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Protein

Mitochondrial fission 1 protein

Gene

FIS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission.7 Publications

GO - Molecular functioni

  • receptor binding Source: UniProtKB

GO - Biological processi

  • calcium-mediated signaling using intracellular calcium source Source: UniProtKB
  • mitochondrial fission Source: UniProtKB
  • mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
  • mitochondrial fusion Source: UniProtKB
  • mitochondrion degradation Source: UniProtKB
  • mitochondrion morphogenesis Source: UniProtKB
  • negative regulation of endoplasmic reticulum calcium ion concentration Source: UniProtKB
  • peroxisome fission Source: UniProtKB
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of mitochondrial calcium ion concentration Source: UniProtKB
  • positive regulation of mitochondrial fission Source: UniProtKB
  • positive regulation of protein targeting to membrane Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein targeting to mitochondrion Source: UniProtKB
  • regulation of mitochondrion organization Source: UniProtKB
  • release of cytochrome c from mitochondria Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial fission 1 protein
Alternative name(s):
FIS1 homolog
Short name:
hFis1
Tetratricopeptide repeat protein 11
Short name:
TPR repeat protein 11
Gene namesi
Name:FIS1
Synonyms:TTC11
ORF Names:CGI-135
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21689. FIS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 122122CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence AnalysisAdd
BLAST
Topological domaini144 – 1529Mitochondrial intermembraneSequence Analysis

GO - Cellular componenti

  • cytosol Source: GOC
  • endoplasmic reticulum Source: GOC
  • integral component of mitochondrial outer membrane Source: UniProtKB
  • integral component of peroxisomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • peroxisome Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141L → P: Approximately 40% of cells display fragmented mitochondria. 1 Publication
Mutagenesisi42 – 421L → P: Less than 15% of cells display fragmented mitochondria. 1 Publication
Mutagenesisi58 – 581L → P: Less than 15% of cells display fragmented mitochondria. 1 Publication
Mutagenesisi77 – 771L → P: Less than 15% of cells display fragmented mitochondria. Shows greatly reduced binding to DNM1L. 1 Publication
Mutagenesisi91 – 911L → P: Less than 15% of cells display fragmented mitochondria. Shows greatly reduced binding to DNM1L. 1 Publication
Mutagenesisi110 – 1101L → P: Approximately 40% of cells display fragmented mitochondria. No change in binding to DNM1L. 1 Publication
Mutagenesisi149 – 1491K → A: Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-151. 1 Publication
Mutagenesisi151 – 1511K → A: Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-149. 1 Publication

Organism-specific databases

PharmGKBiPA134984211.

Polymorphism and mutation databases

BioMutaiFIS1.
DMDMi33112470.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Mitochondrial fission 1 proteinPRO_0000106393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei10 – 101Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated by MARCH5.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y3D6.
PaxDbiQ9Y3D6.
PeptideAtlasiQ9Y3D6.
PRIDEiQ9Y3D6.

2D gel databases

UCD-2DPAGEQ9Y3D6.

PTM databases

PhosphoSiteiQ9Y3D6.

Expressioni

Gene expression databases

BgeeiQ9Y3D6.
CleanExiHS_FIS1.
ExpressionAtlasiQ9Y3D6. baseline and differential.
GenevisibleiQ9Y3D6. HS.

Organism-specific databases

HPAiHPA017430.

Interactioni

Subunit structurei

Interacts with DNM1L/DLP1 through the TPR region. Interacts with MARCH5. Interacts with MIEF1. Interacts with PEX11A, PEX11B and PEX11G (PubMed:20826455).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAP31P515728EBI-3385283,EBI-77683
CCDC155Q8N6L03EBI-3385283,EBI-749265
MIEF1Q9NQG64EBI-3385283,EBI-740987

Protein-protein interaction databases

BioGridi119230. 23 interactions.
IntActiQ9Y3D6. 11 interactions.
MINTiMINT-2844167.
STRINGi9606.ENSP00000223136.

Structurei

Secondary structure

152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 2727Combined sources
Helixi32 – 4211Combined sources
Beta strandi45 – 473Combined sources
Helixi48 – 6114Combined sources
Turni62 – 643Combined sources
Helixi67 – 8317Combined sources
Helixi87 – 10014Combined sources
Helixi105 – 12016Combined sources
Beta strandi129 – 1335Combined sources
Beta strandi142 – 1443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NZNX-ray2.00A1-123[»]
1PC2NMR-A1-145[»]
DisProtiDP00457.
ProteinModelPortaliQ9Y3D6.
SMRiQ9Y3D6. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3D6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati71 – 10434TPRAdd
BLAST

Domaini

The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L.

Sequence similaritiesi

Belongs to the FIS1 family.Curated
Contains 1 TPR repeat.Curated

Keywords - Domaini

TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG235677.
GeneTreeiENSGT00390000000592.
HOGENOMiHOG000165386.
HOVERGENiHBG081530.
InParanoidiQ9Y3D6.
KOiK17969.
OMAiTELPYAA.
PhylomeDBiQ9Y3D6.
TreeFamiTF315180.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR016543. Fis1.
IPR028061. Fis1_TPR_C.
IPR028058. Fis1_TPR_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13247. PTHR13247. 1 hit.
PfamiPF14853. Fis1_TPR_C. 1 hit.
PF14852. Fis1_TPR_N. 1 hit.
[Graphical view]
PIRSFiPIRSF008835. TPR_repeat_11_Fis1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y3D6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD
60 70 80 90 100
IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT
110 120 130 140 150
EPQNNQAKEL ERLIDKAMKK DGLVGMAIVG GMALGVAGLA GLIGLAVSKS

KS
Length:152
Mass (Da):16,938
Last modified:July 19, 2003 - v2
Checksum:i6E76EC02B3731A9B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462SK → TR in AAD34130 (PubMed:10810093).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151893 mRNA. Translation: AAD34130.1.
AC006329 Genomic DNA. Translation: AAP22366.1.
BC003540 mRNA. Translation: AAH03540.1.
BC009428 mRNA. Translation: AAH09428.1.
CCDSiCCDS43626.1.
RefSeqiNP_057152.2. NM_016068.2.
UniGeneiHs.423968.

Genome annotation databases

EnsembliENST00000223136; ENSP00000223136; ENSG00000214253.
GeneIDi51024.
KEGGihsa:51024.
UCSCiuc003uyj.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151893 mRNA. Translation: AAD34130.1.
AC006329 Genomic DNA. Translation: AAP22366.1.
BC003540 mRNA. Translation: AAH03540.1.
BC009428 mRNA. Translation: AAH09428.1.
CCDSiCCDS43626.1.
RefSeqiNP_057152.2. NM_016068.2.
UniGeneiHs.423968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NZNX-ray2.00A1-123[»]
1PC2NMR-A1-145[»]
DisProtiDP00457.
ProteinModelPortaliQ9Y3D6.
SMRiQ9Y3D6. Positions 1-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119230. 23 interactions.
IntActiQ9Y3D6. 11 interactions.
MINTiMINT-2844167.
STRINGi9606.ENSP00000223136.

PTM databases

PhosphoSiteiQ9Y3D6.

Polymorphism and mutation databases

BioMutaiFIS1.
DMDMi33112470.

2D gel databases

UCD-2DPAGEQ9Y3D6.

Proteomic databases

MaxQBiQ9Y3D6.
PaxDbiQ9Y3D6.
PeptideAtlasiQ9Y3D6.
PRIDEiQ9Y3D6.

Protocols and materials databases

DNASUi51024.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000223136; ENSP00000223136; ENSG00000214253.
GeneIDi51024.
KEGGihsa:51024.
UCSCiuc003uyj.4. human.

Organism-specific databases

CTDi51024.
GeneCardsiGC07M100882.
HGNCiHGNC:21689. FIS1.
HPAiHPA017430.
MIMi609003. gene.
neXtProtiNX_Q9Y3D6.
PharmGKBiPA134984211.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG235677.
GeneTreeiENSGT00390000000592.
HOGENOMiHOG000165386.
HOVERGENiHBG081530.
InParanoidiQ9Y3D6.
KOiK17969.
OMAiTELPYAA.
PhylomeDBiQ9Y3D6.
TreeFamiTF315180.

Miscellaneous databases

ChiTaRSiFIS1. human.
EvolutionaryTraceiQ9Y3D6.
GeneWikiiFIS1.
GenomeRNAii51024.
NextBioi53558.
PROiQ9Y3D6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3D6.
CleanExiHS_FIS1.
ExpressionAtlasiQ9Y3D6. baseline and differential.
GenevisibleiQ9Y3D6. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR016543. Fis1.
IPR028061. Fis1_TPR_C.
IPR028058. Fis1_TPR_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13247. PTHR13247. 1 hit.
PfamiPF14853. Fis1_TPR_C. 1 hit.
PF14852. Fis1_TPR_N. 1 hit.
[Graphical view]
PIRSFiPIRSF008835. TPR_repeat_11_Fis1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Pancreas.
  4. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-16, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  5. "hFis1, a novel component of the mammalian mitochondrial fission machinery."
    James D.I., Parone P.A., Mattenberger Y., Martinou J.-C.
    J. Biol. Chem. 278:36373-36379(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1."
    Yoon Y., Krueger E.W., Oswald B.J., McNiven M.A.
    Mol. Cell. Biol. 23:5409-5420(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNM1L.
  7. "Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology."
    Stojanovski D., Koutsopoulos O.S., Okamoto K., Ryan M.T.
    J. Cell Sci. 117:1201-1210(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF LYS-149 AND LYS-151.
  8. "Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1."
    Yu T., Fox R.J., Burwell L.S., Yoon Y.
    J. Cell Sci. 118:4141-4151(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNM1L, MUTAGENESIS OF LEU-14; LEU-42; LEU-58; LEU-77; LEU-91 AND LEU-110.
  9. "A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells."
    Koch A., Yoon Y., Bonekamp N.A., McNiven M.A., Schrader M.
    Mol. Biol. Cell 16:5077-5086(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics."
    Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S.
    EMBO J. 25:3618-3626(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY MARCH5, INTERACTION WITH MARCH5.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance."
    Koch J., Pranjic K., Huber A., Ellinger A., Hartig A., Kragler F., Brocard C.
    J. Cell Sci. 123:3389-3400(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PEX11A; PEX11B AND PEX11G.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission."
    Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M.
    EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIEF1.
  15. "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission."
    Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., Ryan M.T.
    J. Biol. Chem. 288:27584-27593(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
    Loson O.C., Song Z., Chen H., Chan D.C.
    Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
    Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Cytosolic domain of the human mitochondrial fission protein fis1 adopts a TPR fold."
    Dohm J.A., Lee S.J., Hardwick J.M., Hill R.B., Gittis A.G.
    Proteins 54:153-156(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-123.
  20. "The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle."
    Suzuki M., Jeong S.-Y., Karbowski M., Youle R.J., Tjandra N.
    J. Mol. Biol. 334:445-458(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFIS1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3D6
Secondary accession number(s): Q9BTP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: July 19, 2003
Last modified: July 22, 2015
This is version 136 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.