Skip Header

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

Latent-transforming growth factor beta-binding protein 1

Gene

Ltbp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).1 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to mechanical stimulus Source: RGD
  • cellular response to parathyroid hormone stimulus Source: RGD
  • cellular response to platelet-derived growth factor stimulus Source: RGD
  • cellular response to vitamin D Source: RGD
  • positive regulation of collagen biosynthetic process Source: RGD
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Names & Taxonomyi

Protein namesi
Recommended name:
Latent-transforming growth factor beta-binding protein 1
Short name:
LTBP-1
Alternative name(s):
Transforming growth factor beta-1-binding protein 1
Short name:
TGF-beta-1-BP-1
Transforming growth factor beta-1-masking protein large subunit
Gene namesi
Name:Ltbp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68379. Ltbp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • extracellular matrix Source: RGD
  • extracellular space Source: RGD
  • large latent transforming growth factor-beta complex Source: RGD
  • mitochondrion Source: RGD
  • neuronal cell body Source: RGD
  • perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 736716Sequence analysisPRO_0000007639Add
BLAST
Chaini737 – 1577841Latent-transforming growth factor beta-binding protein 1PRO_0000007640Add
BLAST
Propeptidei1578 – 1712135Sequence analysisPRO_0000007641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi185 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 201PROSITE-ProRule annotation
Disulfide bondi203 ↔ 212PROSITE-ProRule annotation
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi395 ↔ 405PROSITE-ProRule annotation
Disulfide bondi399 ↔ 411PROSITE-ProRule annotation
Disulfide bondi413 ↔ 422PROSITE-ProRule annotation
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence analysis
Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence analysis
Disulfide bondi622 ↔ 633PROSITE-ProRule annotation
Disulfide bondi628 ↔ 642PROSITE-ProRule annotation
Disulfide bondi644 ↔ 657PROSITE-ProRule annotation
Disulfide bondi869 ↔ 881PROSITE-ProRule annotation
Disulfide bondi876 ↔ 890PROSITE-ProRule annotation
Disulfide bondi892 ↔ 905PROSITE-ProRule annotation
Disulfide bondi911 ↔ 923PROSITE-ProRule annotation
Disulfide bondi918 ↔ 932PROSITE-ProRule annotation
Disulfide bondi934 ↔ 947PROSITE-ProRule annotation
Disulfide bondi953 ↔ 964PROSITE-ProRule annotation
Disulfide bondi959 ↔ 973PROSITE-ProRule annotation
Modified residuei966 – 9661(3R)-3-hydroxyasparagineBy similarity
Disulfide bondi976 ↔ 988PROSITE-ProRule annotation
Disulfide bondi994 ↔ 1005PROSITE-ProRule annotation
Disulfide bondi1000 ↔ 1014PROSITE-ProRule annotation
Disulfide bondi1017 ↔ 1028PROSITE-ProRule annotation
Disulfide bondi1034 ↔ 1045PROSITE-ProRule annotation
Disulfide bondi1040 ↔ 1054PROSITE-ProRule annotation
Glycosylationi1042 – 10421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1056 ↔ 1069PROSITE-ProRule annotation
Disulfide bondi1075 ↔ 1086PROSITE-ProRule annotation
Disulfide bondi1081 ↔ 1095PROSITE-ProRule annotation
Disulfide bondi1097 ↔ 1110PROSITE-ProRule annotation
Disulfide bondi1116 ↔ 1127PROSITE-ProRule annotation
Disulfide bondi1122 ↔ 1136PROSITE-ProRule annotation
Modified residuei1129 – 11291(3R)-3-hydroxyasparagineBy similarity
Disulfide bondi1138 ↔ 1151PROSITE-ProRule annotation
Disulfide bondi1157 ↔ 1169PROSITE-ProRule annotation
Disulfide bondi1164 ↔ 1178PROSITE-ProRule annotation
Disulfide bondi1180 ↔ 1192PROSITE-ProRule annotation
Disulfide bondi1198 ↔ 1210PROSITE-ProRule annotation
Disulfide bondi1204 ↔ 1219PROSITE-ProRule annotation
Disulfide bondi1221 ↔ 1234PROSITE-ProRule annotation
Disulfide bondi1240 ↔ 1252PROSITE-ProRule annotation
Glycosylationi1242 – 12421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1246 ↔ 1261PROSITE-ProRule annotation
Disulfide bondi1263 ↔ 1276PROSITE-ProRule annotation
Disulfide bondi1282 ↔ 1294PROSITE-ProRule annotation
Disulfide bondi1289 ↔ 1303PROSITE-ProRule annotation
Disulfide bondi1305 ↔ 1319PROSITE-ProRule annotation
Disulfide bondi1340 ↔ 1363PROSITE-ProRule annotation
Disulfide bondi1350 ↔ 1375PROSITE-ProRule annotation
Disulfide bondi1350 – 1350Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Glycosylationi1357 – 13571N-linked (GlcNAc...)By similarity
Disulfide bondi1364 ↔ 1380PROSITE-ProRule annotation
Disulfide bondi1365 ↔ 1392PROSITE-ProRule annotation
Disulfide bondi1375 – 1375Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Modified residuei1405 – 14051PhosphoserineBy similarity
Disulfide bondi1419 ↔ 1432PROSITE-ProRule annotation
Disulfide bondi1427 ↔ 1441PROSITE-ProRule annotation
Disulfide bondi1443 ↔ 1456PROSITE-ProRule annotation
Disulfide bondi1462 ↔ 1473PROSITE-ProRule annotation
Disulfide bondi1468 ↔ 1482PROSITE-ProRule annotation
Disulfide bondi1484 ↔ 1497PROSITE-ProRule annotation
Modified residuei1588 – 15881PhosphoserineBy similarity
Modified residuei1607 – 16071PhosphoserineBy similarity
Disulfide bondi1616 ↔ 1627PROSITE-ProRule annotation
Disulfide bondi1622 ↔ 1636PROSITE-ProRule annotation
Disulfide bondi1638 ↔ 1651PROSITE-ProRule annotation
Disulfide bondi1657 ↔ 1672PROSITE-ProRule annotation
Disulfide bondi1667 ↔ 1681PROSITE-ProRule annotation
Disulfide bondi1683 ↔ 1696PROSITE-ProRule annotation

Post-translational modificationi

Contains hydroxylated asparagine residues.By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
Two intrachain disulfide bonds from the TB3 domain are rearranged upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, anchoring it to the extracellular matrix.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei736 – 7372CleavageSequence analysis
Sitei1577 – 15782CleavageSequence analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiQ00918.
PRIDEiQ00918.

PTM databases

PhosphoSiteiQ00918.

Interactioni

Subunit structurei

The large latent complex of TGFB1 from platelets is composed of the TGFB1 molecule non-covalently associated with a disulfide-bonded complex of a dimer of the N-terminal propeptide of the TGFB1 precursor and LTBP1. LTBP1 does not bind directly to active TGFB1. Binds to FBN1 and FBN2. Interacts with ADAMTSL2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040099.

Structurei

3D structure databases

ProteinModelPortaliQ00918.
SMRiQ00918. Positions 1332-1403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 21333EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini391 – 42333EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini549 – 60153TB 1Add
BLAST
Domaini618 – 65841EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini669 – 72153TB 2Add
BLAST
Domaini865 – 90642EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini907 – 94842EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini949 – 98941EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini990 – 102940EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1030 – 107041EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1071 – 111141EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1112 – 115241EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1153 – 119341EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1194 – 123542EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1236 – 127742EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1278 – 132043EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1338 – 139255TB 3Add
BLAST
Domaini1415 – 145743EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1458 – 149841EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1515 – 156854TB 4Add
BLAST
Domaini1612 – 165241EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1653 – 169745EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 12429Pro-richAdd
BLAST

Domaini

Associates covalently with small latent TGF-beta complex via domain TB 3.By similarity

Sequence similaritiesi

Belongs to the LTBP family.Curated
Contains 18 EGF-like domains.PROSITE-ProRule annotation
Contains 4 TB (TGF-beta binding) domains.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410Z7XK. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ00918.
KOiK19559.
PhylomeDBiQ00918.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 13 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 18 hits.
SM00179. EGF_CA. 16 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 4 hits.
PROSITEiPS00010. ASX_HYDROXYL. 13 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 10 hits.
PS50026. EGF_3. 14 hits.
PS01187. EGF_CA. 15 hits.
PS51364. TB. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q00918-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAWLRWGL LLWAGLLAWS AHGRVRRITY VVRPGPGLPA GTLPLAGPPR
60 70 80 90 100
TFNVALDARY SRSSTATSSR SLAGPPAERT RRTSQPGGAA LPGLRSPLPP
110 120 130 140 150
EPARPGAPSR QLHSKAGAQT AVTRFAKHGR QVVRSKVQQD TQSSGGSRLQ
160 170 180 190 200
VQQKQQLQGI NVCGGQCCHG WSKAPGSQRC TKPSCVPPCQ NGGMCLRPQF
210 220 230 240 250
CVCKPGTKGK ACEITAAQDT MSPVFGGQNP GSSWVPPEPA AKRTSTKKAD
260 270 280 290 300
TLPRVSPVAQ MTLTLKPKPS MGLSQQIHSQ VAPLSSQNVM IRHGQTQEYV
310 320 330 340 350
LKPKYFPAPK VVSGEQSTEG SFSLRYGQEQ GTAPFQVSNH TGRIKVVFTP
360 370 380 390 400
SICKVTCTKG NCHNSCQKGN TTTLISENGH AADTLTATNF RVVICHLPCM
410 420 430 440 450
NGGQCSSRDK CQCPPNFTGK LCQIPVLGAS MPKLYQHAQQ PGKALGSHVI
460 470 480 490 500
HSTHTLPLTM TNQQGVKVKF PPNIVNIHVK HPPEASVQIH QVSRIDGPVG
510 520 530 540 550
QRVKEVQPGQ SQVSYQGLPV QKTQTVHSTY SHQQVIPHVY PVAAKTQLGR
560 570 580 590 600
CFQETIGSQC GKALPGLSKQ EDCCGTVGTS WGFNKCQKCP KKQSYHGYTQ
610 620 630 640 650
MMECLQGYKR VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCSCKMGFGP
660 670 680 690 700
DPTFSSCVPD PPMISEEKGP CYRLVSPGRQ CMHPLSVHLT KQICCCSVGK
710 720 730 740 750
AWGPQCEKCP LPGTAAFKEI CPGGMGYTVS GIHRRRPIHQ HIGKEAVFVK
760 770 780 790 800
PKNTQPVAKS THPPPLPAKE EPVEALTSSR EHGPGVAEPE VVTAPPEKEI
810 820 830 840 850
PSLDQEKTRL EPGQPQLSPG VSTIHLHPQF PVVVEKTSPP VPVEVAPEGS
860 870 880 890 900
TSSASQVIAP TQVTEINECT VNPDICGAGH CINLPVRYTC ICYEGYKFSE
910 920 930 940 950
QQRKCIDIDE CAQAQHLCSQ GRCENTEGSF LCICPAGFIA SEEGSNCIDV
960 970 980 990 1000
DECLRPDVCR DGRCINTAGA FRCEYCDSGY RMSRRGHCED IDECLTPSTC
1010 1020 1030 1040 1050
PEEQCVNSPG SYQCVPCTEG FRGWNGQCLD VDECLQPKVC TNGSCTNLEG
1060 1070 1080 1090 1100
SYMCSCHKGY SPTPDHRHCQ DIDECQQGNL CMNGQCKNTD GSFRCTCGQG
1110 1120 1130 1140 1150
YQLSAAKDQC EDIDECEHRH LCSHGQCRNT EGSFQCLCNQ GYRASVLGDH
1160 1170 1180 1190 1200
CEDINECLED SSVCQGGDCI NTAGSYDCTC PDGLQLNDNK GCQDINECAQ
1210 1220 1230 1240 1250
PGLCAPHGEC LNTQGSFHCV CEQGFSISAD GRTCEDIDEC VNNTVCDSHG
1260 1270 1280 1290 1300
FCDNTAGSFR CLCYQGFQAP QDGQGCVDVN ECELLSGVCG EAFCENVEGS
1310 1320 1330 1340 1350
FLCVCADENQ EYSPMTGQCR SRATEDSGVD RQPKEEKKEC YYNLNDASLC
1360 1370 1380 1390 1400
DNVLAPNVTK QECCCTSGAG WGDNCEIFPC PVQGTAEFSE MCPRGKGFVP
1410 1420 1430 1440 1450
AGESSYETGG ENYKDADECL LFGEEICKNG YCLNTQPGYE CYCKEGTYYD
1460 1470 1480 1490 1500
PVKLQCFDMD ECQDPNSCID GQCVNTEGSY NCFCTHPMVL DASEKRCVQP
1510 1520 1530 1540 1550
TESNEQIEET DVYQDLCWEH LSEEYVCSRP LVGKQTTYTE CCCLYGEAWG
1560 1570 1580 1590 1600
MQCALCPMKD SDDYAQLCNI PVTGRRRPYG RDALVDFSEQ YGPETDPYFI
1610 1620 1630 1640 1650
QDRFLNSFEE LQAEECGILN GCENGRCVRV QEGYTCDCFD GYHLDMAKMT
1660 1670 1680 1690 1700
CVDVNECSEL NNRMSLCKNA KCINTEGSYK CVCLPGYVPS DKPNYCTPLN
1710
TALNLDKDSD LE
Length:1,712
Mass (Da):186,599
Last modified:July 1, 1993 - v1
Checksum:i650BCEAA691FD134
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55431 mRNA. Translation: AAA42235.1.
PIRiA38261.
RefSeqiNP_067598.1. NM_021587.1.
UniGeneiRn.40942.

Genome annotation databases

GeneIDi59107.
KEGGirno:59107.
UCSCiRGD:68379. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55431 mRNA. Translation: AAA42235.1.
PIRiA38261.
RefSeqiNP_067598.1. NM_021587.1.
UniGeneiRn.40942.

3D structure databases

ProteinModelPortaliQ00918.
SMRiQ00918. Positions 1332-1403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000040099.

PTM databases

PhosphoSiteiQ00918.

Proteomic databases

PaxDbiQ00918.
PRIDEiQ00918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi59107.
KEGGirno:59107.
UCSCiRGD:68379. rat.

Organism-specific databases

CTDi4052.
RGDi68379. Ltbp1.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410Z7XK. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ00918.
KOiK19559.
PhylomeDBiQ00918.

Miscellaneous databases

NextBioi611739.
PROiQ00918.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 13 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 18 hits.
SM00179. EGF_CA. 16 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 4 hits.
PROSITEiPS00010. ASX_HYDROXYL. 13 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 10 hits.
PS50026. EGF_3. 14 hits.
PS01187. EGF_CA. 15 hits.
PS51364. TB. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the large subunit of transforming growth factor type beta masking protein and expression of the mRNA in various rat tissues."
    Tsuji T., Okada F., Yamaguchi K., Nakamura T.
    Proc. Natl. Acad. Sci. U.S.A. 87:8835-8839(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Dual role for the latent transforming growth factor-beta binding protein in storage of latent TGF-beta in the extracellular matrix and as a structural matrix protein."
    Dallas S.L., Miyazono K., Skerry T.M., Mundy G.R., Bonewald L.F.
    J. Cell Biol. 131:539-549(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Latent transforming growth factor-beta binding proteins (LTBPs) --structural extracellular matrix proteins for targeting TGF-beta action."
    Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.
    Cytokine Growth Factor Rev. 10:99-117(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "The latent transforming growth factor beta binding protein (LTBP) family."
    Oklu R., Hesketh R.
    Biochem. J. 352:601-610(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLTBP1_RAT
AccessioniPrimary (citable) accession number: Q00918
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.