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Protein

Aggrecan core protein

Gene

ACAN

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1958Calcium 1By similarity1
Metal bindingi1962Calcium 1By similarity1
Metal bindingi1962Calcium 3By similarity1
Metal bindingi1982Calcium 2By similarity1
Metal bindingi1984Calcium 2By similarity1
Metal bindingi1985Calcium 1By similarity1
Metal bindingi1991Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi1991Calcium 2By similarity1
Metal bindingi1992Calcium 1By similarity1
Metal bindingi1992Calcium 3By similarity1
Metal bindingi2005Calcium 2By similarity1
Metal bindingi2006Calcium 2By similarity1
Metal bindingi2006Calcium 2; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandCalcium, Lectin, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aggrecan core protein
Alternative name(s):
Cartilage-specific proteoglycan core protein
Short name:
CSPCP
Gene namesi
Name:ACAN
Synonyms:AGC1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in ACAN are the cause of nanomelia, a lethal connective tissue disorder affecting cartilage development (chondrodystrophy) characterized by shortened and malformed limbs. Aggrecan is truncated at its C-terminus in the CS-2 binding domain and is not anymore secreted from the chondrocytes.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Sequence analysisAdd BLAST16
ChainiPRO_000001750417 – 2109Aggrecan core proteinAdd BLAST2093

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 129By similarity
Glycosylationi76N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi122N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi171 ↔ 242By similarity
Disulfide bondi195 ↔ 216By similarity
Disulfide bondi269 ↔ 345By similarity
Disulfide bondi293 ↔ 314By similarity
Glycosylationi330N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi388N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi439N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi542 ↔ 613By similarity
Disulfide bondi566 ↔ 587By similarity
Disulfide bondi640 ↔ 715By similarity
Glycosylationi644N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi664 ↔ 685By similarity
Glycosylationi700N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi728O-linked (Xyl...) (keratan sulfate) threonine1 Publication1
Glycosylationi765N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi801N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1006O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1010O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1016O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1020O-linked (Xyl...) (chondroitin sulfate) serineCurated1
Glycosylationi1249O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1253O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1259O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1263O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1269O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Glycosylationi1273O-linked (Xyl...) (chondroitin sulfate) serineCurated1
Disulfide bondi1859 ↔ 1870By similarity
Disulfide bondi1864 ↔ 1879By similarity
Disulfide bondi1881 ↔ 1890By similarity
Disulfide bondi1897 ↔ 1908By similarity
Disulfide bondi1925 ↔ 2017By similarity
Disulfide bondi1993 ↔ 2009By similarity
Disulfide bondi2024 ↔ 2067By similarity
Disulfide bondi2053 ↔ 2080By similarity

Post-translational modificationi

Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1001Not glycosylated1

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan

Proteomic databases

PaxDbiP07898

PTM databases

iPTMnetiP07898

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000037775

Structurei

3D structure databases

ProteinModelPortaliP07898
SMRiP07898
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 143Ig-like V-typeAdd BLAST110
Domaini149 – 244Link 1PROSITE-ProRule annotationAdd BLAST96
Domaini250 – 347Link 2PROSITE-ProRule annotationAdd BLAST98
Domaini520 – 615Link 3PROSITE-ProRule annotationAdd BLAST96
Domaini621 – 717Link 4PROSITE-ProRule annotationAdd BLAST97
Repeati1363 – 13821Add BLAST20
Repeati1383 – 14022Add BLAST20
Repeati1403 – 14223Add BLAST20
Repeati1423 – 14424Add BLAST20
Repeati1443 – 14625Add BLAST20
Repeati1463 – 14826Add BLAST20
Repeati1483 – 15027Add BLAST20
Repeati1503 – 15228Add BLAST20
Repeati1523 – 15429Add BLAST20
Repeati1543 – 156210Add BLAST20
Repeati1563 – 158211Add BLAST20
Repeati1583 – 160212Add BLAST20
Repeati1603 – 162213Add BLAST20
Repeati1623 – 164214Add BLAST20
Repeati1643 – 166215Add BLAST20
Repeati1663 – 168216Add BLAST20
Repeati1683 – 170217Add BLAST20
Repeati1703 – 172218Add BLAST20
Repeati1723 – 174219Add BLAST20
Domaini1855 – 1892EGF-likePROSITE-ProRule annotationAdd BLAST38
Domaini1901 – 2019C-type lectinPROSITE-ProRule annotationAdd BLAST119
Domaini2022 – 2082SushiPROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 137G1-AAdd BLAST90
Regioni148 – 243G1-BAdd BLAST96
Regioni249 – 346G1-B'Add BLAST98
Regioni519 – 613G2-BAdd BLAST95
Regioni620 – 715G2-B'Add BLAST96
Regioni718 – 803KSAdd BLAST86
Regioni805 – 1264CS-1Add BLAST460
Regioni1265 – 1742CS-2Add BLAST478
Regioni1363 – 174219 X 20 AA tandem repeats of E-[TA]-S-T-[ADHIFSRVT]-[YQLRH]-E-[IVTAG]-[SR]-[GS]-E-[SAT]-[SP]-[AG]-[FYL]-P-[EA]-[TIV]-[SRTG]-[IVT]Add BLAST380
Regioni1893 – 2109G3Add BLAST217

Domaini

Two globular domains, G1 and G2, comprise the N-terminus of the proteoglycan, while another globular region, G3, makes up the C-terminus. G1 contains Link domains and thus consists of three disulfide-bonded loop structures designated as the A, B, B' motifs. G2 is similar to G1. The keratan sulfate (KS) and the chondroitin sulfate (CS) attachment domains lie between G2 and G3.

Sequence similaritiesi

Keywords - Domaini

EGF-like domain, Immunoglobulin domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiENOG410IJP2 Eukaryota
ENOG410XRES LUCA
HOGENOMiHOG000168421
HOVERGENiHBG007982
InParanoidiP07898
PhylomeDBiP07898

Family and domain databases

CDDicd00033 CCP, 1 hit
cd03588 CLECT_CSPGs, 1 hit
Gene3Di2.60.40.10, 1 hit
3.10.100.10, 5 hits
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR018378 C-type_lectin_CS
IPR033987 CSPG_CTLD
IPR016187 CTDL_fold
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
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR013106 Ig_V-set
IPR000538 Link_dom
IPR035976 Sushi/SCR/CCP_sf
IPR000436 Sushi_SCR_CCP_dom
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00059 Lectin_C, 1 hit
PF00084 Sushi, 1 hit
PF07686 V-set, 1 hit
PF00193 Xlink, 4 hits
PRINTSiPR01265 LINKMODULE
SMARTiView protein in SMART
SM00032 CCP, 1 hit
SM00034 CLECT, 1 hit
SM00181 EGF, 1 hit
SM00179 EGF_CA, 1 hit
SM00409 IG, 1 hit
SM00445 LINK, 4 hits
SUPFAMiSSF48726 SSF48726, 1 hit
SSF56436 SSF56436, 5 hits
SSF57535 SSF57535, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS00615 C_TYPE_LECTIN_1, 1 hit
PS50041 C_TYPE_LECTIN_2, 1 hit
PS00022 EGF_1, 1 hit
PS50026 EGF_3, 1 hit
PS01187 EGF_CA, 1 hit
PS50835 IG_LIKE, 1 hit
PS01241 LINK_1, 4 hits
PS50963 LINK_2, 4 hits
PS50923 SUSHI, 1 hit

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P07898-1) [UniParc]FASTAAdd to basket

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
MTTLLLVFVC LQAITTAASA ELSDSSDGLE VKIPEQSPLR VVLGSSLNIP
60 70 80 90 100
CYFNIPEEED TNALLTPRIK WSKLSNGTEI VLLVATGGKI RLNAEYREVI
110 120 130 140 150
SLPNYPAIPT DATLEIKALR SNHTGIYRCE VMYGIEDRQD TIEVLVKGVV
160 170 180 190 200
FHYRAISTRY TLNFERAKQA CIQNSAVIAT PEQLQAAYED GYEQCDAGWL
210 220 230 240 250
ADQTVRYPIH LPRERCYGDK DEFPGVRTYG VRETDETYDV YCYAEQMQGK
260 270 280 290 300
VFYATSPEKF TFQEAFDKCH SLGARLATTG ELYLAWKDGM DMCSAGWLAD
310 320 330 340 350
RSVRYPISRA RPNCGGNLVG VRTVYLNPAN QTGYPHPSSR YDAICYSGDD
360 370 380 390 400
FEALVPGLFT DEVGTELGSA FTIQTVTQTE VELPLPRNVT EEEARGSIAT
410 420 430 440 450
LEPMEITATA TELYEAFTVL PDLFATSVTV ETASPREENV TREEITGIWA
460 470 480 490 500
VPEEVTTSVS GTAFTTGMAE VSSVEEAIAV TATPGLESAS PFTIEDHLVQ
510 520 530 540 550
VTAAPDVALL PRQPISPTGV VFHYRAATSR YAFSFIQAQQ ACLENNAVIA
560 570 580 590 600
TPEQLQAAYE AGFDQCDAGW LRDQTVRYPI VNPRSNCVGD KESSPGVRSY
610 620 630 640 650
GMRPASETYD VYCYIDRLKG EVFFATQPEQ FTFQEAQLYC ESQNATLASA
660 670 680 690 700
GQLHAAWKQG LDRCYPGWLA DGSLRYPIVS PRPACGGDAP GVRTIYQHHN
710 720 730 740 750
QTGFPDPLSR HHAFCFRALP SVVEEGVTSL FEEEVMVTQL IPGVEGIPSG
760 770 780 790 800
EETTVETELS SEPENQTAQG TEVFPTDVSL LSARPSAFPP ATVIPEETST
810 820 830 840 850
NASIPEVSGE FPESGEHPTS GEPSASGAPD TSGEPTSVGF ELSGEQSGIG
860 870 880 890 900
ESGLPSVDLQ SSGFVPGESG LPSGDVSGLP SGIVDISGLP SAEEEVTVSV
910 920 930 940 950
SRIPEVSGMP SGAESSGLHS GFSGEISGTE LISGLPSGEE SGLASGFPTI
960 970 980 990 1000
SLVDSTLVEV VTAAPGRQEE GKGSIGVSGE EELSGFPSAE WDSSGARGLP
1010 1020 1030 1040 1050
SGAETSGEQS GVPELSGEHS GVPGLSGEAF EVPELSGEHS GVTELSGEHS
1060 1070 1080 1090 1100
GLPELSGEPF GVPELSGFPS GLDISGEPSG APEVSGPVDV SGLTSGVDGS
1110 1120 1130 1140 1150
GEVSGVTFIS TSLQEVTTPS VAEAEAKEIL EISGLPSGET SGMVSGSLDV
1160 1170 1180 1190 1200
SGQPSGHIGF GGSASGVLEM SGFPGGAVES SGEASGVEVT SGLASGEESG
1210 1220 1230 1240 1250
LTSGFPTVSL VDTTLVEVVT QTSVAQEVGE GPSGMIEISG FLSGDRGVSG
1260 1270 1280 1290 1300
EGSGAVQSSG LPSGTGDFSG EPSGIPYFSG DISGATDLSG QPSAVTDISG
1310 1320 1330 1340 1350
EDSGLPEVTL VTSDLVEVVT RPTVSQELGG ETAVTFPYVF GPSGEGSASG
1360 1370 1380 1390 1400
DLSGGASAEG GIETSTAYEI SGESSAFPET SIETSTDQEI SGEASAYPEI
1410 1420 1430 1440 1450
SVETSTHLET SGETSAYPEI STETSTIQEV SGETSAFPEI STETSTIQEI
1460 1470 1480 1490 1500
SGETSAFPEI RIETSTFQEI SGETSAFPEI RIETSTSQEA RGETSAFPEI
1510 1520 1530 1540 1550
TIEASTVHET SGETSAFPEI SIETSTVHET SGETSAFPEI SIETSTVHEI
1560 1570 1580 1590 1600
SGESSAFPEI RIETSTSQEA RGETSAFPEI TIEASTIQEI SGETSAFPEI
1610 1620 1630 1640 1650
SIETSTVREI SGETSAFPEI RIETSTSQEA RGETSALPEI TIETSTVHET
1660 1670 1680 1690 1700
SGEASAFPEI SIETSTRQEA RSEASAYPEV SIEASTTQEV SGESSAFPEI
1710 1720 1730 1740 1750
SVETSTSQEA RGETSAFPEI GIETSTAHEG SGETPGLPAV STDTAATSLA
1760 1770 1780 1790 1800
SGEPSGAPEK ETPDTTSHLI TGVSGETSVP DAVISTSAPD VELAQEPRNT
1810 1820 1830 1840 1850
EETQLEIEPS TPAASGQETE TAAVLDNPHL PATATAALHP ASQEAVDALG
1860 1870 1880 1890 1900
PTTEDTDECH SSPCLNGATC VDGIDSFKCL CLPSYGGDLC EIDLANCEEG
1910 1920 1930 1940 1950
WIKFQGHCYR HFEERETWMD AESRCREHQA HLSSIITPEE QEFVNSHAQD
1960 1970 1980 1990 2000
YQWIGLSDRA VENDFRWSDG HSLQFENWRP NQPDNFFFAG EDCVVMIWHE
2010 2020 2030 2040 2050
QGEWNDVPCN YHLPFTCKKG TVACGDPPVV ENARTFGRKK DRYEINSLVR
2060 2070 2080 2090 2100
YQCDHGYIQR HVPTIRCQPN GHWEEPRISC TNPSSYQRRL YKRSPRSRLR

PGVVHRPTH
Length:2,109
Mass (Da):223,493
Last modified:November 1, 1997 - v2
Checksum:i7F824FD5B3A2ABDA
GO
Isoform 2 (identifier: P07898-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1856-1892: Missing.

Show »
Length:2,072
Mass (Da):219,644
Checksum:i51B75DB9329CBFFF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti362E → D (PubMed:1339285).Curated1
Sequence conflicti601G → D (PubMed:1339285).Curated1
Sequence conflicti1000P → R in M88101 (PubMed:1339285).Curated1
Sequence conflicti1029A → P in M88101 (PubMed:1339285).Curated1
Sequence conflicti1042 – 1043VT → PA in AAA48731 (PubMed:1694853).Curated2
Sequence conflicti1251E → D (PubMed:1339285).Curated1
Sequence conflicti1251E → D (PubMed:2365711).Curated1
Sequence conflicti1587I → T in AAC60751 (PubMed:7827752).Curated1
Sequence conflicti1590I → V in AAC60751 (PubMed:7827752).Curated1
Sequence conflicti1594T → S in AAC60751 (PubMed:7827752).Curated1
Sequence conflicti1602 – 1610IETSTVREI → VLCRCSVLR in AAC60751 (PubMed:7827752).Curated9
Sequence conflicti1603E → A in M88101 (PubMed:1339285).Curated1
Sequence conflicti1672S → G in M88101 (PubMed:1339285).Curated1
Sequence conflicti1796E → G (PubMed:1339285).Curated1
Sequence conflicti1796E → G in AAA48720 (PubMed:3460082).Curated1
Sequence conflicti1988F → S in AAA48719 (PubMed:3170613).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0030731856 – 1892Missing in isoform 2. 2 PublicationsAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21913 mRNA Translation: AAB19128.1
M88101 mRNA No translation available.
M38187 mRNA Translation: AAA48731.1
S74657, S74656 Genomic DNA Translation: AAC60751.1
M13993 mRNA Translation: AAA48720.1
J04028 Genomic DNA Translation: AAA48719.1
PIRiI50421
UniGeneiGga.3977

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21913 mRNA Translation: AAB19128.1
M88101 mRNA No translation available.
M38187 mRNA Translation: AAA48731.1
S74657, S74656 Genomic DNA Translation: AAC60751.1
M13993 mRNA Translation: AAA48720.1
J04028 Genomic DNA Translation: AAA48719.1
PIRiI50421
UniGeneiGga.3977

3D structure databases

ProteinModelPortaliP07898
SMRiP07898
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000037775

PTM databases

iPTMnetiP07898

Proteomic databases

PaxDbiP07898

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IJP2 Eukaryota
ENOG410XRES LUCA
HOGENOMiHOG000168421
HOVERGENiHBG007982
InParanoidiP07898
PhylomeDBiP07898

Family and domain databases

CDDicd00033 CCP, 1 hit
cd03588 CLECT_CSPGs, 1 hit
Gene3Di2.60.40.10, 1 hit
3.10.100.10, 5 hits
InterProiView protein in InterPro
IPR001304 C-type_lectin-like
IPR016186 C-type_lectin-like/link_sf
IPR018378 C-type_lectin_CS
IPR033987 CSPG_CTLD
IPR016187 CTDL_fold
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
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR013106 Ig_V-set
IPR000538 Link_dom
IPR035976 Sushi/SCR/CCP_sf
IPR000436 Sushi_SCR_CCP_dom
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00059 Lectin_C, 1 hit
PF00084 Sushi, 1 hit
PF07686 V-set, 1 hit
PF00193 Xlink, 4 hits
PRINTSiPR01265 LINKMODULE
SMARTiView protein in SMART
SM00032 CCP, 1 hit
SM00034 CLECT, 1 hit
SM00181 EGF, 1 hit
SM00179 EGF_CA, 1 hit
SM00409 IG, 1 hit
SM00445 LINK, 4 hits
SUPFAMiSSF48726 SSF48726, 1 hit
SSF56436 SSF56436, 5 hits
SSF57535 SSF57535, 1 hit
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 1 hit
PS00615 C_TYPE_LECTIN_1, 1 hit
PS50041 C_TYPE_LECTIN_2, 1 hit
PS00022 EGF_1, 1 hit
PS50026 EGF_3, 1 hit
PS01187 EGF_CA, 1 hit
PS50835 IG_LIKE, 1 hit
PS01241 LINK_1, 4 hits
PS50963 LINK_2, 4 hits
PS50923 SUSHI, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPGCA_CHICK
AccessioniPrimary (citable) accession number: P07898
Secondary accession number(s): Q90810
, Q90820, Q90991, Q91047
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: June 20, 2018
This is version 156 of the entry and version 2 of the sequence. See 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
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