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Q9NZM1 (MYOF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myoferlin
Alternative name(s):
Fer-1-like protein 3
Gene names
Name:MYOF
Synonyms:FER1L3, KIAA1207
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2061 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Cofactor

Binds calcium ions. The ions are bound to the C2 1 domain By similarity.

Subunit structure

Interacts with DNM2 and KDR. Interacts with EHD1 By similarity. Interacts with EHD2; the interaction is direct. Ref.11

Subcellular location

Cell membrane; Single-pass type II membrane protein. Nucleus membrane; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Note: Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels By similarity. Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures. Ref.9 Ref.11

Tissue specificity

Expressed in myoblast and endothelial cells (at protein level). Highly expressed in cardiac and skeletal muscles. Also present in lung, and at very low levels in kidney, placenta and brain. Ref.9 Ref.10 Ref.11

Domain

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

Sequence similarities

Belongs to the ferlin family.

Contains 5 C2 domains.

Sequence caution

The sequence AAH40110.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAG52097.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasmic vesicle
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood circulation

Traceable author statement Ref.1. Source: ProtInc

cellular response to heat

Inferred from electronic annotation. Source: Ensembl

muscle contraction

Traceable author statement Ref.1. Source: ProtInc

plasma membrane repair

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcaveola

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay Ref.9. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear envelope

Traceable author statement Ref.1. Source: ProtInc

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionphospholipid binding

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZM1-1)

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.
Isoform 2 (identifier: Q9NZM1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: MLRVIVESAS...NKLIGTATVA → MRPPKEGSGS...DLQQTPTDLQ
Isoform 3 (identifier: Q9NZM1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1442-1442: K → KCLSSMSTALSKMASPATVH
     1757-1787: QGKLQMWVDVFPKSLGPPGPPFNITPRKAKK → R
Isoform 4 (identifier: Q9NZM1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     146-160: DGEEDEGDEDRLDNA → KLTLLKAQPPPGGGC
     161-2061: Missing.
Isoform 5 (identifier: Q9NZM1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1224-1707: Missing.
Isoform 6 (identifier: Q9NZM1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     473-485: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q9NZM1-7)

The sequence of this isoform differs from the canonical sequence as follows:
     446-2061: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: Q9NZM1-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MLRVIVESASNIPKTKFGKPDPIVSVIFK → MIPPNSPPNRT
     438-2061: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20612061Myoferlin
PRO_0000057884

Regions

Topological domain1 – 20252025Cytoplasmic Potential
Transmembrane2026 – 204621Helical; Potential
Topological domain2047 – 206115Extracellular Potential
Domain1 – 8585C2 1
Domain186 – 28196C2 2
Domain345 – 458114C2 3
Domain1126 – 1231106C2 4
Domain1538 – 1638101C2 5
Region186 – 28196Necessary for interaction with EHD2
Compositional bias1072 – 10787Poly-Arg

Amino acid modifications

Modified residue1741Phosphoserine Ref.12
Modified residue5531N6-acetyllysine By similarity
Modified residue8841N6-acetyllysine Ref.13
Modified residue15071N6-acetyllysine By similarity
Modified residue19151Phosphoserine Ref.14

Natural variations

Alternative sequence1 – 8787MLRVI…TATVA → MRPPKEGSGSNICCSAIFAV LQPPLVISRQTRSGMDLQQT PTDLQ in isoform 2.
VSP_001515
Alternative sequence1 – 2929MLRVI…SVIFK → MIPPNSPPNRT in isoform 8.
VSP_023796
Alternative sequence146 – 16015DGEED…RLDNA → KLTLLKAQPPPGGGC in isoform 4.
VSP_023797
Alternative sequence161 – 20611901Missing in isoform 4.
VSP_023798
Alternative sequence438 – 20611624Missing in isoform 8.
VSP_023799
Alternative sequence446 – 20611616Missing in isoform 7.
VSP_023800
Alternative sequence473 – 48513Missing in isoform 6.
VSP_023801
Alternative sequence1224 – 1707484Missing in isoform 5.
VSP_023802
Alternative sequence14421K → KCLSSMSTALSKMASPATVH in isoform 3.
VSP_001516
Alternative sequence1757 – 178731QGKLQ…RKAKK → R in isoform 3.
VSP_001517
Natural variant11361V → I.
Corresponds to variant rs36032890 [ dbSNP | Ensembl ].
VAR_049058
Natural variant11981Y → F.
Corresponds to variant rs12256834 [ dbSNP | Ensembl ].
VAR_031250
Natural variant13991R → C.
Corresponds to variant rs11187393 [ dbSNP | Ensembl ].
VAR_031251
Natural variant17011G → A.
Corresponds to variant rs34000599 [ dbSNP | Ensembl ].
VAR_049059
Natural variant17831R → Q.
Corresponds to variant rs11594445 [ dbSNP | Ensembl ].
VAR_031252

Experimental info

Mutagenesis238 – 2403NPF → SPL: Reduces interaction with EHD2. Ref.11
Sequence conflict2511M → T in AAG23737. Ref.2
Sequence conflict6211R → W in CAB46370. Ref.7
Sequence conflict6591T → A in AAG23737. Ref.2
Sequence conflict6591T → A in CAB46370. Ref.7
Sequence conflict8461E → A in AAF27177. Ref.1
Sequence conflict11361V → D in CAB46370. Ref.7
Sequence conflict11631Y → F in CAB46370. Ref.7
Sequence conflict15441E → G in AAG23737. Ref.2
Sequence conflict15441E → G in CAB46370. Ref.7
Sequence conflict15741C → R in CAB46370. Ref.7
Sequence conflict17231P → H in AAF27177. Ref.1
Sequence conflict18341H → R in CAB46370. Ref.7
Sequence conflict1946 – 19527MKGWWPC → IRMVAM in AAF27177. Ref.1

Secondary structure

........................................... 2061
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 61D9E9447B40781C

FASTA2,061234,709
        10         20         30         40         50         60 
MLRVIVESAS NIPKTKFGKP DPIVSVIFKD EKKKTKKVDN ELNPVWNEIL EFDLRGIPLD 

        70         80         90        100        110        120 
FSSSLGIIVK DFETIGQNKL IGTATVALKD LTGDQSRSLP YKLISLLNEK GQDTGATIDL 

       130        140        150        160        170        180 
VIGYDPPSAP HPNDLSGPSV PGMGGDGEED EGDEDRLDNA VRGPGPKGPV GTVSEAQLAR 

       190        200        210        220        230        240 
RLTKVKNSRR MLSNKPQDFQ IRVRVIEGRQ LSGNNIRPVV KVHVCGQTHR TRIKRGNNPF 

       250        260        270        280        290        300 
FDELFFYNVN MTPSELMDEI ISIRVYNSHS LRADCLMGEF KIDVGFVYDE PGHAVMRKWL 

       310        320        330        340        350        360 
LLNDPEDTSS GSKGYMKVSM FVLGTGDEPP PERRDRDNDS DDVESNLLLP AGIALRWVTF 

       370        380        390        400        410        420 
LLKIYRAEDI PQMDDAFSQT VKEIFGGNAD KKNLVDPFVE VSFAGKKVCT NIIEKNANPE 

       430        440        450        460        470        480 
WNQVVNLQIK FPSVCEKIKL TIYDWDRLTK NDVVGTTYLH LSKIAASGGE VEDFSSSGTG 

       490        500        510        520        530        540 
AASYTVNTGE TEVGFVPTFG PCYLNLYGSP REYTGFPDPY DELNTGKGEG VAYRGRILVE 

       550        560        570        580        590        600 
LATFLEKTPP DKKLEPISND DLLVVEKYQR RRKYSLSAVF HSATMLQDVG EAIQFEVSIG 

       610        620        630        640        650        660 
NYGNKFDTTC KPLASTTQYS RAVFDGNYYY YLPWAHTKPV VTLTSYWEDI SHRLDAVNTL 

       670        680        690        700        710        720 
LAMAERLQTN IEALKSGIQG KIPANQLAEL WLKLIDEVIE DTRYTLPLTE GKANVTVLDT 

       730        740        750        760        770        780 
QIRKLRSRSL SQIHEAAVRM RSEATDVKST LAEIEDWLDK LMQLTEEPQN SMPDIIIWMI 

       790        800        810        820        830        840 
RGEKRLAYAR IPAHQVLYST SGENASGKYC GKTQTIFLKY PQEKNNGPKV PVELRVNIWL 

       850        860        870        880        890        900 
GLSAVEKKFN SFAEGTFTVF AEMYENQALM FGKWGTSGLV GRHKFSDVTG KIKLKREFFL 

       910        920        930        940        950        960 
PPKGWEWEGE WIVDPERSLL TEADAGHTEF TDEVYQNESR YPGGDWKPAE DTYTDANGDK 

       970        980        990       1000       1010       1020 
AASPSELTCP PGWEWEDDAW SYDINRAVDE KGWEYGITIP PDHKPKSWVA AEKMYHTHRR 

      1030       1040       1050       1060       1070       1080 
RRLVRKRKKD LTQTASSTAR AMEELQDQEG WEYASLIGWK FHWKQRSSDT FRRRRWRRKM 

      1090       1100       1110       1120       1130       1140 
APSETHGAAA IFKLEGALGA DTTEDGDEKS LEKQKHSATT VFGANTPIVS CNFDRVYIYH 

      1150       1160       1170       1180       1190       1200 
LRCYVYQARN LLALDKDSFS DPYAHICFLH RSKTTEIIHS TLNPTWDQTI IFDEVEIYGE 

      1210       1220       1230       1240       1250       1260 
PQTVLQNPPK VIMELFDNDQ VGKDEFLGRS IFSPVVKLNS EMDITPKLLW HPVMNGDKAC 

      1270       1280       1290       1300       1310       1320 
GDVLVTAELI LRGKDGSNLP ILPPQRAPNL YMVPQGIRPV VQLTAIEILA WGLRNMKNFQ 

      1330       1340       1350       1360       1370       1380 
MASITSPSLV VECGGERVES VVIKNLKKTP NFPSSVLFMK VFLPKEELYM PPLVIKVIDH 

      1390       1400       1410       1420       1430       1440 
RQFGRKPVVG QCTIERLDRF RCDPYAGKED IVPQLKASLL SAPPCRDIVI EMEDTKPLLA 

      1450       1460       1470       1480       1490       1500 
SKLTEKEEEI VDWWSKFYAS SGEHEKCGQY IQKGYSKLKI YNCELENVAE FEGLTDFSDT 

      1510       1520       1530       1540       1550       1560 
FKLYRGKSDE NEDPSVVGEF KGSFRIYPLP DDPSVPAPPR QFRELPDSVP QECTVRIYIV 

      1570       1580       1590       1600       1610       1620 
RGLELQPQDN NGLCDPYIKI TLGKKVIEDR DHYIPNTLNP VFGRMYELSC YLPQEKDLKI 

      1630       1640       1650       1660       1670       1680 
SVYDYDTFTR DEKVGETIID LENRFLSRFG SHCGIPEEYC VSGVNTWRDQ LRPTQLLQNV 

      1690       1700       1710       1720       1730       1740 
ARFKGFPQPI LSEDGSRIRY GGRDYSLDEF EANKILHQHL GAPEERLALH ILRTQGLVPE 

      1750       1760       1770       1780       1790       1800 
HVETRTLHST FQPNISQGKL QMWVDVFPKS LGPPGPPFNI TPRKAKKYYL RVIIWNTKDV 

      1810       1820       1830       1840       1850       1860 
ILDEKSITGE EMSDIYVKGW IPGNEENKQK TDVHYRSLDG EGNFNWRFVF PFDYLPAEQL 

      1870       1880       1890       1900       1910       1920 
CIVAKKEHFW SIDQTEFRIP PRLIIQIWDN DKFSLDDYLG FLELDLRHTI IPAKSPEKCR 

      1930       1940       1950       1960       1970       1980 
LDMIPDLKAM NPLKAKTASL FEQKSMKGWW PCYAEKDGAR VMAGKVEMTL EILNEKEADE 

      1990       2000       2010       2020       2030       2040 
RPAGKGRDEP NMNPKLDLPN RPETSFLWFT NPCKTMKFIV WRRFKWVIIG LLFLLILLLF 

      2050       2060 
VAVLLYSLPN YLSMKIVKPN V 

« Hide

Isoform 2 [UniParc].

Checksum: 1B35CBF6FAD0479B
Show »

FASTA2,019229,895
Isoform 3 [UniParc].

Checksum: 7E4B68C00BD7941E
Show »

FASTA2,050233,324
Isoform 4 [UniParc].

Checksum: 6187C6E291727B4E
Show »

FASTA16017,135
Isoform 5 [UniParc].

Checksum: E4E3880E7B8C1231
Show »

FASTA1,577179,551
Isoform 6 [UniParc].

Checksum: 1AB532E8DD2A2622
Show »

FASTA2,048233,477
Isoform 7 [UniParc].

Checksum: 6A86A4B03A1CE25A
Show »

FASTA44549,720
Isoform 8 [UniParc].

Checksum: 0E54F263A4C5D385
Show »

FASTA41946,695

References

« Hide 'large scale' references
[1]"Myoferlin, a candidate gene and potential modifier of muscular dystrophy."
Davis D.B., Delmonte A.J., Ly C.T., McNally E.M.
Hum. Mol. Genet. 9:217-226(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Heart and Lung.
[2]"The third human FER-1-like protein is highly similar to dysferlin."
Britton S., Freeman T., Vafiadaki E., Keers S., Harrison R., Bushby K.M.D., Bashir R.
Genomics 68:313-321(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING.
Tissue: Placenta.
[3]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 5 AND 8).
Tissue: Lung.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 621-2061 (ISOFORM 3).
Tissue: Fetal brain.
[8]"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. expand/collapse author list , 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 1389-2061 (ISOFORMS 1/2).
Tissue: Thyroid.
[9]"Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains."
Davis D.B., Doherty K.R., Delmonte A.J., McNally E.M.
J. Biol. Chem. 277:22883-22888(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[10]"Myoferlin regulates vascular endothelial growth factor receptor-2 stability and function."
Bernatchez P.N., Acevedo L., Fernandez-Hernando C., Murata T., Chalouni C., Kim J., Erdjument-Bromage H., Shah V., Gratton J.-P., McNally E.M., Tempst P., Sessa W.C.
J. Biol. Chem. 282:30745-30753(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"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: INTERACTION WITH EHD2, MUTAGENESIS OF 238-ASN--PHE-240, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-884, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-1915, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"The solution structure of the first C2 domain of human myoferlin."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: STRUCTURE BY NMR OF 1-127.
[17]"Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b."
Patel P., Harris R., Geddes S.M., Strehle E.-M., Watson J.D., Bashir R., Bushby K., Driscoll P.C., Keep N.H.
J. Mol. Biol. 379:981-990(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 923-1040.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF182316 mRNA. Translation: AAF27176.1.
AF182317 mRNA. Translation: AAF27177.1.
AF207990 mRNA. Translation: AAG23737.1.
AB033033 mRNA. Translation: BAA86521.2.
AL365364, AL360229 Genomic DNA. Translation: CAI41206.2.
AL365364, AL360229 Genomic DNA. Translation: CAI41207.2.
AL365364, AL360229 Genomic DNA. Translation: CAI41208.1.
AL360229 Genomic DNA. Translation: CAH72370.1.
AL360229, AL365364 Genomic DNA. Translation: CAH72371.2.
AL360229, AL365364 Genomic DNA. Translation: CAH72372.2.
AL360229, AL365364 Genomic DNA. Translation: CAH72373.1.
BC040110 mRNA. Translation: AAH40110.1. Sequence problems.
BC052617 mRNA. Translation: AAH52617.1.
AL096713 mRNA. Translation: CAB46370.1.
AK075258 mRNA. Translation: BAG52097.1. Different initiation.
PIRT12449.
RefSeqNP_038479.1. NM_013451.3.
NP_579899.1. NM_133337.2.
UniGeneHs.602086.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMHNMR-A1-127[»]
2K2ONMR-A923-1040[»]
ProteinModelPortalQ9NZM1.
SMRQ9NZM1. Positions 1-130, 923-1040.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117715. 9 interactions.
IntActQ9NZM1. 3 interactions.
MINTMINT-3320110.

PTM databases

PhosphoSiteQ9NZM1.

Polymorphism databases

DMDM20139241.

Proteomic databases

PaxDbQ9NZM1.
PRIDEQ9NZM1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358334; ENSP00000351094; ENSG00000138119. [Q9NZM1-6]
ENST00000359263; ENSP00000352208; ENSG00000138119. [Q9NZM1-1]
ENST00000371488; ENSP00000360543; ENSG00000138119. [Q9NZM1-4]
ENST00000371489; ENSP00000360544; ENSG00000138119. [Q9NZM1-7]
GeneID26509.
KEGGhsa:26509.
UCSCuc001kin.3. human. [Q9NZM1-1]
uc001kio.3. human. [Q9NZM1-6]
uc001kip.4. human. [Q9NZM1-7]

Organism-specific databases

CTD26509.
GeneCardsGC10M095057.
HGNCHGNC:3656. MYOF.
HPAHPA014245.
MIM604603. gene.
neXtProtNX_Q9NZM1.
PharmGKBPA164723288.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG330124.
HOVERGENHBG018972.
InParanoidQ9NZM1.
OMAQDNNGLC.
PhylomeDBQ9NZM1.
TreeFamTF316871.

Gene expression databases

ArrayExpressQ9NZM1.
BgeeQ9NZM1.
GenevestigatorQ9NZM1.

Family and domain databases

Gene3D2.60.40.150. 8 hits.
InterProIPR000008. C2_dom.
IPR012968. FerIin-domain.
IPR012560. Ferlin_A-domain.
IPR012561. Ferlin_B-domain.
IPR006614. Peroxin/Ferlin.
[Graphical view]
PfamPF00168. C2. 7 hits.
PF08165. FerA. 1 hit.
PF08150. FerB. 1 hit.
PF08151. FerI. 1 hit.
[Graphical view]
SMARTSM00239. C2. 7 hits.
SM00694. DysFC. 2 hits.
SM00693. DysFN. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 7 hits.
PROSITEPS50004. C2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYOF. human.
EvolutionaryTraceQ9NZM1.
GeneWikiFER1L3.
GenomeRNAi26509.
NextBio48802.
PROQ9NZM1.
SOURCESearch...

Entry information

Entry nameMYOF_HUMAN
AccessionPrimary (citable) accession number: Q9NZM1
Secondary accession number(s): B3KQN5 expand/collapse secondary AC list , Q5VWW2, Q5VWW3, Q5VWW4, Q5VWW5, Q7Z642, Q8IWH0, Q9HBU3, Q9NZM0, Q9ULL3, Q9Y4U4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM