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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.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 1818ATPSequence Analysis

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. poly(A) RNA binding Source: Ensembl
  8. protein anchor 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. actomyosin structure organization Source: Ensembl
  4. angiogenesis Source: UniProtKB
  5. blood vessel endothelial cell migration Source: UniProtKB
  6. cell adhesion Source: MGI
  7. cell morphogenesis involved in differentiation Source: MGI
  8. cellular component movement Source: MGI
  9. cytokinesis Source: UniProtKB
  10. establishment of meiotic spindle localization Source: MGI
  11. establishment of T cell polarity Source: MGI
  12. in utero embryonic development Source: MGI
  13. meiotic spindle organization Source: MGI
  14. membrane protein ectodomain proteolysis Source: UniProtKB
  15. monocyte differentiation Source: UniProtKB
  16. myoblast fusion Source: MGI
  17. platelet formation Source: UniProtKB
  18. protein transport Source: UniProtKB
  19. regulation of cell shape Source: UniProtKB
  20. single organismal cell-cell adhesion Source: MGI
  21. 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 1 Publication. Cytoplasmcell cortex 1 Publication
Note: Colocalizes with actin filaments at lamellipodia margins and at the leading edge of migrating cells.

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. myosin II filament Source: Ensembl
  16. nucleus Source: UniProtKB
  17. plasma membrane Source: UniProtKB
  18. protein complex Source: UniProtKB
  19. ruffle Source: UniProtKB
  20. stress fiber Source: UniProtKB
  21. uropod Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
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 – 111PhosphotyrosineBy similarity
Modified residuei102 – 1021N6-acetyllysineBy 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-acetyllysineBy similarity
Modified residuei1392 – 13921N6-acetyllysineBy similarity
Modified residuei1404 – 14041N6-acetyllysineBy similarity
Modified residuei1410 – 14101N6-acetyllysineBy similarity
Modified residuei1459 – 14591N6-acetyllysine1 Publication
Modified residuei1638 – 16381N6-acetyllysineBy similarity
Modified residuei1669 – 16691N6-succinyllysine1 Publication
Modified residuei1714 – 17141PhosphoserineBy 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

BgeeiQ8VDD5.
CleanExiMM_MYH9.
ExpressionAtlasiQ8VDD5. baseline and differential.
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.By similarity2 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, 1902-1930.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 776696Myosin motorAdd
BLAST
Domaini779 – 80830IQPROSITE-ProRule annotationAdd
BLAST

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili841 – 19261086Sequence AnalysisAdd
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.PROSITE-ProRule annotation
Contains 1 myosin motor domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5022.
GeneTreeiENSGT00760000118919.
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

        10         20         30         40         50
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSSKNG FEPASLKEEV
60 70 80 90 100
GEEAIVELVE NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN
110 120 130 140 150
LKERYYSGLI YTYSGLFCVV INPYKNLPIY SEEIVEMYKG KKRHEMPPHI
160 170 180 190 200
YAITDTAYRS MMQDREDQSI LCTGESGAGK TENTKKVIQY LAHVASSHKS
210 220 230 240 250
KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR INFDVNGYIV
260 270 280 290 300
GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
310 320 330 340 350
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG
360 370 380 390 400
NIAFKKERNT DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY
410 420 430 440 450
VQKAQTKEQA DFAIEALAKA TYERMFRWLV LRINKALDKT KRQGASFIGI
460 470 480 490 500
LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF NHTMFILEQE EYQREGIEWN
510 520 530 540 550
FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK SFVEKVVQEQ
560 570 580 590 600
GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
610 620 630 640 650
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY
660 670 680 690 700
KEQLAKLMAT LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG
710 720 730 740 750
IRICRQGFPN RVVFQEFRQR YEILTPNSIP KGFMDGKQAC VLMIKALELD
760 770 780 790 800
SNLYRIGQSK VFFRAGVLAH LEEERDLKIT DVIIGFQACC RGYLARKAFA
810 820 830 840 850
KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS IRHEDELLAK
860 870 880 890 900
EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AETELCAEAE
910 920 930 940 950
ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE
960 970 980 990 1000
QLEEEESARQ KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR
1010 1020 1030 1040 1050
VAEFTTNLME EEEKSKSLAK LKNKHEAMIT DLEERLRREE KQRQELEKTR
1060 1070 1080 1090 1100
RKLEGDSTDL SDQIAELQAQ IAELKMQLAK KEEELQAALA RVEEEAAQKN
1110 1120 1130 1140 1150
MALKKIRELE TQISELQEDL ESERASRNKA EKQKRDLGEE LEALKTELED
1160 1170 1180 1190 1200
TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE
1210 1220 1230 1240 1250
LADQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV
1260 1270 1280 1290 1300
EAQLQELQVK FSEGERVRTE LADKVTKLQV ELDSVTGLLS QSDSKSSKLT
1310 1320 1330 1340 1350
KDFSALESQL QDTQELLQEE NRQKLSLSTK LKQMEDEKNS FREQLEEEEE
1360 1370 1380 1390 1400
AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL ETAEEAKRRL QKDLEGLSQR
1410 1420 1430 1440 1450
LEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSVSNLE KKQKKFDQLL
1460 1470 1480 1490 1500
AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK
1510 1520 1530 1540 1550
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA
1560 1570 1580 1590 1600
TEDAKLRLEV NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED
1610 1620 1630 1640 1650
ERKQRSMAMA ARKKLEMDLK DLEAHIDTAN KNREEAIKQL RKLQAQMKDC
1660 1670 1680 1690 1700
MRELDDTRAS REEILAQAKE NEKKLKSMEA EMIQLQEELA AAERAKRQAQ
1710 1720 1730 1740 1750
QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE EQGNTELIND
1760 1770 1780 1790 1800
RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KAKLQEMESA
1810 1820 1830 1840 1850
VKSKYKASIA ALEAKIAQLE EQLDNETKER QAASKQVRRT EKKLKDVLLQ
1860 1870 1880 1890 1900
VEDERRNAEQ FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL
1910 1920 1930 1940 1950
EDATETADAM NREVSSLKNK LRRGDLPFVV TRRIVRKGTG DCSDEEVDGK
1960
ADGADAKAAE
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1733 – 17331Q → L in CAC85955. (PubMed:11943476)Curated

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, 1902-1930.
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 ENSGT00760000118919.
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

Bgeei Q8VDD5.
CleanExi MM_MYH9.
ExpressionAtlasi Q8VDD5. baseline and differential.
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: October 29, 2014
This is version 118 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