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Protein

Myosin regulatory light polypeptide 9

Gene

Myl9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi42 – 5312Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. myosin heavy chain binding Source: MGI

GO - Biological processi

  1. platelet aggregation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_280640. EPHA-mediated growth cone collapse.
REACT_324232. Smooth Muscle Contraction.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin regulatory light polypeptide 9
Alternative name(s):
Myosin regulatory light chain 2, smooth muscle isoform
Myosin regulatory light chain 9
Gene namesi
Name:Myl9
Synonyms:Myrl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2138915. Myl9.

Subcellular locationi

GO - Cellular componenti

  1. myosin II complex Source: MGI
  2. stress fiber Source: MGI
  3. Z disc Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 172171Myosin regulatory light polypeptide 9PRO_0000198736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei19 – 191Phosphothreonine; by MLCK, CIT and ROCK2By similarity
Modified residuei20 – 201Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1; DAPK2 and ZIPK/DAPK31 Publication

Post-translational modificationi

Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CQ19.
PaxDbiQ9CQ19.
PRIDEiQ9CQ19.

PTM databases

PhosphoSiteiQ9CQ19.

Expressioni

Gene expression databases

BgeeiQ9CQ19.
CleanExiMM_MYL9.
GenevestigatoriQ9CQ19.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi221155. 1 interaction.
IntActiQ9CQ19. 3 interactions.
MINTiMINT-4102187.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ19.
SMRiQ9CQ19. Positions 26-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 6436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini98 – 13336EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini134 – 16936EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ9CQ19.
KOiK12755.
OMAiITPSKTM.
OrthoDBiEOG7992RX.
PhylomeDBiQ9CQ19.
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. 2 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.

Q9CQ19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID
60 70 80 90 100
KEDLHDMLAS LGKNPTDEYL EGMMNEAPGP INFTMFLTMF GEKLNGTDPE
110 120 130 140 150
DVIRNAFACF DEEASGFIHE DHLRELLTTM GDRFTDEEVD EMYREAPIDK
160 170
KGNFNYVEFT RILKHGAKDK DD
Length:172
Mass (Da):19,854
Last modified:January 23, 2007 - v3
Checksum:iD588C708BF5A2D56
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321D → V in BAE35452 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007972 mRNA. Translation: BAB25381.1.
AK020258 mRNA. Translation: BAB32043.1.
AK159880 mRNA. Translation: BAE35452.1.
BC049974 mRNA. Translation: AAH49974.2.
BC055439 mRNA. Translation: AAH55439.1.
CCDSiCCDS50779.1.
RefSeqiNP_742116.1. NM_172118.1.
XP_006500516.1. XM_006500453.2.
UniGeneiMm.271770.

Genome annotation databases

EnsembliENSMUST00000088552; ENSMUSP00000085913; ENSMUSG00000067818.
GeneIDi98932.
KEGGimmu:98932.
UCSCiuc008nnw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007972 mRNA. Translation: BAB25381.1.
AK020258 mRNA. Translation: BAB32043.1.
AK159880 mRNA. Translation: BAE35452.1.
BC049974 mRNA. Translation: AAH49974.2.
BC055439 mRNA. Translation: AAH55439.1.
CCDSiCCDS50779.1.
RefSeqiNP_742116.1. NM_172118.1.
XP_006500516.1. XM_006500453.2.
UniGeneiMm.271770.

3D structure databases

ProteinModelPortaliQ9CQ19.
SMRiQ9CQ19. Positions 26-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221155. 1 interaction.
IntActiQ9CQ19. 3 interactions.
MINTiMINT-4102187.

PTM databases

PhosphoSiteiQ9CQ19.

Proteomic databases

MaxQBiQ9CQ19.
PaxDbiQ9CQ19.
PRIDEiQ9CQ19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000088552; ENSMUSP00000085913; ENSMUSG00000067818.
GeneIDi98932.
KEGGimmu:98932.
UCSCiuc008nnw.2. mouse.

Organism-specific databases

CTDi10398.
MGIiMGI:2138915. Myl9.

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiQ9CQ19.
KOiK12755.
OMAiITPSKTM.
OrthoDBiEOG7992RX.
PhylomeDBiQ9CQ19.
TreeFamiTF314218.

Enzyme and pathway databases

ReactomeiREACT_280640. EPHA-mediated growth cone collapse.
REACT_324232. Smooth Muscle Contraction.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

ChiTaRSiMyl9. mouse.
NextBioi353711.
PROiQ9CQ19.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ19.
CleanExiMM_MYL9.
GenevestigatoriQ9CQ19.

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. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Colon, Osteoclast and Pancreas.
  2. "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].
    Strain: Czech II and FVB/N.
    Tissue: Mammary gland and Salivary gland.
  3. "Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication."
    Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.
    Mol. Cell. Biol. 26:9016-9034(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-20.

Entry informationi

Entry nameiMYL9_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ19
Secondary accession number(s): Q3TW15, Q80X77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 115 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.By similarity

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

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 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.