Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9NZM1

- MYOF_HUMAN

UniProt

Q9NZM1 - MYOF_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Myoferlin

Gene

MYOF

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).By similarity

Cofactori

Ca2+By similarityNote: Binds Ca(2+). The ions are bound to the C2 1 domain.By similarity

GO - Molecular functioni

  1. phospholipid binding Source: UniProtKB

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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 20252025CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei2026 – 204621HelicalSequence AnalysisAdd
BLAST
Topological domaini2047 – 206115ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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. 14 interactions.
IntActiQ9NZM1. 3 interactions.
MINTiMINT-3320110.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9NZM1.

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.
GeneTreeiENSGT00550000074414.
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

        10         20         30         40         50
MLRVIVESAS NIPKTKFGKP DPIVSVIFKD EKKKTKKVDN ELNPVWNEIL
60 70 80 90 100
EFDLRGIPLD FSSSLGIIVK DFETIGQNKL IGTATVALKD LTGDQSRSLP
110 120 130 140 150
YKLISLLNEK GQDTGATIDL VIGYDPPSAP HPNDLSGPSV PGMGGDGEED
160 170 180 190 200
EGDEDRLDNA VRGPGPKGPV GTVSEAQLAR RLTKVKNSRR MLSNKPQDFQ
210 220 230 240 250
IRVRVIEGRQ LSGNNIRPVV KVHVCGQTHR TRIKRGNNPF FDELFFYNVN
260 270 280 290 300
MTPSELMDEI ISIRVYNSHS LRADCLMGEF KIDVGFVYDE PGHAVMRKWL
310 320 330 340 350
LLNDPEDTSS GSKGYMKVSM FVLGTGDEPP PERRDRDNDS DDVESNLLLP
360 370 380 390 400
AGIALRWVTF LLKIYRAEDI PQMDDAFSQT VKEIFGGNAD KKNLVDPFVE
410 420 430 440 450
VSFAGKKVCT NIIEKNANPE WNQVVNLQIK FPSVCEKIKL TIYDWDRLTK
460 470 480 490 500
NDVVGTTYLH LSKIAASGGE VEDFSSSGTG AASYTVNTGE TEVGFVPTFG
510 520 530 540 550
PCYLNLYGSP REYTGFPDPY DELNTGKGEG VAYRGRILVE LATFLEKTPP
560 570 580 590 600
DKKLEPISND DLLVVEKYQR RRKYSLSAVF HSATMLQDVG EAIQFEVSIG
610 620 630 640 650
NYGNKFDTTC KPLASTTQYS RAVFDGNYYY YLPWAHTKPV VTLTSYWEDI
660 670 680 690 700
SHRLDAVNTL LAMAERLQTN IEALKSGIQG KIPANQLAEL WLKLIDEVIE
710 720 730 740 750
DTRYTLPLTE GKANVTVLDT QIRKLRSRSL SQIHEAAVRM RSEATDVKST
760 770 780 790 800
LAEIEDWLDK LMQLTEEPQN SMPDIIIWMI RGEKRLAYAR IPAHQVLYST
810 820 830 840 850
SGENASGKYC GKTQTIFLKY PQEKNNGPKV PVELRVNIWL GLSAVEKKFN
860 870 880 890 900
SFAEGTFTVF AEMYENQALM FGKWGTSGLV GRHKFSDVTG KIKLKREFFL
910 920 930 940 950
PPKGWEWEGE WIVDPERSLL TEADAGHTEF TDEVYQNESR YPGGDWKPAE
960 970 980 990 1000
DTYTDANGDK AASPSELTCP PGWEWEDDAW SYDINRAVDE KGWEYGITIP
1010 1020 1030 1040 1050
PDHKPKSWVA AEKMYHTHRR RRLVRKRKKD LTQTASSTAR AMEELQDQEG
1060 1070 1080 1090 1100
WEYASLIGWK FHWKQRSSDT FRRRRWRRKM APSETHGAAA IFKLEGALGA
1110 1120 1130 1140 1150
DTTEDGDEKS LEKQKHSATT VFGANTPIVS CNFDRVYIYH LRCYVYQARN
1160 1170 1180 1190 1200
LLALDKDSFS DPYAHICFLH RSKTTEIIHS TLNPTWDQTI IFDEVEIYGE
1210 1220 1230 1240 1250
PQTVLQNPPK VIMELFDNDQ VGKDEFLGRS IFSPVVKLNS EMDITPKLLW
1260 1270 1280 1290 1300
HPVMNGDKAC GDVLVTAELI LRGKDGSNLP ILPPQRAPNL YMVPQGIRPV
1310 1320 1330 1340 1350
VQLTAIEILA WGLRNMKNFQ MASITSPSLV VECGGERVES VVIKNLKKTP
1360 1370 1380 1390 1400
NFPSSVLFMK VFLPKEELYM PPLVIKVIDH RQFGRKPVVG QCTIERLDRF
1410 1420 1430 1440 1450
RCDPYAGKED IVPQLKASLL SAPPCRDIVI EMEDTKPLLA SKLTEKEEEI
1460 1470 1480 1490 1500
VDWWSKFYAS SGEHEKCGQY IQKGYSKLKI YNCELENVAE FEGLTDFSDT
1510 1520 1530 1540 1550
FKLYRGKSDE NEDPSVVGEF KGSFRIYPLP DDPSVPAPPR QFRELPDSVP
1560 1570 1580 1590 1600
QECTVRIYIV RGLELQPQDN NGLCDPYIKI TLGKKVIEDR DHYIPNTLNP
1610 1620 1630 1640 1650
VFGRMYELSC YLPQEKDLKI SVYDYDTFTR DEKVGETIID LENRFLSRFG
1660 1670 1680 1690 1700
SHCGIPEEYC VSGVNTWRDQ LRPTQLLQNV ARFKGFPQPI LSEDGSRIRY
1710 1720 1730 1740 1750
GGRDYSLDEF EANKILHQHL GAPEERLALH ILRTQGLVPE HVETRTLHST
1760 1770 1780 1790 1800
FQPNISQGKL QMWVDVFPKS LGPPGPPFNI TPRKAKKYYL RVIIWNTKDV
1810 1820 1830 1840 1850
ILDEKSITGE EMSDIYVKGW IPGNEENKQK TDVHYRSLDG EGNFNWRFVF
1860 1870 1880 1890 1900
PFDYLPAEQL CIVAKKEHFW SIDQTEFRIP PRLIIQIWDN DKFSLDDYLG
1910 1920 1930 1940 1950
FLELDLRHTI IPAKSPEKCR LDMIPDLKAM NPLKAKTASL FEQKSMKGWW
1960 1970 1980 1990 2000
PCYAEKDGAR VMAGKVEMTL EILNEKEADE RPAGKGRDEP NMNPKLDLPN
2010 2020 2030 2040 2050
RPETSFLWFT NPCKTMKFIV WRRFKWVIIG LLFLLILLLF VAVLLYSLPN
2060
YLSMKIVKPN V
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.Curated
The sequence BAG52097.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 14 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.
GeneTreei ENSGT00550000074414.
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

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: November 26, 2014
This is version 134 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