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Protein

Myosin regulatory light chain 12B

Gene

MYL12B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi42 – 5312PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5625900. RHO GTPases activate CIT.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5627123. RHO GTPases activate PAKs.
SIGNORiO14950.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin regulatory light chain 12B
Alternative name(s):
MLC-2A
Short name:
MLC-2
Myosin regulatory light chain 2-B, smooth muscle isoform
Myosin regulatory light chain 20 kDa
Short name:
MLC20
Myosin regulatory light chain MRLC2
SHUJUN-1
Gene namesi
Name:MYL12B
Synonyms:MRLC2, MYLC2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:29827. MYL12B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 202TS → AA: Shows a decrease in the number of actin filament bundles. 3 Publications
Mutagenesisi19 – 202TS → DD: Shows a larger number of actin filament bundles. 3 Publications

Organism-specific databases

PharmGKBiPA164723274.

Polymorphism and mutation databases

BioMutaiMYL12B.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Myosin regulatory light chain 12BPRO_0000349364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphothreonine; by MLCK and ZIPK/DAPK33 Publications
Modified residuei20 – 201Phosphoserine; by MLCK and ZIPK/DAPK33 Publications

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. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO14950.
MaxQBiO14950.
PaxDbiO14950.
PeptideAtlasiO14950.
PRIDEiO14950.
TopDownProteomicsiO14950.

PTM databases

iPTMnetiO14950.
PhosphoSiteiO14950.
SwissPalmiO14950.

Expressioni

Tissue specificityi

Ubiquitously expressed in various hematopoietic cells.2 Publications

Gene expression databases

BgeeiO14950.
GenevisibleiO14950. HS.

Organism-specific databases

HPAiHPA039262.
HPA045244.
HPA059197.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTBP607093EBI-1642165,EBI-353944
MYH11P357492EBI-1642165,EBI-1052928

Protein-protein interaction databases

BioGridi125182. 18 interactions.
IntActiO14950. 15 interactions.
STRINGi9606.ENSP00000237500.

Structurei

3D structure databases

ProteinModelPortaliO14950.
SMRiO14950. 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

eggNOGiKOG0031. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
InParanoidiO14950.
KOiK12757.
OMAiTTMGERY.
OrthoDBiEOG7992RX.
PhylomeDBiO14950.
TreeFamiTF314218.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR015070. EF_hand_DJBP.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF08976. EF-hand_11. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14950-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID
60 70 80 90 100
KEDLHDMLAS LGKNPTDAYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE
110 120 130 140 150
DVIRNAFACF DEEATGTIQE DYLRELLTTM GDRFTDEEVD ELYREAPIDK
160 170
KGNFNYIEFT RILKHGAKDK DD
Length:172
Mass (Da):19,779
Last modified:September 2, 2008 - v2
Checksum:i78FF911630F3870B
GO

Sequence cautioni

The sequence AAP73808.1 differs from that shown. Reason: Frameshift at position 4. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721A → V in AAP73808 (Ref. 5) Curated
Sequence conflicti89 – 891M → T in AAP73808 (Ref. 5) Curated
Sequence conflicti104 – 1041R → G in AAP73808 (Ref. 5) Curated
Sequence conflicti138 – 1381E → G in BAA23323 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411E → G.
Corresponds to variant rs14720 [ dbSNP | Ensembl ].
VAR_046371

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82058 mRNA. Translation: BAB88918.1.
AB046614 mRNA. Translation: BAB62403.1.
D50372 mRNA. Translation: BAA23323.1.
U26162 mRNA. Translation: AAA67367.1.
AY320408 mRNA. Translation: AAP73808.1. Frameshift.
AK291726 mRNA. Translation: BAF84415.1.
CH471113 Genomic DNA. Translation: EAX01675.1.
CH471113 Genomic DNA. Translation: EAX01676.1.
CH471113 Genomic DNA. Translation: EAX01677.1.
BC004994 mRNA. Translation: AAH04994.1.
CCDSiCCDS11831.1.
RefSeqiNP_001138416.1. NM_001144944.1.
NP_001138417.1. NM_001144945.1.
NP_001289978.1. NM_001303049.1.
NP_291024.1. NM_033546.3.
UniGeneiHs.190086.
Hs.464472.

Genome annotation databases

EnsembliENST00000237500; ENSP00000237500; ENSG00000118680.
ENST00000400175; ENSP00000383037; ENSG00000118680.
ENST00000581193; ENSP00000463559; ENSG00000118680.
ENST00000584539; ENSP00000464464; ENSG00000118680.
GeneIDi103910.
10627.
KEGGihsa:103910.
UCSCiuc002klt.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82058 mRNA. Translation: BAB88918.1.
AB046614 mRNA. Translation: BAB62403.1.
D50372 mRNA. Translation: BAA23323.1.
U26162 mRNA. Translation: AAA67367.1.
AY320408 mRNA. Translation: AAP73808.1. Frameshift.
AK291726 mRNA. Translation: BAF84415.1.
CH471113 Genomic DNA. Translation: EAX01675.1.
CH471113 Genomic DNA. Translation: EAX01676.1.
CH471113 Genomic DNA. Translation: EAX01677.1.
BC004994 mRNA. Translation: AAH04994.1.
CCDSiCCDS11831.1.
RefSeqiNP_001138416.1. NM_001144944.1.
NP_001138417.1. NM_001144945.1.
NP_001289978.1. NM_001303049.1.
NP_291024.1. NM_033546.3.
UniGeneiHs.190086.
Hs.464472.

3D structure databases

ProteinModelPortaliO14950.
SMRiO14950. Positions 26-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125182. 18 interactions.
IntActiO14950. 15 interactions.
STRINGi9606.ENSP00000237500.

PTM databases

iPTMnetiO14950.
PhosphoSiteiO14950.
SwissPalmiO14950.

Polymorphism and mutation databases

BioMutaiMYL12B.

Proteomic databases

EPDiO14950.
MaxQBiO14950.
PaxDbiO14950.
PeptideAtlasiO14950.
PRIDEiO14950.
TopDownProteomicsiO14950.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237500; ENSP00000237500; ENSG00000118680.
ENST00000400175; ENSP00000383037; ENSG00000118680.
ENST00000581193; ENSP00000463559; ENSG00000118680.
ENST00000584539; ENSP00000464464; ENSG00000118680.
GeneIDi103910.
10627.
KEGGihsa:103910.
UCSCiuc002klt.5. human.

Organism-specific databases

CTDi103910.
10627.
GeneCardsiMYL12B.
H-InvDBHIX0014302.
HGNCiHGNC:29827. MYL12B.
HPAiHPA039262.
HPA045244.
HPA059197.
neXtProtiNX_O14950.
PharmGKBiPA164723274.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0031. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
InParanoidiO14950.
KOiK12757.
OMAiTTMGERY.
OrthoDBiEOG7992RX.
PhylomeDBiO14950.
TreeFamiTF314218.

Enzyme and pathway databases

ReactomeiR-HSA-3928663. EPHA-mediated growth cone collapse.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-445355. Smooth Muscle Contraction.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5625900. RHO GTPases activate CIT.
R-HSA-5627117. RHO GTPases Activate ROCKs.
R-HSA-5627123. RHO GTPases activate PAKs.
SIGNORiO14950.

Miscellaneous databases

PROiO14950.

Gene expression databases

BgeeiO14950.
GenevisibleiO14950. HS.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR015070. EF_hand_DJBP.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF08976. EF-hand_11. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Diphosphorylated MRLC is required for organization of stress fibers in interphase cells and the contractile ring in dividing cells."
    Iwasaki T., Murata-Hori M., Ishitobi S., Hosoya H.
    Cell Struct. Funct. 26:677-683(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-19 AND SER-20, MUTAGENESIS OF 19-THR-SER-20.
  2. "Molecular cloning and sequencing of myosin light chains in human megakaryoblastic leukemia cells."
    Watanabe M., Kohri M., Takaishi M., Horie R., Higashihara M.
    J. Smooth Muscle Res. 37:25-38(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Molecular cloning of a novel human myosin regulatory light chain."
    Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S., Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M., Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E., Hirai Y.
    Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  4. "Human myosin regulatory light chain cDNA homologous to the rat myosin regulatory light chain B (MLC-B)."
    Brodie S.G., Rubin S.E., Montoya G.D., Garry P.J., Williams T.M.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Construction of cDNA expression library from nasopharyngeal carcinoma tissue and screening of antigenic genes."
    Shu J., Li G., He X.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Nasopharyngeal carcinoma.
  6. "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].
    Tissue: Placenta.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Tissue: Skin.
  9. "Activation of actin-activated MgATPase activity of myosin II by phosphorylation with MAPK-activated protein kinase-1b (RSK-2)."
    Suizu F., Ueda K., Iwasaki T., Murata-Hori M., Hosoya H.
    J. Biochem. 128:435-440(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Phosphorylation of myosin II regulatory light chain is necessary for migration of HeLa cells but not for localization of myosin II at the leading edge."
    Fumoto K., Uchimura T., Iwasaki T., Ueda K., Hosoya H.
    Biochem. J. 370:551-556(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-19 AND SER-20, MUTAGENESIS OF 19-THR-SER-20.
  11. "Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport."
    Duran J.M., Valderrama F., Castel S., Magdalena J., Tomas M., Hosoya H., Renau-Piqueras J., Malhotra V., Egea G.
    Mol. Biol. Cell 14:445-459(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 19-THR-SER-20.
  12. "Epigallocatechin-3-O-gallate disrupts stress fibers and the contractile ring by reducing myosin regulatory light chain phosphorylation mediated through the target molecule 67 kDa laminin receptor."
    Umeda D., Tachibana H., Yamada K.
    Biochem. Biophys. Res. Commun. 333:628-635(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-19 AND SER-20.
  13. Cited for: PHOSPHORYLATION BY ZIPK/DAPK3.
  14. "Smooth muscle type isoform of 20 kDa myosin light chain is expressed in monocyte/macrophage cell lineage."
    Higashihara M., Watanabe M., Usuda S., Miyazaki K.
    J. Smooth Muscle Res. 44:29-40(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiML12B_HUMAN
AccessioniPrimary (citable) accession number: O14950
Secondary accession number(s): D3DUH6, Q13182, Q7Z5Z4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: July 6, 2016
This is version 129 of the entry and version 2 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

Miscellaneous

This chain binds calcium.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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. 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.