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Protein

Unconventional myosin-IXb

Gene

MYO9B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Binds actin with high affinity both in the absence and presence of ATP and its mechanochemical activity is inhibited by calcium ions (PubMed:9490638). Also acts as a GTPase activator for RHOA (PubMed:9490638, PubMed:26529257). Plays a role in the regulation of cell migration via its role as RHOA GTPase activator. This is regulated by its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs interaction with RHOA and subsequent activation of RHOA GTPase activity, and thereby leads to increased levels of active, GTP-bound RHOA (PubMed:26529257).2 Publications

Regions

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

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin-dependent ATPase activity Source: Ensembl
  • ADP binding Source: UniProtKB
  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • GTPase activator activity Source: UniProtKB
  • microfilament motor activity Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB
  • Roundabout binding Source: UniProtKB
  • zinc ion binding Source: Ensembl

GO - Biological processi

  • actin filament-based movement Source: UniProtKB
  • regulation of Rho protein signal transduction Source: UniProtKB
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • Rho protein signal transduction Source: UniProtKB
  • Roundabout signaling pathway Source: UniProtKB
  • 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

ReactomeiR-HSA-194840. Rho GTPase cycle.
R-HSA-2029482. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:7609. MYO9B.

Subcellular locationi

  • Cytoplasmcell cortex 1 Publication
  • Cytoplasmperinuclear region 1 Publication
  • Cytoplasmcytoskeleton 2 Publications

  • 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.1 Publication

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • actin filament Source: UniProtKB
  • cell cortex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • lamellipodium Source: Ensembl
  • membrane Source: UniProtKB
  • myosin complex Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: UniProtKB
  • ruffle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Celiac disease 4 (CELIAC4)
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:609753

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1739 – 17391A → E or N: Decreases interaction with RHOA. Strongly decreases stimulation of RHOA GTPase activity. 1 Publication
Mutagenesisi1741 – 17411N → E: Decreases interaction with RHOA. Decreases stimulation of RHOA GTPase activity. 1 Publication
Mutagenesisi1742 – 17421R → E: Strongly decreases interaction with RHOA. Strongly decreases stimulation of RHOA GTPase activity. 1 Publication

Organism-specific databases

MalaCardsiMYO9B.
MIMi609753. phenotype.

Polymorphism and mutation databases

BioMutaiMYO9B.
DMDMi325511388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 21572156Unconventional myosin-IXbPRO_0000123469Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei716 – 7161PhosphoserineCombined sources
Modified residuei1045 – 10451PhosphoserineBy similarity
Modified residuei1242 – 12421PhosphoserineBy similarity
Modified residuei1253 – 12531PhosphoserineBy similarity
Modified residuei1261 – 12611PhosphoserineCombined sources
Modified residuei1267 – 12671PhosphoserineCombined sources
Modified residuei1271 – 12711PhosphothreonineCombined sources
Modified residuei1290 – 12901PhosphoserineCombined sources
Modified residuei1323 – 13231PhosphoserineCombined sources
Modified residuei1346 – 13461PhosphothreonineCombined sources
Modified residuei1354 – 13541PhosphoserineCombined sources
Modified residuei1356 – 13561PhosphoserineCombined sources
Modified residuei1405 – 14051PhosphoserineCombined sources
Modified residuei1992 – 19921PhosphoserineCombined sources
Modified residuei1999 – 19991PhosphoserineBy similarity
Modified residuei2005 – 20051PhosphothreonineBy similarity
Modified residuei2141 – 21411PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13459.
MaxQBiQ13459.
PaxDbiQ13459.
PRIDEiQ13459.

PTM databases

iPTMnetiQ13459.
PhosphoSiteiQ13459.

Expressioni

Tissue specificityi

Detected in peripheral blood leukocytes (at protein level) (PubMed:9490638). Expressed predominantly in peripheral blood leukocytes and at lower levels, in thymus, spleen, testis, prostate, ovary, brain, small intestine and lung.2 Publications

Gene expression databases

BgeeiQ13459.
CleanExiHS_MYO9B.
ExpressionAtlasiQ13459. baseline and differential.
GenevisibleiQ13459. HS.

Organism-specific databases

HPAiCAB037190.
HPA042043.

Interactioni

Subunit structurei

Interacts (via IQ domains) with CALM (PubMed:9490638). Interacts with RHOA (PubMed:26529257). Interacts (via Rho-GAP domain) with ROBO1; this inhibits the interaction with RHOA and the stimulation of RHOA GTPase activity, and thereby increases the levels of active RHOA (PubMed:26529257).1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB
  • Roundabout binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110734. 24 interactions.
IntActiQ13459. 10 interactions.
MINTiMINT-1419073.
STRINGi9606.ENSP00000380444.

Structurei

Secondary structure

1
2157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1697 – 17004Combined sources
Helixi1702 – 17054Combined sources
Helixi1714 – 172613Combined sources
Turni1727 – 17293Combined sources
Turni1731 – 17355Combined sources
Helixi1740 – 175213Combined sources
Helixi1759 – 17613Combined sources
Helixi1764 – 177613Combined sources
Beta strandi1778 – 17803Combined sources
Helixi1788 – 17958Combined sources
Beta strandi1797 – 17993Combined sources
Helixi1800 – 181112Combined sources
Helixi1816 – 183419Combined sources
Helixi1836 – 18394Combined sources
Helixi1843 – 185412Combined sources
Helixi1866 – 189530Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5C5SX-ray2.20A/B/C/D1691-1916[»]
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-bindingCuratedAdd
BLAST
Regioni940 – 1044105Neck or regulatory domainCuratedAdd
BLAST
Regioni1045 – 21571113TailCuratedAdd
BLAST
Regioni1739 – 17446Interaction with RHOA1 Publication

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

eggNOGiKOG1453. Eukaryota.
KOG4229. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129687.
HOGENOMiHOG000113707.
HOVERGENiHBG052558.
InParanoidiQ13459.
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. PE/DAG-bd.
IPR000159. RA_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR13140:SF306. PTHR13140:SF306. 4 hits.
PfamiPF00612. IQ. 4 hits.
PF00063. Myosin_head. 2 hits.
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. AlignAdd to basket

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

        10         20         30         40         50
MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD
60 70 80 90 100
AIASLRLDGT KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP
110 120 130 140 150
QEDGYYFLLQ ERNADGTIKY VHMQLVAQAT ATRRLVERGL LPRQQADFDD
160 170 180 190 200
LCNLPELTEG NLLKNLKHRF LQQKIYTYAG SILVAINPFK FLPIYNPKYV
210 220 230 240 250
KMYENQQLGK LEPHVFALAD VAYYTMLRKR VNQCIVISGE SGSGKTQSTN
260 270 280 290 300
FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
310 320 330 340 350
QVSYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER
360 370 380 390 400
QEFQLKQPED YFYLNQHNLK IEDGEDLKHD FERLKQAMEM VGFLPATKKQ
410 420 430 440 450
IFAVLSAILY LGNVTYKKRA TGREEGLEVG PPEVLDTLSQ LLKVKREILV
460 470 480 490 500
EVLTKRKTVT VNDKLILPYS LSEAITARDS MAKSLYSALF DWIVLRINHA
510 520 530 540 550
LLNKKDVEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA NEQLQYYFNQ
560 570 580 590 600
HIFKLEQEEY QGEGITWHNI GYTDNVGCIH LISKKPTGLF YLLDEESNFP
610 620 630 640 650
HATSQTLLAK FKQQHEDNKY FLGTPVMEPA FIIQHFAGKV KYQIKDFREK
660 670 680 690 700
NMDYMRPDIV ALLRGSDSSY VRELIGMDPV AVFRWAVLRA AIRAMAVLRE
710 720 730 740 750
AGRLRAERAE KAAGMSSPGA QSHPEELPRG ASTPSEKLYR DLHNQMIKSI
760 770 780 790 800
KGLPWQGEDP RSLLQSLSRL QKPRAFILKS KGIKQKQIIP KNLLDSKSLK
810 820 830 840 850
LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE ALGKAEPFFI
860 870 880 890 900
RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE
910 920 930 940 950
QFQVLLPKDA QPCREVISTL LEKMKIDKRN YQIGKTKVFL KETERQALQE
960 970 980 990 1000
TLHREVVRKI LLLQSWFRMV LERRHFLQMK RAAVTIQACW RSYRVRRALE
1010 1020 1030 1040 1050
RTQAAVYLQA SWRGYWQRKL YRHQKQSIIR LQSLCRGHLQ RKSFSQMISE
1060 1070 1080 1090 1100
KQKAEEKERE ALEAARAGAE EGGQGQAAGG QQVAEQGPEP AEDGGHLASE
1110 1120 1130 1140 1150
PEVQPSDRSP LEHSSPEKEA PSPEKTLPPQ KTVAAESHEK VPSSREKRES
1160 1170 1180 1190 1200
RRQRGLEHVK FQNKHIQSCK EESALREPSR RVTQEQGVSL LEDKKESRED
1210 1220 1230 1240 1250
ETLLVVETEA ENTSQKQPTE QPQAMAVGKV SEETEKTLPS GSPRPGQLER
1260 1270 1280 1290 1300
PTSLALDSRV SPPAPGSAPE TPEDKSKPCG SPRVQEKPDS PGGSTQIQRY
1310 1320 1330 1340 1350
LDAERLASAV ELWRGKKLVA AASPSAMLSQ SLDLSDRHRA TGAALTPTEE
1360 1370 1380 1390 1400
RRTSFSTSDV SKLLPSLAKA QPAAETTDGE RSAKKPAVQK KKPGDASSLP
1410 1420 1430 1440 1450
DAGLSPGSQV DSKSTFKRLF LHKTKDKKYS LEGAEELENA VSGHVVLEAT
1460 1470 1480 1490 1500
TMKKGLEAPS GQQHRHAAGE KRTKEPGGKG KKNRNVKIGK ITVSEKWRES
1510 1520 1530 1540 1550
VFRQITNANE LKYLDEFLLN KINDLRSQKT PIESLFIEAT EKFRSNIKTM
1560 1570 1580 1590 1600
YSVPNGKIHV GYKDLMENYQ IVVSNLATER GQKDTNLVLN LFQSLLDEFT
1610 1620 1630 1640 1650
RGYTKNDFEP VKQSKAQKKK RKQERAVQEH NGHVFASYQV SIPQSCEQCL
1660 1670 1680 1690 1700
SYIWLMDKAL LCSVCKMTCH KKCVHKIQSH CSYTYGRKGE PGVEPGHFGV
1710 1720 1730 1740 1750
CVDSLTSDKA SVPIVLEKLL EHVEMHGLYT EGLYRKSGAA NRTRELRQAL
1760 1770 1780 1790 1800
QTDPAAVKLE NFPIHAITGV LKQWLRELPE PLMTFAQYGD FLRAVELPEK
1810 1820 1830 1840 1850
QEQLAAIYAV LEHLPEANHN SLERLIFHLV KVALLEDVNR MSPGALAIIF
1860 1870 1880 1890 1900
APCLLRCPDN SDPLTSMKDV LKITTCVEML IKEQMRKYKV KMEEISQLEA
1910 1920 1930 1940 1950
AESIAFRRLS LLRQNAPWPL KLGFSSPYEG VLNKSPKTRD IQEEELEVLL
1960 1970 1980 1990 2000
EEEAAGGDED REKEILIERI QSIKEEKEDI TYRLPELDPR GSDEENLDSE
2010 2020 2030 2040 2050
TSASTESLLE ERAGRGASEG PPAPALPCPG APTPSPLPTV AAPPRRRPSS
2060 2070 2080 2090 2100
FVTVRVKTPR RTPIMPTANI KLPPGLPSHL PRWAPGAREA AAPVRRREPP
2110 2120 2130 2140 2150
ARRPDQIHSV YITPGADLPV QGALEPLEED GQPPGAKRRY SDPPTYCLPP

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

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:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.123198.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

MYO9B entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.123198.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5C5SX-ray2.20A/B/C/D1691-1916[»]
ProteinModelPortaliQ13459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110734. 24 interactions.
IntActiQ13459. 10 interactions.
MINTiMINT-1419073.
STRINGi9606.ENSP00000380444.

PTM databases

iPTMnetiQ13459.
PhosphoSiteiQ13459.

Polymorphism and mutation databases

BioMutaiMYO9B.
DMDMi325511388.

Proteomic databases

EPDiQ13459.
MaxQBiQ13459.
PaxDbiQ13459.
PRIDEiQ13459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4650.
GeneCardsiMYO9B.
HGNCiHGNC:7609. MYO9B.
HPAiCAB037190.
HPA042043.
MalaCardsiMYO9B.
MIMi602129. gene.
609753. phenotype.
neXtProtiNX_Q13459.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1453. Eukaryota.
KOG4229. Eukaryota.
COG5022. LUCA.
GeneTreeiENSGT00840000129687.
HOGENOMiHOG000113707.
HOVERGENiHBG052558.
InParanoidiQ13459.
OrthoDBiEOG7CK35Z.
PhylomeDBiQ13459.
TreeFamiTF319651.

Enzyme and pathway databases

ReactomeiR-HSA-194840. Rho GTPase cycle.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

ChiTaRSiMYO9B. human.
GeneWikiiMYO9B.
GenomeRNAii4650.
NextBioi17928.
PROiQ13459.
SOURCEiSearch...

Gene expression databases

BgeeiQ13459.
CleanExiHS_MYO9B.
ExpressionAtlasiQ13459. baseline and differential.
GenevisibleiQ13459. HS.

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. PE/DAG-bd.
IPR000159. RA_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR13140:SF306. PTHR13140:SF306. 4 hits.
PfamiPF00612. IQ. 4 hits.
PF00063. Myosin_head. 2 hits.
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]
ProtoNetiSearch...

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), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    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), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1261; SER-1267; THR-1271; SER-1290; THR-1346 AND SER-1356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppression."
    Kong R., Yi F., Wen P., Liu J., Chen X., Ren J., Li X., Shang Y., Nie Y., Wu K., Fan D., Zhu L., Feng W., Wu J.Y.
    J. Clin. Invest. 125:4407-4420(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1691-1916, FUNCTION, INTERACTION WITH ROBO1 AND RHOA, MUTAGENESIS OF ALA-1739; ASN-1741 AND ARG-1742.

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: May 11, 2016
This is version 170 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.