CREB-binding protein - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P45481 (CBP_MOUSE)

Last modified February 9, 2010. Version 110. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
CREB-binding protein
EC=2.3.1.48

Gene names

Name:	Crebbp
Synonyms:	Cbp

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	2441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Acetylates histones, giving a specific tag for transcriptional activation. Also acetylates non-histone proteins, like NCOA3 coactivator. Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes By similarity. Ref.5 Ref.8
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and IKBKG. Probably part of a complex with HIF1A and EP300. Interacts with phosphorylated CREB1. Interacts with the C-terminal region of CITED4. The TAZ-type 1 domain interacts with HIF1A. Interacts with SRCAP, CARM1, ELF3, MLLT7/FOXO4, N4BP2, NCOA1, NCOA3, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB, TRERF1 and ZCCHC12. Interacts with KLF1; the interaction results in acetylation and enhancement of transcriptional activity of KLF1 By similarity. Interacts with DAXX; the interaction is dependent on CBP sumoylation and results in suppression of the transcriptional activity via recruitment of HDAC2 to DAAX. Interacts with MAF. Interacts with MTDH By similarity. Interacts with MAFG; the interaction acetylates MAFG in the basic region and stimulates NFE2 transcriptional activity through increasing its DNA-binding activity. Interacts with IRF2; the interaction acetylates IRF2 and regulates its activity on the H4 promoter. Interacts (via N-terminus) with SS18L1/CREST (via C-terminus) By similarity. Interacts with MECOM By similarity. Ref.5 Ref.8 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.9
Subcellular location	Nucleus. Note: Recruited to nuclear bodies by SS18L1/CREST By similarity.
Post-translational modification	Methylation of the KIX domain by CARM1 blocks association with CREB. This results in the blockade of CREB signaling, and in activation of apoptotic response. Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Sumoylation negatively regulates transcriptional activity via the recruitment of DAAX.
Sequence similarities	Contains 1 bromo domain. Contains 1 KIX domain. Contains 2 TAZ-type zinc fingers. Contains 1 ZZ-type zinc finger.

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Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Bromodomain Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Transferase
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	N-terminal peptidyl-lysine acetylation Inferred from sequence or structural similarity. Source: UniProtKB germ-line stem cell maintenance Inferred from mutant phenotype. Source: MGI histone acetylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription factor activity Traceable author statement. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: MGI transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	histone acetyltransferase complex Inferred from direct assay. Source: MGI outer kinetochore of condensed chromosome Inferred from direct assay. Source: MGI transcription factor complex Inferred from direct assay. Source: MGI
Molecular function	DNA binding Inferred from direct assay. Source: MGI MyoD binding Inferred from sequence or structural similarity. Source: UniProtKB chromatin binding Inferred from direct assay. Source: MGI histone acetyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB transcription coactivator activity Traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P88946	4	EBI-296306,EBI-936023	From a different organism.
CREB1	P16220	1	EBI-296306,EBI-711855	From a different organism.
Khdrbs1	Q60749	3	EBI-296306,EBI-519077
MYB	P10242	1	EBI-296306,EBI-298355	From a different organism.
Rela	Q04207	1	EBI-296306,EBI-644400
SREBF1	P36956-1	1	EBI-296306,EBI-948328	From a different organism.
TP53	P04637	2	EBI-296306,EBI-366083	From a different organism.
Trp53	Q64451	1	EBI-296306,EBI-493476
Wwtr1	Q9EPK5	1	EBI-296306,EBI-1211920

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 2441

2440

CREB-binding protein

PRO_0000211191

Regions

Domain

586 – 665

KIX

Domain

1104 – 1176

Bromo

Zinc finger

346 – 432

TAZ-type 1

Zinc finger

1702 – 1745

ZZ-type

Zinc finger

1766 – 1847

TAZ-type 2

Region

226 – 409

184

Interaction with SRCAP By similarity

Compositional bias

1062 – 1065

Poly-Glu

Compositional bias

1556 – 1563

Poly-Glu

Compositional bias

1944 – 1949

Poly-Pro

Compositional bias

1968 – 1971

Poly-Gln

Compositional bias

2082 – 2086

Poly-Gln

Compositional bias

2200 – 2216

Poly-Gln

Compositional bias

2296 – 2299

Poly-Gln

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

120

Phosphoserine By similarity

Modified residue

273

Phosphoserine By similarity

Modified residue

600

Omega-N-methylated arginine Probable

Modified residue

624

Omega-N-methylated arginine Probable

Modified residue

1015

N6-acetyllysine By similarity

Modified residue

1031

Phosphoserine By similarity

Modified residue

1073

Phosphoserine By similarity

Modified residue

1217

N6-acetyllysine By similarity

Modified residue

1584

N6-acetyllysine By similarity

Modified residue

1589

N6-acetyllysine By similarity

Modified residue

1592

N6-acetyllysine By similarity

Modified residue

1593

N6-acetyllysine By similarity

Modified residue

1596

N6-acetyllysine By similarity

Modified residue

1598

N6-acetyllysine By similarity

Modified residue

1742

N6-acetyllysine By similarity

Modified residue

1745

N6-acetyllysine By similarity

Modified residue

1756

Phosphoserine By similarity

Modified residue

2064

Phosphoserine By similarity

Modified residue

2077

Phosphoserine By similarity

Modified residue

2080

Phosphoserine By similarity

Cross-link

999

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.8

Cross-link

1034

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.8

Cross-link

1057

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.8

Experimental info

Mutagenesis

600

R → N: Abolishes binding to CREB. Ref.3

Mutagenesis

999

K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-1034 and R-1057. Ref.8

Mutagenesis

1015

K → R: No change in sumoylation. Ref.8

Mutagenesis

1034

K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-999 and R-1057. Ref.8

Mutagenesis

1043

K → R: No change in sumoylation. Ref.8

Mutagenesis

1053

K → R: No change in sumoylation. Ref.8

Mutagenesis

1057

K → R: Enhanced transcriptional activity. No sumoylation, loss of recruitment of HDAC2 to DAAX and greatly enhanced transcritional activity; when associated with R-999 and R-1034. Ref.8

Mutagenesis

1061

K → R: No change in sumoylation. Ref.8

Mutagenesis

1087

K → R: No change in sumoylation.

Secondary structure

2441

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P45481-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 0ABB028C3112F419
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FASTA

2,441

265,474

        10         20         30         40         50         60 
MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP 

        70         80         90        100        110        120 
DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG QAQGQPNSTN MASLGAMGKS 

       130        140        150        160        170        180 
PLNQGDSSTP NLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF 

       190        200        210        220        230        240 
NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE 

       250        260        270        280        290        300 
TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ 

       310        320        330        340        350        360 
SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR KLIQQQLVLL 

       370        380        390        400        410        420 
LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAP KACQVAHCAS SRQIISHWKN 

       430        440        450        460        470        480 
CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM 

       490        500        510        520        530        540 
QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSV PAGGITTDQQ 

       550        560        570        580        590        600 
PPNLISESAL PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR 

       610        620        630        640        650        660 
SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI 

       670        680        690        700        710        720 
QKELEEKRRT RLHKQGILGN QPALPASGAQ PPVIPPAQSV RPPNGPLPLP VNRMQVSQGM 

       730        740        750        760        770        780 
NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN 

       790        800        810        820        830        840 
NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPAAQAG VSQGQEPGAA LPNPLNMLAP 

       850        860        870        880        890        900 
QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP 

       910        920        930        940        950        960 
TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT 

       970        980        990       1000       1010       1020 
PLSQAAASID NRVPTPSTVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPE PTESKGEPRS 

      1030       1040       1050       1060       1070       1080 
EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSSND TASQSTSPSQ 

      1090       1100       1110       1120       1130       1140 
PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK 

      1150       1160       1170       1180       1190       1200 
RKLDTGQYQE PWQYVDDVRL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC 

      1210       1220       1230       1240       1250       1260 
CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCGK CFTEIQGENV TLGDDPSQPQ 

      1270       1280       1290       1300       1310       1320 
TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR 

      1330       1340       1350       1360       1370       1380 
KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF 

      1390       1400       1410       1420       1430       1440 
VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQDTAL IAPHQIQGCV YISYLDSIHF 

      1450       1460       1470       1480       1490       1500 
FRPRCLRTAV YHEILIGYLE YVKKLVYVTA HIWACPPSEG DDYIFHCHPP DQKIPKPKRL 

      1510       1520       1530       1540       1550       1560 
QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE 

      1570       1580       1590       1600       1610       1620 
EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ 

      1630       1640       1650       1660       1670       1680 
KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS 

      1690       1700       1710       1720       1730       1740 
SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT 

      1750       1760       1770       1780       1790       1800 
HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK 

      1810       1820       1830       1840       1850       1860 
RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHN VRQQQIQHCL 

      1870       1880       1890       1900       1910       1920 
QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA 

      1930       1940       1950       1960       1970       1980 
GFPNVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREAQQQ QHLYRANINN 

      1990       2000       2010       2020       2030       2040 
GMPPGRDGMG TPGSQMTPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV 

      2050       2060       2070       2080       2090       2100 
MSMQAQAAVA GPRMPNVQPN RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA 

      2110       2120       2130       2140       2150       2160 
FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQP 

      2170       2180       2190       2200       2210       2220 
AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQNSAS 

      2230       2240       2250       2260       2270       2280 
LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA 

      2290       2300       2310       2320       2330       2340 
DSTPNIQQAL QQRILQQQQM KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN 

      2350       2360       2370       2380       2390       2400 
QVRSPAPVQS PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG TPHPGLAVTM ASSMDQGHLG 

      2410       2420       2430       2440 
NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L

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References

[1]	"Phosphorylated CREB binds specifically to the nuclear protein CBP." Chrivia J.C., Kwok R.P.S., Lamb N., Hagiwara M., Montminy M.R., Goodman R.H. Nature 365:855-859(1993) [PubMed: 8413673] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors." Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G. Cell 85:403-414(1996) [PubMed: 8616895] [Abstract] Cited for: INTERACTION WITH NCOA1.
[3]	"Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism." Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., Hoeger C., Montminy M.R. Mol. Cell. Biol. 16:694-703(1996) [PubMed: 8552098] [Abstract] Cited for: INTERACTION WITH CREB1, MUTAGENESIS OF ARG-600.
[4]	"The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function." Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G. Nature 387:677-684(1997) [PubMed: 9192892] [Abstract] Cited for: INTERACTION WITH NCOA3.
[5]	"A transcriptional switch mediated by cofactor methylation." Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M. Science 294:2507-2511(2001) [PubMed: 11701890] [Abstract] Cited for: INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, FUNCTION.
[6]	"Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding transcriptional coactivators: induced expression in mammary epithelial cells." Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T., Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S., Shioda T. Genomics 80:601-613(2002) [PubMed: 12504852] [Abstract] Cited for: INTERACTION WITH CITED4.
[7]	"CREB-binding protein/p300 co-activation of crystallin gene expression." Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A. J. Biol. Chem. 277:24081-24089(2002) [PubMed: 11943779] [Abstract] Cited for: INTERACTION WITH MAF.
[8]	"SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx." Kuo H.-Y., Chang C.-C., Jeng J.-C., Hu H.-M., Lin D.-Y., Maul G.G., Kwok R.P.S., Shih H.-M. Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005) [PubMed: 16287980] [Abstract] Cited for: SUMOYLATION AT LYS-999; LYS-1015; LYS-1034 AND LYS-1057, INTERACTION WITH DAXX, FUNCTION, MUTAGENESIS OF LYS-999; LYS-1015; LYS-1034; LYS-1043; LYS-1053; LYS-1057 AND LYS-1061.
[9]	"Sizn1 is a novel protein that functions as a transcriptional coactivator of bone morphogenic protein signaling." Cho G., Lim Y., Zand D., Golden J.A. Mol. Cell. Biol. 28:1565-1572(2008) [PubMed: 18160706] [Abstract] Cited for: INTERACTION WITH ZCCHC12.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S66385 mRNA. Translation: AAB28651.1.

IPI

IPI00875480.

PIR

S39161.

UniGene

Mm.132238
Mm.392384

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F81	NMR	-	A	1764-1849	[»]
1JJS	NMR	-	A	2067-2112	[»]
1KBH	NMR	-	B	2059-2117	[»]
1KDX	NMR	-	A	586-666	[»]
1L8C	NMR	-	A	345-439	[»]
1R8U	NMR	-	B	340-439	[»]
1SB0	NMR	-	A	586-672	[»]
1TOT	NMR	-	A	1700-1751	[»]
1U2N	NMR	-	A	340-439	[»]
2AGH	NMR	-	B	586-672	[»]
2C52	NMR	-	A	2059-2117	[»]
2KA4	NMR	-	A	340-439	[»]
2KA6	NMR	-	A	1764-1855	[»]

SMR

P45481. Positions 1079-1198, 1324-1702.

DisProt

DP00348.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5974N.

IntAct

P45481. 11 interactions.

STRING

P45481.

PTM databases

PhosphoSite

P45481.

Proteomic databases

PRIDE

P45481.

Genome annotation databases

Ensembl

ENSMUST00000080297; ENSMUSP00000079177; ENSMUSG00000022521; Mus musculus. [Genome view]

Organism-specific databases

MGI

MGI:1098280. Crebbp.

Phylogenomic databases

eggNOG

roNOG05886.

HOVERGEN

P45481.

Enzyme and pathway databases

BRENDA

2.3.1.48. 244.

Gene expression databases

ArrayExpress

P45481.

Bgee

P45481.

CleanEx

MM_CREBBP.

Genevestigator

P45481.

GermOnline

ENSMUSG00000022521. Mus musculus.

Family and domain databases

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR010303. DUF902_CREBbp.
IPR003101. KIX.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 1 hit.
G3DSA:1.10.246.20. KIX. 1 hit.
G3DSA:1.10.1630.10. Nuc_rcpt_coact_CREBbp. 1 hit.
G3DSA:1.20.1020.10. Znf_TAZ. 2 hits.

Pfam

PF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50952. KIX. 1 hit.
PS50134. ZF_TAZ. 2 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

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Entry information

Entry name

CBP_MOUSE

Accession

Primary (citable) accession number: P45481

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	February 1, 1996
Last modified:	February 9, 2010
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents