Full text data of TMOD4
TMOD4
[Confidence: low (only semi-automatic identification from reviews)]
Tropomodulin-4 (Skeletal muscle tropomodulin; Sk-Tmod)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tropomodulin-4 (Skeletal muscle tropomodulin; Sk-Tmod)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NZQ9
ID TMOD4_HUMAN Reviewed; 345 AA.
AC Q9NZQ9; Q5JR83; Q8WVL3; Q9UKH2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Tropomodulin-4;
DE AltName: Full=Skeletal muscle tropomodulin;
DE Short=Sk-Tmod;
GN Name=TMOD4;
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 [MRNA].
RX PubMed=10497209; DOI=10.1074/jbc.274.40.28466;
RA Almenar-Queralt A., Lee A., Conley C.A., Ribas de Pouplana L.,
RA Fowler V.M.;
RT "Identification of a novel tropomodulin isoform, skeletal
RT tropomodulin, that caps actin filament pointed ends in fast skeletal
RT muscle.";
RL J. Biol. Chem. 274:28466-28475(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10662549; DOI=10.1006/geno.1999.6061;
RA Cox P.R., Zoghbi H.Y.;
RT "Sequencing, expression analysis, and mapping of three unique human
RT tropomodulin genes and their mouse orthologs.";
RL Genomics 63:97-107(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Durling H.J., Laing N.G.;
RT "Homo sapiens tropomodulin 4 (TMOD4) genomic sequence.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cox P.R., Siddique T., Zoghbi H.Y.;
RT "Genomic organization of tropomodulins 2 and 4 and intergenic splicing
RT of YL-1 and TMOD4.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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).
CC -!- FUNCTION: Blocks the elongation and depolymerization of the actin
CC filaments at the pointed end. The Tmod/TM complex contributes to
CC the formation of the short actin protofilament, which in turn
CC defines the geometry of the membrane skeleton.
CC -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle.
CC -!- SIMILARITY: Belongs to the tropomodulin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF165217; AAF01277.1; -; mRNA.
DR EMBL; AF177173; AAF31672.1; -; mRNA.
DR EMBL; AF321183; AAK06765.1; -; Genomic_DNA.
DR EMBL; AF393375; AAM73676.1; -; Genomic_DNA.
DR EMBL; AL592424; CAI16383.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53465.1; -; Genomic_DNA.
DR EMBL; BC017810; AAH17810.1; -; mRNA.
DR RefSeq; NP_037485.2; NM_013353.2.
DR UniGene; Hs.709681; -.
DR ProteinModelPortal; Q9NZQ9; -.
DR SMR; Q9NZQ9; 179-343.
DR STRING; 9606.ENSP00000295314; -.
DR PhosphoSite; Q9NZQ9; -.
DR DMDM; 23396885; -.
DR PaxDb; Q9NZQ9; -.
DR PRIDE; Q9NZQ9; -.
DR DNASU; 29765; -.
DR Ensembl; ENST00000295314; ENSP00000295314; ENSG00000163157.
DR GeneID; 29765; -.
DR KEGG; hsa:29765; -.
DR UCSC; uc001exb.3; human.
DR CTD; 29765; -.
DR GeneCards; GC01M151142; -.
DR HGNC; HGNC:11874; TMOD4.
DR HPA; HPA028203; -.
DR MIM; 605834; gene.
DR neXtProt; NX_Q9NZQ9; -.
DR PharmGKB; PA36575; -.
DR eggNOG; NOG329422; -.
DR HOGENOM; HOG000261624; -.
DR HOVERGEN; HBG056172; -.
DR InParanoid; Q9NZQ9; -.
DR KO; K10370; -.
DR OMA; TNTYVRS; -.
DR PhylomeDB; Q9NZQ9; -.
DR GeneWiki; TMOD4; -.
DR GenomeRNAi; 29765; -.
DR NextBio; 52264; -.
DR PRO; PR:Q9NZQ9; -.
DR ArrayExpress; Q9NZQ9; -.
DR Bgee; Q9NZQ9; -.
DR CleanEx; HS_TMOD4; -.
DR Genevestigator; Q9NZQ9; -.
DR GO; GO:0005865; C:striated muscle thin filament; IEA:Ensembl.
DR GO; GO:0005523; F:tropomyosin binding; TAS:ProtInc.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR InterPro; IPR004934; Tropomodulin.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Polymorphism; Reference proteome.
FT CHAIN 1 345 Tropomodulin-4.
FT /FTId=PRO_0000186136.
FT VARIANT 336 336 N -> S (in dbSNP:rs11800088).
FT /FTId=VAR_052400.
FT CONFLICT 283 283 T -> I (in Ref. 1; AAF01277).
FT CONFLICT 309 309 C -> R (in Ref. 7; AAH17810).
SQ SEQUENCE 345 AA; 39335 MW; 3ACE2692EF52E2CB CRC64;
MSSYQKELEK YRDIDEDEIL RTLSPEELEQ LDCELQEMDP ENMLLPAGLR QRDQTKKSPT
GPLDREALLQ YLEQQALEVK ERDDLVPFTG EKKGKPYIQP KREIPAEEQI TLEPELEEAL
AHATDAEMCD IAAILDMYTL MSNKQYYDAL CSGEICNTEG ISSVVQPDKY KPVPDEPPNP
TNIEEILKRV RSNDKELEEV NLNNIQDIPI PMLSELCEAM KANTYVRSFS LVATRSGDPI
ANAVADMLRE NRSLQSLNIE SNFISSTGLM AVLKAVRENA TLTELRVDNQ RQWPGDAVEM
EMATVLEQCP SIVRFGYHFT QQGPRARAAQ AMTRNNELRR QQKKR
//
ID TMOD4_HUMAN Reviewed; 345 AA.
AC Q9NZQ9; Q5JR83; Q8WVL3; Q9UKH2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Tropomodulin-4;
DE AltName: Full=Skeletal muscle tropomodulin;
DE Short=Sk-Tmod;
GN Name=TMOD4;
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 [MRNA].
RX PubMed=10497209; DOI=10.1074/jbc.274.40.28466;
RA Almenar-Queralt A., Lee A., Conley C.A., Ribas de Pouplana L.,
RA Fowler V.M.;
RT "Identification of a novel tropomodulin isoform, skeletal
RT tropomodulin, that caps actin filament pointed ends in fast skeletal
RT muscle.";
RL J. Biol. Chem. 274:28466-28475(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10662549; DOI=10.1006/geno.1999.6061;
RA Cox P.R., Zoghbi H.Y.;
RT "Sequencing, expression analysis, and mapping of three unique human
RT tropomodulin genes and their mouse orthologs.";
RL Genomics 63:97-107(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Durling H.J., Laing N.G.;
RT "Homo sapiens tropomodulin 4 (TMOD4) genomic sequence.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cox P.R., Siddique T., Zoghbi H.Y.;
RT "Genomic organization of tropomodulins 2 and 4 and intergenic splicing
RT of YL-1 and TMOD4.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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).
CC -!- FUNCTION: Blocks the elongation and depolymerization of the actin
CC filaments at the pointed end. The Tmod/TM complex contributes to
CC the formation of the short actin protofilament, which in turn
CC defines the geometry of the membrane skeleton.
CC -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle.
CC -!- SIMILARITY: Belongs to the tropomodulin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF165217; AAF01277.1; -; mRNA.
DR EMBL; AF177173; AAF31672.1; -; mRNA.
DR EMBL; AF321183; AAK06765.1; -; Genomic_DNA.
DR EMBL; AF393375; AAM73676.1; -; Genomic_DNA.
DR EMBL; AL592424; CAI16383.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53465.1; -; Genomic_DNA.
DR EMBL; BC017810; AAH17810.1; -; mRNA.
DR RefSeq; NP_037485.2; NM_013353.2.
DR UniGene; Hs.709681; -.
DR ProteinModelPortal; Q9NZQ9; -.
DR SMR; Q9NZQ9; 179-343.
DR STRING; 9606.ENSP00000295314; -.
DR PhosphoSite; Q9NZQ9; -.
DR DMDM; 23396885; -.
DR PaxDb; Q9NZQ9; -.
DR PRIDE; Q9NZQ9; -.
DR DNASU; 29765; -.
DR Ensembl; ENST00000295314; ENSP00000295314; ENSG00000163157.
DR GeneID; 29765; -.
DR KEGG; hsa:29765; -.
DR UCSC; uc001exb.3; human.
DR CTD; 29765; -.
DR GeneCards; GC01M151142; -.
DR HGNC; HGNC:11874; TMOD4.
DR HPA; HPA028203; -.
DR MIM; 605834; gene.
DR neXtProt; NX_Q9NZQ9; -.
DR PharmGKB; PA36575; -.
DR eggNOG; NOG329422; -.
DR HOGENOM; HOG000261624; -.
DR HOVERGEN; HBG056172; -.
DR InParanoid; Q9NZQ9; -.
DR KO; K10370; -.
DR OMA; TNTYVRS; -.
DR PhylomeDB; Q9NZQ9; -.
DR GeneWiki; TMOD4; -.
DR GenomeRNAi; 29765; -.
DR NextBio; 52264; -.
DR PRO; PR:Q9NZQ9; -.
DR ArrayExpress; Q9NZQ9; -.
DR Bgee; Q9NZQ9; -.
DR CleanEx; HS_TMOD4; -.
DR Genevestigator; Q9NZQ9; -.
DR GO; GO:0005865; C:striated muscle thin filament; IEA:Ensembl.
DR GO; GO:0005523; F:tropomyosin binding; TAS:ProtInc.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR InterPro; IPR004934; Tropomodulin.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Polymorphism; Reference proteome.
FT CHAIN 1 345 Tropomodulin-4.
FT /FTId=PRO_0000186136.
FT VARIANT 336 336 N -> S (in dbSNP:rs11800088).
FT /FTId=VAR_052400.
FT CONFLICT 283 283 T -> I (in Ref. 1; AAF01277).
FT CONFLICT 309 309 C -> R (in Ref. 7; AAH17810).
SQ SEQUENCE 345 AA; 39335 MW; 3ACE2692EF52E2CB CRC64;
MSSYQKELEK YRDIDEDEIL RTLSPEELEQ LDCELQEMDP ENMLLPAGLR QRDQTKKSPT
GPLDREALLQ YLEQQALEVK ERDDLVPFTG EKKGKPYIQP KREIPAEEQI TLEPELEEAL
AHATDAEMCD IAAILDMYTL MSNKQYYDAL CSGEICNTEG ISSVVQPDKY KPVPDEPPNP
TNIEEILKRV RSNDKELEEV NLNNIQDIPI PMLSELCEAM KANTYVRSFS LVATRSGDPI
ANAVADMLRE NRSLQSLNIE SNFISSTGLM AVLKAVRENA TLTELRVDNQ RQWPGDAVEM
EMATVLEQCP SIVRFGYHFT QQGPRARAAQ AMTRNNELRR QQKKR
//
MIM
605834
*RECORD*
*FIELD* NO
605834
*FIELD* TI
*605834 TROPOMODULIN 4; TMOD4
*FIELD* TX
DESCRIPTION
Tropomodulin-4 is a member of a family of proteins that cap the pointed
read moreends of actin filaments (summary by Cox et al., 2001).
CLONING
Using EST database searches, sequencing, and RT-PCR, Cox and Zoghbi
(2000) cloned human and mouse cDNAs corresponding to the TMOD4 gene.
Human TMOD4 encodes a deduced 345-amino acid protein. Northern blot
analysis on human tissues detected a prominent 1.3- to 1.5-kb transcript
in skeletal muscle. Three faint transcripts were detected: a 6.8-kb
transcript in heart and skeletal muscle, and 2.4 and 3.0 transcripts in
skeletal muscle.
GENE STRUCTURE
Cox et al. (2001) determined that the TMOD4 gene contains 9 coding exons
and spans 4.7 kb. They also found that the YL1 gene (600607)
intergenically splices into TMOD4.
MAPPING
By radiation hybrid analysis, Cox and Zoghbi (2000) mapped the TMOD4
gene to human chromosome 1q12 and the mouse ortholog to a region of
syntenic homology on chromosome 3.
*FIELD* RF
1. Cox, P. R.; Siddique, T.; Zoghbi, H.: Genomic organization of
tropomodulins 2 and 4 and unusual intergenic and intraexonic splicing
of YL-1 and tropomodulin 4. BMC Genomics 2: 7, 2001. Note: Electronic
Article.
2. Cox, P. R.; Zoghbi, H. Y.: Sequencing, expression analysis, and
mapping of three unique human tropomodulin genes and their mouse orthologs. Genomics 63:
97-107, 2000.
*FIELD* CD
Carol A. Bocchini: 4/11/2001
*FIELD* ED
carol: 03/13/2012
carol: 12/14/2011
mcapotos: 4/12/2001
carol: 4/12/2001
*RECORD*
*FIELD* NO
605834
*FIELD* TI
*605834 TROPOMODULIN 4; TMOD4
*FIELD* TX
DESCRIPTION
Tropomodulin-4 is a member of a family of proteins that cap the pointed
read moreends of actin filaments (summary by Cox et al., 2001).
CLONING
Using EST database searches, sequencing, and RT-PCR, Cox and Zoghbi
(2000) cloned human and mouse cDNAs corresponding to the TMOD4 gene.
Human TMOD4 encodes a deduced 345-amino acid protein. Northern blot
analysis on human tissues detected a prominent 1.3- to 1.5-kb transcript
in skeletal muscle. Three faint transcripts were detected: a 6.8-kb
transcript in heart and skeletal muscle, and 2.4 and 3.0 transcripts in
skeletal muscle.
GENE STRUCTURE
Cox et al. (2001) determined that the TMOD4 gene contains 9 coding exons
and spans 4.7 kb. They also found that the YL1 gene (600607)
intergenically splices into TMOD4.
MAPPING
By radiation hybrid analysis, Cox and Zoghbi (2000) mapped the TMOD4
gene to human chromosome 1q12 and the mouse ortholog to a region of
syntenic homology on chromosome 3.
*FIELD* RF
1. Cox, P. R.; Siddique, T.; Zoghbi, H.: Genomic organization of
tropomodulins 2 and 4 and unusual intergenic and intraexonic splicing
of YL-1 and tropomodulin 4. BMC Genomics 2: 7, 2001. Note: Electronic
Article.
2. Cox, P. R.; Zoghbi, H. Y.: Sequencing, expression analysis, and
mapping of three unique human tropomodulin genes and their mouse orthologs. Genomics 63:
97-107, 2000.
*FIELD* CD
Carol A. Bocchini: 4/11/2001
*FIELD* ED
carol: 03/13/2012
carol: 12/14/2011
mcapotos: 4/12/2001
carol: 4/12/2001