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Q9CQ19 (MYL9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin regulatory light polypeptide 9
Alternative name(s):
Myosin regulatory light chain 2, smooth muscle isoform
Myosin regulatory light chain 9
Gene names
Name:Myl9
Synonyms:Myrl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Post-translational modification

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.

Miscellaneous

This chain binds calcium By similarity.

Sequence similarities

Contains 3 EF-hand domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 172171Myosin regulatory light polypeptide 9
PRO_0000198736

Regions

Domain29 – 6436EF-hand 1
Domain98 – 13336EF-hand 2
Domain134 – 16936EF-hand 3
Calcium binding42 – 5312

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue191Phosphothreonine; by MLCK, CIT and ROCK2 Ref.4 Ref.5
Modified residue201Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1; DAPK2 and ZIPK/DAPK3 Probable
Modified residue291Phosphoserine Ref.4
Modified residue1351Phosphothreonine Ref.4

Experimental info

Sequence conflict1321D → V in BAE35452. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CQ19 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D588C708BF5A2D56

FASTA17219,854
        10         20         30         40         50         60 
MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS 

        70         80         90        100        110        120 
LGKNPTDEYL EGMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE 

       130        140        150        160        170 
DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-20; SER-29 AND THR-135, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-20, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00750595.
RefSeqNP_742116.1. NM_172118.1.
UniGeneMm.271770.

3D structure databases

ProteinModelPortalQ9CQ19.
SMRQ9CQ19. Positions 26-168.
ModBaseSearch...

PTM databases

PhosphoSiteQ9CQ19.

Proteomic databases

PaxDbQ9CQ19.
PRIDEQ9CQ19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000088552; ENSMUSP00000085913; ENSMUSG00000067818.
GeneID98932.
KEGGmmu:98932.

Organism-specific databases

CTD10398.
MGIMGI:2138915. Myl9.

Phylogenomic databases

eggNOGCOG5126.
GeneTreeENSGT00590000082808.
HOGENOMHOG000233018.
HOVERGENHBG012180.
InParanoidQ9CQ19.
KOK12755.
OMARKTVNRR.
OrthoDBEOG4FTW1S.

Gene expression databases

ArrayExpressQ9CQ19.
BgeeQ9CQ19.
CleanExMM_MYL9.
GenevestigatorQ9CQ19.
GermOnlineENSMUSG00000067818. Mus musculus.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF00036. efhand. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio353711.
SOURCESearch...

Entry information

Entry nameMYL9_MOUSE
AccessionPrimary (citable) accession number: Q9CQ19
Secondary accession number(s): Q3TW15, Q80X77
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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