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TPM4

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

TPM4

Identifiers

Aliases

TPM4, HEL-S-108, tropomyosin 4

External IDs

OMIM:600317;MGI:2449202;HomoloGene:100849;GeneCards:TPM4;OMA:TPM4 - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19p13.12-p13.11	Start	16,067,021bp^[1]
Band	19p13.12-p13.11	End	16,103,002bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8\|8 B3.3	Start	72,884,018bp^[2]
Band	8\|8 B3.3	End	72,906,986bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

tendon of biceps brachii

stromal cell of endometrium

right coronary artery

gallbladder

ascending aorta

body of uterus

left uterine tube

smooth muscle tissue

Descending thoracic aorta

tibial arteries

Top expressed in

genital tubercle

tail of embryo

umbilical cord

left lung lobe

mandibular prominence

maxillary prominence

dermis

endothelial cell of lymphatic vessel

vas deferens

abdominal wall

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	calcium ion binding actin binding structural constituent of muscle protein binding metal ion binding identical protein binding protein homodimerization activity protein heterodimerization activity actin filament binding
Cellular component	cytoplasm filamentous actin podosome cytosol muscle thin filament tropomyosin cortical cytoskeleton extracellular exosome cytoskeleton membrane stress fiber focal adhesion actin filament actin cytoskeleton
Biological process	osteoblast differentiation muscle filament sliding muscle contraction actin filament organization
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


7171


326618

Ensembl


ENSG00000167460


ENSMUSG00000031799

UniProt


P67936


Q6IRU2

RefSeq (mRNA)


NM_001145160 NM_003290 NM_001367836 NM_001367837 NM_001367838


NM_001001491

RefSeq (protein)


NP_001138632 NP_003281 NP_001354765 NP_001354766 NP_001354767


NP_001001491

Location (UCSC)

Chr 19: 16.07 – 16.1 Mb

Chr 8: 72.88 – 72.91 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Tropomyosin alpha-4 chain is aprotein that in humans is encoded by theTPM4gene.^[5]^[6]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000167460 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000031799 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Wilton SD, Lim L, Dorosz SD, Gunn HC, Eyre HJ, Callen DF, Laing NG (Jul 1996). "Assignment of the human alpha-tropomyosin gene TPM4 to band 19p13.1 by fluorescence in situ hybridization".Cytogenet Cell Genet.72 (4):294–6.doi:10.1159/000134206.PMID 8641132.
^"Entrez Gene: TPM4 tropomyosin 4".

Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes".Electrophoresis.13 (12):960–9.doi:10.1002/elps.11501301199.PMID 1286667.S2CID 41855774.
MacLeod AR, Talbot K, Smillie LB, Houlker C (1987). "Characterization of a cDNA defining a gene family encoding TM30p1, a human fibroblast tropomyosin".J. Mol. Biol.194 (1):1–10.doi:10.1016/0022-2836(87)90710-8.PMID 3612796.
MacLeod AR, Houlker C, Reinach FC, et al. (1986)."A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism".Proc. Natl. Acad. Sci. U.S.A.82 (23):7835–9.doi:10.1073/pnas.82.23.7835.PMC 390864.PMID 3865200.
Lawrence B, Perez-Atayde A, Hibbard MK, et al. (2000)."TPM3-ALK and TPM4-ALK oncogenes in inflammatory myofibroblastic tumors".Am. J. Pathol.157 (2):377–84.doi:10.1016/S0002-9440(10)64550-6.PMC 1850130.PMID 10934142.
Meech SJ, McGavran L, Odom LF, et al. (2001)."Unusual childhood extramedullary hematologic malignancy with natural killer cell properties that contains tropomyosin 4--anaplastic lymphoma kinase gene fusion".Blood.98 (4):1209–16.doi:10.1182/blood.V98.4.1209.PMID 11493472.
Yi J, Kloeker S, Jensen CC, et al. (2002)."Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers".J. Biol. Chem.277 (11):9580–9.doi:10.1074/jbc.M106922200.PMID 11782456.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003)."Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences".Proc. Natl. Acad. Sci. U.S.A.99 (26):16899–903.Bibcode:2002PNAS...9916899M.doi:10.1073/pnas.242603899.PMC 139241.PMID 12477932.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides".Nat. Biotechnol.21 (5):566–9.doi:10.1038/nbt810.PMID 12665801.S2CID 23783563.
Ota T, Suzuki Y, Nishikawa T, et al. (2004)."Complete sequencing and characterization of 21,243 full-length human cDNAs".Nat. Genet.36 (1):40–5.doi:10.1038/ng1285.PMID 14702039.
Lin KT, Lu RM, Tarn WY (2004)."The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo".Mol. Cell. Biol.24 (20):9176–85.doi:10.1128/MCB.24.20.9176-9185.2004.PMC 517884.PMID 15456888.
Gerhard DS, Wagner L, Feingold EA, et al. (2004)."The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)".Genome Res.14 (10B):2121–7.doi:10.1101/gr.2596504.PMC 528928.PMID 15489334.
Bruneel A, Labas V, Mailloux A, et al. (2006). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis".Proteomics.5 (15):3876–84.doi:10.1002/pmic.200401239.PMID 16130169.S2CID 26007149.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network".Nature.437 (7062):1173–8.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.

Proteins of thecytoskeleton

Human

Microfilaments
andABPs

Myofilament

Actins	A1 A2 B C1 G1 G2
Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1
Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

Intermediate
filaments

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 9 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 6C 7 8
Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86
Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80
Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Microtubules
andMAPs

Tubulins	TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 TUBB TUBB1 TUBB2A TUBB2B TUBB2C TUBB3 TUBB4 TUBB4Q TUBB6 TUBB8 TUBG1 TUBG2 TUBGCP2 TUBGCP3 TUBGCP4 TUBGCP5 TUBGCP6 TUBD1 TUBE1
MAPs	EB1 EB2 EB3 MAP1A MAP1B MAP2 MAP4
Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3
Dyneins	axonemal:DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic:DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3
Microtubule organising proteins	CAMSAP1 CAMSAP2 CAMSAP3 Centrin 1 Centrin 2 Centrin 3 PCM1
Microtubule severing proteins	Katanin Spastin
Other	Tau protein Dynactin DCTN1 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3