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Protein

Cation-independent mannose-6-phosphate receptor

Gene

IGF2R

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a positive regulator of T-cell coactivation, by binding DPP4 (By similarity). Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2.By similarity

GO - Molecular functioni

  • glycoprotein binding Source: UniProtKB
  • insulin-like growth factor binding Source: AgBase
  • kringle domain binding Source: AgBase
  • mannose binding Source: AgBase
  • phosphoprotein binding Source: UniProtKB
  • transporter activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Cation-independent mannose-6-phosphate receptor
Short name:
CI Man-6-P receptor
Short name:
CI-MPR
Short name:
M6PR
Alternative name(s):
300 kDa mannose 6-phosphate receptor
Short name:
MPR 300
Insulin-like growth factor 2 receptor
Insulin-like growth factor II receptor
Short name:
IGF-II receptor
CD_antigen: CD222
Gene namesi
Name:IGF2R
Synonyms:M6P
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini45 – 2313LumenalSequence analysisAdd BLAST2269
Transmembranei2314 – 2336HelicalSequence analysisAdd BLAST23
Topological domaini2337 – 2499CytoplasmicSequence analysisAdd BLAST163

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • endocytic vesicle Source: UniProtKB
  • Golgi apparatus Source: AgBase
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB-SubCell
  • plasma membrane Source: AgBase
  • trans-Golgi network Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi723Y → F: No noticeable change in Man-6-P and Man-P-GlcNAc recognition. 1 Publication1
Mutagenesisi723Y → L: Severely impairs both Man-6-P and Man-P-GlcNAc recognition. 1 Publication1
Mutagenesisi2360 – 2362YKY → AKV: Loss of interaction between HA-II adapters and these tails, but does not affect the interaction between them and HA-I. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 44Sequence analysisAdd BLAST44
ChainiPRO_000001922845 – 2499Cation-independent mannose-6-phosphate receptorAdd BLAST2455

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi57 ↔ 77
Disulfide bondi85 ↔ 92
Glycosylationi120N-linked (GlcNAc...)1 Publication1
Disulfide bondi125 ↔ 155
Disulfide bondi140 ↔ 167
Disulfide bondi180 ↔ 218
Disulfide bondi234 ↔ 241
Disulfide bondi281 ↔ 312
Disulfide bondi294 ↔ 324
Disulfide bondi334 ↔ 375
Disulfide bondi383 ↔ 391
Glycosylationi409N-linked (GlcNAc...)1 Publication1
Disulfide bondi429 ↔ 463
Disulfide bondi443 ↔ 475
Glycosylationi444N-linked (GlcNAc...)Sequence analysis1
Glycosylationi552N-linked (GlcNAc...)Sequence analysis1
Glycosylationi590N-linked (GlcNAc...)Sequence analysis1
Glycosylationi635N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi636 ↔ 672
Disulfide bondi680 ↔ 687
Disulfide bondi739 ↔ 768
Glycosylationi755N-linked (GlcNAc...)Sequence analysis1
Glycosylationi879N-linked (GlcNAc...)Sequence analysis1
Glycosylationi959N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1030N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1173N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1255N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1321N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1525 ↔ 1562PROSITE-ProRule annotation
Disulfide bondi1568 ↔ 1575PROSITE-ProRule annotation
Disulfide bondi1607 ↔ 1643PROSITE-ProRule annotation
Disulfide bondi1623 ↔ 1655PROSITE-ProRule annotation
Disulfide bondi1661 ↔ 1704PROSITE-ProRule annotation
Glycosylationi1665N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1715 ↔ 1722PROSITE-ProRule annotation
Disulfide bondi1759 ↔ 1792PROSITE-ProRule annotation
Glycosylationi1766N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1775 ↔ 1804PROSITE-ProRule annotation
Disulfide bondi1813 ↔ 1848PROSITE-ProRule annotation
Glycosylationi1825N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1859 ↔ 1865PROSITE-ProRule annotation
Disulfide bondi1902 ↔ 1984PROSITE-ProRule annotation
Disulfide bondi1912 ↔ 1936PROSITE-ProRule annotation
Disulfide bondi1926 ↔ 1951PROSITE-ProRule annotation
Disulfide bondi1966 ↔ 1996PROSITE-ProRule annotation
Disulfide bondi2003 ↔ 2038PROSITE-ProRule annotation
Disulfide bondi2048 ↔ 2055PROSITE-ProRule annotation
Disulfide bondi2091 ↔ 2122PROSITE-ProRule annotation
Glycosylationi2094N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2105 ↔ 2134PROSITE-ProRule annotation
Glycosylationi2145N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2220N-linked (GlcNAc...)Sequence analysis1
Modified residuei2361N6-acetyllysineBy similarity1
Modified residuei2421PhosphoserineBy similarity1
Modified residuei2438Omega-N-methylarginineBy similarity1
Modified residuei2492PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP08169.
PRIDEiP08169.

Interactioni

Subunit structurei

Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3 (By similarity). Binds HA-I and HA-II plasma membrane adapters.By similarity1 Publication

GO - Molecular functioni

  • insulin-like growth factor binding Source: AgBase
  • kringle domain binding Source: AgBase
  • phosphoprotein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi159160. 5 interactors.
STRINGi9913.ENSBTAP00000037502.

Structurei

Secondary structure

12499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi51 – 53Combined sources3
Helixi54 – 56Combined sources3
Beta strandi61 – 65Combined sources5
Helixi66 – 68Combined sources3
Beta strandi70 – 74Combined sources5
Turni83 – 85Combined sources3
Beta strandi89 – 95Combined sources7
Turni96 – 99Combined sources4
Beta strandi100 – 106Combined sources7
Helixi107 – 109Combined sources3
Beta strandi110 – 113Combined sources4
Beta strandi116 – 124Combined sources9
Beta strandi131 – 140Combined sources10
Beta strandi147 – 152Combined sources6
Beta strandi154 – 163Combined sources10
Helixi164 – 166Combined sources3
Beta strandi167 – 169Combined sources3
Helixi170 – 172Combined sources3
Beta strandi175 – 177Combined sources3
Beta strandi181 – 183Combined sources3
Beta strandi189 – 191Combined sources3
Helixi193 – 195Combined sources3
Beta strandi198 – 200Combined sources3
Beta strandi212 – 215Combined sources4
Beta strandi217 – 219Combined sources3
Helixi231 – 233Combined sources3
Beta strandi239 – 243Combined sources5
Beta strandi248 – 254Combined sources7
Beta strandi259 – 262Combined sources4
Beta strandi265 – 271Combined sources7
Helixi279 – 281Combined sources3
Beta strandi287 – 293Combined sources7
Beta strandi305 – 319Combined sources15
Helixi321 – 323Combined sources3
Helixi326 – 328Combined sources3
Beta strandi330 – 336Combined sources7
Helixi338 – 341Combined sources4
Helixi348 – 350Combined sources3
Beta strandi359 – 364Combined sources6
Beta strandi366 – 372Combined sources7
Helixi381 – 383Combined sources3
Beta strandi389 – 394Combined sources6
Helixi395 – 397Combined sources3
Beta strandi401 – 403Combined sources3
Beta strandi409 – 415Combined sources7
Beta strandi418 – 423Combined sources6
Beta strandi432 – 434Combined sources3
Beta strandi436 – 443Combined sources8
Turni448 – 452Combined sources5
Beta strandi456 – 461Combined sources6
Beta strandi464 – 471Combined sources8
Helixi472 – 474Combined sources3
Beta strandi630 – 632Combined sources3
Beta strandi635 – 640Combined sources6
Turni641 – 644Combined sources4
Beta strandi645 – 648Combined sources4
Helixi650 – 652Combined sources3
Beta strandi658 – 661Combined sources4
Beta strandi663 – 669Combined sources7
Beta strandi671 – 673Combined sources3
Beta strandi684 – 693Combined sources10
Beta strandi696 – 701Combined sources6
Beta strandi706 – 709Combined sources4
Beta strandi712 – 718Combined sources7
Beta strandi732 – 738Combined sources7
Beta strandi748 – 750Combined sources3
Beta strandi755 – 763Combined sources9
Helixi765 – 767Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q25X-ray1.80A45-476[»]
1SYOX-ray2.20A/B45-476[»]
1SZ0X-ray2.10A/B45-476[»]
2KVANMR-A628-769[»]
2KVBNMR-A628-769[»]
ProteinModelPortaliP08169.
SMRiP08169.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08169.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati45 – 1701Add BLAST126
Repeati171 – 3272Add BLAST157
Repeati328 – 4783Add BLAST151
Repeati479 – 6294Add BLAST151
Repeati630 – 7715Add BLAST142
Repeati772 – 9336Add BLAST162
Repeati934 – 10897Add BLAST156
Repeati1090 – 12298Add BLAST140
Repeati1230 – 13739Add BLAST144
Repeati1374 – 151810Add BLAST145
Repeati1519 – 165811Add BLAST140
Repeati1659 – 180712Add BLAST149
Repeati1808 – 199913Add BLAST192
Domaini1907 – 1953Fibronectin type-IIPROSITE-ProRule annotationAdd BLAST47
Repeati2000 – 213714Add BLAST138
Repeati2138 – 229015Add BLAST153

Domaini

Sequence similaritiesi

Belongs to the MRL1/IGF2R family.Curated
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4504. Eukaryota.
ENOG410ZWHP. LUCA.
HOGENOMiHOG000113638.
HOVERGENiHBG000334.
InParanoidiP08169.
KOiK06564.

Family and domain databases

CDDicd00062. FN2. 1 hit.
Gene3Di2.10.10.10. 1 hit.
2.70.130.10. 16 hits.
InterProiIPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]
PfamiPF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view]
SMARTiSM01404. CIMR. 14 hits.
SM00059. FN2. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 16 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAAAGRSSH LGPAPAGRPP RCPLLLQLQL LLLLLLLPPG WVPGAAGTQG
60 70 80 90 100
AEFPELCSYT WEAVDTKNNM LYKINICGNM GVAQCGPSSA VCMHDLKTDS
110 120 130 140 150
FHSVGDSLLK TASRSLLEFN TTVNCKQQNH KIQSSITFLC GKTLGTPEFV
160 170 180 190 200
TATDCVHYFE WRTTAACKKN IFKANKEVPC YAFDRELKKH DLNPLIKTSG
210 220 230 240 250
AYLVDDSDPD TSLFINVCRD IEVLRASSPQ VRVCPTGAAA CLVRGDRAFD
260 270 280 290 300
VGRPQEGLKL VSNDRLVLSY VKEGAGQPDF CDGHSPAVTI TFVCPSERRE
310 320 330 340 350
GTIPKLTAKS NCRFEIEWVT EYACHRDYLE SRSCSLSSAQ HDVAVDLQPL
360 370 380 390 400
SRVEASDSLF YTSEADEYTY YLSICGGSQA PICNKKDAAV CQVKKADSTQ
410 420 430 440 450
VKVAGRPQNL TLRYSDGDLT LIYFGGEECS SGFQRMSVIN FECNQTAGNN
460 470 480 490 500
GRGAPVFTGE VDCTYFFTWD TKYACVHEKE ALLCGVSDGK QRFDLSALAR
510 520 530 540 550
HSELEQNWEA VDGSQREAEK KHFFINICHR VLQTGQARGC PEDAAVCAVD
560 570 580 590 600
KNGSKNLGRF ISSPTREKGN IQLSYSDGDE CGGGQKIITN ITLMCKPGDL
610 620 630 640 650
ESAPVLTTSR ADGCFYEFEW RTAAACVLSR TEGDNCTVFD SQAGFSFDLT
660 670 680 690 700
PLTKKDAYKV ETDKYEFHIN VCGPVSVGAC PPDSGACQVS RSDRKSWNLG
710 720 730 740 750
RSNAKLSYYD GMIQLTYRDG TPYNNEKRTP RATLITFLCD RDAGVGFPEY
760 770 780 790 800
QEEDNSTYNF RWYTSYACPE EPLECIVTDP VTLDQYDLSR LAKSEGGPGG
810 820 830 840 850
NWYSLDNGGA RSTWRKYYIN VCRPLNPVPG CDRYASACQM KYQGEQGSYS
860 870 880 890 900
ETVSISNLGV AKTGPMVEDS GSLLLEYVNG SACTTSDQRR TTYTTRIHLV
910 920 930 940 950
CSTGSLYTHP IFSLNWECVV SFLWNTAAAC PIRITTDIDQ VCSIKDPNSG
960 970 980 990 1000
YVFDLNPLNN SRGYVVLGIG KTFLFNVCGD MPACGTLDGK PASGCEAEVQ
1010 1020 1030 1040 1050
MDDMKTLKPG RLVGLEKSLQ LSTEGFITLN YTGLPSHPNG RADAFIIRFV
1060 1070 1080 1090 1100
CNDDVYPGTP KFLHQDIDSS LGIRDTFFEF ETALACVPSP VDCQVTDPAG
1110 1120 1130 1140 1150
NEYDLSGLSK ARKPWTAVDT FDEGKKRTFY LSVCTPLPYI PGCHGTAVGC
1160 1170 1180 1190 1200
CLVTEDSKLN LGVVQISPQV GANGSLSLVY VNGDKCKNQR FSTRINLECA
1210 1220 1230 1240 1250
HTTGSPTFQL QNDCEYVFLW RTVEACPVVR AEGDYCEVRD PRHGNLYNLI
1260 1270 1280 1290 1300
PLGLNDTVVR AGEYTYYFRV CGELTSGVCP TSDKSKVISS CQEKRGPQGF
1310 1320 1330 1340 1350
QKVAGLFNQK LTYENGVLKM NYTGGDTCHK VYQRSTTIFF YCDRSTQAPV
1360 1370 1380 1390 1400
FLQETSDCSY LFEWRTQYAC PPYDLTECSF KNEAGETYDL SSLSRYSDNW
1410 1420 1430 1440 1450
EAVTGTGSTE HYLINVCKSL SPQAGSDPCP PEAAVCLLGG PKPVNLGRVR
1460 1470 1480 1490 1500
DSPQWSQGLT LLKYVDGDLC PDQIRKKSTT IRFTCSESHV NSRPMFISAV
1510 1520 1530 1540 1550
EDCEYTFSWP TAAACAVKSN VHDDCQVTNP ATGHLFDLSS LSGRAGFTAA
1560 1570 1580 1590 1600
YSEKGLVYLS VCGDNENCAN GVGACFGQTR ISVGKASKRL TYVDQVLQLV
1610 1620 1630 1640 1650
YEGGSPCPSK TGLSYKSVIS FVCRPEVGPT NRPMLISLDK RTCTLFFSWH
1660 1670 1680 1690 1700
TPLACEQTTE CSVRNGSSLI DLSPLIHRTG GYEAYDESED DGSDTSPDFY
1710 1720 1730 1740 1750
INICQPLNPM HGLACPAGTA VCKVPVDGPP IDIGRVAGPP ILNPIANEVY
1760 1770 1780 1790 1800
LNFESSTPCL ADRHFNYTSL ITFHCKRGVS MGTPKLLRTS VCDFVFEWET
1810 1820 1830 1840 1850
PLVCPDEVKT DGCSLTDEQL YYSFNLSSLS KSTFKVTRGP HTYSVGVCTA
1860 1870 1880 1890 1900
AAGLDEGGCK DGAVCLLSGS KGASFGRLAS MKLDYRHQDE AVILSYANGD
1910 1920 1930 1940 1950
TCPPETEDGE PCVFPFVFNG KSYEECVVES RARLWCATTA NYDRDHEWGF
1960 1970 1980 1990 2000
CKHSTSHRTS VIIFKCDEDA DVGRPQVFSE VRGCEVTFEW KTKVVCPPKK
2010 2020 2030 2040 2050
MECKFVQKHR TYDLRLLSSL TGSWSFVHNG ASYYINLCQK IYKGPQDCSE
2060 2070 2080 2090 2100
RASVCKKSTS GEVQVLGLVH TQKLDVVDDR VIVTYSKGHY CGDNKTASAV
2110 2120 2130 2140 2150
IELTCAKTVG RPSFTRFDVD SCTYHFSWDS RAACAVKPQE VQMVNGTITN
2160 2170 2180 2190 2200
PANGRSFSLG DIYFKRFSAS GDVRTNGDRY IYEIQLSSIT GSSSPACSGA
2210 2220 2230 2240 2250
SICQRKANDQ HFSRKVGTSN QTRYYVQDGD LDVVFTSSSK CGKDKTKSVS
2260 2270 2280 2290 2300
STIFFHCDPL VKDGIPEFSH ETADCQYLFS WHTSAVCPLG AGFDEEIAGD
2310 2320 2330 2340 2350
DAQEHKGLSE RSQAVGAVLS LLLVALTACL LTLLLYKKER REMVMSRLTN
2360 2370 2380 2390 2400
CCRRSANVSY KYSKVNKEEE ADENETEWLM EEIQPPAPRP GKEGQENGHV
2410 2420 2430 2440 2450
AAKSVRAADT LSALHGDEQD SEDEVLTLPE VKVRPPGRAP GAEGGPPLRP
2460 2470 2480 2490
LPRKAPPPLR ADDRVGLVRG EPARRGRPRA AATPISTFHD DSDEDLLHV
Length:2,499
Mass (Da):274,529
Last modified:October 1, 1989 - v2
Checksum:i3C1C9DEF2875159D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03527 mRNA. Translation: AAA30455.1.
AF342811 mRNA. Translation: AAL23908.1.
PIRiA25908. A30788.
RefSeqiNP_776777.1. NM_174352.2.
UniGeneiBt.4977.

Genome annotation databases

GeneIDi281849.
KEGGibta:281849.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03527 mRNA. Translation: AAA30455.1.
AF342811 mRNA. Translation: AAL23908.1.
PIRiA25908. A30788.
RefSeqiNP_776777.1. NM_174352.2.
UniGeneiBt.4977.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q25X-ray1.80A45-476[»]
1SYOX-ray2.20A/B45-476[»]
1SZ0X-ray2.10A/B45-476[»]
2KVANMR-A628-769[»]
2KVBNMR-A628-769[»]
ProteinModelPortaliP08169.
SMRiP08169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159160. 5 interactors.
STRINGi9913.ENSBTAP00000037502.

Proteomic databases

PaxDbiP08169.
PRIDEiP08169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281849.
KEGGibta:281849.

Organism-specific databases

CTDi3482.

Phylogenomic databases

eggNOGiKOG4504. Eukaryota.
ENOG410ZWHP. LUCA.
HOGENOMiHOG000113638.
HOVERGENiHBG000334.
InParanoidiP08169.
KOiK06564.

Miscellaneous databases

EvolutionaryTraceiP08169.

Family and domain databases

CDDicd00062. FN2. 1 hit.
Gene3Di2.10.10.10. 1 hit.
2.70.130.10. 16 hits.
InterProiIPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]
PfamiPF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view]
SMARTiSM01404. CIMR. 14 hits.
SM00059. FN2. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 16 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMPRI_BOVIN
AccessioniPrimary (citable) accession number: P08169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.