type=Frameshift; Positions=261;
CC Sequence=BAD18787.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC -----------------------------------------------------------------------
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DR EMBL; AY139834; AAN17740.1; -; mRNA.
DR EMBL; AL392163; CAH73851.1; -; Genomic_DNA.
DR EMBL; AL445624; CAH73851.1; JOINED; Genomic_DNA.
DR EMBL; AL662879; CAH73851.1; JOINED; Genomic_DNA.
DR EMBL; AK000382; BAA91129.1; ALT_FRAME; mRNA.
DR EMBL; AK056522; BAB71203.1; -; mRNA.
DR EMBL; AK172818; BAD18787.1; ALT_INIT; mRNA.
DR EMBL; AB058700; BAB47426.1; -; mRNA.
DR EMBL; CH471071; EAW58627.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58628.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58629.1; -; Genomic_DNA.
DR EMBL; BC001246; AAH01246.2; -; mRNA.
DR RefSeq; NP_060264.3; NM_017794.3.
DR RefSeq; XP_005251551.1; XM_005251494.1.
DR UniGene; Hs.136247; -.
DR ProteinModelPortal; Q5VW36; -.
DR SMR; Q5VW36; 690-716.
DR IntAct; Q5VW36; 1.
DR MINT; MINT-8247615; -.
DR PhosphoSite; Q5VW36; -.
DR DMDM; 74747342; -.
DR PaxDb; Q5VW36; -.
DR PRIDE; Q5VW36; -.
DR Ensembl; ENST00000338382; ENSP00000344307; ENSG00000188352.
DR Ensembl; ENST00000380249; ENSP00000369599; ENSG00000188352.
DR GeneID; 54914; -.
DR KEGG; hsa:54914; -.
DR UCSC; uc003zog.1; human.
DR CTD; 54914; -.
DR GeneCards; GC09P020659; -.
DR HGNC; HGNC:23377; FOCAD.
DR HPA; HPA055015; -.
DR MIM; 614606; gene.
DR neXtProt; NX_Q5VW36; -.
DR PharmGKB; PA134934777; -.
DR eggNOG; NOG27815; -.
DR HOVERGEN; HBG095600; -.
DR InParanoid; Q5VW36; -.
DR OMA; SPKLSCD; -.
DR OrthoDB; EOG7N0C3T; -.
DR GeneWiki; KIAA1797; -.
DR GenomeRNAi; 54914; -.
DR NextBio; 57970; -.
DR PRO; PR:Q5VW36; -.
DR Bgee; Q5VW36; -.
DR CleanEx; HS_KIAA1797; -.
DR Genevestigator; Q5VW36; -.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021392; DUF3028.
DR InterPro; IPR022542; DUF3730.
DR Pfam; PF11229; DUF3028; 1.
DR Pfam; PF12530; DUF3730; 2.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell junction; Complete proteome; Membrane; Polymorphism;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1 1801 Focadhesin.
FT /FTId=PRO_0000314457.
FT TRANSMEM 404 424 Helical; (Potential).
FT TRANSMEM 441 461 Helical; (Potential).
FT TRANSMEM 1036 1056 Helical; (Potential).
FT MOD_RES 819 819 N6-acetyllysine.
FT VARIANT 166 166 L -> S (in dbSNP:rs10511687).
FT /FTId=VAR_037877.
FT VARIANT 234 234 V -> I (in dbSNP:rs10441706).
FT /FTId=VAR_037878.
FT VARIANT 523 523 I -> V (in dbSNP:rs17832431).
FT /FTId=VAR_037879.
FT VARIANT 718 718 T -> S (in dbSNP:rs7875872).
FT /FTId=VAR_037880.
FT VARIANT 721 721 E -> K (in dbSNP:rs10964742).
FT /FTId=VAR_049528.
FT VARIANT 1373 1373 T -> A (in dbSNP:rs3206852).
FT /FTId=VAR_061251.
FT VARIANT 1373 1373 T -> P (in dbSNP:rs3206852).
FT /FTId=VAR_037881.
FT VARIANT 1373 1373 T -> S (in dbSNP:rs3206852).
FT /FTId=VAR_061252.
FT VARIANT 1668 1668 K -> E (in dbSNP:rs4977881).
FT /FTId=VAR_037882.
FT CONFLICT 481 481 A -> V (in Ref. 1; AAN17740 and 4;
FT BAB71203).
FT CONFLICT 1430 1430 E -> D (in Ref. 6; AAH01246).
SQ SEQUENCE 1801 AA; 200072 MW; D9E96037C621FB80 CRC64;
MSDDIRKRFE FPNSLIQSQA VGHLIAAVLK ENGFSEKIHQ STNQTPALNL LWEKCCSDNV
VVRTACCEGL VALVAQDHAE FSYVLNGILN LIPSTRNTHG LIKAIMHLLQ MQALKEGQGG
EKNIQSIYTI RNHPHPLITV LEHRPDCWPV FLQQLTAFFQ QCPERLEVSC IQIMAPFLWY
LYCEPSQLQE YAKLRLALLK VLLQPQVLCD KDQPSILEQQ ILQLCCDIVP CLQVKDLIQT
TEAMMFIEEV CLSLLRHPVF WKIQLTQMSL QLLCVSEVSL KITGECSSSI HLLEHSVELL
KEDFPVELVI IGIALLLLQT PASQQKPILN LALKLLSVTE DQKIPKSSLL LVMPILQILS
STALEDCISV DEEGPSRQQL ALNLLEMIQQ ECYRDDHQKL SYKLVCPVTS MYGTIFTAWR
ILEVMTDSSA ASDWLASVES LLPITAVIPA PAFLLLAHLL VEDKGQNLHQ ILKVTTELAQ
ADSSQVPNLI PVLMFKLGRP LEPILYNDIL YTLPKLGVHK VCIGQILRII QLLGTTPRLR
AVTLRLLTSL WEKQDRVYPE LQRFMAVSDV PSLSVGKEVQ WEKLIAKAAS IRDICKQRPY
QHGADMLAAI SQVLNECTKP DQATPAALVL QGLHALCQAE VVCIRSTWNA LSPKLSCDTR
PLILKTLSEL FSLVPSLTVN TTEYENFKVQ VLSFLWTHTQ NKDPIVANAA YRSLANFTAG
EHTILHLPEK IRPEIPIPEE LDDDEDVEDV DLSVPGSCYL KLLSLTPPLV LPALEEFFTS
LVKQEMVNMP RGIYHSALKG GARSDQGKTV AGIPNFILKM YETNKQPGLK PGLAGGMLFC
YDVSMYQSKD GKPLNRLMAS RGRSFKQTSL ALVHEVHIQL SEWHRAIFLP QAWLAYMNRA
YHAILQGRLG ELELQLKHGK EEPEEVQYKK STAWLWVRDM LTDEITKAAA KESPVVKGNA
LLALSSLAVV VSRHEASLSS DSDGLLEVQP NFLSMKEWVS MVLDTLLVIV DSHYQPRGQL
LSWFYYKSYS GENTASAIAR SAAATALSLL VPVFIISCKE KVEEILNMLT ARLPGKPSAD
ESQAVQIHMG LALGMFLSRL CEEKLSDISG QEMNLLLMKS LDALENCCFD TSLEYNTGCI
LGVGLVLSLM SHSSQMQSRV HVAALLRKLS AHVDDSGSQS RTFQEVLAYT LSCVCTSAFS
AGIIEATEAE DVMNKLRLLV ENSQQTSGFA LALGNIVHGL SVCGHGKAED LGSKLLPAWI
RIVLTEGTPT MLCLAALHGM VALVGSEGDV MQLKSEAIQT SHFQGRLNEV IRTLTQVISV
SGVIGLQSNA VWLLGHLHLS TLSSSQSRAS VPTDYSYLPE SSFIGAAIGF FITGGKKGPE
SVPPSLLKVV MKPIATVGES YQYPPVNWAA LLSPLMRLNF GEEIQQLCLE IMVTQAQSSQ
NAAALLGLWV TPPLIHSLSL NTKRYLLISA PLWIKHISDE QILGFVENLM VAVFKAASPL
GSPELCPSAL HGLSQAMKLP SPAHHLWSLL SEATGKIFDL LPNKIRRKDL ELYISIAKCL
LEMTDDDANR IAQVTKSNIE KAAFVKLYLV SQGRFPLVNL TDMLSVAVQH REKEVLAWMI
LHSLYQARIV SHANTGVLKR MEWLLELMGY IRNVAYQSTS FHNTALDKAL DFFLLIFATA
VVAWADHTAP LLLGLSASWL PWHQENGPAG PVPSFLGRSP MHRVTLQEVL TLLPNSMALL
LQKEPWKEQT QKFIDWLFSI MESPKEALSA QSRDLLKATL LSLRVLPEFK KKAVWTRAYG
W
//
MIM
614606
*RECORD*
*FIELD* NO
614606
*FIELD* TI
*614606 FOCADHESIN; FOCAD
;;KIAA1797
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
read morelibrary, Nagase et al. (2001) cloned FOCAD, which they designated
KIAA1797. The deduced protein contains 1,281 amino acids. RT-PCR
analysis revealed low to moderate FOCAD expression in all adult and
fetal tissues examined except spleen, which showed little to no
expression. Expression was highest in adult brain, liver, kidney, ovary,
and spinal cord and in fetal brain and liver. Low to moderate expression
was detected in all specific adult brain regions examined, with highest
levels in amygdala, cerebellum, caudate nucleus, and hippocampus.
Using real-time RT-PCR, Brockschmidt et al. (2012) detected variable
KIAA1797 expression in all adult and fetal tissues examined. In adult
tissues, expression was highest in brain, followed by testis, muscle,
pancreas, heart, ovary, small intestine, placenta, prostate, thymus,
kidney, colon, liver, lung, spleen, and leukocytes. In fetal tissues,
expression was highest in brain, followed by muscle, kidney, heart,
thymus, lung, liver, and spleen. Kiaa1797 was expressed in granule cell
layer and hilus of mouse dentate gyrus. Immunofluorescence analysis of
human astrocytes revealed colocalization of KIAA1797 with vinculin (VCL;
193065) at focal adhesions at the ends of actin stress fibers. Western
blot analysis revealed KIAA1797 protein at an apparent molecular mass of
about 200 kD in human white matter, cortex, and astrocytes.
GENE STRUCTURE
Brockschmidt et al. (2012) determined that the FOCAD gene contains 46
exons and spans 337.6 kb.
MAPPING
Melton et al. (2010) stated that the FOCAD gene maps to chromosome
9p21.3.
GENE FUNCTION
Using real-time RT-PCR, Brockschmidt et al. (2012) found that expression
of KIAA1797 was reduced in nearly all primary glioblastomas and in all
glioblastoma primary cultures and cell lines examined. Reexpression of
KIAA1797 in the LN18 and U87MG glioblastoma cell lines, which have
homozygous KIAA1797 deletions, led to reduced colony formation and
invasion capacity in vitro and reduced tumor lesions following
implantation in nude mice. Immunoprecipitation analysis of transfected
LN18 cells revealed direct interaction between KIAA1797 and vinculin.
CYTOGENETICS
Using FISH, Brockschmidt et al. (2012) found that the KIAA1797 gene was
disrupted by a t(7;9) translocation and deletion in a human glioblastoma
primary culture. The 5-prime UTR of KIAA1797 was translocated to the
derivative chromosome 7, but the remainder of KIAA1797 was deleted and
absent from the derivative chromosome 9. Array-based comparative genomic
hybridization revealed that 6 of 13 primary glioblastomas had complete
or partial deletions of KIAA1797, and microdeletions involving KIAA1797
were present in 5 of 10 glioblastoma primary cultures and gliobastoma
cell lines. No glioblastomas or gliobastoma cell lines or primary
cultures analyzed showed hypermethylation of the KIAA1797 gene.
*FIELD* RF
1. Brockschmidt, A.; Trost, D.; Peterziel, H.; Zimmermann, K.; Ehrler,
M.; Grassmann, H.; Pfenning, P.-N.; Waha, A.; Wohlleber, D.; Brockschmidt,
F. F.; Jugold, M.; Hoischen, A.; and 10 others: KIAA1797/FOCAD
encodes a novel focal adhesion protein with tumour suppressor function
in gliomas. Brain 135: 1027-1041, 2012.
2. Melton, P. E.; Rutherford, S.; Voruganti, V. S.; Goring, H. H.
H.; Laston, S.; Haack, K.; Comuzzie, A. G.; Dyer, T. D.; Johnson,
M. P.; Kent, J. W., Jr.; Curran, J. E.; Moses, E. K.; and 13 others
: Bivariate genetic association of KIAA1797 with heart rate in American
Indians: the Strong Heart Family Study. Hum. Molec. Genet. 19: 3662-3671,
2010.
3. Nagase, T.; Nakayama, M.; Nakajima, D.; Kikuno, R.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 8: 85-95, 2001.
*FIELD* CD
Patricia A. Hartz: 4/27/2012
*FIELD* ED
mgross: 04/27/2012
*RECORD*
*FIELD* NO
614606
*FIELD* TI
*614606 FOCADHESIN; FOCAD
;;KIAA1797
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
read morelibrary, Nagase et al. (2001) cloned FOCAD, which they designated
KIAA1797. The deduced protein contains 1,281 amino acids. RT-PCR
analysis revealed low to moderate FOCAD expression in all adult and
fetal tissues examined except spleen, which showed little to no
expression. Expression was highest in adult brain, liver, kidney, ovary,
and spinal cord and in fetal brain and liver. Low to moderate expression
was detected in all specific adult brain regions examined, with highest
levels in amygdala, cerebellum, caudate nucleus, and hippocampus.
Using real-time RT-PCR, Brockschmidt et al. (2012) detected variable
KIAA1797 expression in all adult and fetal tissues examined. In adult
tissues, expression was highest in brain, followed by testis, muscle,
pancreas, heart, ovary, small intestine, placenta, prostate, thymus,
kidney, colon, liver, lung, spleen, and leukocytes. In fetal tissues,
expression was highest in brain, followed by muscle, kidney, heart,
thymus, lung, liver, and spleen. Kiaa1797 was expressed in granule cell
layer and hilus of mouse dentate gyrus. Immunofluorescence analysis of
human astrocytes revealed colocalization of KIAA1797 with vinculin (VCL;
193065) at focal adhesions at the ends of actin stress fibers. Western
blot analysis revealed KIAA1797 protein at an apparent molecular mass of
about 200 kD in human white matter, cortex, and astrocytes.
GENE STRUCTURE
Brockschmidt et al. (2012) determined that the FOCAD gene contains 46
exons and spans 337.6 kb.
MAPPING
Melton et al. (2010) stated that the FOCAD gene maps to chromosome
9p21.3.
GENE FUNCTION
Using real-time RT-PCR, Brockschmidt et al. (2012) found that expression
of KIAA1797 was reduced in nearly all primary glioblastomas and in all
glioblastoma primary cultures and cell lines examined. Reexpression of
KIAA1797 in the LN18 and U87MG glioblastoma cell lines, which have
homozygous KIAA1797 deletions, led to reduced colony formation and
invasion capacity in vitro and reduced tumor lesions following
implantation in nude mice. Immunoprecipitation analysis of transfected
LN18 cells revealed direct interaction between KIAA1797 and vinculin.
CYTOGENETICS
Using FISH, Brockschmidt et al. (2012) found that the KIAA1797 gene was
disrupted by a t(7;9) translocation and deletion in a human glioblastoma
primary culture. The 5-prime UTR of KIAA1797 was translocated to the
derivative chromosome 7, but the remainder of KIAA1797 was deleted and
absent from the derivative chromosome 9. Array-based comparative genomic
hybridization revealed that 6 of 13 primary glioblastomas had complete
or partial deletions of KIAA1797, and microdeletions involving KIAA1797
were present in 5 of 10 glioblastoma primary cultures and gliobastoma
cell lines. No glioblastomas or gliobastoma cell lines or primary
cultures analyzed showed hypermethylation of the KIAA1797 gene.
*FIELD* RF
1. Brockschmidt, A.; Trost, D.; Peterziel, H.; Zimmermann, K.; Ehrler,
M.; Grassmann, H.; Pfenning, P.-N.; Waha, A.; Wohlleber, D.; Brockschmidt,
F. F.; Jugold, M.; Hoischen, A.; and 10 others: KIAA1797/FOCAD
encodes a novel focal adhesion protein with tumour suppressor function
in gliomas. Brain 135: 1027-1041, 2012.
2. Melton, P. E.; Rutherford, S.; Voruganti, V. S.; Goring, H. H.
H.; Laston, S.; Haack, K.; Comuzzie, A. G.; Dyer, T. D.; Johnson,
M. P.; Kent, J. W., Jr.; Curran, J. E.; Moses, E. K.; and 13 others
: Bivariate genetic association of KIAA1797 with heart rate in American
Indians: the Strong Heart Family Study. Hum. Molec. Genet. 19: 3662-3671,
2010.
3. Nagase, T.; Nakayama, M.; Nakajima, D.; Kikuno, R.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 8: 85-95, 2001.
*FIELD* CD
Patricia A. Hartz: 4/27/2012
*FIELD* ED
mgross: 04/27/2012