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Protein

Myoferlin

Gene

Myof

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

Functioni

Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR.3 Publications

Cofactori

Ca2+Note: Binds Ca2+. The ions are bound to the C2 1 domain.

GO - Molecular functioni

  • phospholipid binding Source: UniProtKB

GO - Biological processi

  • cellular response to heat Source: MGI
  • plasma membrane repair Source: UniProtKB
  • regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Myoferlin
Alternative name(s):
Fer-1-like protein 3
Gene namesi
Name:Myof
Synonyms:Fer1l3, Kiaa1207
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1919192. Myof.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 20122012CytoplasmicSequence analysisAdd
BLAST
Transmembranei2013 – 203321HelicalSequence analysisAdd
BLAST
Topological domaini2034 – 204815ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671I → D: Reduces calcium-sensitive phospholipid binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20482048MyoferlinPRO_0000281646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701PhosphoserineCombined sources
Modified residuei174 – 1741PhosphoserineCombined sources
Modified residuei540 – 5401N6-acetyllysineCombined sources
Modified residuei871 – 8711N6-acetyllysineBy similarity
Modified residuei1494 – 14941N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ69ZN7.
PaxDbiQ69ZN7.
PRIDEiQ69ZN7.

PTM databases

iPTMnetiQ69ZN7.
PhosphoSiteiQ69ZN7.
SwissPalmiQ69ZN7.

Expressioni

Tissue specificityi

Expressed in myoblasts (at protein level). Expressed in endothelial cells.2 Publications

Inductioni

Up-regulated during myotube formation.1 Publication

Gene expression databases

BgeeiQ69ZN7.
CleanExiMM_FER1L3.
ExpressionAtlasiQ69ZN7. baseline and differential.
GenevisibleiQ69ZN7. MM.

Interactioni

Subunit structurei

Interacts with EHD2; the interaction is direct (By similarity). Interacts with DNM2 and KDR. Interacts with EHD1. Interacts with FAM65B (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi230471. 1 interaction.
IntActiQ69ZN7. 4 interactions.
MINTiMINT-1853509.
STRINGi10090.ENSMUSP00000045036.

Structurei

3D structure databases

ProteinModelPortaliQ69ZN7.
SMRiQ69ZN7. Positions 1-130, 910-1027.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini186 – 28196C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini345 – 458114C2 3PROSITE-ProRule annotationAdd
BLAST
Domaini1113 – 1218106C2 4PROSITE-ProRule annotationAdd
BLAST
Domaini1525 – 1625101C2 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 28196Necessary for interaction with EHD2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi145 – 1495Poly-Glu
Compositional biasi615 – 6184Poly-Tyr
Compositional biasi1006 – 10094Poly-Arg
Compositional biasi1059 – 10657Poly-Arg
Compositional biasi2018 – 20269Poly-Leu

Domaini

The C2 1 domain associates with lipid membranes in a calcium-dependent manner.By similarity

Sequence similaritiesi

Belongs to the ferlin family.Curated
Contains 5 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1326. Eukaryota.
ENOG410XPT2. LUCA.
GeneTreeiENSGT00550000074414.
HOVERGENiHBG018972.
InParanoidiQ69ZN7.
OMAiQDNNGLC.
OrthoDBiEOG7CVPWR.
PhylomeDBiQ69ZN7.
TreeFamiTF316871.

Family and domain databases

Gene3Di2.60.40.150. 8 hits.
InterProiIPR000008. C2_dom.
IPR012968. FerIin_dom.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR032362. Ferlin_C.
IPR006614. Peroxin/Ferlin.
[Graphical view]
PfamiPF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
PF16165. Ferlin_C. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
SM01200. FerA. 1 hit.
SM01201. FerB. 1 hit.
SM01202. FerI. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 7 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q69ZN7-1) [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
MLRVIVESAT NIPKTKFGKP DPIVSVIFKD EKKKTKKVDN ELNPVWNEIL
60 70 80 90 100
EFDLRGIPLD SSSSLVIVVK DFETIGQNKL IGTATVSLKD LIGDQNRSLP
110 120 130 140 150
YKQTSLLNEK GQDTGATIDL VIGYTPPSAP HPNDPSGTSV PGMGEEEEED
160 170 180 190 200
QGDEDRVDGI VRGPGPKGPS GTVSEAQLAR RITKGKSSRR MLSNKPQDFQ
210 220 230 240 250
IRVRVIEGRQ LCGNNIRPVV KVHICGQTHR TRIKRGNNPF FDELFFYNVH
260 270 280 290 300
ITPSELMDEI ISIRVYNSHS LRADCLMGEF KIDVGFVYDE PGHAVMRKWL
310 320 330 340 350
LLNDPEDTSS GAKGYMKVSM FVLGTGDEPP PEKRDRDNDS DDVESNLLLP
360 370 380 390 400
AGIALRWVTF MLKIYRAEDI PQMDDAFSQT VKEIFGGNAD KKNLVDPFVE
410 420 430 440 450
VSFAGKKVCT NIIERNANPE WNQVVNLQIK FPSMCEKIKL TVYDWDRLTK
460 470 480 490 500
NDVVGTTYLY LSKIAASGGE VEATTGETEV GFVPTFGPCY LNLYGSPREY
510 520 530 540 550
TGFPDPYDEL NSGKGEGVAY RGRIFVELNT FLEKKPPEKK LEPISSDDLL
560 570 580 590 600
VVEKYQRRRK YSLSAVFHSA TMLQDVGEAI QFEVSIGNYG NKFDATCKPL
610 620 630 640 650
ASTTQYSRAV FDGNYYYYLP WAHTKPVVTL TSYWEDISHR LDAVNTLLVM
660 670 680 690 700
AERLQSNIEA VKSGIQGKIP ANQLAEVWLK LIDEVIEDTR YTLPVTEGKA
710 720 730 740 750
NVTVLDTQIR KLRSRFLSQI HEAALRMRSE ATDVKSTLLE IEEWLDKLMQ
760 770 780 790 800
LTEEPQNSMP DIIIWMIRGE KRLAYARIPA HQVLYSTSGG NASGKYCGKT
810 820 830 840 850
QTILLKYPQE KTNGPKVPVE LRVNIWLGLS AVEKKFNSFA EGTFTVFAEM
860 870 880 890 900
YENQALVFGK WGTSGLVGRH KFSDVTGKIK LKREFFLPPK GWEWEGDWVV
910 920 930 940 950
DPERSLLTEA DAGHTEFTDE VYQNENRYPG GEWKQAEDTY TDANGDKAAS
960 970 980 990 1000
PSEMTCPPGW EWEDDAWIYD INRAVDEKGW EYGITIPPDN KPKSWVAAEK
1010 1020 1030 1040 1050
MYHTHRRRRL VRKRKKDLTQ TASSTARAME ELEDREGWEY ASLIGWKFHW
1060 1070 1080 1090 1100
KQRSSDTFRR RRWRRKMAPS ETHGAAAIFK LEGALGADTT EDGEEKGPEK
1110 1120 1130 1140 1150
QKHSATTVFG ANTPIVSCNF DRVYIYHLRC YIYQARNLMA LDKDSFSDPY
1160 1170 1180 1190 1200
AHVSFLHRSK TTEIIHSTLN PTWDQTIIFD EVEIFGEPQT VLQNPPNVTI
1210 1220 1230 1240 1250
ELFDNDQVGK DEFLGRSICS PLVKLNSETD ITPKLLWHPV MNGDKACGDV
1260 1270 1280 1290 1300
LVTAELILRN KDGSNLPILP SQRAPNLYMV PQGIRPVVQL TAIEILAWGL
1310 1320 1330 1340 1350
RNMKNYQMAS VTSPSLVVEC GGERVESVVI KSLKKTPNFP SSVLFMKVFL
1360 1370 1380 1390 1400
PKEELYMPPL VIKVIDHRQF GRKPVVGQCT IDHLDRFRCD PYAGKEDIVP
1410 1420 1430 1440 1450
QLKASLMSAP PCREVVIEIE DTKPLLASKL SEKEEEIVDW WSKFYASSGE
1460 1470 1480 1490 1500
HEKCGQYIQK GYSKLKIYDC ELEDVADFEG LTDFSDTFKL YRGKSDENED
1510 1520 1530 1540 1550
PSVVGEFKGS FRIYPLPDDP SVPAPPRQFR ELPDSVPQEC TVRIYIVQGL
1560 1570 1580 1590 1600
QLQPQDNNGL CDPYIKITLG KKVIEDRDHY IPNTLNPVFG RMYELSCYLP
1610 1620 1630 1640 1650
QEKDLKISVY DYDTFTRDEK VGETTIDLEN RFLSRFGSHC GIPEQYCVSG
1660 1670 1680 1690 1700
VNTWRDQLRP TQLLQNVARF KGFPPPVLSE DGSRIRYGGR DYHLDEFEAN
1710 1720 1730 1740 1750
KILHQHLGAP EERLALHILR TQGLVPEHVE TRTLHSTFQP NISQGKLQMW
1760 1770 1780 1790 1800
VDVFPKSLGP PGPPFNITPR KAKKYYLRVI IWNTKDVILD EKSITGEDMS
1810 1820 1830 1840 1850
DIYVKGWISG SEENKQKTDV HYRSLDGEGN FNWRFVFPFD YLPAEQLCIV
1860 1870 1880 1890 1900
AKKEHFWSID QTEFRVPPRL IIQIWDNDKF SLDDYLGFLE LDLHRTIIPA
1910 1920 1930 1940 1950
KTSEKCSLDM IPDLKAMDPL KAKTASLFEQ RSMKGWWPCY ADKDGTRVMA
1960 1970 1980 1990 2000
GKVEMTLEVL NEREADERPA GKGRSEPNMN PKLDPPNRPE TSFLWFTNPC
2010 2020 2030 2040
KTMRFIVWRR FKWVIIGLLL LLILLLFVAV LLYSLPNYLS MKIVRPNA
Length:2,048
Mass (Da):233,324
Last modified:March 20, 2007 - v2
Checksum:i00D1596472CDFB8E
GO
Isoform 2 (identifier: Q69ZN7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     472-472: E → EDFSSSGAGAASYT
     906-908: LLT → SPR
     909-2048: Missing.

Show »
Length:921
Mass (Da):103,418
Checksum:i76A64E2BC25F2B93
GO
Isoform 3 (identifier: Q69ZN7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     282-292: IDVGFVYDEPG → VSDSSILLSMI
     293-2048: Missing.

Show »
Length:292
Mass (Da):32,410
Checksum:iA854517A1C76D948
GO
Isoform 4 (identifier: Q69ZN7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1346-1570: Missing.

Show »
Length:1,823
Mass (Da):207,604
Checksum:i0D5CFD8AFE594A61
GO

Sequence cautioni

The sequence AAH25649.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD32409.1 differs from that shown. Reason: Frameshift at position 2020. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861K → E in BAC39820 (PubMed:16141072).Curated
Sequence conflicti1322 – 13221G → R in BAC36043 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei282 – 29211IDVGFVYDEPG → VSDSSILLSMI in isoform 3. 1 PublicationVSP_024013Add
BLAST
Alternative sequencei293 – 20481756Missing in isoform 3. 1 PublicationVSP_024014Add
BLAST
Alternative sequencei472 – 4721E → EDFSSSGAGAASYT in isoform 2. 1 PublicationVSP_024015
Alternative sequencei906 – 9083LLT → SPR in isoform 2. 1 PublicationVSP_024016
Alternative sequencei909 – 20481140Missing in isoform 2. 1 PublicationVSP_024017Add
BLAST
Alternative sequencei1346 – 1570225Missing in isoform 4. 1 PublicationVSP_035934Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173131 mRNA. Translation: BAD32409.1. Sequence problems.
AK031666 mRNA. Translation: BAC27500.1.
AK075903 mRNA. Translation: BAC36043.1.
AK086107 mRNA. Translation: BAC39611.1.
AK087176 mRNA. Translation: BAC39820.2.
AK087302 mRNA. Translation: BAC39840.1.
AC115360 Genomic DNA. No translation available.
BC025649 mRNA. Translation: AAH25649.1. Different initiation.
BC044825 mRNA. Translation: AAH44825.1.
BC055953 mRNA. Translation: AAH55953.1.
CCDSiCCDS37970.1. [Q69ZN7-1]
RefSeqiNP_001093104.1. NM_001099634.1. [Q69ZN7-1]
NP_001289069.1. NM_001302140.1.
UniGeneiMm.34674.

Genome annotation databases

EnsembliENSMUST00000041475; ENSMUSP00000045036; ENSMUSG00000048612. [Q69ZN7-1]
GeneIDi226101.
KEGGimmu:226101.
UCSCiuc008hit.1. mouse. [Q69ZN7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173131 mRNA. Translation: BAD32409.1. Sequence problems.
AK031666 mRNA. Translation: BAC27500.1.
AK075903 mRNA. Translation: BAC36043.1.
AK086107 mRNA. Translation: BAC39611.1.
AK087176 mRNA. Translation: BAC39820.2.
AK087302 mRNA. Translation: BAC39840.1.
AC115360 Genomic DNA. No translation available.
BC025649 mRNA. Translation: AAH25649.1. Different initiation.
BC044825 mRNA. Translation: AAH44825.1.
BC055953 mRNA. Translation: AAH55953.1.
CCDSiCCDS37970.1. [Q69ZN7-1]
RefSeqiNP_001093104.1. NM_001099634.1. [Q69ZN7-1]
NP_001289069.1. NM_001302140.1.
UniGeneiMm.34674.

3D structure databases

ProteinModelPortaliQ69ZN7.
SMRiQ69ZN7. Positions 1-130, 910-1027.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230471. 1 interaction.
IntActiQ69ZN7. 4 interactions.
MINTiMINT-1853509.
STRINGi10090.ENSMUSP00000045036.

PTM databases

iPTMnetiQ69ZN7.
PhosphoSiteiQ69ZN7.
SwissPalmiQ69ZN7.

Proteomic databases

MaxQBiQ69ZN7.
PaxDbiQ69ZN7.
PRIDEiQ69ZN7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041475; ENSMUSP00000045036; ENSMUSG00000048612. [Q69ZN7-1]
GeneIDi226101.
KEGGimmu:226101.
UCSCiuc008hit.1. mouse. [Q69ZN7-1]

Organism-specific databases

CTDi26509.
MGIiMGI:1919192. Myof.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1326. Eukaryota.
ENOG410XPT2. LUCA.
GeneTreeiENSGT00550000074414.
HOVERGENiHBG018972.
InParanoidiQ69ZN7.
OMAiQDNNGLC.
OrthoDBiEOG7CVPWR.
PhylomeDBiQ69ZN7.
TreeFamiTF316871.

Miscellaneous databases

PROiQ69ZN7.
SOURCEiSearch...

Gene expression databases

BgeeiQ69ZN7.
CleanExiMM_FER1L3.
ExpressionAtlasiQ69ZN7. baseline and differential.
GenevisibleiQ69ZN7. MM.

Family and domain databases

Gene3Di2.60.40.150. 8 hits.
InterProiIPR000008. C2_dom.
IPR012968. FerIin_dom.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR032362. Ferlin_C.
IPR006614. Peroxin/Ferlin.
[Graphical view]
PfamiPF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
PF16165. Ferlin_C. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
SM01200. FerA. 1 hit.
SM01201. FerB. 1 hit.
SM01202. FerI. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 7 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-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., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pancreatic islet.
  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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1322-2048 (ISOFORMS 1/2/3).
    Strain: C57BL/6J and FVB/N.
    Tissue: Embryonic head, Embryonic lung, Embryonic testis and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 517-2048 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 968-2048 (ISOFORMS 1/2/3).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Cited for: FUNCTION, MUTAGENESIS OF ILE-67, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. Cited for: FUNCTION, INTERACTION WITH DNM2 AND KDR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "The endocytic recycling protein EHD2 interacts with myoferlin to regulate myoblast fusion."
    Doherty K.R., Demonbreun A.R., Wallace G.Q., Cave A., Posey A.D., Heretis K., Pytel P., McNally E.M.
    J. Biol. Chem. 283:20252-20260(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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 SER-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5 (Fer1L5) and mediate myoblast fusion."
    Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M., George M., Band H., McNally E.M.
    J. Biol. Chem. 286:7379-7388(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EHD1 AND EHD2, INDUCTION.
  12. "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 LYS-540 AND LYS-1494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiMYOF_MOUSE
AccessioniPrimary (citable) accession number: Q69ZN7
Secondary accession number(s): Q7TMG0
, Q80V33, Q8BU64, Q8BU70, Q8BUC1, Q8BVY6, Q8C0D1, Q8R3B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: June 8, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mice lacking Myof display fewer large multinucleated myotubes and are impaired in their ability to regenerate skeletal muscle after injury. They display a defective membrane repair in endothelial cells. They show also a delayed endocytic recycling.

Keywords - Technical termi

Complete proteome, 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

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.