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P19105

- ML12A_HUMAN

UniProt

P19105 - ML12A_HUMAN

Protein

Myosin regulatory light chain 12A

Gene

MYL12A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 bindingi41 – 5212Add
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. protein targeting to plasma membrane Source: Ensembl
    2. regulation of cell shape Source: Ensembl

    Keywords - Molecular functioni

    Motor protein, Muscle protein, Myosin

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin regulatory light chain 12A
    Alternative name(s):
    Epididymis secretory protein Li 24
    Short name:
    HEL-S-24
    MLC-2B
    Myosin RLC
    Myosin regulatory light chain 2, nonsarcomeric
    Myosin regulatory light chain MRLC3
    Gene namesi
    Name:MYL12A
    Synonyms:MLCB, MRLC3, RLC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:16701. MYL12A.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. myosin II complex Source: Ensembl
    3. stress fiber Source: Ensembl
    4. Z disc Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164723273.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 171171Myosin regulatory light chain 12APRO_0000198733Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphothreonine; by MLCK1 Publication
    Modified residuei19 – 191Phosphoserine; by MLCK1 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

    Phosphoprotein

    Proteomic databases

    PaxDbiP19105.
    PRIDEiP19105.

    2D gel databases

    OGPiP19105.
    SWISS-2DPAGEP19105.

    PTM databases

    PhosphoSiteiP19105.

    Expressioni

    Gene expression databases

    ArrayExpressiP19105.
    BgeeiP19105.
    GenevestigatoriP19105.

    Organism-specific databases

    HPAiCAB004503.
    HPA045244.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rock2Q628682EBI-354418,EBI-1569209From a different organism.

    Protein-protein interaction databases

    BioGridi115871. 38 interactions.
    IntActiP19105. 19 interactions.
    MINTiMINT-1159148.
    STRINGi9606.ENSP00000217652.

    Structurei

    3D structure databases

    ProteinModelPortaliP19105.
    SMRiP19105. Positions 25-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 6336EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 13236EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini133 – 16836EF-hand 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5126.
    HOGENOMiHOG000233018.
    InParanoidiP19105.
    KOiK12757.
    OrthoDBiEOG7992RX.
    PhylomeDBiP19105.
    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.

    P19105-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSKRTKTKT KKRPQRATSN VFAMFDQSQI QEFKEAFNMI DQNRDGFIDK    50
    EDLHDMLASL GKNPTDEYLD AMMNEAPGPI NFTMFLTMFG EKLNGTDPED 100
    VIRNAFACFD EEATGTIQED YLRELLTTMG DRFTDEEVDE LYREAPIDKK 150
    GNFNYIEFTR ILKHGAKDKD D 171
    Length:171
    Mass (Da):19,794
    Last modified:January 23, 2007 - v2
    Checksum:iC871AA881BF5C215
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54304 mRNA. Translation: CAA38201.1.
    D82059 mRNA. Translation: BAB88919.1.
    EU794621 mRNA. Translation: ACJ13675.1.
    AK291145 mRNA. Translation: BAF83834.1.
    CH471113 Genomic DNA. Translation: EAX01678.1.
    CH471113 Genomic DNA. Translation: EAX01680.1.
    CH471113 Genomic DNA. Translation: EAX01681.1.
    BC016372 mRNA. Translation: AAH16372.1.
    BC031972 mRNA. Translation: AAH31972.1.
    BC032748 mRNA. Translation: AAH32748.1.
    CCDSiCCDS11830.1.
    PIRiS11493. MOHULP.
    RefSeqiNP_006462.1. NM_006471.2.
    XP_005258133.1. XM_005258076.1.
    XP_005258135.1. XM_005258078.1.
    UniGeneiHs.190086.

    Genome annotation databases

    EnsembliENST00000217652; ENSP00000217652; ENSG00000101608.
    ENST00000536605; ENSP00000441231; ENSG00000101608.
    ENST00000578611; ENSP00000463614; ENSG00000101608.
    ENST00000579226; ENSP00000462171; ENSG00000101608.
    GeneIDi10627.
    KEGGihsa:10627.
    UCSCiuc002klr.3. human.

    Polymorphism databases

    DMDMi127169.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54304 mRNA. Translation: CAA38201.1 .
    D82059 mRNA. Translation: BAB88919.1 .
    EU794621 mRNA. Translation: ACJ13675.1 .
    AK291145 mRNA. Translation: BAF83834.1 .
    CH471113 Genomic DNA. Translation: EAX01678.1 .
    CH471113 Genomic DNA. Translation: EAX01680.1 .
    CH471113 Genomic DNA. Translation: EAX01681.1 .
    BC016372 mRNA. Translation: AAH16372.1 .
    BC031972 mRNA. Translation: AAH31972.1 .
    BC032748 mRNA. Translation: AAH32748.1 .
    CCDSi CCDS11830.1.
    PIRi S11493. MOHULP.
    RefSeqi NP_006462.1. NM_006471.2.
    XP_005258133.1. XM_005258076.1.
    XP_005258135.1. XM_005258078.1.
    UniGenei Hs.190086.

    3D structure databases

    ProteinModelPortali P19105.
    SMRi P19105. Positions 25-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115871. 38 interactions.
    IntActi P19105. 19 interactions.
    MINTi MINT-1159148.
    STRINGi 9606.ENSP00000217652.

    PTM databases

    PhosphoSitei P19105.

    Polymorphism databases

    DMDMi 127169.

    2D gel databases

    OGPi P19105.
    SWISS-2DPAGE P19105.

    Proteomic databases

    PaxDbi P19105.
    PRIDEi P19105.

    Protocols and materials databases

    DNASUi 10627.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217652 ; ENSP00000217652 ; ENSG00000101608 .
    ENST00000536605 ; ENSP00000441231 ; ENSG00000101608 .
    ENST00000578611 ; ENSP00000463614 ; ENSG00000101608 .
    ENST00000579226 ; ENSP00000462171 ; ENSG00000101608 .
    GeneIDi 10627.
    KEGGi hsa:10627.
    UCSCi uc002klr.3. human.

    Organism-specific databases

    CTDi 10627.
    GeneCardsi GC18P003238.
    HGNCi HGNC:16701. MYL12A.
    HPAi CAB004503.
    HPA045244.
    MIMi 609211. gene.
    neXtProti NX_P19105.
    PharmGKBi PA164723273.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5126.
    HOGENOMi HOG000233018.
    InParanoidi P19105.
    KOi K12757.
    OrthoDBi EOG7992RX.
    PhylomeDBi P19105.
    TreeFami TF314218.

    Miscellaneous databases

    ChiTaRSi MYL12A. human.
    GeneWikii MRCL3.
    GenomeRNAii 10627.
    NextBioi 40378.
    PROi P19105.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19105.
    Bgeei P19105.
    Genevestigatori P19105.

    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. 2 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human nonsarcomeric 20,000 Da myosin regulatory light chain cDNA."
      Grant J.W., Zhong R.Q., McEwen P., Church S.L.
      Nucleic Acids Res. 18:5892-5892(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    2. "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-18 AND SER-19.
    3. Li J.Y., Wang H.Y., Liu F.J., Liu J.
      Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Skeletal muscle, Skin and Testis.

    Entry informationi

    Entry nameiML12A_HUMAN
    AccessioniPrimary (citable) accession number: P19105
    Secondary accession number(s): Q53X45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3