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Q8IUG5

- MY18B_HUMAN

UniProt

Q8IUG5 - MY18B_HUMAN

Protein

Unconventional myosin-XVIIIb

Gene

MYO18B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    May be involved in intracellular trafficking of the muscle cell when in the cytoplasm, whereas entering the nucleus, may be involved in the regulation of muscle specific genes. May play a role in the control of tumor development and progression; restored MYO18B expression in lung cancer cells suppresses anchorage-independent growth.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi660 – 6678ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. motor activity Source: InterPro

    Keywords - Molecular functioni

    Motor protein, Myosin

    Keywords - Ligandi

    Actin-binding, ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Unconventional myosin-XVIIIb
    Gene namesi
    Name:MYO18B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:18150. MYO18B.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmmyofibrilsarcomere
    Note: Punctate pattern in undifferentiated myoblasts. Nuclear, on primary cardiomyocytes and adult muscle. A partial sarcomeric location was found in some cardiomyocytes.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. sarcomere Source: UniProtKB-SubCell
    3. unconventional myosin complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38300.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25672567Unconventional myosin-XVIIIbPRO_0000123478Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1829 – 18291Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IUG5.
    PaxDbiQ8IUG5.
    PRIDEiQ8IUG5.

    PTM databases

    PhosphoSiteiQ8IUG5.

    Expressioni

    Tissue specificityi

    Selectively expressed in cardiac and skeletal muscles. Weakly expressed in testis, pancreas, placenta, prostate, lung and thymus.

    Developmental stagei

    Reaches an expression peak in the third day after induction and remains at similar level during successive myotubule maturation.

    Gene expression databases

    ArrayExpressiQ8IUG5.
    BgeeiQ8IUG5.
    CleanExiHS_MYO18B.
    GenevestigatoriQ8IUG5.

    Organism-specific databases

    HPAiHPA000953.

    Interactioni

    Subunit structurei

    Homodimer. May interact with F actin through the GPA motif (Gly/Pro/Ala-rich).

    Protein-protein interaction databases

    BioGridi124214. 2 interactions.
    IntActiQ8IUG5. 3 interactions.
    STRINGi9606.ENSP00000386096.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IUG5.
    SMRiQ8IUG5. Positions 505-1395.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini571 – 1333763Myosin motorAdd
    BLAST
    Domaini1336 – 136530IQPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1213 – 124028GPASequence AnalysisAdd
    BLAST
    Regioni1426 – 2083658TailAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1396 – 1783388Sequence AnalysisAdd
    BLAST
    Coiled coili1825 – 1961137Sequence AnalysisAdd
    BLAST
    Coiled coili2014 – 209077Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi71 – 11444Ser-richAdd
    BLAST
    Compositional biasi799 – 8046Poly-Ala
    Compositional biasi1217 – 12226Poly-Pro
    Compositional biasi1643 – 1769127Gln-richAdd
    BLAST
    Compositional biasi2506 – 25149Poly-Ser

    Sequence similaritiesi

    Contains 1 IQ domain.PROSITE-ProRule annotation
    Contains 1 myosin motor domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5022.
    HOVERGENiHBG052544.
    KOiK10362.
    OrthoDBiEOG71P29W.
    PhylomeDBiQ8IUG5.
    TreeFamiTF339614.

    Family and domain databases

    Gene3Di4.10.270.10. 1 hit.
    InterProiIPR000048. IQ_motif_EF-hand-BS.
    IPR028561. MYO18B.
    IPR027401. Myosin-like_IQ_dom.
    IPR001609. Myosin_head_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR13140:SF254. PTHR13140:SF254. 1 hit.
    PfamiPF00063. Myosin_head. 2 hits.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00015. IQ. 1 hit.
    SM00242. MYSc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS50096. IQ. 1 hit.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8IUG5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAISSRLALW EQKIREEDKS PPPSSPPPLF SVIPGGFIKQ LVRGTEKEAK     50
    EARQRKQLAV ASPEREIPEI SISQPNSKSS SGTRSGSQQI SQDDQSSSPG 100
    SSDILGKESE GSRSPDPEQM TSINGEKAQE LGSSATPTKK TVPFKRGVRR 150
    GDVLLMVAKL DPDSAKPEKT HPHDAPPCKT SPPATDTGKE KKGETSRTPC 200
    GSQASTEILA PKAEKTRTGG LGDPGQGTVA LKKGEEGQSI VGKGLGTPKT 250
    TELKEAEPQG KDRQGTRPQA QGPGEGVRPG KAEKEGAEPT NTVEKGNVSK 300
    DVGSEGKHVR PQIPGRKWGG FLGRRSKWDG PQNKKDKEGV LLSKAEKTGE 350
    PQTQMEKTSQ VQGELGDDLR MGEKAGELRS TTGKAGESWD KKEKMGQPQG 400
    KSGNAGEARS QTEKGCEAPK EVSTMVESPA APGKGGWPGS RGQEAEEPCS 450
    RAGDGAGALE TELEGPSQPA LEKDAERPRI RKENQDGPAP QEEGKGGQSR 500
    DSDQAPEDRW YEAEKVWLAQ KDGFTLATVL KPDEGTADLP AGRVRLWIDA 550
    DKTITEVDEE HVHRANPPEL DQVEDLASLI SVNESSVLNT LLQRYKAQLL 600
    HTCTGPDLIV LQPRGPSVPS AGKVPKGRRD GLPAHIGSMA QRAYWALLNQ 650
    RRDQSIVALG RSGAGKTTCC EQVLEHLVGM AGSVDGRVSV EKIRATFTVL 700
    RAFGSVSMAH SRSATRFSMV MSLDFNATGR ITAAQLQTML LEKSRVARQP 750
    EGESNFLVFS QMLAGLDLDL RTELNLHQMA DSSSFGMGVW SKPEDKQKAA 800
    AAFAQLQGAM EMLGISESEQ RAVWRVLAAI YHLGAAGACK VGRKQFMRFE 850
    WANYAAEALG CEYEELNTAT FKHHLRQIIQ QMTFGPSRWG LEDEETSSGL 900
    KMTGVDCVEG MASGLYQELF AAVVSLINRS FSSHHLSMAS IMVVDSPGFQ 950
    NPRHQGKDRA ATFEELCHNY AHERLQLLFY QRTFVSTLQR YQEEGVPVQF 1000
    DLPDPSPGTT VAVVDQNPSQ VRLPAGGGAQ DARGLFWVLD EEVHVEGSSD 1050
    SVVLERLCAA FEKKGAGTEG SSALRTCEQP LQCEIFHQLG WDPVRYDLTG 1100
    WLHRAKPNLS ALDAPQVLHQ SKREELRSLF QARAKLPPVC RAVAGLEGTS 1150
    QQALQRSRMV RRTFASSLAA VRRKAPCSQI KLQMDALTSM IKRSRLHFIH 1200
    CLVPNPVVES RSGQESPPPP QPGRDKPGAG GPLALDIPAL RVQLAGFHIL 1250
    EALRLHRTGY ADHMGLTRFR RQFQVLDAPL LKKLMSTSEG IDERKAVEEL 1300
    LETLDLEKKA VAVGHSQVFL KAGVISRLEK QREKLVSQSI VLFQAACKGF 1350
    LSRQEFKKLK IRRLAAQCIQ KNVAVFLAVK DWPWWQLLGS LQPLLSATIG 1400
    TEQLRAKEEE LTTLRRKLEK SEKLRNELRQ NTDLLESKIA DLTSDLADER 1450
    FKGDVACQVL ESERAERLQA FREVQELKSK HEQVQKKLGD VNKQLEEAQQ 1500
    KIQLNDLERN PTGGADEWQM RFDCAQMENE FLRKRLQQCE ERLDSELTAR 1550
    KELEQKLGEL QSAYDGAKKM AHQLKRKCHH LTCDLEDTCV LLENQQSRNH 1600
    ELEKKQKKFD LQLAQALGES VFEKGLREKV TQENTSVRWE LGQLQQQLKQ 1650
    KEQEASQLKQ QVEMLQDHKR ELLGSPSLGE NCVAGLKERL WKLESSALEQ 1700
    QKIQSQQENT IKQLEQLRQR FELEIERMKQ MHQKDREDQE EELEDVRQSC 1750
    QKRLHQLEMQ LEQEYEEKQM VLHEKQDLEG LIGTLCDQIG HRDFDVEKRL 1800
    RRDLRRTHAL LSDVQLLLGT MEDGKTSVSK EELEKVHSQL EQSEAKCEEA 1850
    LKTQKVLTAD LESMHSELEN MTRNKSLVDE QLYRLQFEKA DLLKRIDEDQ 1900
    DDLNELMQKH KDLIAQSAAD IGQIQELQLQ LEEAKKEKHK LQEQLQVAQM 1950
    RIEYLEQSTV DRAIVSRQEA VICDLENKTE FQKVQIKRFE VLVIRLRDSL 2000
    IKMGEELSQA ATSESQQRES SQYYQRRLEE LKADMEELVQ REAEASRRCM 2050
    ELEKYVEELA AVRQTLQTDL ETSIRRIADL QAALEEVASS DSDTESVQTA 2100
    VDCGSSGRKE MDNVSILSSQ PEGSLQSWLS CTLSLATDTM RTPSRQSATS 2150
    SRILSPRINE EAGDTERTQS ALALSRARST NVHSKTSGDK PVSPHFVRRQ 2200
    KYCHFGDGEV LAVQRKSTER LEPASSPLAS RSTNTSPLSR EKLPSPSAAL 2250
    SEFVEGLRRK RAQRGQGSTL GLEDWPTLPI YQTTGASTLR RGRAGSDEGN 2300
    LSLRVGAKSP LEIEGAAGGL LRSTSLKCIS SDGVGGTTLL PEKSKTQFSS 2350
    CESLLESRPS MGRKLSSPTT PRDMLLSPTL RPRRRCLESS VDDAGCPDLG 2400
    KEPLVFQNRQ FAHLMEEPLG SDPFSWKLPS LDYERKTKVD FDDFLPAIRK 2450
    PQTPTSLAGS AKGGQDGSQR SSIHFETEEA NRSFLSGIKT ILKKSPEPKE 2500
    DPAHLSDSSS SSGSIVSFKS ADSIKSRPGI PRLAGDGGER TSPERREPGT 2550
    GRKDDDVASI MKKYLQK 2567
    Length:2,567
    Mass (Da):285,185
    Last modified:March 1, 2003 - v1
    Checksum:i9ABC2F64C644F110
    GO
    Isoform 2 (identifier: Q8IUG5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-487: Missing.
         488-503: PAPQEEGKGGQSRDSD → MGSGAICWFNLRDVGS

    Note: No experimental confirmation available.

    Show »
    Length:2,080
    Mass (Da):233,671
    Checksum:iF7ABF4EF5BD30755
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31I → M in CAC70712. (PubMed:12547197)Curated
    Sequence conflicti828 – 8281A → T in AAI50627. (PubMed:15489334)Curated
    Sequence conflicti828 – 8281A → T in AAI44598. (PubMed:15489334)Curated
    Sequence conflicti1020 – 10201Q → QQ in AAL75811. 1 PublicationCurated
    Sequence conflicti1060 – 10601A → T in AAL75811. 1 PublicationCurated
    Sequence conflicti1510 – 15101N → D in AAL75811. 1 PublicationCurated
    Sequence conflicti1515 – 15151Missing in AAI50627. (PubMed:15489334)Curated
    Sequence conflicti1515 – 15151Missing in AAI44598. (PubMed:15489334)Curated
    Sequence conflicti2343 – 23442KS → LT1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441G → E.
    Corresponds to variant rs133885 [ dbSNP | Ensembl ].
    VAR_056190
    Natural varianti177 – 1771P → L.
    Corresponds to variant rs13058434 [ dbSNP | Ensembl ].
    VAR_056191
    Natural varianti234 – 2341G → V in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015862
    Natural varianti347 – 3471K → N in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015863
    Natural varianti379 – 3791R → Q in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015864
    Natural varianti389 – 3891W → C in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_015865
    Natural varianti547 – 5471W → C.2 Publications
    Corresponds to variant rs3859866 [ dbSNP | Ensembl ].
    VAR_056192
    Natural varianti590 – 5901T → M in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015866
    Natural varianti661 – 6611R → W in a lung adenocarcinoma sample; somatic mutation. 2 Publications
    Corresponds to variant rs5761170 [ dbSNP | Ensembl ].
    VAR_015867
    Natural varianti835 – 8351A → G in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015868
    Natural varianti925 – 9251S → L.1 Publication
    Corresponds to variant rs9624909 [ dbSNP | Ensembl ].
    VAR_056193
    Natural varianti1037 – 10371W → S.
    Corresponds to variant rs17704912 [ dbSNP | Ensembl ].
    VAR_056194
    Natural varianti1095 – 10951R → L in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_015869
    Natural varianti1119 – 11191H → Q.2 Publications
    Corresponds to variant rs5761268 [ dbSNP | Ensembl ].
    VAR_056195
    Natural varianti1195 – 11951R → Q in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015870
    Natural varianti1238 – 12381P → Q in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015871
    Natural varianti1238 – 12381P → T in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_015872
    Natural varianti1390 – 13901S → F.
    Corresponds to variant rs35578357 [ dbSNP | Ensembl ].
    VAR_056196
    Natural varianti1399 – 13991I → V.
    Corresponds to variant rs695633 [ dbSNP | Ensembl ].
    VAR_056197
    Natural varianti1444 – 14441S → T.
    Corresponds to variant rs33928909 [ dbSNP | Ensembl ].
    VAR_056198
    Natural varianti1708 – 17081E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_015873
    Natural varianti1715 – 17151E → D in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_015874
    Natural varianti1970 – 19701A → E in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015875
    Natural varianti2294 – 22941A → D.
    Corresponds to variant rs35370367 [ dbSNP | Ensembl ].
    VAR_056199
    Natural varianti2295 – 22951G → C in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015876
    Natural varianti2347 – 23471Q → R.1 Publication
    Corresponds to variant rs2236005 [ dbSNP | Ensembl ].
    VAR_015877
    Natural varianti2381 – 23811R → H in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_015878
    Natural varianti2395 – 23951G → A.
    Corresponds to variant rs6004901 [ dbSNP | Ensembl ].
    VAR_056200
    Natural varianti2513 – 25131G → S.
    Corresponds to variant rs7284177 [ dbSNP | Ensembl ].
    VAR_056201
    Natural varianti2532 – 25321R → Q.
    Corresponds to variant rs34875296 [ dbSNP | Ensembl ].
    VAR_056202
    Natural varianti2554 – 25541D → E in a lung large cell carcinoma sample; somatic mutation. 1 Publication
    VAR_015879

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 487487Missing in isoform 2. 1 PublicationVSP_007764Add
    BLAST
    Alternative sequencei488 – 50316PAPQE…SRDSD → MGSGAICWFNLRDVGS in isoform 2. 1 PublicationVSP_007765Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB075376 mRNA. Translation: BAC16363.1.
    AB042648 mRNA. Translation: BAB55550.2.
    AJ310931 mRNA. Translation: CAC70712.2.
    AJ310932 Genomic DNA. Translation: CAC70714.3.
    AY077700 mRNA. Translation: AAL75811.1.
    Z98949 Genomic DNA. No translation available.
    AL080245 Genomic DNA. No translation available.
    AL022329 Genomic DNA. No translation available.
    AL079300 Genomic DNA. No translation available.
    BC144597 mRNA. Translation: AAI44598.1.
    BC150626 mRNA. Translation: AAI50627.1.
    AJ271918 mRNA. Translation: CAC81082.1.
    AL833890 mRNA. Translation: CAD38746.1.
    CCDSiCCDS54507.1. [Q8IUG5-1]
    RefSeqiNP_115997.5. NM_032608.5.
    UniGeneiHs.417959.

    Genome annotation databases

    EnsembliENST00000540454; ENSP00000441301; ENSG00000133454.
    GeneIDi84700.
    KEGGihsa:84700.
    UCSCiuc003abz.1. human. [Q8IUG5-1]

    Polymorphism databases

    DMDMi32699565.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB075376 mRNA. Translation: BAC16363.1 .
    AB042648 mRNA. Translation: BAB55550.2 .
    AJ310931 mRNA. Translation: CAC70712.2 .
    AJ310932 Genomic DNA. Translation: CAC70714.3 .
    AY077700 mRNA. Translation: AAL75811.1 .
    Z98949 Genomic DNA. No translation available.
    AL080245 Genomic DNA. No translation available.
    AL022329 Genomic DNA. No translation available.
    AL079300 Genomic DNA. No translation available.
    BC144597 mRNA. Translation: AAI44598.1 .
    BC150626 mRNA. Translation: AAI50627.1 .
    AJ271918 mRNA. Translation: CAC81082.1 .
    AL833890 mRNA. Translation: CAD38746.1 .
    CCDSi CCDS54507.1. [Q8IUG5-1 ]
    RefSeqi NP_115997.5. NM_032608.5.
    UniGenei Hs.417959.

    3D structure databases

    ProteinModelPortali Q8IUG5.
    SMRi Q8IUG5. Positions 505-1395.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124214. 2 interactions.
    IntActi Q8IUG5. 3 interactions.
    STRINGi 9606.ENSP00000386096.

    PTM databases

    PhosphoSitei Q8IUG5.

    Polymorphism databases

    DMDMi 32699565.

    Proteomic databases

    MaxQBi Q8IUG5.
    PaxDbi Q8IUG5.
    PRIDEi Q8IUG5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000540454 ; ENSP00000441301 ; ENSG00000133454 .
    GeneIDi 84700.
    KEGGi hsa:84700.
    UCSCi uc003abz.1. human. [Q8IUG5-1 ]

    Organism-specific databases

    CTDi 84700.
    GeneCardsi GC22P026138.
    H-InvDB HIX0016319.
    HGNCi HGNC:18150. MYO18B.
    HPAi HPA000953.
    MIMi 607295. gene.
    neXtProti NX_Q8IUG5.
    PharmGKBi PA38300.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5022.
    HOVERGENi HBG052544.
    KOi K10362.
    OrthoDBi EOG71P29W.
    PhylomeDBi Q8IUG5.
    TreeFami TF339614.

    Miscellaneous databases

    GeneWikii MYO18B.
    GenomeRNAii 84700.
    NextBioi 74784.
    PROi Q8IUG5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IUG5.
    Bgeei Q8IUG5.
    CleanExi HS_MYO18B.
    Genevestigatori Q8IUG5.

    Family and domain databases

    Gene3Di 4.10.270.10. 1 hit.
    InterProi IPR000048. IQ_motif_EF-hand-BS.
    IPR028561. MYO18B.
    IPR027401. Myosin-like_IQ_dom.
    IPR001609. Myosin_head_motor_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR13140:SF254. PTHR13140:SF254. 1 hit.
    Pfami PF00063. Myosin_head. 2 hits.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00015. IQ. 1 hit.
    SM00242. MYSc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS50096. IQ. 1 hit.
    PS51456. MYOSIN_MOTOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MYO18B, a candidate tumor suppressor gene at chromosome 22q12.1, deleted, mutated, and methylated in human lung cancer."
      Nishioka M., Kohno T., Tani M., Yanaihara N., Tomizawa Y., Otsuka A., Sasaki S., Kobayashi K., Niki T., Maeshima A., Sekido Y., Minna J.D., Sone S., Yokota J.
      Proc. Natl. Acad. Sci. U.S.A. 99:12269-12274(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-234; ASN-347; GLN-379; CYS-389; MET-590; TRP-661; GLY-835; LEU-1095; GLN-1195; GLN-1238; THR-1238; LYS-1708; ASP-1715; GLU-1970; CYS-2295; HIS-2381 AND GLU-2554, POSSIBLE ROLE IN TUMOR SUPPRESSION.
      Tissue: Skeletal muscle.
    2. "Human MYO18B, a novel unconventional myosin heavy chain expressed in striated muscles moves into the myonuclei upon differentiation."
      Salamon M., Millino C., Raffaello A., Mongillo M., Sandri C., Bean C., Negrisolo E., Pallavicini A., Valle G., Zaccolo M., Schiaffino S., Lanfranchi G.
      J. Mol. Biol. 326:137-149(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), CHARACTERIZATION, VARIANT LEU-925.
      Tissue: Skeletal muscle.
    3. "Myosin-like gene expressed in human heart and muscle."
      Gu Y., Ji Y., Penn S.G., Hanzel D.K., Rank D.R., Chen W., Shannon M.E.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS CYS-547 AND GLN-1119.
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-661.
    5. "Full-length sequencing of 100 cDNA clones from human adult skeletal muscle."
      Stanchi F., Lanfranchi G.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2343-2567.
      Tissue: Skeletal muscle.
    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] (ISOFORM 1), VARIANTS CYS-547; GLN-1119 AND ARG-2347.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2359-2567.
      Tissue: Testis.
    8. "Genetic alterations responsible for metastatic phenotypes of lung cancer cells."
      Yokota J., Nishioka M., Tani M., Kohno T.
      Clin. Exp. Metastasis 20:189-193(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE INVOLVEMENT IN SUPPRESSION OF CELL ANCHORAGE-INDEPENDENT GROWTH.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    Entry informationi

    Entry nameiMY18B_HUMAN
    AccessioniPrimary (citable) accession number: Q8IUG5
    Secondary accession number(s): B2RWP3
    , F5GYU7, Q8NDI8, Q8TE65, Q8WWS0, Q96KH2, Q96KR8, Q96KR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 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

    Frequently deleted, mutated, and hypermethylated in lung cancers.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3