Collagen alpha-1(I) chain precursor - Gallus gallus (Chicken)

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P02457 (CO1A1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Collagen alpha-1(I) chain

Alternative name(s):
Alpha-1 type I collagen

Gene names

Name:

COL1A1

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	1453 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Type I collagen is a member of group I collagen (fibrillar forming collagen).
Subunit structure	Trimers of one alpha 2(I) and two alpha 1(I) chains.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
Domain	The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.
Post-translational modification	Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are 4-hydroxylated in some or all of the chains. Pro-1153 is the only 3-hydroxyproline and the only hydroxylated proline in position X. Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. O-linked glycans consist of Glc-Gal disaccharide bound to the hydroxyl group of 5-hydroxylysine.
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	collagen Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	extracellular matrix structural constituent Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Propeptide

23 – 151

129

N-terminal propeptide

PRO_0000005716

Chain

152 – 1205

1054

Collagen alpha-1(I) chain

PRO_0000005717

Propeptide

1206 – 1453

248

C-terminal propeptide

PRO_0000005718

Regions

Domain

31 – 89

VWFC

Domain

1218 – 1453

236

Fibrillar collagen NC1

Sites

Metal binding

1266

Calcium By similarity

Metal binding

1268

Calcium By similarity

Metal binding

1269

Calcium; via carbonyl oxygen By similarity

Metal binding

1271

Calcium; via carbonyl oxygen By similarity

Metal binding

1274

Calcium By similarity

Site

1022

Not glycosylated

Site

1085

Not glycosylated

Amino acid modifications

Modified residue

152

Pyrrolidone carboxylic acid

Modified residue

160

Allysine By similarity

Modified residue

179

4-hydroxyproline Ref.3

Modified residue

182

4-hydroxyproline Ref.3

Modified residue

185

4-hydroxyproline Ref.3

Modified residue

194

4-hydroxyproline Ref.3

Modified residue

197

4-hydroxyproline Ref.3

Modified residue

200

4-hydroxyproline Ref.3

Modified residue

215

4-hydroxyproline Ref.4

Modified residue

230

4-hydroxyproline Ref.4

Modified residue

236

4-hydroxyproline Ref.4

Modified residue

245

4-hydroxyproline Ref.4

Modified residue

251

4-hydroxyproline Ref.4

Modified residue

254

5-hydroxylysine Ref.4

Modified residue

269

4-hydroxyproline Ref.4

Modified residue

278

4-hydroxyproline Ref.4

Modified residue

281

4-hydroxyproline Ref.4

Modified residue

287

4-hydroxyproline Ref.4

Modified residue

296

4-hydroxyproline Ref.5

Modified residue

302

4-hydroxyproline Ref.5

Modified residue

317

4-hydroxyproline Ref.5

Modified residue

323

4-hydroxyproline Ref.5

Modified residue

332

4-hydroxyproline Ref.5

Modified residue

335

4-hydroxyproline Ref.5

Modified residue

362

4-hydroxyproline Ref.5

Modified residue

365

4-hydroxyproline Ref.5

Modified residue

377

4-hydroxyproline Ref.5

Modified residue

383

4-hydroxyproline Ref.5

Modified residue

392

4-hydroxyproline Ref.5

Modified residue

398

4-hydroxyproline Ref.5

Modified residue

401

4-hydroxyproline Ref.5

Modified residue

416

4-hydroxyproline Ref.5

Modified residue

419

5-hydroxylysine Ref.5

Modified residue

425

4-hydroxyproline Ref.5

Modified residue

428

4-hydroxyproline Ref.5

Modified residue

440

4-hydroxyproline Ref.5

Modified residue

449

4-hydroxyproline Ref.5

Modified residue

464

4-hydroxyproline Ref.5

Modified residue

470

4-hydroxyproline Ref.5

Modified residue

479

4-hydroxyproline Ref.5

Modified residue

485

4-hydroxyproline Ref.5

Modified residue

494

5-hydroxylysine Ref.5

Modified residue

497

4-hydroxyproline Ref.5

Modified residue

503

4-hydroxyproline Ref.5

Modified residue

512

4-hydroxyproline Ref.5

Modified residue

518

4-hydroxyproline Ref.5

Modified residue

524

4-hydroxyproline Ref.5

Modified residue

533

4-hydroxyproline Ref.5

Modified residue

536

4-hydroxyproline Ref.5

Modified residue

545

4-hydroxyproline Ref.5

Modified residue

554

4-hydroxyproline Ref.5

Modified residue

560

4-hydroxyproline Ref.5

Modified residue

572

4-hydroxyproline Ref.6

Modified residue

581

4-hydroxyproline Ref.6

Modified residue

584

4-hydroxyproline Ref.6

Modified residue

590

4-hydroxyproline Ref.6

Modified residue

593

4-hydroxyproline Ref.6

Modified residue

611

4-hydroxyproline Ref.6

Modified residue

629

4-hydroxyproline Ref.6

Modified residue

635

4-hydroxyproline Ref.6

Modified residue

641

4-hydroxyproline Ref.6

Modified residue

647

4-hydroxyproline Ref.6

Modified residue

653

4-hydroxyproline Ref.6

Modified residue

659

4-hydroxyproline Ref.6

Modified residue

671

4-hydroxyproline Ref.6

Modified residue

680

4-hydroxyproline Ref.6

Modified residue

692

4-hydroxyproline Ref.6

Modified residue

704

4-hydroxyproline Ref.6

Modified residue

707

4-hydroxyproline Ref.6

Modified residue

713

4-hydroxyproline Ref.6

Modified residue

719

4-hydroxyproline Ref.7

Modified residue

728

4-hydroxyproline Ref.7

Modified residue

737

4-hydroxyproline Ref.7

Modified residue

740

5-hydroxylysine Ref.7

Modified residue

746

4-hydroxyproline Ref.7

Modified residue

761

4-hydroxyproline Ref.7

Modified residue

767

4-hydroxyproline Ref.7

Modified residue

776

4-hydroxyproline Ref.7

Modified residue

788

4-hydroxyproline Ref.7

Modified residue

794

4-hydroxyproline Ref.7

Modified residue

797

4-hydroxyproline Ref.7

Modified residue

806

4-hydroxyproline Ref.7

Modified residue

812

4-hydroxyproline Ref.7

Modified residue

830

4-hydroxyproline Ref.7

Modified residue

839

4-hydroxyproline Ref.7

Modified residue

848

4-hydroxyproline Ref.7

Modified residue

851

5-hydroxylysine Ref.7

Modified residue

860

4-hydroxyproline Ref.7

Modified residue

866

4-hydroxyproline Ref.7

Modified residue

875

4-hydroxyproline Ref.7

Modified residue

884

4-hydroxyproline Ref.7

Modified residue

887

4-hydroxyproline Ref.7

Modified residue

908

4-hydroxyproline Ref.7

Modified residue

911

4-hydroxyproline Ref.7

Modified residue

917

4-hydroxyproline Ref.7

Modified residue

920

4-hydroxyproline Ref.7

Modified residue

926

4-hydroxyproline Ref.7

Modified residue

935

4-hydroxyproline Ref.7

Modified residue

953

4-hydroxyproline Ref.7

Modified residue

962

4-hydroxyproline Ref.7

Modified residue

965

4-hydroxyproline Ref.7

Modified residue

971

4-hydroxyproline Ref.7

Modified residue

986

4-hydroxyproline Ref.7

Modified residue

992

4-hydroxyproline Ref.8

Modified residue

998

4-hydroxyproline Ref.8

Modified residue

1007

4-hydroxyproline Ref.8

Modified residue

1013

4-hydroxyproline Ref.8

Modified residue

1022

5-hydroxylysine; partial Ref.8

Modified residue

1034

4-hydroxyproline Ref.8

Modified residue

1037

4-hydroxyproline Ref.8

Modified residue

1040

4-hydroxyproline Ref.8

Modified residue

1067

4-hydroxyproline Ref.8

Modified residue

1085

5-hydroxylysine; partial Ref.8

Modified residue

1097

5-hydroxylysine Ref.9

Modified residue

1109

4-hydroxyproline Ref.9

Modified residue

1112

4-hydroxyproline Ref.9

Modified residue

1115

4-hydroxyproline Ref.9

Modified residue

1133

4-hydroxyproline Ref.9

Modified residue

1148

4-hydroxyproline Ref.9

Modified residue

1153

3-hydroxyproline Ref.9

Modified residue

1154

4-hydroxyproline Ref.9

Modified residue

1169

4-hydroxyproline Ref.9

Modified residue

1172

4-hydroxyproline Ref.9

Modified residue

1175

4-hydroxyproline Ref.9

Modified residue

1178

4-hydroxyproline Ref.9

Glycosylation

254

O-linked (Gal...); partial Ref.4

Glycosylation

1097

O-linked (Gal...); partial Ref.9

Glycosylation

1354

N-linked (GlcNAc...) By similarity

Disulfide bond

1248 ↔ 1280

By similarity

Disulfide bond

1254

Interchain (with C-1271) By similarity

Disulfide bond

1271

Interchain (with C-1254) By similarity

Disulfide bond

1288 ↔ 1451

By similarity

Disulfide bond

1359 ↔ 1404

By similarity

Experimental info

Sequence conflict

1441

Q → H in AAA48671. Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P02457 [UniParc].

Last modified July 10, 2007. Version 3.
Checksum: 61C617239E271A82
Show »

FASTA

1,453

137,755

        10         20         30         40         50         60 
MFSFVDSRLL LLIAATVLLT RGEGEEDIQT GSCVQDGLTY NDKDVWKPEP CQICVCDSGN 

        70         80         90        100        110        120 
ILCDEVICED TSDCPNAEIP FGECCPICPD VDASPVYPES AGVEGPKGDT GPRGDRGLPG 

       130        140        150        160        170        180 
PPGRDGIPGQ PGLPGPPGPP GPPGLGGNFA PQMSYGYDEK SAGVAVPGPM GPAGPRGLPG 

       190        200        210        220        230        240 
PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PAGPPGKNGD DGEAGKPGRP GQRGPPGPQG 

       250        260        270        280        290        300 
ARGLPGTAGL PGMKGHRGFS GLDGAKGQPG PAGPKGEPGS PGENGAPGQM GPRGLPGERG 

       310        320        330        340        350        360 
RPGPSGPAGA RGNDGAPGAA GPPGPTGPAG PPGFPGAAGA KGETGPQGAR GSEGPQGSRG 

       370        380        390        400        410        420 
EPGPPGPAGA AGPAGNPGAD GQPGAKGATG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG 

       430        440        450        460        470        480 
NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPAGLP GPAGERGAPG 

       490        500        510        520        530        540 
SRGFPGADGI AGPKGPPGER GSPGAVGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG 

       550        560        570        580        590        600 
KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGAAGE PGKPGERGAP GPPGAVGAAG 

       610        620        630        640        650        660 
KDGEAGAQGP PGPTGPAGER GEQGPAGAPG FQGLPGPAGP PGEAGKPGEQ GVPGNAGAPG 

       670        680        690        700        710        720 
PAGARGERGF PGERGVQGPP GPQGPRGANG APGNDGAKGD AGAPGAPGNE GPPGLEGMPG 

       730        740        750        760        770        780 
ERGAAGLPGA KGDRGDPGPK GADGAPGKDG LRGLTGPIGP PGPAGAPGDK GEAGPPGPAG 

       790        800        810        820        830        840 
PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGETGD AGAKGDAGPP GPAGPTGAPG 

       850        860        870        880        890        900 
PAGZVGAPGP KGARGSAGPP GATGFPGAAG RVGPPGPSGN IGLPGPPGPA GKZGSKGPRG 

       910        920        930        940        950        960 
ETGPAGRPGE PGPAGPPGPP GEKGSPGADG PIGAPGTPGP QGIAGQRGVV GLPGQRGERG 

       970        980        990       1000       1010       1020 
FPGLPGPSGE PGKQGPSGAS GERGPPGPMG PPGLAGPPGE AGREGAPGAE GAPGRDGAAG 

      1030       1040       1050       1060       1070       1080 
PKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPPGPA GARGPAGPQG 

      1090       1100       1110       1120       1130       1140 
PRGDKGETGE QGDRGMKGHR GFSGLQGPPG PPGAPGEQGP SGASGPAGPR GPPGSAGAAG 

      1150       1160       1170       1180       1190       1200 
KDGLNGLPGP IGPPGPRGRT GEVGPVGPPG PPGPPGPPGP PSGGFDLSFL PQPPQEKAHD 

      1210       1220       1230       1240       1250       1260 
GGRYYRADDA NVMRDRDLEV DTTLKSLSQQ IENIRSPEGT RKNPARTCRD LKMCHGDWKS 

      1270       1280       1290       1300       1310       1320 
GEYWIDPNQG CNLDAIKVYC NMETGETCVY PTQATIAQKN WYLSKNPKEK KHVWFGETMS 

      1330       1340       1350       1360       1370       1380 
DGFQFEYGGE GSNPADVAIQ LTFLRLMSTE ATQNVTYHCK NSVAYMDHDT GNLKKALLLQ 

      1390       1400       1410       1420       1430       1440 
GANEIEIRAE GNSRFTYGVT EDGCTSHTGA WGKTVIEYKT TKTSRLPIID LAPMDVGAPD 

      1450 
QEFGIDIGPV CFL

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References

[1]	"Construction and characterization of cDNA clones encoding the 5' end of the chicken pro alpha 1(I) collagen mRNA." Finer M.H., Boedtker H., Doty P. Gene 56:71-78(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
[2]	"Unusual DNA sequences located within the promoter region and the first intron of the chicken pro-alpha 1(I) collagen gene." Finer M.H., Aho S., Gerstenfeld L.C., Boedtker H., Doty P. J. Biol. Chem. 262:13323-13332(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-144.
[3]	"Amino acid sequence of cyanogen bromide peptides from the amino-terminal region of chick skicollagen." Kang A.H., Gross J. Biochemistry 9:796-804(1970) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 152-206, HYDROXYLATION AT PRO-179; PRO-182; PRO-185; PRO-194; PRO-197 AND PRO-200.
[4]	"The covalent structure of collagen. Amino acid sequence of alpha1-CB5 glycopeptide and alpha1-CB4 from chick skin collagen." Kang A.H., Dixit S.N., Corbett C., Gross J. J. Biol. Chem. 250:7428-7434(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 207-290, HYDROXYLATION AT PRO-215; PRO-230; PRO-236; PRO-245; PRO-251; LYS-254; PRO-269; PRO-278; PRO-281 AND PRO-287, GLYCOSYLATION AT LYS-254.
[5]	"Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the complete primary structure of the helical portion of the chick skin collagen alpha 1(I) chain." Highberger J.H., Corbett C., Dixit S.N., Yu W., Seyer J.M., Kang A.H., Gross J. Biochemistry 21:2048-2055(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 291-569, HYDROXYLATION AT PRO-296; PRO-302; PRO-317; PRO-323; PRO-332; PRO-335; PRO-362; PRO-365; PRO-377; PRO-383; PRO-392; PRO-398; PRO-401; PRO-416; LYS-419; PRO-425; PRO-428; PRO-440; PRO-449; PRO-464; PRO-470; PRO-479; PRO-485; LYS-494; PRO-497; PRO-503; PRO-512; PRO-518; PRO-524; PRO-533; PRO-536; PRO-545; PRO-554 AND PRO-560.
[6]	"Covalent structure of collagen: amino acid sequence of alpha1-CB3 of chick skin collagen." Dixit S.N., Kang A.H., Gross J. Biochemistry 14:1929-1933(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 570-718, HYDROXYLATION AT PRO-572; PRO-581; PRO-584; PRO-590; PRO-593; PRO-611; PRO-629; PRO-635; PRO-641; PRO-647; PRO-653; PRO-659; PRO-671; PRO-680; PRO-692; PRO-704; PRO-707 AND PRO-713.
[7]	"The amino acid sequence of chick skin collagen alpha1-CB7." Highberger J.H., Corbett C., Kang A.H., Gross J. Biochemistry 14:2872-2881(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 719-989, HYDROXYLATION AT PRO-719; PRO-728; PRO-737; LYS-740; PRO-746; PRO-761; PRO-767; PRO-776; PRO-788; PRO-794; PRO-797; PRO-806; PRO-812; PRO-830; PRO-839; PRO-848; LYS-851; PRO-860; PRO-866; PRO-875; PRO-884; PRO-887; PRO-908; PRO-911; PRO-917; PRO-920; PRO-926; PRO-935; PRO-953; PRO-962; PRO-965; PRO-971 AND PRO-986.
[8]	"Covalent structure of collagen: amino acid sequence of alpha1-CB6A of chick skin collagen." Dixit S.N., Seyer J.M., Oronsky A.O., Corbett C., Kang A.H., Gross J. Biochemistry 14:1933-1938(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 990-1096, HYDROXYLATION AT PRO-992; PRO-998; PRO-1007; PRO-1013; LYS-1022; PRO-1034; PRO-1037; PRO-1040; PRO-1067 AND LYS-1085, ABSENCE OF GLYCOSYLATION AT LYS-1022 AND LYS-1085.
[9]	"Covalent structure of collagen: amino acid sequence of chick skin collagen alpha1(1)-CB6B." Dixit S.N., Seyer J.M., Kang A.H., Gross J. Biochemistry 17:5719-5722(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1097-1187, HYDROXYLATION AT LYS-1097; PRO-1109; PRO-1112; PRO-1115; PRO-1133; PRO-1148; PRO-1153; PRO-1154; PRO-1169; PRO-1172; PRO-1175 AND PRO-1178, GLYCOSYLATION AT LYS-1097.
[10]	"Evidence for a previously undetected sequence at the carboxyterminus of the alpha 1 chain of chicken bone collagen." Eyre D.R., Glimcher M.J. Biochem. Biophys. Res. Commun. 48:720-726(1972) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1200-1205.
[11]	"Sequence determination and analysis of the 3' region of chicken pro-alpha 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids including the carboxy-terminal propeptide sequences." Fuller F., Boedtker H. Biochemistry 20:996-1006(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 981-1453.
[12]	"Nucleotide sequence of a collagen cDNA-fragment coding for the carboxyl end of pro alpha 1(I)-chains." Showalter A.M., Pesciotta D.M., Eikenberry E.F., Yamamoto T., Pastan I., Decrombrugghe B., Fietzek P.P., Olsen B.R. FEBS Lett. 111:61-65(1980) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1453.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M17839, M17838 Genomic DNA. Translation: AAA48704.1. V00401 mRNA. Translation: CAA23695.1. M10571 mRNA. Translation: AAA48671.1. Sequence problems. M17607 mRNA. Translation: AAA48672.1.
IPI	IPI00572548.
PIR	A27179. CGCH1S. A90458. I50629. S07234.
UniGene	Gga.2073. Gga.43371.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P02457. 1 interaction.
Proteomic databases
PRIDE	P02457.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG004933.
Family and domain databases
InterPro	IPR008160. Collagen. IPR000885. Fib_collagen_C. IPR001007. VWF_C. [Graphical view]
Pfam	PF01410. COLFI. 1 hit. PF01391. Collagen. 12 hits. PF00093. VWC. 1 hit. [Graphical view]
ProDom	PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00038. COLFI. 1 hit. SM00214. VWC. 1 hit. [Graphical view]
PROSITE	PS51461. NC1_FIB. 1 hit. PS01208. VWFC_1. 1 hit. PS50184. VWFC_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CO1A1_CHICK

Accession

Primary (citable) accession number: P02457

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 10, 2007
Last modified:	April 3, 2013
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents