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Protein

Mitofusin-1

Gene

MFN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:12475957, PubMed:12759376, PubMed:27920125, PubMed:28114303). Membrane clustering requires GTPase activity (PubMed:27920125). It may involve a major rearrangement of the coiled coil domains (PubMed:27920125, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:12475957, PubMed:12759376). Overexpression induces the formation of mitochondrial networks (in vitro) (PubMed:12759376). Has low GTPase activity (PubMed:27920125, PubMed:28114303).4 Publications

Miscellaneous

A truncated MFN1 construct containing the GTPase domain and the associated helix bundle is a monomer in the absence of bound GTP and a homodimer in the GTP-bound form; GDP cannot replace GTP and induce dimerization.2 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei284GTPCombined sources2 Publications1
Binding sitei286GTPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 90GTPCombined sources2 Publications6
Nucleotide bindingi237 – 240GTPCombined sources2 Publications4

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • GTP metabolic process Source: UniProtKB
  • macroautophagy Source: Reactome
  • mitochondrial fusion Source: BHF-UCL
  • mitochondrial membrane fusion Source: UniProtKB
  • mitochondrion localization Source: UniProtKB

Keywordsi

Molecular functionHydrolase
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-5205685 Pink/Parkin Mediated Mitophagy
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

Protein family/group databases

TCDBi1.N.6.1.2 the mitochondrial inner/outer membrane fusion (mmf) family

Names & Taxonomyi

Protein namesi
Recommended name:
Mitofusin-1 (EC:3.6.5.-2 Publications)
Alternative name(s):
Fzo homolog1 Publication
Transmembrane GTPase MFN1
Gene namesi
Name:MFN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000171109.18
HGNCiHGNC:18262 MFN1
MIMi608506 gene
neXtProtiNX_Q8IWA4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 584CytoplasmicSequence analysisAdd BLAST584
Transmembranei585 – 605Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini606 – 608Mitochondrial intermembraneSequence analysis3
Transmembranei609 – 629Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini630 – 741CytoplasmicSequence analysisAdd BLAST112

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15K → A: Decreases GTPase activity. Impairs mitochondrial fusion. 2 Publications1
Mutagenesisi74R → P: Mildly decreases GTPase activity and impairs mitochondrial fusion. 1 Publication1
Mutagenesisi88K → A: Abolishes GTPase activity. Abolishes dimerization. 1 Publication1
Mutagenesisi88K → T: Induces a strong decrease in mitochondrial clustering. 1 Publication1
Mutagenesisi99K → A: Mildly decreases GTPase activity. 1 Publication1
Mutagenesisi102P → L: Impairs protein folding. Decreases GTPase activity. 1 Publication1
Mutagenesisi107H → A: Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding. 1 Publication1
Mutagenesisi109T → A: Acts as a dominant negative mutant; induces fragmentation of mitochondria. 1 Publication1
Mutagenesisi144H → A: Abolishes GTPase activity. Abolishes dimerization. 1 Publication1
Mutagenesisi173D → A: Decreases GTPase activity. 1 Publication1
Mutagenesisi189D → A: Causes mitochondrial clumping. 1 Publication1
Mutagenesisi209E → A: Abolishes dimerization. Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding. 1 Publication1
Mutagenesisi238R → A: Abolishes dimerization. Loss of function in mitochondrial fusion. Abolishes GTPase activity, but has no effect on GTP binding. 1 Publication1
Mutagenesisi239W → A: Abolishes GTP binding and GTPase activity. Loss of function in mitochondrial fusion. 1 Publication1
Mutagenesisi245E → A: Decreases GTPase activity. Abolishes dimerization. Impairs mitochondrial fusion. 1 Publication1
Mutagenesisi309G → P: Mildly decreases GTPase activity and impairs mitochondrial fusion. 1 Publication1
Mutagenesisi328I → A: Slightly decreases GTPase activity. 1 Publication1
Mutagenesisi336K → N: Loss of function in mitochondrial fusion. Abolishes dimerization. Decreases GTPase activity. 1 Publication1
Mutagenesisi336K → P: Decreases GTPase activity and impairs mitochondrial fusion. 1 Publication1
Mutagenesisi705L → P: Impairs protein folding. Decreases GTPase activity. 2 Publications1
Mutagenesisi733F → P: Impairs protein folding. 1 Publication1

Organism-specific databases

DisGeNETi55669
OpenTargetsiENSG00000171109
PharmGKBiPA134945973

Polymorphism and mutation databases

BioMutaiMFN1
DMDMi150421594

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001276721 – 741Mitofusin-1Add BLAST741

Post-translational modificationi

Ubiquitinated by non-degradative ubiquitin by PRKN (PubMed:23933751). Deubiquitination by USP30 inhibits mitochondrial fusion (By similarity). Ubiquitinated by MARCH5 (PubMed:20103533). When mitochondria are depolarized and dysfunctional, it is ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex that contains FBXO7 and PRKN (PubMed:23933751).By similarity2 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ8IWA4
MaxQBiQ8IWA4
PaxDbiQ8IWA4
PeptideAtlasiQ8IWA4
PRIDEiQ8IWA4
ProteomicsDBi70826
70827 [Q8IWA4-2]
70828 [Q8IWA4-3]

PTM databases

iPTMnetiQ8IWA4
PhosphoSitePlusiQ8IWA4

Expressioni

Tissue specificityi

Detected in kidney and heart (at protein level) (PubMed:12759376). Ubiquitous (PubMed:11950885, PubMed:12759376). Expressed at slightly higher level in kidney and heart (PubMed:12759376). Isoform 2 may be overexpressed in some tumors, such as lung cancers (PubMed:11751411).3 Publications

Gene expression databases

BgeeiENSG00000171109 Expressed in 227 organ(s), highest expression level in secondary oocyte
CleanExiHS_MFN1
ExpressionAtlasiQ8IWA4 baseline and differential
GenevisibleiQ8IWA4 HS

Organism-specific databases

HPAiHPA059230

Interactioni

Subunit structurei

Homodimer, also in the absence of bound GTP (PubMed:27920125, PubMed:28114303). Forms higher oligomers in the presence of a transition state GTP analog (PubMed:28114303). Forms homomultimers and heteromultimers with MFN2 (By similarity). Oligomerization is essential for mitochondrion fusion (PubMed:27920125, PubMed:28114303). Component of a high molecular weight multiprotein complex (PubMed:12759376). Interacts with VAT1 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAVSQ7Z4342EBI-1048197,EBI-995373

Protein-protein interaction databases

BioGridi120801, 15 interactors
DIPiDIP-50289N
IntActiQ8IWA4, 6 interactors
MINTiQ8IWA4
STRINGi9606.ENSP00000263969

Structurei

Secondary structure

1741
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ8IWA4
SMRiQ8IWA4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 321Dynamin-type GPROSITE-ProRule annotationAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 73Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions2 PublicationsAdd BLAST65
Regioni82 – 89G1 motifPROSITE-ProRule annotation8
Regioni108 – 109G2 motifPROSITE-ProRule annotation2
Regioni178 – 181G3 motifPROSITE-ProRule annotation4
Regioni237 – 240G4 motifPROSITE-ProRule annotation4
Regioni266G5 motifPROSITE-ProRule annotation1
Regioni338 – 364Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions2 PublicationsAdd BLAST27
Regioni703 – 734Part of a helix bundle domain, formed by helices from N-terminal and C-terminal regions2 PublicationsAdd BLAST32

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili371 – 408Sequence analysisAdd BLAST38
Coiled coili679 – 734Sequence analysisAdd BLAST56

Domaini

A helix bundle is formed by helices from the N-terminal and the C-terminal part of the protein. The GTPase domain cannot be expressed by itself, without the helix bundle. Rearrangement of the helix bundle and/or of the coiled coil domains may bring membranes from adjacent mitochondria into close contact, and thereby play a role in mitochondrial fusion.2 Publications

Sequence similaritiesi

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0448 Eukaryota
COG0699 LUCA
GeneTreeiENSGT00390000013727
HOVERGENiHBG052465
InParanoidiQ8IWA4
KOiK21356
OMAiAMTDEIC
OrthoDBiEOG091G02ES
PhylomeDBiQ8IWA4
TreeFamiTF314289

Family and domain databases

InterProiView protein in InterPro
IPR022812 Dynamin_SF
IPR006884 Fzo/mitofusin_HR2
IPR030381 G_DYNAMIN_dom
IPR027088 Mitofusin-1
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase
PANTHERiPTHR10465 PTHR10465, 1 hit
PTHR10465:SF2 PTHR10465:SF2, 1 hit
PfamiView protein in Pfam
PF00350 Dynamin_N, 1 hit
PF04799 Fzo_mitofusin, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51718 G_DYNAMIN_2, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8IWA4-1) [UniParc]FASTAAdd to basket
Also known as: TG7411 Publication

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
MAEPVSPLKH FVLAKKAITA IFDQLLEFVT EGSHFVEATY KNPELDRIAT
60 70 80 90 100
EDDLVEMQGY KDKLSIIGEV LSRRHMKVAF FGRTSSGKSS VINAMLWDKV
110 120 130 140 150
LPSGIGHITN CFLSVEGTDG DKAYLMTEGS DEKKSVKTVN QLAHALHMDK
160 170 180 190 200
DLKAGCLVRV FWPKAKCALL RDDLVLVDSP GTDVTTELDS WIDKFCLDAD
210 220 230 240 250
VFVLVANSES TLMNTEKHFF HKVNERLSKP NIFILNNRWD ASASEPEYME
260 270 280 290 300
DVRRQHMERC LHFLVEELKV VNALEAQNRI FFVSAKEVLS ARKQKAQGMP
310 320 330 340 350
ESGVALAEGF HARLQEFQNF EQIFEECISQ SAVKTKFEQH TIRAKQILAT
360 370 380 390 400
VKNIMDSVNL AAEDKRHYSV EEREDQIDRL DFIRNQMNLL TLDVKKKIKE
410 420 430 440 450
VTEEVANKVS CAMTDEICRL SVLVDEFCSE FHPNPDVLKI YKSELNKHIE
460 470 480 490 500
DGMGRNLADR CTDEVNALVL QTQQEIIENL KPLLPAGIQD KLHTLIPCKK
510 520 530 540 550
FDLSYNLNYH KLCSDFQEDI VFRFSLGWSS LVHRFLGPRN AQRVLLGLSE
560 570 580 590 600
PIFQLPRSLA STPTAPTTPA TPDNASQEEL MITLVTGLAS VTSRTSMGII
610 620 630 640 650
IVGGVIWKTI GWKLLSVSLT MYGALYLYER LSWTTHAKER AFKQQFVNYA
660 670 680 690 700
TEKLRMIVSS TSANCSHQVK QQIATTFARL CQQVDITQKQ LEEEIARLPK
710 720 730 740
EIDQLEKIQN NSKLLRNKAV QLENELENFT KQFLPSSNEE S
Length:741
Mass (Da):84,160
Last modified:March 28, 2018 - v3
Checksum:iB7BDC22437E30A58
GO
Isoform 2 (identifier: Q8IWA4-2) [UniParc]FASTAAdd to basket
Also known as: TG3701 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     367-370: HYSV → FHVQ
     371-741: Missing.

Show »
Length:370
Mass (Da):41,883
Checksum:i187B06EA1E971C6E
GO
Isoform 3 (identifier: Q8IWA4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     444-554: Missing.

Show »
Length:630
Mass (Da):71,401
Checksum:iD173A310365208BD
GO

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C5H5H7C5H5_HUMAN
Mitofusin-1
MFN1
493Annotation score:
C9JQT7C9JQT7_HUMAN
Mitofusin-1
MFN1
124Annotation score:
C9JXQ1C9JXQ1_HUMAN
Mitofusin-1
MFN1
154Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti17A → G in AAK06840 (PubMed:11181170).Curated1
Sequence conflicti21I → V in BAA91327 (PubMed:14702039).Curated1
Sequence conflicti162W → C in AAB64220 (PubMed:9230308).Curated1
Sequence conflicti226R → W in AAK06840 (PubMed:11181170).Curated1
Sequence conflicti271V → A in AAK06840 (PubMed:11181170).Curated1
Sequence conflicti406A → P in AAB64220 (PubMed:9230308).Curated1
Sequence conflicti688Q → H in AAB64220 (PubMed:9230308).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036115415D → H in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_018606523R → P. Corresponds to variant dbSNP:rs7637065Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010362367 – 370HYSV → FHVQ in isoform 2. 1 Publication4
Alternative sequenceiVSP_010363371 – 741Missing in isoform 2. 1 PublicationAdd BLAST371
Alternative sequenceiVSP_010364444 – 554Missing in isoform 3. 1 PublicationAdd BLAST111

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329637 mRNA Translation: AAK06840.1
AK000700 mRNA Translation: BAA91327.1
AK314306 mRNA Translation: BAG36958.1
AC007823 Genomic DNA No translation available.
AC007620 Genomic DNA No translation available.
KF457722 Genomic DNA No translation available.
CH471052 Genomic DNA Translation: EAW78406.1
CH471052 Genomic DNA Translation: EAW78410.1
CH471052 Genomic DNA Translation: EAW78411.1
BC040557 mRNA Translation: AAH40557.1
U95822 mRNA Translation: AAB64220.1
AF054986 mRNA Translation: AAC09347.1
CCDSiCCDS3228.1 [Q8IWA4-1]
RefSeqiNP_284941.2, NM_033540.2 [Q8IWA4-1]
XP_005247653.2, XM_005247596.3 [Q8IWA4-1]
UniGeneiHs.478383

Genome annotation databases

EnsembliENST00000263969; ENSP00000263969; ENSG00000171109 [Q8IWA4-1]
ENST00000357390; ENSP00000349963; ENSG00000171109 [Q8IWA4-2]
ENST00000471841; ENSP00000420617; ENSG00000171109 [Q8IWA4-1]
GeneIDi55669
KEGGihsa:55669
UCSCiuc003fjs.4 human [Q8IWA4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329637 mRNA Translation: AAK06840.1
AK000700 mRNA Translation: BAA91327.1
AK314306 mRNA Translation: BAG36958.1
AC007823 Genomic DNA No translation available.
AC007620 Genomic DNA No translation available.
KF457722 Genomic DNA No translation available.
CH471052 Genomic DNA Translation: EAW78406.1
CH471052 Genomic DNA Translation: EAW78410.1
CH471052 Genomic DNA Translation: EAW78411.1
BC040557 mRNA Translation: AAH40557.1
U95822 mRNA Translation: AAB64220.1
AF054986 mRNA Translation: AAC09347.1
CCDSiCCDS3228.1 [Q8IWA4-1]
RefSeqiNP_284941.2, NM_033540.2 [Q8IWA4-1]
XP_005247653.2, XM_005247596.3 [Q8IWA4-1]
UniGeneiHs.478383

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GNRX-ray2.65A1-364[»]
A696-741[»]
5GNSX-ray2.70A1-364[»]
A696-741[»]
5GNTX-ray2.67A1-364[»]
A696-741[»]
5GNUX-ray4.11A1-364[»]
A696-741[»]
5GO4X-ray2.20A1-365[»]
A696-741[»]
5GOEX-ray1.80A1-369[»]
A696-741[»]
5GOFX-ray1.60A1-362[»]
A696-741[»]
5GOMX-ray2.80A/B1-362[»]
A/B696-741[»]
5YEWX-ray3.20A/B/C1-364[»]
A/B/C694-741[»]
ProteinModelPortaliQ8IWA4
SMRiQ8IWA4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120801, 15 interactors
DIPiDIP-50289N
IntActiQ8IWA4, 6 interactors
MINTiQ8IWA4
STRINGi9606.ENSP00000263969

Protein family/group databases

TCDBi1.N.6.1.2 the mitochondrial inner/outer membrane fusion (mmf) family

PTM databases

iPTMnetiQ8IWA4
PhosphoSitePlusiQ8IWA4

Polymorphism and mutation databases

BioMutaiMFN1
DMDMi150421594

Proteomic databases

EPDiQ8IWA4
MaxQBiQ8IWA4
PaxDbiQ8IWA4
PeptideAtlasiQ8IWA4
PRIDEiQ8IWA4
ProteomicsDBi70826
70827 [Q8IWA4-2]
70828 [Q8IWA4-3]

Protocols and materials databases

DNASUi55669
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263969; ENSP00000263969; ENSG00000171109 [Q8IWA4-1]
ENST00000357390; ENSP00000349963; ENSG00000171109 [Q8IWA4-2]
ENST00000471841; ENSP00000420617; ENSG00000171109 [Q8IWA4-1]
GeneIDi55669
KEGGihsa:55669
UCSCiuc003fjs.4 human [Q8IWA4-1]

Organism-specific databases

CTDi55669
DisGeNETi55669
EuPathDBiHostDB:ENSG00000171109.18
GeneCardsiMFN1
HGNCiHGNC:18262 MFN1
HPAiHPA059230
MIMi608506 gene
neXtProtiNX_Q8IWA4
OpenTargetsiENSG00000171109
PharmGKBiPA134945973
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0448 Eukaryota
COG0699 LUCA
GeneTreeiENSGT00390000013727
HOVERGENiHBG052465
InParanoidiQ8IWA4
KOiK21356
OMAiAMTDEIC
OrthoDBiEOG091G02ES
PhylomeDBiQ8IWA4
TreeFamiTF314289

Enzyme and pathway databases

ReactomeiR-HSA-5205685 Pink/Parkin Mediated Mitophagy
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

GeneWikiiMFN1
GenomeRNAii55669
PROiPR:Q8IWA4
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171109 Expressed in 227 organ(s), highest expression level in secondary oocyte
CleanExiHS_MFN1
ExpressionAtlasiQ8IWA4 baseline and differential
GenevisibleiQ8IWA4 HS

Family and domain databases

InterProiView protein in InterPro
IPR022812 Dynamin_SF
IPR006884 Fzo/mitofusin_HR2
IPR030381 G_DYNAMIN_dom
IPR027088 Mitofusin-1
IPR027094 Mitofusin_fam
IPR027417 P-loop_NTPase
PANTHERiPTHR10465 PTHR10465, 1 hit
PTHR10465:SF2 PTHR10465:SF2, 1 hit
PfamiView protein in Pfam
PF00350 Dynamin_N, 1 hit
PF04799 Fzo_mitofusin, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51718 G_DYNAMIN_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMFN1_HUMAN
AccessioniPrimary (citable) accession number: Q8IWA4
Secondary accession number(s): A0A0C4DFN1
, B2RAR1, D3DNR6, O15323, O60639, Q9BZB5, Q9NWQ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 28, 2018
Last modified: October 10, 2018
This is version 146 of the entry and version 3 of the sequence. See 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 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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