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Q9NZM1

- MYOF_HUMAN

UniProt

Q9NZM1 - MYOF_HUMAN

Protein

Myoferlin

Gene

MYOF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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 By similarity.By similarity

    Cofactori

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

    GO - Molecular functioni

    1. phospholipid binding Source: UniProtKB
    2. protein binding Source: UniProt

    GO - Biological processi

    1. blood circulation Source: ProtInc
    2. cellular response to heat Source: Ensembl
    3. muscle contraction Source: ProtInc
    4. plasma membrane repair Source: UniProtKB
    5. regulation of vascular endothelial growth factor receptor signaling pathway Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myoferlin
    Alternative name(s):
    Fer-1-like protein 3
    Gene namesi
    Name:MYOF
    Synonyms:FER1L3, KIAA1207
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:3656. MYOF.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. cytoplasmic vesicle Source: UniProtKB
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. intracellular membrane-bounded organelle Source: HPA
    7. nuclear envelope Source: ProtInc
    8. nuclear membrane Source: UniProtKB-SubCell
    9. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi238 – 2403NPF → SPL: Reduces interaction with EHD2. 1 Publication

    Organism-specific databases

    PharmGKBiPA164723288.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20612061MyoferlinPRO_0000057884Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei174 – 1741Phosphoserine1 Publication
    Modified residuei553 – 5531N6-acetyllysineBy similarity
    Modified residuei884 – 8841N6-acetyllysine1 Publication
    Modified residuei1507 – 15071N6-acetyllysineBy similarity
    Modified residuei1915 – 19151Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NZM1.
    PaxDbiQ9NZM1.
    PRIDEiQ9NZM1.

    PTM databases

    PhosphoSiteiQ9NZM1.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Gene expression databases

    ArrayExpressiQ9NZM1.
    BgeeiQ9NZM1.
    GenevestigatoriQ9NZM1.

    Organism-specific databases

    HPAiHPA014245.

    Interactioni

    Subunit structurei

    Interacts with DNM2 and KDR. Interacts with EHD1 By similarity. Interacts with EHD2; the interaction is direct.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi117715. 12 interactions.
    IntActiQ9NZM1. 3 interactions.
    MINTiMINT-3320110.

    Structurei

    Secondary structure

    2061
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 1111
    Beta strandi16 – 183
    Beta strandi22 – 276
    Beta strandi32 – 343
    Beta strandi45 – 539
    Beta strandi64 – 718
    Beta strandi75 – 773
    Beta strandi82 – 876
    Helixi88 – 903
    Beta strandi93 – 953
    Beta strandi97 – 10711
    Beta strandi113 – 12412
    Turni924 – 9274
    Beta strandi929 – 93911
    Beta strandi942 – 9443
    Beta strandi947 – 9548
    Turni964 – 9663
    Beta strandi977 – 9793
    Beta strandi985 – 9873
    Beta strandi994 – 9963
    Beta strandi1017 – 102812
    Turni1030 – 10345

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DMHNMR-A1-127[»]
    2K2ONMR-A923-1040[»]
    ProteinModelPortaliQ9NZM1.
    SMRiQ9NZM1. Positions 1-130, 923-1040.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZM1.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 20252025CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2047 – 206115ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2026 – 204621HelicalSequence AnalysisAdd
    BLAST

    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
    Domaini1126 – 1231106C2 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1538 – 1638101C2 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 28196Necessary for interaction with EHD2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1072 – 10787Poly-Arg

    Domaini

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

    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

    eggNOGiNOG330124.
    HOVERGENiHBG018972.
    InParanoidiQ9NZM1.
    OMAiQDNNGLC.
    PhylomeDBiQ9NZM1.
    TreeFamiTF316871.

    Family and domain databases

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

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NZM1-1) [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

    MLRVIVESAS NIPKTKFGKP DPIVSVIFKD EKKKTKKVDN ELNPVWNEIL     50
    EFDLRGIPLD FSSSLGIIVK DFETIGQNKL IGTATVALKD LTGDQSRSLP 100
    YKLISLLNEK GQDTGATIDL VIGYDPPSAP HPNDLSGPSV PGMGGDGEED 150
    EGDEDRLDNA VRGPGPKGPV GTVSEAQLAR RLTKVKNSRR MLSNKPQDFQ 200
    IRVRVIEGRQ LSGNNIRPVV KVHVCGQTHR TRIKRGNNPF FDELFFYNVN 250
    MTPSELMDEI ISIRVYNSHS LRADCLMGEF KIDVGFVYDE PGHAVMRKWL 300
    LLNDPEDTSS GSKGYMKVSM FVLGTGDEPP PERRDRDNDS DDVESNLLLP 350
    AGIALRWVTF LLKIYRAEDI PQMDDAFSQT VKEIFGGNAD KKNLVDPFVE 400
    VSFAGKKVCT NIIEKNANPE WNQVVNLQIK FPSVCEKIKL TIYDWDRLTK 450
    NDVVGTTYLH LSKIAASGGE VEDFSSSGTG AASYTVNTGE TEVGFVPTFG 500
    PCYLNLYGSP REYTGFPDPY DELNTGKGEG VAYRGRILVE LATFLEKTPP 550
    DKKLEPISND DLLVVEKYQR RRKYSLSAVF HSATMLQDVG EAIQFEVSIG 600
    NYGNKFDTTC KPLASTTQYS RAVFDGNYYY YLPWAHTKPV VTLTSYWEDI 650
    SHRLDAVNTL LAMAERLQTN IEALKSGIQG KIPANQLAEL WLKLIDEVIE 700
    DTRYTLPLTE GKANVTVLDT QIRKLRSRSL SQIHEAAVRM RSEATDVKST 750
    LAEIEDWLDK LMQLTEEPQN SMPDIIIWMI RGEKRLAYAR IPAHQVLYST 800
    SGENASGKYC GKTQTIFLKY PQEKNNGPKV PVELRVNIWL GLSAVEKKFN 850
    SFAEGTFTVF AEMYENQALM FGKWGTSGLV GRHKFSDVTG KIKLKREFFL 900
    PPKGWEWEGE WIVDPERSLL TEADAGHTEF TDEVYQNESR YPGGDWKPAE 950
    DTYTDANGDK AASPSELTCP PGWEWEDDAW SYDINRAVDE KGWEYGITIP 1000
    PDHKPKSWVA AEKMYHTHRR RRLVRKRKKD LTQTASSTAR AMEELQDQEG 1050
    WEYASLIGWK FHWKQRSSDT FRRRRWRRKM APSETHGAAA IFKLEGALGA 1100
    DTTEDGDEKS LEKQKHSATT VFGANTPIVS CNFDRVYIYH LRCYVYQARN 1150
    LLALDKDSFS DPYAHICFLH RSKTTEIIHS TLNPTWDQTI IFDEVEIYGE 1200
    PQTVLQNPPK VIMELFDNDQ VGKDEFLGRS IFSPVVKLNS EMDITPKLLW 1250
    HPVMNGDKAC GDVLVTAELI LRGKDGSNLP ILPPQRAPNL YMVPQGIRPV 1300
    VQLTAIEILA WGLRNMKNFQ MASITSPSLV VECGGERVES VVIKNLKKTP 1350
    NFPSSVLFMK VFLPKEELYM PPLVIKVIDH RQFGRKPVVG QCTIERLDRF 1400
    RCDPYAGKED IVPQLKASLL SAPPCRDIVI EMEDTKPLLA SKLTEKEEEI 1450
    VDWWSKFYAS SGEHEKCGQY IQKGYSKLKI YNCELENVAE FEGLTDFSDT 1500
    FKLYRGKSDE NEDPSVVGEF KGSFRIYPLP DDPSVPAPPR QFRELPDSVP 1550
    QECTVRIYIV RGLELQPQDN NGLCDPYIKI TLGKKVIEDR DHYIPNTLNP 1600
    VFGRMYELSC YLPQEKDLKI SVYDYDTFTR DEKVGETIID LENRFLSRFG 1650
    SHCGIPEEYC VSGVNTWRDQ LRPTQLLQNV ARFKGFPQPI LSEDGSRIRY 1700
    GGRDYSLDEF EANKILHQHL GAPEERLALH ILRTQGLVPE HVETRTLHST 1750
    FQPNISQGKL QMWVDVFPKS LGPPGPPFNI TPRKAKKYYL RVIIWNTKDV 1800
    ILDEKSITGE EMSDIYVKGW IPGNEENKQK TDVHYRSLDG EGNFNWRFVF 1850
    PFDYLPAEQL CIVAKKEHFW SIDQTEFRIP PRLIIQIWDN DKFSLDDYLG 1900
    FLELDLRHTI IPAKSPEKCR LDMIPDLKAM NPLKAKTASL FEQKSMKGWW 1950
    PCYAEKDGAR VMAGKVEMTL EILNEKEADE RPAGKGRDEP NMNPKLDLPN 2000
    RPETSFLWFT NPCKTMKFIV WRRFKWVIIG LLFLLILLLF VAVLLYSLPN 2050
    YLSMKIVKPN V 2061
    Length:2,061
    Mass (Da):234,709
    Last modified:October 1, 2000 - v1
    Checksum:i61D9E9447B40781C
    GO
    Isoform 2 (identifier: Q9NZM1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-87: MLRVIVESAS...NKLIGTATVA → MRPPKEGSGS...DLQQTPTDLQ

    Show »
    Length:2,019
    Mass (Da):229,895
    Checksum:i1B35CBF6FAD0479B
    GO
    Isoform 3 (identifier: Q9NZM1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1442-1442: K → KCLSSMSTALSKMASPATVH
         1757-1787: QGKLQMWVDVFPKSLGPPGPPFNITPRKAKK → R

    Show »
    Length:2,050
    Mass (Da):233,324
    Checksum:i7E4B68C00BD7941E
    GO
    Isoform 4 (identifier: Q9NZM1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         146-160: DGEEDEGDEDRLDNA → KLTLLKAQPPPGGGC
         161-2061: Missing.

    Show »
    Length:160
    Mass (Da):17,135
    Checksum:i6187C6E291727B4E
    GO
    Isoform 5 (identifier: Q9NZM1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1224-1707: Missing.

    Show »
    Length:1,577
    Mass (Da):179,551
    Checksum:iE4E3880E7B8C1231
    GO
    Isoform 6 (identifier: Q9NZM1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         473-485: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,048
    Mass (Da):233,477
    Checksum:i1AB532E8DD2A2622
    GO
    Isoform 7 (identifier: Q9NZM1-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-2061: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:445
    Mass (Da):49,720
    Checksum:i6A86A4B03A1CE25A
    GO
    Isoform 8 (identifier: Q9NZM1-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-29: MLRVIVESASNIPKTKFGKPDPIVSVIFK → MIPPNSPPNRT
         438-2061: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:419
    Mass (Da):46,695
    Checksum:i0E54F263A4C5D385
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511M → T in AAG23737. (PubMed:10995573)Curated
    Sequence conflicti621 – 6211R → W in CAB46370. (PubMed:17974005)Curated
    Sequence conflicti659 – 6591T → A in AAG23737. (PubMed:10995573)Curated
    Sequence conflicti659 – 6591T → A in CAB46370. (PubMed:17974005)Curated
    Sequence conflicti846 – 8461E → A in AAF27177. (PubMed:10607832)Curated
    Sequence conflicti1136 – 11361V → D in CAB46370. (PubMed:17974005)Curated
    Sequence conflicti1163 – 11631Y → F in CAB46370. (PubMed:17974005)Curated
    Sequence conflicti1544 – 15441E → G in AAG23737. (PubMed:10995573)Curated
    Sequence conflicti1544 – 15441E → G in CAB46370. (PubMed:17974005)Curated
    Sequence conflicti1574 – 15741C → R in CAB46370. (PubMed:17974005)Curated
    Sequence conflicti1723 – 17231P → H in AAF27177. (PubMed:10607832)Curated
    Sequence conflicti1834 – 18341H → R in CAB46370. (PubMed:17974005)Curated
    Sequence conflicti1946 – 19527MKGWWPC → IRMVAM in AAF27177. (PubMed:10607832)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1136 – 11361V → I.
    Corresponds to variant rs36032890 [ dbSNP | Ensembl ].
    VAR_049058
    Natural varianti1198 – 11981Y → F.
    Corresponds to variant rs12256834 [ dbSNP | Ensembl ].
    VAR_031250
    Natural varianti1399 – 13991R → C.
    Corresponds to variant rs11187393 [ dbSNP | Ensembl ].
    VAR_031251
    Natural varianti1701 – 17011G → A.
    Corresponds to variant rs34000599 [ dbSNP | Ensembl ].
    VAR_049059
    Natural varianti1783 – 17831R → Q.
    Corresponds to variant rs11594445 [ dbSNP | Ensembl ].
    VAR_031252

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8787MLRVI…TATVA → MRPPKEGSGSNICCSAIFAV LQPPLVISRQTRSGMDLQQT PTDLQ in isoform 2. 1 PublicationVSP_001515Add
    BLAST
    Alternative sequencei1 – 2929MLRVI…SVIFK → MIPPNSPPNRT in isoform 8. 1 PublicationVSP_023796Add
    BLAST
    Alternative sequencei146 – 16015DGEED…RLDNA → KLTLLKAQPPPGGGC in isoform 4. CuratedVSP_023797Add
    BLAST
    Alternative sequencei161 – 20611901Missing in isoform 4. CuratedVSP_023798Add
    BLAST
    Alternative sequencei438 – 20611624Missing in isoform 8. 1 PublicationVSP_023799Add
    BLAST
    Alternative sequencei446 – 20611616Missing in isoform 7. CuratedVSP_023800Add
    BLAST
    Alternative sequencei473 – 48513Missing in isoform 6. 1 PublicationVSP_023801Add
    BLAST
    Alternative sequencei1224 – 1707484Missing in isoform 5. 1 PublicationVSP_023802Add
    BLAST
    Alternative sequencei1442 – 14421K → KCLSSMSTALSKMASPATVH in isoform 3. 1 PublicationVSP_001516
    Alternative sequencei1757 – 178731QGKLQ…RKAKK → R in isoform 3. 1 PublicationVSP_001517Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS41550.1. [Q9NZM1-6]
    CCDS41551.1. [Q9NZM1-1]
    PIRiT12449.
    RefSeqiNP_038479.1. NM_013451.3. [Q9NZM1-1]
    NP_579899.1. NM_133337.2. [Q9NZM1-6]
    UniGeneiHs.602086.

    Genome annotation databases

    EnsembliENST00000358334; ENSP00000351094; ENSG00000138119. [Q9NZM1-6]
    ENST00000359263; ENSP00000352208; ENSG00000138119. [Q9NZM1-1]
    ENST00000371488; ENSP00000360543; ENSG00000138119. [Q9NZM1-4]
    ENST00000371489; ENSP00000360544; ENSG00000138119. [Q9NZM1-7]
    GeneIDi26509.
    KEGGihsa:26509.
    UCSCiuc001kin.3. human. [Q9NZM1-1]
    uc001kio.3. human. [Q9NZM1-6]
    uc001kip.4. human. [Q9NZM1-7]

    Polymorphism databases

    DMDMi20139241.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS41550.1. [Q9NZM1-6 ]
    CCDS41551.1. [Q9NZM1-1 ]
    PIRi T12449.
    RefSeqi NP_038479.1. NM_013451.3. [Q9NZM1-1 ]
    NP_579899.1. NM_133337.2. [Q9NZM1-6 ]
    UniGenei Hs.602086.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DMH NMR - A 1-127 [» ]
    2K2O NMR - A 923-1040 [» ]
    ProteinModelPortali Q9NZM1.
    SMRi Q9NZM1. Positions 1-130, 923-1040.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117715. 12 interactions.
    IntActi Q9NZM1. 3 interactions.
    MINTi MINT-3320110.

    PTM databases

    PhosphoSitei Q9NZM1.

    Polymorphism databases

    DMDMi 20139241.

    Proteomic databases

    MaxQBi Q9NZM1.
    PaxDbi Q9NZM1.
    PRIDEi Q9NZM1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358334 ; ENSP00000351094 ; ENSG00000138119 . [Q9NZM1-6 ]
    ENST00000359263 ; ENSP00000352208 ; ENSG00000138119 . [Q9NZM1-1 ]
    ENST00000371488 ; ENSP00000360543 ; ENSG00000138119 . [Q9NZM1-4 ]
    ENST00000371489 ; ENSP00000360544 ; ENSG00000138119 . [Q9NZM1-7 ]
    GeneIDi 26509.
    KEGGi hsa:26509.
    UCSCi uc001kin.3. human. [Q9NZM1-1 ]
    uc001kio.3. human. [Q9NZM1-6 ]
    uc001kip.4. human. [Q9NZM1-7 ]

    Organism-specific databases

    CTDi 26509.
    GeneCardsi GC10M095057.
    HGNCi HGNC:3656. MYOF.
    HPAi HPA014245.
    MIMi 604603. gene.
    neXtProti NX_Q9NZM1.
    PharmGKBi PA164723288.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG330124.
    HOVERGENi HBG018972.
    InParanoidi Q9NZM1.
    OMAi QDNNGLC.
    PhylomeDBi Q9NZM1.
    TreeFami TF316871.

    Miscellaneous databases

    ChiTaRSi MYOF. human.
    EvolutionaryTracei Q9NZM1.
    GeneWikii FER1L3.
    GenomeRNAii 26509.
    NextBioi 48802.
    PROi Q9NZM1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZM1.
    Bgeei Q9NZM1.
    Genevestigatori Q9NZM1.

    Family and domain databases

    Gene3Di 2.60.40.150. 8 hits.
    InterProi IPR000008. C2_dom.
    IPR012968. FerIin-domain.
    IPR012560. Ferlin_A-domain.
    IPR012561. Ferlin_B-domain.
    IPR006614. Peroxin/Ferlin.
    [Graphical view ]
    Pfami PF00168. C2. 7 hits.
    PF08165. FerA. 1 hit.
    PF08150. FerB. 1 hit.
    PF08151. FerI. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 7 hits.
    SM00694. DysFC. 2 hits.
    SM00693. DysFN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 7 hits.
    PROSITEi PS50004. C2. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiMYOF_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZM1
    Secondary accession number(s): B3KQN5
    , Q5VWW2, Q5VWW3, Q5VWW4, Q5VWW5, Q7Z642, Q8IWH0, Q9HBU3, Q9NZM0, Q9ULL3, Q9Y4U4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3