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Protein

Insulin-like growth factor-binding protein 2

Gene

IGFBP2

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

Functioni

Inhibits IGF-mediated growth and developmental rates. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.1 Publication

GO - Molecular functioni

  1. insulin-like growth factor I binding Source: UniProtKB
  2. insulin-like growth factor II binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular protein metabolic process Source: Reactome
  3. cellular response to hormone stimulus Source: Ensembl
  4. female pregnancy Source: Ensembl
  5. positive regulation of activated T cell proliferation Source: BHF-UCL
  6. regulation of cell growth Source: InterPro
  7. regulation of insulin-like growth factor receptor signaling pathway Source: UniProtKB
  8. response to drug Source: Ensembl
  9. response to estradiol Source: Ensembl
  10. response to glucocorticoid Source: Ensembl
  11. response to lithium ion Source: Ensembl
  12. response to mechanical stimulus Source: Ensembl
  13. response to nutrient Source: Ensembl
  14. response to retinoic acid Source: Ensembl
  15. signal transduction Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Growth regulation

Keywords - Ligandi

Growth factor binding

Enzyme and pathway databases

ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Protein family/group databases

MEROPSiI31.953.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor-binding protein 2
Short name:
IBP-2
Short name:
IGF-binding protein 2
Short name:
IGFBP-2
Gene namesi
Name:IGFBP2
Synonyms:BP2, IBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:5471. IGFBP2.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cytoplasmic vesicle Source: Ensembl
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi216 – 2194KKLR → NNLA: Does not disrupt growth-inhibiting activity. 1 Publication
Mutagenesisi303 – 3031D → E: Does not disrupt growth-inhibiting activity. 1 Publication

Organism-specific databases

PharmGKBiPA29704.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Add
BLAST
Chaini36 – 325290Insulin-like growth factor-binding protein 2PRO_0000014370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi227 ↔ 2611 PublicationPROSITE-ProRule annotation
Disulfide bondi272 ↔ 2831 PublicationPROSITE-ProRule annotation
Disulfide bondi285 ↔ 3061 PublicationPROSITE-ProRule annotation

Post-translational modificationi

O-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP18065.
PRIDEiP18065.

PTM databases

PhosphoSiteiP18065.

Miscellaneous databases

PMAP-CutDBP18065.

Expressioni

Gene expression databases

BgeeiP18065.
CleanExiHS_IGFBP2.
ExpressionAtlasiP18065. baseline and differential.
GenevestigatoriP18065.

Interactioni

Subunit structurei

Binds IGF2 more than IGF1.

Binary interactionsi

WithEntry#Exp.IntActNotes
INO80BQ9C0864EBI-2504392,EBI-715611

Protein-protein interaction databases

BioGridi109706. 3 interactions.
IntActiP18065. 3 interactions.
STRINGi9606.ENSP00000233809.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi226 – 24015Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi269 – 2768Combined sources
Turni277 – 2793Combined sources
Beta strandi282 – 2854Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H7TNMR-A220-325[»]
ProteinModelPortaliP18065.
SMRiP18065. Positions 42-138, 220-325.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18065.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 13497IGFBP N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini224 – 30683Thyroglobulin type-1PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 3033Cell attachment site

Domaini

The C-terminus is required for IGF-binding and growth inhibition.1 Publication

Sequence similaritiesi

Contains 1 IGFBP N-terminal domain.PROSITE-ProRule annotation
Contains 1 thyroglobulin type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG47500.
GeneTreeiENSGT00550000074457.
HOGENOMiHOG000253012.
HOVERGENiHBG002631.
InParanoidiP18065.
OMAiGAGTCEK.
PhylomeDBiP18065.
TreeFamiTF331211.

Family and domain databases

Gene3Di4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR012210. IGFBP-2.
IPR000867. IGFBP-like.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERiPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF5. PTHR11551:SF5. 1 hit.
PfamiPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSiPR01976. IGFBPFAMILY.
PR01978. IGFBPFAMILY2.
SMARTiSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEiPS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18065-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPRVGCPAL PLPPPPLLPL LLLLLGASGG GGGARAEVLF RCPPCTPERL
60 70 80 90 100
AACGPPPVAP PAAVAAVAGG ARMPCAELVR EPGCGCCSVC ARLEGEACGV
110 120 130 140 150
YTPRCGQGLR CYPHPGSELP LQALVMGEGT CEKRRDAEYG ASPEQVADNG
160 170 180 190 200
DDHSEGGLVE NHVDSTMNML GGGGSAGRKP LKSGMKELAV FREKVTEQHR
210 220 230 240 250
QMGKGGKHHL GLEEPKKLRP PPARTPCQQE LDQVLERIST MRLPDERGPL
260 270 280 290 300
EHLYSLHIPN CDKHGLYNLK QCKMSLNGQR GECWCVNPNT GKLIQGAPTI
310 320
RGDPECHLFY NEQQEARGVH TQRMQ
Length:325
Mass (Da):34,814
Last modified:March 2, 2010 - v2
Checksum:i9E1436DBCCC6EA2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151P → PPLL in CAA34373. (PubMed:2479552)Curated
Sequence conflicti15 – 151P → PPLL in AAA36048. (PubMed:1710112)Curated
Sequence conflicti15 – 151P → PPLL in AAA03246. (PubMed:1712312)Curated
Sequence conflicti15 – 151P → PPLL in AAB22308. (PubMed:1376411)Curated
Sequence conflicti15 – 151P → PPLL in AAQ87876. 1 PublicationCurated
Sequence conflicti15 – 151P → PPLL in AAH04312. (PubMed:15489334)Curated
Sequence conflicti15 – 151P → PPLL in AAH09902. (PubMed:15489334)Curated
Sequence conflicti15 – 151P → PPLL in AAH12769. (PubMed:15489334)Curated
Sequence conflicti15 – 151P → PPLL in AAH71967. (PubMed:15489334)Curated
Sequence conflicti57 – 571P → R in AAA36048. (PubMed:1710112)Curated
Sequence conflicti317 – 3171R → C in CAA34373. (PubMed:2479552)Curated
Sequence conflicti320 – 3201H → D in AAA36048. (PubMed:1710112)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371A → D.1 Publication
Corresponds to variant rs9341096 [ dbSNP | Ensembl ].
VAR_018871

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16302 mRNA. Translation: CAA34373.1.
M69241
, M69237, M69239, M69240 Genomic DNA. Translation: AAA36048.1.
M35410 mRNA. Translation: AAA03246.1.
S37730
, S37712, S37722, S37726 Genomic DNA. Translation: AAB22308.1.
CR610845 mRNA. No translation available.
AY398667 Genomic DNA. Translation: AAQ87876.1.
AC073321 Genomic DNA. No translation available.
AC007563 Genomic DNA. No translation available.
BC004312 mRNA. Translation: AAH04312.1.
BC009902 mRNA. Translation: AAH09902.1.
BC012769 mRNA. Translation: AAH12769.1.
BC071967 mRNA. Translation: AAH71967.1.
PIRiA41927.
RefSeqiNP_000588.2. NM_000597.2.
UniGeneiHs.438102.

Genome annotation databases

EnsembliENST00000233809; ENSP00000233809; ENSG00000115457.
GeneIDi3485.
KEGGihsa:3485.
UCSCiuc010zju.2. human.

Polymorphism databases

DMDMi290457647.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16302 mRNA. Translation: CAA34373.1.
M69241
, M69237, M69239, M69240 Genomic DNA. Translation: AAA36048.1.
M35410 mRNA. Translation: AAA03246.1.
S37730
, S37712, S37722, S37726 Genomic DNA. Translation: AAB22308.1.
CR610845 mRNA. No translation available.
AY398667 Genomic DNA. Translation: AAQ87876.1.
AC073321 Genomic DNA. No translation available.
AC007563 Genomic DNA. No translation available.
BC004312 mRNA. Translation: AAH04312.1.
BC009902 mRNA. Translation: AAH09902.1.
BC012769 mRNA. Translation: AAH12769.1.
BC071967 mRNA. Translation: AAH71967.1.
PIRiA41927.
RefSeqiNP_000588.2. NM_000597.2.
UniGeneiHs.438102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2H7TNMR-A220-325[»]
ProteinModelPortaliP18065.
SMRiP18065. Positions 42-138, 220-325.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109706. 3 interactions.
IntActiP18065. 3 interactions.
STRINGi9606.ENSP00000233809.

Chemistry

ChEMBLiCHEMBL3088.

Protein family/group databases

MEROPSiI31.953.

PTM databases

PhosphoSiteiP18065.

Polymorphism databases

DMDMi290457647.

Proteomic databases

PaxDbiP18065.
PRIDEiP18065.

Protocols and materials databases

DNASUi3485.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233809; ENSP00000233809; ENSG00000115457.
GeneIDi3485.
KEGGihsa:3485.
UCSCiuc010zju.2. human.

Organism-specific databases

CTDi3485.
GeneCardsiGC02P217497.
HGNCiHGNC:5471. IGFBP2.
MIMi146731. gene.
neXtProtiNX_P18065.
PharmGKBiPA29704.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47500.
GeneTreeiENSGT00550000074457.
HOGENOMiHOG000253012.
HOVERGENiHBG002631.
InParanoidiP18065.
OMAiGAGTCEK.
PhylomeDBiP18065.
TreeFamiTF331211.

Enzyme and pathway databases

ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

ChiTaRSiIGFBP2. human.
EvolutionaryTraceiP18065.
GeneWikiiIGFBP2.
GenomeRNAii3485.
NextBioi13704.
PMAP-CutDBP18065.
PROiP18065.
SOURCEiSearch...

Gene expression databases

BgeeiP18065.
CleanExiHS_IGFBP2.
ExpressionAtlasiP18065. baseline and differential.
GenevestigatoriP18065.

Family and domain databases

Gene3Di4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR012210. IGFBP-2.
IPR000867. IGFBP-like.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERiPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF5. PTHR11551:SF5. 1 hit.
PfamiPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSiPR01976. IGFBPFAMILY.
PR01978. IGFBPFAMILY2.
SMARTiSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEiPS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequence analysis and expression of a cDNA encoding a novel insulin-like growth factor binding protein (IGFBP-2)."
    Binkert C., Landwehr J., Mary J.L., Schwander J., Heinrich G.
    EMBO J. 8:2497-2502(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver.
  2. "Isolation from adult human serum of four insulin-like growth factor (IGF) binding proteins and molecular cloning of one of them that is increased by IGF I administration and in extrapancreatic tumor hypoglycemia."
    Zapf J., Kiefer M., Merryweather J., Musiarz F., Bauer D., Born W., Fischer J.A., Froesch E.R.
    J. Biol. Chem. 265:14892-14898(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-74.
  3. "Structure and localization of the human insulin-like growth factor-binding protein 2 gene."
    Ehrenborg E., Vilhelmsdotter S., Bajalica S., Larsson C., Sterm I., Koch J., Brondum-Nielsen K., Luthman H.
    Biochem. Biophys. Res. Commun. 176:1250-1255(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  4. "Sequence analysis, expression and chromosomal localization of a gene, isolated from a subtracted human retina cDNA library, that encodes an insulin-like growth factor binding protein (IGFBP2)."
    Agarwal N., Hsieh C.L., Sills D., Swaroop M., Desai B., Francke U., Swaroop A.
    Exp. Eye Res. 52:549-561(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Retina.
  5. "Structure of the human insulin-like growth factor binding protein-2 gene."
    Binkert C., Margot J.B., Landwehr J., Heinrich G., Schwander J.
    Mol. Endocrinol. 6:826-836(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  6. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  7. NIEHS SNPs program
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-137.
  8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Brain, Ovary and Uterus.
  10. "Purification from human cerebrospinal fluid of insulin-like growth factor binding proteins (IGFBPs). Isolation of IGFBP-2, an altered form of IGFBP-3 and a new IGFBP species."
    Roghani M., Segovia B., Whitechurch O., Binoux M.
    Growth Regul. 1:125-130(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-58, INTERACTION WITH IGF2, GLYCOSYLATION.
    Tissue: Cerebrospinal fluid.
  11. "Duplication of the IGFBP-2 gene in teleost fish: protein structure and functionality conservation and gene expression divergence."
    Zhou J., Li W., Kamei H., Duan C.
    PLoS ONE 3:E3926-E3926(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IGF1-BINDING, DOMAIN, MUTAGENESIS OF 216-LYS--ARG-219 AND ASP-303.
  12. "Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2)."
    Kuang Z., Yao S., Keizer D.W., Wang C.C., Bach L.A., Forbes B.E., Wallace J.C., Norton R.S.
    J. Mol. Biol. 364:690-704(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 220-325, DISULFIDE BONDS.

Entry informationi

Entry nameiIBP2_HUMAN
AccessioniPrimary (citable) accession number: P18065
Secondary accession number(s): Q14619, Q9UCL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 2, 2010
Last modified: January 7, 2015
This is version 159 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 2
    Human chromosome 2: 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

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.