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Protein

Tropomodulin-2

Gene

TMOD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity).By similarity

GO - Molecular functioni

  • tropomyosin binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomodulin-2
Alternative name(s):
Neuronal tropomodulin
Short name:
N-Tmod
Gene namesi
Name:TMOD2
Synonyms:NTMOD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:11872. TMOD2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36573.

Polymorphism and mutation databases

BioMutaiTMOD2.
DMDMi23396886.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Tropomodulin-2PRO_0000186131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NZR1.
MaxQBiQ9NZR1.
PaxDbiQ9NZR1.
PeptideAtlasiQ9NZR1.
PRIDEiQ9NZR1.

2D gel databases

UCD-2DPAGEQ9NZR1.

PTM databases

iPTMnetiQ9NZR1.
PhosphoSiteiQ9NZR1.

Expressioni

Tissue specificityi

Neuronal-tissue specific.1 Publication

Gene expression databases

BgeeiQ9NZR1.
CleanExiHS_TMOD2.
ExpressionAtlasiQ9NZR1. baseline and differential.
GenevisibleiQ9NZR1. HS.

Organism-specific databases

HPAiHPA041365.

Interactioni

Subunit structurei

Binds to the N-terminus of tropomyosin and to actin.

GO - Molecular functioni

  • tropomyosin binding Source: ProtInc

Protein-protein interaction databases

BioGridi118900. 27 interactions.
STRINGi9606.ENSP00000249700.

Structurei

3D structure databases

ProteinModelPortaliQ9NZR1.
SMRiQ9NZR1. Positions 61-101, 181-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tropomodulin family.Curated

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ9NZR1.
KOiK10370.
OMAiVNNPKFD.
OrthoDBiEOG7D59Q1.
PhylomeDBiQ9NZR1.
TreeFamiTF315841.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR004934. TMOD.
IPR030130. TMOD2.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF15. PTHR10901:SF15. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NZR1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALPFQKELE KYKNIDEDEL LGKLSEEELK QLENVLDDLD PESAMLPAGF
60 70 80 90 100
RQKDQTQKAA TGPFDREHLL MYLEKEALEQ KDREDFVPFT GEKKGRVFIP
110 120 130 140 150
KEKPIETRKE EKVTLDPELE EALASASDTE LYDLAAVLGV HNLLNNPKFD
160 170 180 190 200
EETANNKGGK GPVRNVVKGE KVKPVFEEPP NPTNVEISLQ QMKANDPSLQ
210 220 230 240 250
EVNLNNIKNI PIPTLREFAK ALETNTHVKK FSLAATRSND PVAIAFADML
260 270 280 290 300
KVNKTLTSLN IESNFITGTG ILALVEALKE NDTLTEIKID NQRQQLGTAV
310 320 330 340 350
EMEIAQMLEE NSRILKFGYQ FTKQGPRTRV AAAITKNNDL VRKKRVEADR

R
Length:351
Mass (Da):39,595
Last modified:October 1, 2000 - v1
Checksum:i547004595FCD6385
GO
Isoform 2 (identifier: Q9NZR1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-244: Missing.

Show »
Length:315
Mass (Da):35,648
Checksum:iEA9F902EA74B4ADD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2841L → M in BAG57227 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631P → A.
Corresponds to variant rs34791185 [ dbSNP | Ensembl ].
VAR_052399

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei209 – 24436Missing in isoform 2. 1 PublicationVSP_041506Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177169 mRNA. Translation: AAF31668.1.
AK293823 mRNA. Translation: BAG57227.1.
AC026770 Genomic DNA. No translation available.
AC090971 Genomic DNA. No translation available.
BC064961 mRNA. Translation: AAH64961.1.
CCDSiCCDS10144.1. [Q9NZR1-1]
CCDS45260.1. [Q9NZR1-2]
RefSeqiNP_001136357.1. NM_001142885.1. [Q9NZR1-2]
NP_055363.1. NM_014548.3. [Q9NZR1-1]
UniGeneiHs.513734.

Genome annotation databases

EnsembliENST00000249700; ENSP00000249700; ENSG00000128872. [Q9NZR1-1]
ENST00000435126; ENSP00000404590; ENSG00000128872. [Q9NZR1-2]
GeneIDi29767.
KEGGihsa:29767.
UCSCiuc002abk.4. human. [Q9NZR1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177169 mRNA. Translation: AAF31668.1.
AK293823 mRNA. Translation: BAG57227.1.
AC026770 Genomic DNA. No translation available.
AC090971 Genomic DNA. No translation available.
BC064961 mRNA. Translation: AAH64961.1.
CCDSiCCDS10144.1. [Q9NZR1-1]
CCDS45260.1. [Q9NZR1-2]
RefSeqiNP_001136357.1. NM_001142885.1. [Q9NZR1-2]
NP_055363.1. NM_014548.3. [Q9NZR1-1]
UniGeneiHs.513734.

3D structure databases

ProteinModelPortaliQ9NZR1.
SMRiQ9NZR1. Positions 61-101, 181-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118900. 27 interactions.
STRINGi9606.ENSP00000249700.

PTM databases

iPTMnetiQ9NZR1.
PhosphoSiteiQ9NZR1.

Polymorphism and mutation databases

BioMutaiTMOD2.
DMDMi23396886.

2D gel databases

UCD-2DPAGEQ9NZR1.

Proteomic databases

EPDiQ9NZR1.
MaxQBiQ9NZR1.
PaxDbiQ9NZR1.
PeptideAtlasiQ9NZR1.
PRIDEiQ9NZR1.

Protocols and materials databases

DNASUi29767.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249700; ENSP00000249700; ENSG00000128872. [Q9NZR1-1]
ENST00000435126; ENSP00000404590; ENSG00000128872. [Q9NZR1-2]
GeneIDi29767.
KEGGihsa:29767.
UCSCiuc002abk.4. human. [Q9NZR1-1]

Organism-specific databases

CTDi29767.
GeneCardsiTMOD2.
HGNCiHGNC:11872. TMOD2.
HPAiHPA041365.
MIMi602928. gene.
neXtProtiNX_Q9NZR1.
PharmGKBiPA36573.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ9NZR1.
KOiK10370.
OMAiVNNPKFD.
OrthoDBiEOG7D59Q1.
PhylomeDBiQ9NZR1.
TreeFamiTF315841.

Enzyme and pathway databases

ReactomeiR-HSA-390522. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSiTMOD2. human.
GeneWikiiTMOD2.
GenomeRNAii29767.
PROiQ9NZR1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZR1.
CleanExiHS_TMOD2.
ExpressionAtlasiQ9NZR1. baseline and differential.
GenevisibleiQ9NZR1. HS.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR004934. TMOD.
IPR030130. TMOD2.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF15. PTHR10901:SF15. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs."
    Cox P.R., Zoghbi H.Y.
    Genomics 63:97-107(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  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] (ISOFORM 2).
    Tissue: Cerebellum.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Retina.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 14-23; 82-93; 194-208 AND 238-251, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.

Entry informationi

Entry nameiTMOD2_HUMAN
AccessioniPrimary (citable) accession number: Q9NZR1
Secondary accession number(s): B4DEW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.