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Q13459

- MYO9B_HUMAN

UniProt

Q13459 - MYO9B_HUMAN

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Protein

Unconventional myosin-IXb

Gene
MYO9B, MYR5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2468ATP Reviewed prediction
Zinc fingeri1632 – 168150Phorbol-ester/DAG-typeAdd
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
Complete GO annotation...

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. myosin complex Source: UniProtKB-KW
  9. perinuclear region of cytoplasm Source: UniProtKB
  10. ruffle Source: Ensembl
Complete GO annotation...

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.1 Publication

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 – 12421Phosphoserine By 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 114100Ras-associatingAdd
BLAST
Domaini146 – 953808Myosin motorAdd
BLAST
Domaini957 – 97721IQ 1Add
BLAST
Domaini979 – 100022IQ 2Add
BLAST
Domaini1001 – 102323IQ 3Add
BLAST
Domaini1024 – 105330IQ 4Add
BLAST
Domaini1703 – 1888186Rho-GAPAdd
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 – 107126 Reviewed predictionAdd
BLAST
Coiled coili1880 – 190122 Reviewed predictionAdd
BLAST
Coiled coili1959 – 198931 Reviewed predictionAdd
BLAST

Sequence similaritiesi

Contains 4 IQ domains.
Contains 1 Rho-GAP domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1632 – 168150Phorbol-ester/DAG-typeAdd
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2021 – 20222PP → QY in isoform Short. VSP_003361
Alternative sequencei2023 – 2157135Missing in isoform Short. VSP_003362Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2382IS → YP in AAC50402. 1 Publication
Sequence conflicti276 – 2761G → C in AAC50402. 1 Publication
Sequence conflicti1011 – 10111S → A in AAC50402. 1 Publication
Sequence conflicti1693 – 16931V → A in AAC50402. 1 Publication
Sequence conflicti1946 – 19461L → P in BAA92132. 1 Publication
Sequence conflicti2039 – 20446TVAAPP → PWPPLH in AAC26597. 1 Publication
Sequence conflicti2048 – 20481P → L in AAC26597. 1 Publication
Sequence conflicti2066 – 20661P → S in AAC26597. 1 Publication
Sequence conflicti2156 – 21572NG → MAESHS in AAC26597. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 150 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).

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

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