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Reviewed, UniProtKB/Swiss-Prot P67936 (TPM4_HUMAN)

Last modified November 25, 2008. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tropomyosin alpha-4 chain
Alternative name(s):
    Tropomyosin-4
    TM30p1
Gene names
Name: TPM4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Subcellular location

Cytoplasmcytoskeleton.

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 componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandActin-binding
   Molecular functionMuscle protein
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processcell motion

Traceable author statement. Source: UniProtKB

   Cellular componentmuscle thin filament tropomyosin

Traceable author statement. Source: ProtInc

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of muscle

Traceable author statement. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 248247Tropomyosin alpha-4 chain
PRO_0000205635

Regions

Coiled coil2 – 248247 By similarity

Amino acid modifications

Modified residue21N-acetylalanine
Modified residue1261Phosphotyrosine

Natural variations

Alternative sequence1 – 4444MAGLN…ERREK → MEAIKKKMQMLKLDKENAID RAEQAEADKKAAEDKCKQVE EELTHLQKKLKGTEDELDKY SEDLKDAQEKLELTEKKASD in isoform 2.
VSP_006611
Natural variant2041E → Q in a breast cancer sample; somatic mutation.
VAR_036535

Experimental info

Sequence conflict591V → F in AAH02827. Ref.3
Sequence conflict1521L → S in AAA36774. Ref.7
Sequence conflict162 – 1632KN → RT in AAA36774. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5D5CDF6BF76552A8

FASTA24828,522
        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 

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: 29C0F6ADF4C87F0C
Show »

28432,723

References

« Hide '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: 3612796] [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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Ovarian carcinoma.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye, Placenta and Testis.
[4]"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: 12665801] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Tissue: Platelet.
[5]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.
[6]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 56-65 AND 132-142, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[7]"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: 3865200] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-248.
Tissue: Fibroblast.
[8]"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: 1286667] [Abstract]
Cited for: PROTEIN SEQUENCE OF 177-189 AND 228-247.
Tissue: Keratinocyte.
[9]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-126, MASS SPECTROMETRY.
[10]"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. expand/collapse author list , 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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-204.

Cross-references

Sequence databases

X05276 mRNA. Translation: CAA28888.1.
AK023385 mRNA. Translation: BAB14554.1.
BC002827 mRNA. Translation: AAH02827.1.
BC037576 mRNA. Translation: AAH37576.1.
BC067225 mRNA. Translation: AAH67225.1.
M12127 mRNA. Translation: AAA36774.1.
PIRS07282.
RefSeqNP_003281.1.
UniGeneHs.631618

3D structure databases

HSSPHSSP built from PDB template 1C1G based on UniProtKB P42639.
ModBaseSearch...

PTM databases

PhosphoSiteP67936.

2-D gel databases

Aarhus/Ghent-2DPAGE9122. IEF.
DOSAC-COBS-2DPAGEP67936.
OGPP07226.

Proteomic databases

PeptideAtlasP67936.

Genome annotation databases

EnsemblENSG00000167460. Homo sapiens. [Contig view]
GeneID7171.
KEGGhsa:7171.

Organism-specific databases

H-InvDBHIX0014859.
HIX0022609.
HIX0055475.
HGNCHGNC:12013. TPM4.
HPACAB004685.
MIM600317. gene.
PharmGKBPA36693.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP67936.

Gene expression databases

ArrayExpressP67936.
CleanExHS_TPM4.
GermOnlineENSG00000167460. Homo sapiens.

Family and domain databases

InterProIPR000533. Tropomyosin.
[Graphical view]
PfamPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSPR00194. TROPOMYOSIN.
PROSITEPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP67936.
NextBio28104.
SOURCESearch...

Entry information

Entry nameTPM4_HUMAN
AccessionPrimary (citable) accession number: P67936
Secondary accession number(s): P07226 expand/collapse secondary AC list , Q15659, Q9BU85, Q9H8Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 49 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents