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Q8VDD5

- MYH9_MOUSE

UniProt

Q8VDD5 - MYH9_MOUSE

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Protein

Myosin-9

Gene
Myh9
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 By similarity. Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1818ATP Reviewed prediction

GO - Molecular functioni

  1. actin-dependent ATPase activity Source: Ensembl
  2. actin filament binding Source: UniProtKB
  3. ADP binding Source: Ensembl
  4. ATPase activity Source: UniProtKB
  5. ATP binding Source: UniProtKB-KW
  6. microfilament motor activity Source: UniProtKB
  7. protein anchor Source: UniProtKB
  8. protein binding Source: UniProtKB
  9. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. actin filament-based movement Source: UniProtKB
  3. angiogenesis Source: UniProtKB
  4. blood vessel endothelial cell migration Source: UniProtKB
  5. cell adhesion Source: MGI
  6. cell morphogenesis involved in differentiation Source: MGI
  7. cellular component movement Source: MGI
  8. cytokinesis Source: UniProtKB
  9. establishment of meiotic spindle localization Source: MGI
  10. establishment of T cell polarity Source: MGI
  11. in utero embryonic development Source: MGI
  12. meiotic spindle organization Source: MGI
  13. membrane protein ectodomain proteolysis Source: UniProtKB
  14. monocyte differentiation Source: UniProtKB
  15. myoblast fusion Source: MGI
  16. platelet formation Source: UniProtKB
  17. protein transport Source: UniProtKB
  18. regulation of cell shape Source: UniProtKB
  19. single organismal cell-cell adhesion Source: MGI
  20. uropod organization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Myosin

Keywords - Biological processi

Cell adhesion, Cell shape

Keywords - Ligandi

Actin-binding, ATP-binding, Calmodulin-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-9
Alternative name(s):
Cellular myosin heavy chain, type A
Myosin heavy chain 9
Myosin heavy chain, non-muscle IIa
Non-muscle myosin heavy chain A
Short name:
NMMHC-A
Non-muscle myosin heavy chain IIa
Short name:
NMMHC II-a
Short name:
NMMHC-IIA
Gene namesi
Name:Myh9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:107717. Myh9.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmcell cortex
Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells.1 Publication

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. actomyosin contractile ring Source: UniProtKB
  3. cell-cell adherens junction Source: MGI
  4. cell cortex Source: MGI
  5. cell leading edge Source: UniProtKB
  6. cleavage furrow Source: UniProtKB
  7. COP9 signalosome Source: Ensembl
  8. cortical cytoskeleton Source: MGI
  9. cytoplasm Source: UniProtKB
  10. cytosol Source: UniProtKB
  11. extracellular vesicular exosome Source: Ensembl
  12. integrin complex Source: Ensembl
  13. myosin complex Source: MGI
  14. myosin II complex Source: MGI
  15. nucleus Source: UniProtKB
  16. plasma membrane Source: UniProtKB
  17. protein complex Source: UniProtKB
  18. ruffle Source: UniProtKB
  19. stress fiber Source: UniProtKB
  20. uropod Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 19601959Myosin-9PRO_0000123417Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei8 – 81N6-acetyllysine1 Publication
Modified residuei11 – 111Phosphotyrosine By similarity
Modified residuei102 – 1021N6-acetyllysine By similarity
Modified residuei299 – 2991N6-acetyllysine1 Publication
Modified residuei613 – 6131N6-acetyllysine1 Publication
Modified residuei754 – 7541Phosphotyrosine1 Publication
Modified residuei850 – 8501N6-succinyllysine1 Publication
Modified residuei860 – 8601N6-acetyllysine1 Publication
Modified residuei975 – 9751N6-acetyllysine1 Publication
Modified residuei1024 – 10241N6-acetyllysine1 Publication
Modified residuei1249 – 12491N6-acetyllysine1 Publication
Modified residuei1357 – 13571N6-acetyllysine By similarity
Modified residuei1392 – 13921N6-acetyllysine By similarity
Modified residuei1404 – 14041N6-acetyllysine By similarity
Modified residuei1410 – 14101N6-acetyllysine By similarity
Modified residuei1459 – 14591N6-acetyllysine1 Publication
Modified residuei1638 – 16381N6-acetyllysine By similarity
Modified residuei1669 – 16691N6-succinyllysine1 Publication
Modified residuei1714 – 17141Phosphoserine By similarity
Modified residuei1793 – 17931N6-acetyllysine1 Publication
Modified residuei1802 – 18021N6-acetyllysine1 Publication
Modified residuei1845 – 18451N6-acetyllysine1 Publication
Modified residuei1939 – 19391Phosphothreonine2 Publications
Modified residuei1943 – 19431Phosphoserine5 Publications

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8VDD5.
PaxDbiQ8VDD5.
PRIDEiQ8VDD5.

PTM databases

PhosphoSiteiQ8VDD5.

Expressioni

Gene expression databases

ArrayExpressiQ8VDD5.
BgeeiQ8VDD5.
CleanExiMM_MYH9.
GenevestigatoriQ8VDD5.

Interactioni

Subunit structurei

Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). Interacts with SVIL, HTRA3 and SLC6A4 By similarity. Interacts with PDLIM2. Interacts with RASIP1. Interacts with DDR1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Trpm7Q923J13EBI-400906,EBI-8010314

Protein-protein interaction databases

BioGridi201650. 14 interactions.
DIPiDIP-29546N.
IntActiQ8VDD5. 14 interactions.
MINTiMINT-2524850.

Structurei

3D structure databases

ProteinModelPortaliQ8VDD5.
SMRiQ8VDD5. Positions 7-897, 1894-1934.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 776696Myosin motorAdd
BLAST
Domaini779 – 80830IQAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni654 – 67623Actin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili841 – 19261086 Reviewed predictionAdd
BLAST

Domaini

The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.

Sequence similaritiesi

Contains 1 IQ domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00650000092896.
HOGENOMiHOG000173958.
HOVERGENiHBG004704.
InParanoidiQ8VDD5.
KOiK10352.
OMAiMANSSGK.
OrthoDBiEOG71CFK3.
PhylomeDBiQ8VDD5.
TreeFamiTF333601.

Family and domain databases

Gene3Di4.10.270.10. 1 hit.
InterProiIPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[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]

Sequencei

Sequence statusi: Complete.

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

Q8VDD5-1 [UniParc]FASTAAdd to Basket

« Hide

MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSSKNG FEPASLKEEV     50
GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN 100
LKERYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVEMYKG KKRHEMPPHI 150
YAITDTAYRS MMQDREDQSI LCTGESGAGK TENTKKVIQY LAHVASSHKS 200
KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVNGYIV 250
GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY 300
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG 350
NIAFKKERNT DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY 400
VQKAQTKEQA DFAIEALAKA TYERMFRWLV LRINKALDKT KRQGASFIGI 450
LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF NHTMFILEQE EYQREGIEWN 500
FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK SFVEKVVQEQ 550
GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL 600
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY 650
KEQLAKLMAT LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG 700
IRICRQGFPN RVVFQEFRQR YEILTPNSIP KGFMDGKQAC VLMIKALELD 750
SNLYRIGQSK VFFRAGVLAH LEEERDLKIT DVIIGFQACC RGYLARKAFA 800
KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS IRHEDELLAK 850
EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AETELCAEAE 900
ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE 950
QLEEEESARQ KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR 1000
VAEFTTNLME EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR 1050
RKLEGDSTDL SDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEAAQKN 1100
MALKKIRELE TQISELQEDL ESERASRNKA EKQKRDLGEE LEALKTELED 1150
TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE 1200
LADQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV 1250
EAQLQELQVK FSEGERVRTE LADKVTKLQV ELDSVTGLLS QSDSKSSKLT 1300
KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQMEDEKNS FREQLEEEEE 1350
AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL ETAEEAKRRL QKDLEGLSQR 1400
LEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSVSNLE KKQKKFDQLL 1450
AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK 1500
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA 1550
TEDAKLRLEV NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED 1600
ERKQRSMAMA ARKKLEMDLK DLEAHIDTAN KNREEAIKQL RKLQAQMKDC 1650
MRELDDTRAS REEILAQAKE NEKKLKSMEA EMIQLQEELA AAERAKRQAQ 1700
QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE EQGNTELIND 1750
RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KAKLQEMESA 1800
VKSKYKASIA ALEAKIAQLE EQLDNETKER QAASKQVRRT EKKLKDVLLQ 1850
VEDERRNAEQ FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL 1900
EDATETADAM NREVSSLKNK LRRGDLPFVV TRRIVRKGTG DCSDEEVDGK 1950
ADGADAKAAE 1960
Length:1,960
Mass (Da):226,372
Last modified:September 2, 2008 - v4
Checksum:iAAAC0E83A0A4F24A
GO

Sequence cautioni

The sequence BAE27768.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1733 – 17331Q → L in CAC85955. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ312390 mRNA. Translation: CAC85955.1.
AK147203 mRNA. Translation: BAE27761.1.
AK147206 mRNA. Translation: BAE27763.1.
AK147208 mRNA. Translation: BAE27765.1.
AK147209 mRNA. Translation: BAE27766.1.
AK147210 mRNA. Translation: BAE27767.1.
AK147211 mRNA. Translation: BAE27768.1. Different initiation.
AK147215 mRNA. Translation: BAE27772.1.
AK147216 mRNA. Translation: BAE27773.1.
AK147221 mRNA. Translation: BAE27776.1.
AK147222 mRNA. Translation: BAE27777.1.
AK147223 mRNA. Translation: BAE27778.1.
AK147233 mRNA. Translation: BAE27783.1.
AK147235 mRNA. Translation: BAE27785.1.
AK147296 mRNA. Translation: BAE27829.1.
AK147407 mRNA. Translation: BAE27894.1.
AK147430 mRNA. Translation: BAE27906.1.
AL583886 Genomic DNA. Translation: CAM23428.1.
AK131171 mRNA. Translation: BAD21421.1.
BC044834 mRNA. Translation: AAH44834.1.
CCDSiCCDS27605.1.
RefSeqiNP_071855.2. NM_022410.3.
UniGeneiMm.29677.

Genome annotation databases

EnsembliENSMUST00000016771; ENSMUSP00000016771; ENSMUSG00000022443.
GeneIDi17886.
KEGGimmu:17886.
UCSCiuc007woc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ312390 mRNA. Translation: CAC85955.1 .
AK147203 mRNA. Translation: BAE27761.1 .
AK147206 mRNA. Translation: BAE27763.1 .
AK147208 mRNA. Translation: BAE27765.1 .
AK147209 mRNA. Translation: BAE27766.1 .
AK147210 mRNA. Translation: BAE27767.1 .
AK147211 mRNA. Translation: BAE27768.1 . Different initiation.
AK147215 mRNA. Translation: BAE27772.1 .
AK147216 mRNA. Translation: BAE27773.1 .
AK147221 mRNA. Translation: BAE27776.1 .
AK147222 mRNA. Translation: BAE27777.1 .
AK147223 mRNA. Translation: BAE27778.1 .
AK147233 mRNA. Translation: BAE27783.1 .
AK147235 mRNA. Translation: BAE27785.1 .
AK147296 mRNA. Translation: BAE27829.1 .
AK147407 mRNA. Translation: BAE27894.1 .
AK147430 mRNA. Translation: BAE27906.1 .
AL583886 Genomic DNA. Translation: CAM23428.1 .
AK131171 mRNA. Translation: BAD21421.1 .
BC044834 mRNA. Translation: AAH44834.1 .
CCDSi CCDS27605.1.
RefSeqi NP_071855.2. NM_022410.3.
UniGenei Mm.29677.

3D structure databases

ProteinModelPortali Q8VDD5.
SMRi Q8VDD5. Positions 7-897, 1894-1934.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201650. 14 interactions.
DIPi DIP-29546N.
IntActi Q8VDD5. 14 interactions.
MINTi MINT-2524850.

PTM databases

PhosphoSitei Q8VDD5.

Proteomic databases

MaxQBi Q8VDD5.
PaxDbi Q8VDD5.
PRIDEi Q8VDD5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000016771 ; ENSMUSP00000016771 ; ENSMUSG00000022443 .
GeneIDi 17886.
KEGGi mmu:17886.
UCSCi uc007woc.1. mouse.

Organism-specific databases

CTDi 4627.
MGIi MGI:107717. Myh9.

Phylogenomic databases

eggNOGi COG5022.
GeneTreei ENSGT00650000092896.
HOGENOMi HOG000173958.
HOVERGENi HBG004704.
InParanoidi Q8VDD5.
KOi K10352.
OMAi MANSSGK.
OrthoDBi EOG71CFK3.
PhylomeDBi Q8VDD5.
TreeFami TF333601.

Enzyme and pathway databases

Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

ChiTaRSi MYH9. mouse.
NextBioi 292701.
PROi Q8VDD5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8VDD5.
Bgeei Q8VDD5.
CleanExi MM_MYH9.
Genevestigatori Q8VDD5.

Family and domain databases

Gene3Di 4.10.270.10. 1 hit.
InterProi IPR000048. IQ_motif_EF-hand-BS.
IPR027401. Myosin-like_IQ_dom.
IPR001609. Myosin_head_motor_dom.
IPR004009. Myosin_N.
IPR002928. Myosin_tail.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00612. IQ. 1 hit.
PF00063. Myosin_head. 1 hit.
PF02736. Myosin_N. 1 hit.
PF01576. Myosin_tail_1. 1 hit.
[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

« Hide 'large scale' publications
  1. "Cloning of the murine non-muscle myosin heavy chain IIA gene ortholog of human MYH9 responsible for May-Hegglin, Sebastian, Fechtner, and Epstein syndromes."
    D'Apolito M., Guarnieri V., Boncristiano M., Zelante L., Savoia A.
    Gene 286:215-222(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Brain, Embryo, Embryonic liver and Placenta.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.
    Submitted (MAR-2008) to UniProtKB
    Tissue: Embryonic fibroblast.
  5. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 626-1960.
    Strain: ICR.
    Tissue: Embryonic tail.
  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] OF 1066-1960.
    Strain: FVB/N.
    Tissue: Mammary tumor.
  7. Cited for: ISGYLATION.
  8. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The collagen receptor DDR1 regulates cell spreading and motility by associating with myosin IIA."
    Huang Y., Arora P., McCulloch C.A., Vogel W.F.
    J. Cell Sci. 122:1637-1646(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DDR1, IDENTIFICATION BY MASS SPECTROMETRY.
  14. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  15. "Blood vessel tubulogenesis requires Rasip1 regulation of GTPase signaling."
    Xu K., Sacharidou A., Fu S., Chong D.C., Skaug B., Chen Z.J., Davis G.E., Cleaver O.
    Dev. Cell 20:526-539(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RASIP1.
  16. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-299; LYS-613; LYS-860; LYS-975; LYS-1024; LYS-1249; LYS-1459; LYS-1793; LYS-1802 AND LYS-1845, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-850 AND LYS-1669, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiMYH9_MOUSE
AccessioniPrimary (citable) accession number: Q8VDD5
Secondary accession number(s): Q3UHT9
, Q3UHU4, Q6KAN6, Q811I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: September 2, 2008
Last modified: September 3, 2014
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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