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Q9NZM1

- MYOF_HUMAN

UniProt

Q9NZM1 - MYOF_HUMAN

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Protein

Myoferlin

Gene
MYOF, FER1L3, KIAA1207
Organism
Homo sapiens (Human)
Status
Reviewed - 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 By similarity.

Cofactori

Binds calcium ions. The ions are bound to the C2 1 domain 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
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
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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 20252025Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei2026 – 204621Helical; Reviewed predictionAdd
BLAST
Topological domaini2047 – 206115Extracellular Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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-acetyllysine By similarity
Modified residuei884 – 8841N6-acetyllysine1 Publication
Modified residuei1507 – 15071N6-acetyllysine By 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.1 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.

Miscellaneous databases

EvolutionaryTraceiQ9NZM1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8585C2 1Add
BLAST
Domaini186 – 28196C2 2Add
BLAST
Domaini345 – 458114C2 3Add
BLAST
Domaini1126 – 1231106C2 4Add
BLAST
Domaini1538 – 1638101C2 5Add
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.
Contains 5 C2 domains.

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.

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. VSP_001515Add
BLAST
Alternative sequencei1 – 2929MLRVI…SVIFK → MIPPNSPPNRT in isoform 8. VSP_023796Add
BLAST
Alternative sequencei146 – 16015DGEED…RLDNA → KLTLLKAQPPPGGGC in isoform 4. VSP_023797Add
BLAST
Alternative sequencei161 – 20611901Missing in isoform 4. VSP_023798Add
BLAST
Alternative sequencei438 – 20611624Missing in isoform 8. VSP_023799Add
BLAST
Alternative sequencei446 – 20611616Missing in isoform 7. VSP_023800Add
BLAST
Alternative sequencei473 – 48513Missing in isoform 6. VSP_023801Add
BLAST
Alternative sequencei1224 – 1707484Missing in isoform 5. VSP_023802Add
BLAST
Alternative sequencei1442 – 14421K → KCLSSMSTALSKMASPATVH in isoform 3. VSP_001516
Alternative sequencei1757 – 178731QGKLQ…RKAKK → R in isoform 3. VSP_001517Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511M → T in AAG23737. 1 Publication
Sequence conflicti621 – 6211R → W in CAB46370. 1 Publication
Sequence conflicti659 – 6591T → A in AAG23737. 1 Publication
Sequence conflicti659 – 6591T → A in CAB46370. 1 Publication
Sequence conflicti846 – 8461E → A in AAF27177. 1 Publication
Sequence conflicti1136 – 11361V → D in CAB46370. 1 Publication
Sequence conflicti1163 – 11631Y → F in CAB46370. 1 Publication
Sequence conflicti1544 – 15441E → G in AAG23737. 1 Publication
Sequence conflicti1544 – 15441E → G in CAB46370. 1 Publication
Sequence conflicti1574 – 15741C → R in CAB46370. 1 Publication
Sequence conflicti1723 – 17231P → H in AAF27177. 1 Publication
Sequence conflicti1834 – 18341H → R in CAB46370. 1 Publication
Sequence conflicti1946 – 19527MKGWWPC → IRMVAM in AAF27177. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 131 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

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