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P51667

- MLRV_MOUSE

UniProt

P51667 - MLRV_MOUSE

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Protein

Myosin regulatory light chain 2, ventricular/cardiac muscle isoform

Gene

Myl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi37 – 4812Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: MGI

GO - Biological processi

  1. cardiac muscle contraction Source: MGI
  2. cardiac myofibril assembly Source: MGI
  3. heart contraction Source: MGI
  4. heart development Source: MGI
  5. heart morphogenesis Source: MGI
  6. muscle cell fate specification Source: MGI
  7. muscle fiber development Source: MGI
  8. negative regulation of cell growth Source: Ensembl
  9. post-embryonic development Source: MGI
  10. ventricular cardiac muscle tissue morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
Short name:
MLC-2
Short name:
MLC-2v
Gene namesi
Name:Myl2
Synonyms:Mylpc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:97272. Myl2.

Subcellular locationi

CytoplasmmyofibrilsarcomereA band By similarity

GO - Cellular componenti

  1. myofibril Source: MGI
  2. myosin complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 166165Myosin regulatory light chain 2, ventricular/cardiac muscle isoformPRO_0000198728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N,N-trimethylalanine1 Publication

Post-translational modificationi

N-terminus is methylated by METTL11A/NTM1.1 Publication
Phosphorylated by MYLK3.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP51667.
PaxDbiP51667.
PRIDEiP51667.

PTM databases

PhosphoSiteiP51667.

Expressioni

Gene expression databases

BgeeiP51667.
ExpressionAtlasiP51667. baseline and differential.
GenevestigatoriP51667.

Interactioni

Subunit structurei

Myosin is a hexamer of 2 heavy chains and 4 light chains. Interacts with MYOC By similarity.By similarity

Protein-protein interaction databases

IntActiP51667. 3 interactions.
MINTiMINT-4130491.

Structurei

3D structure databases

ProteinModelPortaliP51667.
SMRiP51667. Positions 16-165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 5936EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 12936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini130 – 16536EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP51667.
KOiK10351.
OMAiTQMLTTQ.
OrthoDBiEOG7992RX.
PhylomeDBiP51667.
TreeFamiTF314218.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00036. EF-hand_1. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51667-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPKKAKKRI EGGSSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR
60 70 80 90 100
DTFAALGRVN VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL
110 120 130 140 150
NAFKVFDPEG KGSLKADYVR EMLTTQAERF SKEEIDQMFA AFPPDVTGNL
160
DYKNLVHIIT HGEEKD
Length:166
Mass (Da):18,864
Last modified:April 3, 2007 - v3
Checksum:iEA25C1FAA18E2EA8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 52KK → LF in AAA39796. (PubMed:1379240)Curated
Sequence conflicti14 – 141S → T in AAA39796. (PubMed:1379240)Curated
Sequence conflicti128 – 1281E → G in AAH61144. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M91602 mRNA. Translation: AAA39796.1.
AK002367 mRNA. Translation: BAB22045.1.
AK146674 mRNA. Translation: BAE27350.1.
BC061144 mRNA. Translation: AAH61144.1.
CCDSiCCDS39252.1.
PIRiA42858.
RefSeqiNP_034991.3. NM_010861.3.
UniGeneiMm.1529.

Genome annotation databases

EnsembliENSMUST00000014080; ENSMUSP00000014080; ENSMUSG00000013936.
ENSMUST00000111751; ENSMUSP00000107380; ENSMUSG00000013936.
GeneIDi17906.
KEGGimmu:17906.
UCSCiuc008zkp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M91602 mRNA. Translation: AAA39796.1 .
AK002367 mRNA. Translation: BAB22045.1 .
AK146674 mRNA. Translation: BAE27350.1 .
BC061144 mRNA. Translation: AAH61144.1 .
CCDSi CCDS39252.1.
PIRi A42858.
RefSeqi NP_034991.3. NM_010861.3.
UniGenei Mm.1529.

3D structure databases

ProteinModelPortali P51667.
SMRi P51667. Positions 16-165.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P51667. 3 interactions.
MINTi MINT-4130491.

PTM databases

PhosphoSitei P51667.

Proteomic databases

MaxQBi P51667.
PaxDbi P51667.
PRIDEi P51667.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000014080 ; ENSMUSP00000014080 ; ENSMUSG00000013936 .
ENSMUST00000111751 ; ENSMUSP00000107380 ; ENSMUSG00000013936 .
GeneIDi 17906.
KEGGi mmu:17906.
UCSCi uc008zkp.1. mouse.

Organism-specific databases

CTDi 4633.
MGIi MGI:97272. Myl2.

Phylogenomic databases

eggNOGi COG5126.
GeneTreei ENSGT00760000119196.
HOGENOMi HOG000233018.
HOVERGENi HBG012180.
InParanoidi P51667.
KOi K10351.
OMAi TQMLTTQ.
OrthoDBi EOG7992RX.
PhylomeDBi P51667.
TreeFami TF314218.

Miscellaneous databases

ChiTaRSi MYL2. mouse.
NextBioi 292733.
PROi P51667.
SOURCEi Search...

Gene expression databases

Bgeei P51667.
ExpressionAtlasi P51667. baseline and differential.
Genevestigatori P51667.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
Pfami PF00036. EF-hand_1. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 3 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Myosin light chain-2 luciferase transgenic mice reveal distinct regulatory programs for cardiac and skeletal muscle-specific expression of a single contractile protein gene."
    Lee K.J., Ross R.S., Rockman H.A., Harris A.N., O'Brien T.X., Bilsen M., Shubeita H.E., Kandolf R., Brem G., Price J., Evans S.M., Zhu H., Franz W.M., Chien K.R.
    J. Biol. Chem. 267:15875-15885(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Heart muscle.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic heart and Kidney.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein."
    Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L., Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.
    Nature 466:1125-1128(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT ALA-2.

Entry informationi

Entry nameiMLRV_MOUSE
AccessioniPrimary (citable) accession number: P51667
Secondary accession number(s): Q6P8P4, Q9QVP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This chain binds calcium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3