P67936 (TPM4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tropomyosin alpha-4 chain

Alternative name(s):
TM30p1
Tropomyosin-4

Gene names

Name:

TPM4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium. Ref.8
Subunit structure	Heterodimer of an alpha and a beta chain By similarity.
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Detected in cardiac tissue and platelets, the form found in cardiac tissue is a higher molecular weight than the form found in platelets. Expressed at higher levels in the platelets of hypertensive patients with cardiac hypertrophy than in the platelets of hypertensive patients without cardiac hypertrophy (at protein level). Ref.8
Domain	The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.
Sequence similarities	Belongs to the tropomyosin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	Actin-binding Calcium Metal-binding
Molecular function	Muscle protein
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	muscle filament sliding Traceable author statement. Source: Reactome response to oxidative stress Inferred from expression pattern PubMed 16551573. Source: BHF-UCL
Cellular_component	cortical cytoskeleton Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome filamentous actin Inferred from electronic annotation. Source: Compara muscle thin filament tropomyosin Traceable author statement PubMed 8641132. Source: ProtInc podosome Inferred from electronic annotation. Source: Compara stress fiber Inferred from direct assay PubMed 16236705. Source: MGI
Molecular_function	calcium ion binding Non-traceable author statement Ref.8. Source: UniProtKB structural constituent of muscle Traceable author statement PubMed 8641132. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P67936-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P67936-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MAGLNSLEAV...LDGERERREK → MEAIKKKMQM...LELTEKKASD

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6 Ref.7
	Chain	2 – 248	247	Tropomyosin alpha-4 chain		PRO_0000205635
Regions
	Coiled coil	2 – 248	247	By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	177	1	N6-acetyllysine Ref.12
	Modified residue	215	1	N6-acetyllysine Ref.12
Natural variations
	Alternative sequence	1 – 44	44	MAGLN…ERREK → MEAIKKKMQMLKLDKENAID RAEQAEADKKAAEDKCKQVE EELTHLQKKLKGTEDELDKY SEDLKDAQEKLELTEKKASD in isoform 2.		VSP_006611
	Natural variant	204	1	E → Q in a breast cancer sample; somatic mutation. Ref.14		VAR_036535
Experimental info
	Sequence conflict	59	1	V → F in AAH02827. Ref.5
	Sequence conflict	152	1	L → S in AAA36774. Ref.10
	Sequence conflict	162 – 163	2	KN → RT in AAA36774. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5D5CDF6BF76552A8	FASTA	248	28,522
	10 20 30 40 50 60 MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA ALNRRIQLVE 70 80 90 100 110 120 EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK DEEKMEIQEM QLKEAKHIAE 130 140 150 160 170 180 EADRKYEEVA RKLVILEGEL ERAEERAEVS ELKCGDLEEE LKNVTNNLKS LEAASEKYSE 190 200 210 220 230 240 KEDKYEEEIK LLSDKLKEAE TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI
	Isoform 2 [UniParc] [UniParc]. Checksum: 29C0F6ADF4C87F0C	FASTA	284	32,723
	10 20 30 40 50 60 MEAIKKKMQM LKLDKENAID RAEQAEADKK AAEDKCKQVE EELTHLQKKL KGTEDELDKY 70 80 90 100 110 120 SEDLKDAQEK LELTEKKASD AEGDVAALNR RIQLVEEELD RAQERLATAL QKLEEAEKAA 130 140 150 160 170 180 DESERGMKVI ENRAMKDEEK MEIQEMQLKE AKHIAEEADR KYEEVARKLV ILEGELERAE 190 200 210 220 230 240 ERAEVSELKC GDLEEELKNV TNNLKSLEAA SEKYSEKEDK YEEEIKLLSD KLKEAETRAE 250 260 270 280 FAERTVAKLE KTIDDLEEKL AQAKEENVGL HQTLDQTLNE LNCI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a cDNA defining a gene family encoding TM30p1, a human fibroblast tropomyosin." McLeod A.R., Talbot K., Smillie L.B., Houlker C. J. Mol. Biol. 194:1-10(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Fibroblast.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Ovarian carcinoma and Tongue.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye, Placenta and Testis.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-12. Tissue: Platelet.
[7]	Bienvenut W.V., Claeys D. Submitted (NOV-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11; 45-54; 56-69; 77-89; 133-146 AND 216-223, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Platelet.
[8]	"The calcium binding protein tropomyosin in human platelets and cardiac tissue: elevation in hypertensive cardiac hypertrophy." Crabos M., Yamakado T., Heizmann C.W., Cerletti N., Buehler F.R., Erne P. Eur. J. Clin. Invest. 21:472-478(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 9-31; 44-61; 89-95; 205-214 AND 231-243 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Tissue: Platelet.
[9]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 13-27; 45-82; 132-142; 154-169 AND 216-228, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]	"A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism." MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K., Modi G., Walsh F.S. Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-248. Tissue: Fibroblast.
[11]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 177-189 AND 228-247. Tissue: Keratinocyte.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 AND LYS-215, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-204.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	X05276 mRNA. Translation: CAA28888.1. AK023385 mRNA. Translation: BAB14554.1. AK315076 mRNA. Translation: BAG37545.1. BT019634 mRNA. Translation: AAV38440.1. CH471106 Genomic DNA. Translation: EAW84521.1. BC002827 mRNA. Translation: AAH02827.1. BC037576 mRNA. Translation: AAH37576.1. BC067225 mRNA. Translation: AAH67225.1. M12127 mRNA. Translation: AAA36774.1.
IPI	IPI00010779. IPI00216975.
PIR	S07282.
RefSeq	NP_001138632.1. NM_001145160.1. NP_003281.1. NM_003290.2.
UniGene	Hs.631618.
3D structure databases
ProteinModelPortal	P67936.
ModBase	Search...
Protein-protein interaction databases
IntAct	P67936. 4 interactions.
PTM databases
PhosphoSite	P67936.
Polymorphism databases
DMDM	54039751.
2D gel databases
DOSAC-COBS-2DPAGE	P67936.
OGP	P07226.
Proteomic databases
PaxDb	P67936.
PeptideAtlas	P67936.
PRIDE	P67936.
Protocols and materials databases
DNASU	7171.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000300933; ENSP00000300933; ENSG00000167460. ENST00000344824; ENSP00000345230; ENSG00000167460. ENST00000538887; ENSP00000439135; ENSG00000167460.
GeneID	7171.
KEGG	hsa:7171.
UCSC	uc002ndi.2. human. uc002ndj.2. human.
Organism-specific databases
CTD	7171.
GeneCards	GC19P016178.
H-InvDB	HIX0022609.
HGNC	HGNC:12013. TPM4.
HPA	CAB004685.
MIM	600317. gene.
neXtProt	NX_P67936.
PharmGKB	PA36693.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG304012.
HOVERGEN	HBG107404.
KO	K10375.
OMA	EKCKQVE.
OrthoDB	EOG4TXBSM.
Enzyme and pathway databases
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P67936.
Bgee	P67936.
CleanEx	HS_TPM4.
Genevestigator	P67936.
GermOnline	ENSG00000167460. Homo sapiens.
Family and domain databases
InterPro	IPR000533. Tropomyosin. [Graphical view]
Pfam	PF00261. Tropomyosin. 1 hit. [Graphical view]
PRINTS	PR00194. TROPOMYOSIN.
PROSITE	PS00326. TROPOMYOSIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TPM4. human.
GenomeRNAi	7171.
NextBio	28104.
SOURCE	Search...

Entry information

Entry name

TPM4_HUMAN

Accession

Primary (citable) accession number: P67936
Secondary accession number(s): P07226 , Q15659, Q5U0D9, Q9BU85, Q9H8Q3, Q9UCS1, Q9UCS2, Q9UCS3, Q9UCS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.