Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13459

- MYO9B_HUMAN

UniProt

Q13459 - MYO9B_HUMAN

Protein

Unconventional myosin-IXb

Gene

MYO9B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (08 Mar 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. May be involved in the remodeling of the actin cytoskeleton. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions. Also acts as a GTPase activating protein on Rho.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi239 – 2468ATPSequence Analysis
    Zinc fingeri1632 – 168150Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. actin-dependent ATPase activity Source: Ensembl
    3. ADP binding Source: UniProtKB
    4. ATPase activity Source: UniProtKB
    5. ATP binding Source: UniProtKB
    6. calmodulin binding Source: UniProtKB
    7. microfilament motor activity Source: UniProtKB
    8. protein binding Source: IntAct
    9. Rho GTPase activator activity Source: UniProtKB
    10. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. actin filament-based movement Source: UniProtKB
    2. establishment of cell polarity Source: Ensembl
    3. lamellipodium morphogenesis Source: Ensembl
    4. macrophage chemotaxis Source: Ensembl
    5. monocyte chemotaxis Source: Ensembl
    6. regulation of small GTPase mediated signal transduction Source: Reactome
    7. Rho protein signal transduction Source: UniProtKB
    8. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation, Motor protein, Myosin

    Keywords - Ligandi

    Actin-binding, ATP-binding, Calmodulin-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Unconventional myosin-IXb
    Alternative name(s):
    Unconventional myosin-9b
    Gene namesi
    Name:MYO9B
    Synonyms:MYR5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:7609. MYO9B.

    Subcellular locationi

    Cytoplasmcell cortex. Cytoplasmperinuclear region. Cytoplasmcytoskeleton
    Note: In undifferentiated cells colocalizes with F-actin in the cell periphery while in differentiated cells its localization is cytoplasmic with the highest levels in the perinuclear region.

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cell cortex Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. cytosol Source: Reactome
    5. filamentous actin Source: UniProtKB
    6. filopodium tip Source: Ensembl
    7. lamellipodium Source: Ensembl
    8. membrane Source: UniProtKB
    9. myosin complex Source: UniProtKB-KW
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. ruffle Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Celiac disease 4 (CELIAC4) [MIM:609753]: A multifactorial, chronic disorder of the small intestine caused by intolerance to gluten. It is characterized by immune-mediated enteropathy associated with failed intestinal absorption, and malnutrition. In predisposed individuals, the ingestion of gluten-containing food such as wheat and rye induces a flat jejunal mucosa with infiltration of lymphocytes.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi609753. phenotype.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 21572156Unconventional myosin-IXbPRO_0000123469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei716 – 7161Phosphoserine1 Publication
    Modified residuei1242 – 12421PhosphoserineBy similarity
    Modified residuei1267 – 12671Phosphoserine3 Publications
    Modified residuei1271 – 12711Phosphothreonine3 Publications
    Modified residuei1290 – 12901Phosphoserine7 Publications
    Modified residuei1323 – 13231Phosphoserine1 Publication
    Modified residuei1346 – 13461Phosphothreonine1 Publication
    Modified residuei1354 – 13541Phosphoserine2 Publications
    Modified residuei1405 – 14051Phosphoserine1 Publication
    Modified residuei1992 – 19921Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13459.
    PaxDbiQ13459.
    PRIDEiQ13459.

    PTM databases

    PhosphoSiteiQ13459.

    Expressioni

    Tissue specificityi

    Expressed predominantly in peripheral blood leukocytes and at lower levels, in thymus, spleen, testis, prostate, ovary, brain, small intestine and lung.

    Gene expression databases

    ArrayExpressiQ13459.
    BgeeiQ13459.
    CleanExiHS_MYO9B.
    GenevestigatoriQ13459.

    Organism-specific databases

    HPAiCAB037190.
    HPA042043.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARFGEF1Q9Y6D62EBI-6251250,EBI-1044254

    Protein-protein interaction databases

    BioGridi110734. 7 interactions.
    IntActiQ13459. 8 interactions.
    MINTiMINT-1419073.
    STRINGi9606.ENSP00000380444.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 114100Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini146 – 953808Myosin motorAdd
    BLAST
    Domaini957 – 97721IQ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini979 – 100022IQ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1001 – 102323IQ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1024 – 105330IQ 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1703 – 1888186Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni844 – 85512Actin-bindingAdd
    BLAST
    Regioni940 – 1044105Neck or regulatory domainAdd
    BLAST
    Regioni1045 – 21571113TailAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1046 – 107126Sequence AnalysisAdd
    BLAST
    Coiled coili1880 – 190122Sequence AnalysisAdd
    BLAST
    Coiled coili1959 – 198931Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 4 IQ domains.PROSITE-ProRule annotation
    Contains 1 myosin motor domain.Curated
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 Ras-associating domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1632 – 168150Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5022.
    HOGENOMiHOG000113707.
    HOVERGENiHBG052558.
    InParanoidiQ13459.
    KOiK10360.
    OrthoDBiEOG7CK35Z.
    PhylomeDBiQ13459.
    TreeFamiTF319651.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR000048. IQ_motif_EF-hand-BS.
    IPR028557. MYO9B.
    IPR001609. Myosin_head_motor_dom.
    IPR027417. P-loop_NTPase.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000159. Ras-assoc.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR13140:SF306. PTHR13140:SF306. 1 hit.
    PfamiPF00612. IQ. 4 hits.
    PF00063. Myosin_head. 1 hit.
    PF00788. RA. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    PRINTSiPR00193. MYOSINHEAVY.
    SMARTiSM00109. C1. 1 hit.
    SM00015. IQ. 4 hits.
    SM00242. MYSc. 1 hit.
    SM00314. RA. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF52540. SSF52540. 3 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50096. IQ. 3 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    PS50200. RA. 1 hit.
    PS50238. RHOGAP. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q13459-1) [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

    MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD     50
    AIASLRLDGT KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP 100
    QEDGYYFLLQ ERNADGTIKY VHMQLVAQAT ATRRLVERGL LPRQQADFDD 150
    LCNLPELTEG NLLKNLKHRF LQQKIYTYAG SILVAINPFK FLPIYNPKYV 200
    KMYENQQLGK LEPHVFALAD VAYYTMLRKR VNQCIVISGE SGSGKTQSTN 250
    FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI 300
    QVSYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER 350
    QEFQLKQPED YFYLNQHNLK IEDGEDLKHD FERLKQAMEM VGFLPATKKQ 400
    IFAVLSAILY LGNVTYKKRA TGREEGLEVG PPEVLDTLSQ LLKVKREILV 450
    EVLTKRKTVT VNDKLILPYS LSEAITARDS MAKSLYSALF DWIVLRINHA 500
    LLNKKDVEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA NEQLQYYFNQ 550
    HIFKLEQEEY QGEGITWHNI GYTDNVGCIH LISKKPTGLF YLLDEESNFP 600
    HATSQTLLAK FKQQHEDNKY FLGTPVMEPA FIIQHFAGKV KYQIKDFREK 650
    NMDYMRPDIV ALLRGSDSSY VRELIGMDPV AVFRWAVLRA AIRAMAVLRE 700
    AGRLRAERAE KAAGMSSPGA QSHPEELPRG ASTPSEKLYR DLHNQMIKSI 750
    KGLPWQGEDP RSLLQSLSRL QKPRAFILKS KGIKQKQIIP KNLLDSKSLK 800
    LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE ALGKAEPFFI 850
    RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE 900
    QFQVLLPKDA QPCREVISTL LEKMKIDKRN YQIGKTKVFL KETERQALQE 950
    TLHREVVRKI LLLQSWFRMV LERRHFLQMK RAAVTIQACW RSYRVRRALE 1000
    RTQAAVYLQA SWRGYWQRKL YRHQKQSIIR LQSLCRGHLQ RKSFSQMISE 1050
    KQKAEEKERE ALEAARAGAE EGGQGQAAGG QQVAEQGPEP AEDGGHLASE 1100
    PEVQPSDRSP LEHSSPEKEA PSPEKTLPPQ KTVAAESHEK VPSSREKRES 1150
    RRQRGLEHVK FQNKHIQSCK EESALREPSR RVTQEQGVSL LEDKKESRED 1200
    ETLLVVETEA ENTSQKQPTE QPQAMAVGKV SEETEKTLPS GSPRPGQLER 1250
    PTSLALDSRV SPPAPGSAPE TPEDKSKPCG SPRVQEKPDS PGGSTQIQRY 1300
    LDAERLASAV ELWRGKKLVA AASPSAMLSQ SLDLSDRHRA TGAALTPTEE 1350
    RRTSFSTSDV SKLLPSLAKA QPAAETTDGE RSAKKPAVQK KKPGDASSLP 1400
    DAGLSPGSQV DSKSTFKRLF LHKTKDKKYS LEGAEELENA VSGHVVLEAT 1450
    TMKKGLEAPS GQQHRHAAGE KRTKEPGGKG KKNRNVKIGK ITVSEKWRES 1500
    VFRQITNANE LKYLDEFLLN KINDLRSQKT PIESLFIEAT EKFRSNIKTM 1550
    YSVPNGKIHV GYKDLMENYQ IVVSNLATER GQKDTNLVLN LFQSLLDEFT 1600
    RGYTKNDFEP VKQSKAQKKK RKQERAVQEH NGHVFASYQV SIPQSCEQCL 1650
    SYIWLMDKAL LCSVCKMTCH KKCVHKIQSH CSYTYGRKGE PGVEPGHFGV 1700
    CVDSLTSDKA SVPIVLEKLL EHVEMHGLYT EGLYRKSGAA NRTRELRQAL 1750
    QTDPAAVKLE NFPIHAITGV LKQWLRELPE PLMTFAQYGD FLRAVELPEK 1800
    QEQLAAIYAV LEHLPEANHN SLERLIFHLV KVALLEDVNR MSPGALAIIF 1850
    APCLLRCPDN SDPLTSMKDV LKITTCVEML IKEQMRKYKV KMEEISQLEA 1900
    AESIAFRRLS LLRQNAPWPL KLGFSSPYEG VLNKSPKTRD IQEEELEVLL 1950
    EEEAAGGDED REKEILIERI QSIKEEKEDI TYRLPELDPR GSDEENLDSE 2000
    TSASTESLLE ERAGRGASEG PPAPALPCPG APTPSPLPTV AAPPRRRPSS 2050
    FVTVRVKTPR RTPIMPTANI KLPPGLPSHL PRWAPGAREA AAPVRRREPP 2100
    ARRPDQIHSV YITPGADLPV QGALEPLEED GQPPGAKRRY SDPPTYCLPP 2150
    ASGQTNG 2157
    Length:2,157
    Mass (Da):243,401
    Last modified:March 8, 2011 - v3
    Checksum:iA3E72CAB759CD5FD
    GO
    Isoform Short (identifier: Q13459-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2021-2022: PP → QY
         2023-2157: Missing.

    Show »
    Length:2,022
    Mass (Da):229,143
    Checksum:iD0E47A7EAF86A929
    GO

    Sequence cautioni

    The sequence AAC50402.1 differs from that shown. Reason: The C-terminal sequence from position 1917 onwards appears to be not correctly spliced.
    The sequence BAA92132.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2382IS → YP in AAC50402. (PubMed:8907710)Curated
    Sequence conflicti276 – 2761G → C in AAC50402. (PubMed:8907710)Curated
    Sequence conflicti1011 – 10111S → A in AAC50402. (PubMed:8907710)Curated
    Sequence conflicti1693 – 16931V → A in AAC50402. (PubMed:8907710)Curated
    Sequence conflicti1946 – 19461L → P in BAA92132. (PubMed:9490638)Curated
    Sequence conflicti2039 – 20446TVAAPP → PWPPLH in AAC26597. (PubMed:10580159)Curated
    Sequence conflicti2048 – 20481P → L in AAC26597. (PubMed:10580159)Curated
    Sequence conflicti2066 – 20661P → S in AAC26597. (PubMed:10580159)Curated
    Sequence conflicti2156 – 21572NG → MAESHS in AAC26597. (PubMed:10580159)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2021 – 20222PP → QY in isoform Short. 1 PublicationVSP_003361
    Alternative sequencei2023 – 2157135Missing in isoform Short. 1 PublicationVSP_003362Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42391 mRNA. Translation: AAC50402.1. Sequence problems.
    AC020913 Genomic DNA. No translation available.
    AC020908 Genomic DNA. No translation available.
    AF143684 mRNA. Translation: AAF00119.1.
    AF020267 mRNA. Translation: AAC26597.1.
    AK002201 mRNA. Translation: BAA92132.1. Different initiation.
    CCDSiCCDS46010.1. [Q13459-2]
    RefSeqiNP_004136.2. NM_004145.3. [Q13459-1]
    XP_006722818.1. XM_006722755.1. [Q13459-1]
    UniGeneiHs.123198.

    Genome annotation databases

    EnsembliENST00000397274; ENSP00000380444; ENSG00000099331. [Q13459-2]
    ENST00000595618; ENSP00000471457; ENSG00000099331. [Q13459-2]
    GeneIDi4650.
    KEGGihsa:4650.
    UCSCiuc002nfi.3. human. [Q13459-2]
    uc002nfj.1. human. [Q13459-1]

    Polymorphism databases

    DMDMi325511388.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    MYO9B entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42391 mRNA. Translation: AAC50402.1 . Sequence problems.
    AC020913 Genomic DNA. No translation available.
    AC020908 Genomic DNA. No translation available.
    AF143684 mRNA. Translation: AAF00119.1 .
    AF020267 mRNA. Translation: AAC26597.1 .
    AK002201 mRNA. Translation: BAA92132.1 . Different initiation.
    CCDSi CCDS46010.1. [Q13459-2 ]
    RefSeqi NP_004136.2. NM_004145.3. [Q13459-1 ]
    XP_006722818.1. XM_006722755.1. [Q13459-1 ]
    UniGenei Hs.123198.

    3D structure databases

    ProteinModelPortali Q13459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110734. 7 interactions.
    IntActi Q13459. 8 interactions.
    MINTi MINT-1419073.
    STRINGi 9606.ENSP00000380444.

    PTM databases

    PhosphoSitei Q13459.

    Polymorphism databases

    DMDMi 325511388.

    Proteomic databases

    MaxQBi Q13459.
    PaxDbi Q13459.
    PRIDEi Q13459.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397274 ; ENSP00000380444 ; ENSG00000099331 . [Q13459-2 ]
    ENST00000595618 ; ENSP00000471457 ; ENSG00000099331 . [Q13459-2 ]
    GeneIDi 4650.
    KEGGi hsa:4650.
    UCSCi uc002nfi.3. human. [Q13459-2 ]
    uc002nfj.1. human. [Q13459-1 ]

    Organism-specific databases

    CTDi 4650.
    GeneCardsi GC19P017186.
    HGNCi HGNC:7609. MYO9B.
    HPAi CAB037190.
    HPA042043.
    MIMi 602129. gene.
    609753. phenotype.
    neXtProti NX_Q13459.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5022.
    HOGENOMi HOG000113707.
    HOVERGENi HBG052558.
    InParanoidi Q13459.
    KOi K10360.
    OrthoDBi EOG7CK35Z.
    PhylomeDBi Q13459.
    TreeFami TF319651.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    ChiTaRSi MYO9B. human.
    GeneWikii MYO9B.
    GenomeRNAii 4650.
    NextBioi 17928.
    PROi Q13459.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13459.
    Bgeei Q13459.
    CleanExi HS_MYO9B.
    Genevestigatori Q13459.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR000048. IQ_motif_EF-hand-BS.
    IPR028557. MYO9B.
    IPR001609. Myosin_head_motor_dom.
    IPR027417. P-loop_NTPase.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000159. Ras-assoc.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR13140:SF306. PTHR13140:SF306. 1 hit.
    Pfami PF00612. IQ. 4 hits.
    PF00063. Myosin_head. 1 hit.
    PF00788. RA. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    PRINTSi PR00193. MYOSINHEAVY.
    SMARTi SM00109. C1. 1 hit.
    SM00015. IQ. 4 hits.
    SM00242. MYSc. 1 hit.
    SM00314. RA. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF52540. SSF52540. 3 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50096. IQ. 3 hits.
    PS51456. MYOSIN_MOTOR. 1 hit.
    PS50200. RA. 1 hit.
    PS50238. RHOGAP. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail."
      Wirth J.A., Jensen K.A., Post P.L., Bement W.M., Mooseker M.S.
      J. Cell Sci. 109:653-661(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG/SHORT).
      Tissue: Liver and Small intestine.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Cloning of the murine unconventional myosin gene Myo9b and identification of alternative splicing."
      Grewal P.K., Jones A.-M., Maconochie M., Lemmers R.J.F., Frants R.R., Hewitt J.E.
      Gene 240:389-398(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    4. "Human myosin-IXb is a mechanochemically active motor and a GAP for rho."
      Post P.L., Bokoch G.M., Mooseker M.S.
      J. Cell Sci. 111:941-950(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1940-2157 (ISOFORM LONG).
    5. "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] OF 1828-2022 (ISOFORM SHORT).
      Tissue: Placenta.
    6. Cited for: ASSOCIATION WITH CELIAC DISEASE 4.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271 AND SER-1290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290 AND SER-1405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716; SER-1290; SER-1354 AND SER-1992, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290 AND SER-1992, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271 AND SER-1992, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290; SER-1323 AND THR-1346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271; SER-1290; SER-1354 AND SER-1992, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMYO9B_HUMAN
    AccessioniPrimary (citable) accession number: Q13459
    Secondary accession number(s): O75314, Q9NUJ2, Q9UHN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: March 8, 2011
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 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

    Caution

    Represents an unconventional myosin. This protein should not be confused with the conventional myosin-9 (MYH9).Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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