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P01026

- CO3_RAT

UniProt

P01026 - CO3_RAT

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Protein

Complement C3

Gene

C3

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

Functioni

C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.1 Publication
Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. In chronic inflammation, acts as a chemoattractant for neutrophils (PubMed:8352775).1 Publication
C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.1 Publication
Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2 By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei747 – 7482Cleavage; by carboxypeptidasesBy similarity
Sitei748 – 7492Cleavage; by C3 convertase
Sitei959 – 9602Cleavage; by factor ISequence Analysis
Sitei1303 – 13042Cleavage; by factor IBy similarity
Sitei1320 – 13212Cleavage; by factor IBy similarity

GO - Molecular functioni

  1. C5L2 anaphylatoxin chemotactic receptor binding Source: UniProtKB
  2. cofactor binding Source: RGD
  3. endopeptidase inhibitor activity Source: InterPro
  4. lipid binding Source: RGD

GO - Biological processi

  1. blood coagulation Source: RGD
  2. chemotaxis Source: UniProtKB-KW
  3. complement activation Source: RGD
  4. complement activation, alternative pathway Source: UniProtKB-KW
  5. complement activation, classical pathway Source: RGD
  6. fatty acid metabolic process Source: UniProtKB-KW
  7. inflammatory response Source: UniProtKB-KW
  8. positive regulation of developmental growth Source: RGD
  9. positive regulation of ERK1 and ERK2 cascade Source: RGD
  10. positive regulation of glucose transport Source: UniProtKB
  11. positive regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  12. positive regulation of lipid storage Source: UniProtKB
  13. positive regulation of protein phosphorylation Source: UniProtKB
  14. regulation of triglyceride biosynthetic process Source: UniProtKB
  15. response to estradiol Source: RGD
  16. response to estrogen Source: RGD
  17. response to glucocorticoid Source: RGD
  18. response to magnesium ion Source: RGD
  19. response to progesterone Source: RGD
  20. tolerance induction Source: RGD
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Complement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism

Protein family/group databases

MEROPSiI39.950.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C3
Cleaved into the following 12 chains:
Gene namesi
Name:C3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2232. C3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 16631639Complement C3PRO_0000005937Add
BLAST
Chaini25 – 666642Complement C3 beta chainPRO_0000005938Add
BLAST
Chaini568 – 66699C3-beta-cPRO_0000395292Add
BLAST
Chaini671 – 1663993Complement C3 alpha chainPRO_0000005939Add
BLAST
Chaini671 – 74878C3a anaphylatoxinPRO_0000005940Add
BLAST
Chaini671 – 74777Acylation stimulating proteinBy similarityPRO_0000419937Add
BLAST
Chaini749 – 1663915Complement C3b alpha' chainPRO_0000005941Add
BLAST
Chaini749 – 959211Complement C3c alpha' chain fragment 1PRO_0000273950Add
BLAST
Chaini960 – 1303344Complement C3dg fragmentBy similarityPRO_0000273951Add
BLAST
Chaini960 – 100142Complement C3g fragmentBy similarityPRO_0000273952Add
BLAST
Chaini1002 – 1303302Complement C3d fragmentBy similarityPRO_0000273953Add
BLAST
Peptidei1304 – 132017Complement C3f fragmentBy similarityPRO_0000273954Add
BLAST
Chaini1321 – 1663343Complement C3c alpha' chain fragment 2By similarityPRO_0000273955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi558 ↔ 816Interchain (between beta and alpha chains)PROSITE-ProRule annotation
Disulfide bondi626 ↔ 661By similarity
Disulfide bondi693 ↔ 720By similarity
Disulfide bondi694 ↔ 727By similarity
Disulfide bondi707 ↔ 728By similarity
Disulfide bondi873 ↔ 1513By similarity
Glycosylationi939 – 9391N-linked (GlcNAc...)Curated
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Disulfide bondi1101 ↔ 1158By similarity
Disulfide bondi1358 ↔ 1489By similarity
Disulfide bondi1389 ↔ 1458By similarity
Disulfide bondi1506 ↔ 1511By similarity
Disulfide bondi1518 ↔ 1590By similarity
Disulfide bondi1537 ↔ 1661By similarity
Glycosylationi1617 – 16171N-linked (GlcNAc...)Curated

Post-translational modificationi

C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons By similarity.By similarity
Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

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

Proteomic databases

PRIDEiP01026.

PTM databases

PhosphoSiteiP01026.

Expressioni

Gene expression databases

GenevestigatoriP01026.

Interactioni

Subunit structurei

C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). Interacts with VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77 By similarity.By similarity

Protein-protein interaction databases

BioGridi246419. 1 interaction.

Structurei

Secondary structure

1
1663
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1013 – 103119
Helixi1034 – 10374
Helixi1039 – 10413
Helixi1042 – 105716
Helixi1076 – 108914
Turni1090 – 10923
Helixi1097 – 111115
Helixi1127 – 11348
Helixi1139 – 115820
Turni1159 – 11613
Helixi1165 – 118016
Helixi1186 – 119813
Helixi1206 – 12138
Turni1216 – 12183
Helixi1226 – 124217
Turni1246 – 12483
Helixi1249 – 125810
Helixi1269 – 128517

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QQFX-ray1.45A1010-1286[»]
1QSJX-ray1.90A/B/C/D1010-1286[»]
ProteinModelPortaliP01026.
SMRiP01026. Positions 25-663, 672-1663.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01026.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini693 – 72836Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1518 – 1661144NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1424 – 145633Properdin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005110.
InParanoidiP01026.
KOiK03990.
PhylomeDBiP01026.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P01026-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGPTSGSQLL VLLLLLASSL LALGSPMYSI ITPNVLRLES EETFILEAHD
60 70 80 90 100
AQGDVPVTVT VQDFLKKQVL TSEKTVLTGA TGHLNRVFIK IPASKEFNAD
110 120 130 140 150
KGHKYVTVVA NFGATVVEKA VLVSFQSGYL FIQTDKTIYT PGSTVFYRIF
160 170 180 190 200
TVDNNLLPVG KTVVIVIETP DGVPIKRDIL SSHNQYGILP LSWNIPELVN
210 220 230 240 250
MGQWKIRAFY EHAPKQTFSA EFEVKEYVLP SFEVLVEPTE KFYYIHGPKG
260 270 280 290 300
LEVSITARFL YGKNVDGTAF VIFGVQDEDK KISLALSLTR VLIEDGSGEA
310 320 330 340 350
VLSRKVLMDG VRPSSPEALV GKSLYVSVTV ILHSGSDMVE AERSGIPIVT
360 370 380 390 400
SPYQIHFTKT PKFFKPAMPF DLMVFVTNPD GSPARRVPVV TQGSDAQALT
410 420 430 440 450
QDDGVAKLSV NTPNNRQPLT ITVSTKKEGI PDARQATRTM QAQPYSTMHN
460 470 480 490 500
SNNYLHLSVS RVELKPGDNL NVNFHLRTDA GQEAKIRYYT YLVMNKGKLL
510 520 530 540 550
KAGRQVREPG QDLVVLSLPI TPEFIPSFRL VAYYTLIGAN GQREVVADSV
560 570 580 590 600
WVDVKDSCVG TLVVKGDPRD NRQPAPGHQT TLRIEGNQGA RVGLVAVDKG
610 620 630 640 650
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLTFKTNQG
660 670 680 690 700
LQTDQREDPE CAKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD
710 720 730 740 750
IPMPYSCQRR ARLITQGESC LKAFMDCCNY ITKLREQHRR DHVLGLARSD
760 770 780 790 800
VDEDIIPEED IISRSHFPES WLWTIEELKE PEKNGISTKV MNIFLKDSIT
810 820 830 840 850
TWEILAVSLS DKKGICVADP YEITVMQDFF IDLRLPYSVV RNEQVEIRAV
860 870 880 890 900
LFNYREQEKL KVRVELLHNP AFCSMATAKK RYYQTIEIPP KSSVAVPYVI
910 920 930 940 950
VPLKIGLQEV EVKAAVFNHF ISDGVKKILK VVPEGMRVNK TVAVRTLDPE
960 970 980 990 1000
HLNQGGVQRE DVNAADLSDQ VPDTDSETRI LLQGTPVAQM AEDAVDGERL
1010 1020 1030 1040 1050
KHLIVTPSGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGLE KRQEALELIK
1060 1070 1080 1090 1100
KGYTQQLAFK QPISAYAAFN NRPPSTWLTA MWSRSFSLAA NLIAIDSQVL
1110 1120 1130 1140 1150
CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNTKEAD VSLTAFVLIA
1160 1170 1180 1190 1200
LQEARDICEG QVNSLPGSIN KAGEYLEASY LNLQRPYTVA IAGYALALMN
1210 1220 1230 1240 1250
KLEEPYLTKF LNTAKDRNRW EEPGQQLYNV EATSYALLAL LLLKDFDSVP
1260 1270 1280 1290 1300
PVVRWLNDER YYGGGYGSTQ ATFMVFQALA QYRADVPDHK DLNMDVSLHL
1310 1320 1330 1340 1350
PSRSSPTVFR LLWESGSLLR SEETKQNEGF SLTAKGKGQG TLSVVTVYHA
1360 1370 1380 1390 1400
KVKGKTTCKK FDLRVTIKPA PETAKKPQDA KSSMILDICT RYLGDVDATM
1410 1420 1430 1440 1450
SILDISMMTG FIPDTNDLEL LSSGVDRYIS KYEMDKAFSN KNTLIIYLEK
1460 1470 1480 1490 1500
ISHSEEDCLS FKVHQFFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
1510 1520 1530 1540 1550
MLSKLCHNEM CRCAEENCFM HQSQDQVSLN ERLDKACEPG VDYVYKTKLT
1560 1570 1580 1590 1600
TIELSDDFDE YIMTIEQVIK SGSDEVQAGQ ERRFISHVKC RNALKLQKGK
1610 1620 1630 1640 1650
QYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEERQDQ KNQKQCEDLG
1660
AFTETMVVFG CPN
Length:1,663
Mass (Da):186,460
Last modified:August 1, 1990 - v3
Checksum:i2F87CCB143CDD4BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti704 – 7041P → K in AAG00532. 1 PublicationCurated
Sequence conflicti721 – 7222LK → KL AA sequence (PubMed:309768)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52477 mRNA. Translation: CAA36716.1.
AF286158 mRNA. Translation: AAG00532.1.
M29866 mRNA. Translation: AAA40837.1.
PIRiS15764. C3RT.
RefSeqiNP_058690.2. NM_016994.2.
UniGeneiRn.11378.

Genome annotation databases

GeneIDi24232.
KEGGirno:24232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52477 mRNA. Translation: CAA36716.1 .
AF286158 mRNA. Translation: AAG00532.1 .
M29866 mRNA. Translation: AAA40837.1 .
PIRi S15764. C3RT.
RefSeqi NP_058690.2. NM_016994.2.
UniGenei Rn.11378.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QQF X-ray 1.45 A 1010-1286 [» ]
1QSJ X-ray 1.90 A/B/C/D 1010-1286 [» ]
ProteinModelPortali P01026.
SMRi P01026. Positions 25-663, 672-1663.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246419. 1 interaction.

Protein family/group databases

MEROPSi I39.950.

PTM databases

PhosphoSitei P01026.

Proteomic databases

PRIDEi P01026.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24232.
KEGGi rno:24232.

Organism-specific databases

CTDi 718.
RGDi 2232. C3.

Phylogenomic databases

HOVERGENi HBG005110.
InParanoidi P01026.
KOi K03990.
PhylomeDBi P01026.

Miscellaneous databases

EvolutionaryTracei P01026.
NextBioi 602683.

Gene expression databases

Genevestigatori P01026.

Family and domain databases

Gene3Di 1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProi IPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view ]
Pfami PF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view ]
PRINTSi PR00004. ANAPHYLATOXN.
SMARTi SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view ]
SUPFAMi SSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide and deduced amino acid sequence of rat complement C3."
    Misumi Y., Sohda M., Ikehara Y.
    Nucleic Acids Res. 18:2178-2178(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. "Complement component C3-derived neutrophil chemotactic factors purified from exudate of rat carrageenin-induced inflammation."
    Nakagawa H., Komorita N.
    Biochem. Biophys. Res. Commun. 194:1181-1187(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 568-592 AND 671-687, IDENTIFICATION OF C3A ANAPHYLATOXIN AND C3-BETA-C, FUNCTION.
    Tissue: Neutrophil.
  3. "Purification, characterization, and amino acid sequence of rat anaphylatoxin (C3a)."
    Jacobs J.W., Rubin J.S., Hugli T.E., Bogardt R.A. Jr., Mariz I.K., Daniels J.S., Daughaday W.H., Bradshaw R.A.
    Biochemistry 17:5031-5038(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 671-748.
  4. "Nucleotide and deduced amino acid sequence of rat complement component C3a derived from Sprague-Dawley strain."
    Wahrmann M., Krieger S., Liewehr A.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 671-748.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "Structure at 1.44 A resolution of an N-terminally truncated form of the rat serum complement C3d fragment."
    Zanotti G., Bassetto A., Battistutta R., Folli C., Arcidiaco P., Stoppini M., Berni R.
    Biochim. Biophys. Acta 1478:232-238(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 960-969, X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 1010-1286.
  6. "Estrogen regulation of tissue-specific expression of complement C3."
    Sundstrom S.A., Komm B.S., Ponce-De-Leon H., Yi Z., Teuscher C., Lyttle C.R.
    J. Biol. Chem. 264:16941-16947(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1316-1595.

Entry informationi

Entry nameiCO3_RAT
AccessioniPrimary (citable) accession number: P01026
Secondary accession number(s): Q9ET19, Q9QV57, Q9QV58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1990
Last modified: October 29, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3