Paired amphipathic helix protein Sin3b

Preferred order of sections

Names and origin

Protein names

Recommended name:
Paired amphipathic helix protein Sin3b

Alternative name(s):
Histone deacetylase complex subunit Sin3b
Transcriptional corepressor Sin3b

Gene names

Name:	Sin3b
Synonyms:	Kiaa0700

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 › Mus

Protein attributes

Sequence length	1098 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription. Ref.1 Ref.2
Subunit structure	Interacts with HCFC1 By similarity. Interacts with FOXK1/MNF, MXI1, MAD, NCOR1 and SAP30. Interaction with SDS3 enhances the interaction with HDAC1 to form a complex. Interacts with MAD3, MAD4, MAEL, REST and SETDB1. Interacts with RNF220. Ref.1 Ref.2 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14
Subcellular location	Nucleus Ref.1 Ref.12.
Post-translational modification	Ubiquitinated by RNF220 that leads to proteasomal degradation. Ref.12
Sequence similarities	Contains 3 PAH (paired amphipathic helix) domains.
Sequence caution	The sequence BAD32283.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Repressor
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cardiac muscle tissue development Inferred from direct assay Ref.2. Source: UniProtKB negative regulation of cell cycle Traceable author statement Ref.2. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.1. Source: UniProtKB skeletal muscle tissue development Inferred from direct assay Ref.2. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	X chromosome Inferred from direct assay Ref.11. Source: MGI XY body Inferred from direct assay Ref.11. Source: UniProtKB Y chromosome Inferred from direct assay Ref.11. Source: MGI autosome Inferred from direct assay Ref.11. Source: MGI cytoplasm Inferred from direct assay Ref.11. Source: MGI nucleus Inferred from direct assay Ref.2 Ref.12. Source: UniProtKB
Molecular function	chromatin binding Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction Ref.2 Ref.9 Ref.11 Ref.8. Source: UniProtKB transcription corepressor activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
Foxk1	P42128	8	EBI-591466,EBI-878270
Rnf220	Q6PDX6	5	EBI-591450,EBI-2795840
Suds3	Q8BR65	5	EBI-591450,EBI-591431

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 4 (identifier: Q62141-4) 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.
Note: No experimental confirmation available.

Isoform 1 (identifier: Q62141-1) The sequence of this isoform differs from the canonical sequence as follows: 955-1098: Missing.

Isoform 2 (identifier: Q62141-2) The sequence of this isoform differs from the canonical sequence as follows: 275-293: KKMKLRGTKDLSIAAVGKY → VGLQLKCAVVWFGYCTAEE 294-954: Missing. 955-1098: Missing.

Isoform 3 (identifier: Q62141-3) The sequence of this isoform differs from the canonical sequence as follows: 275-302: KKMKLRGTKDLSIAAVGKYGTLQEFSFF → VLVHVWVLPAHGRSGVEAQAAGEPEARA 303-954: Missing. 955-1098: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1098

1098

Paired amphipathic helix protein Sin3b

PRO_0000121540

Regions

Domain

30 – 100

71

PAH 1

Domain

145 – 230

86

PAH 2

Domain

283 – 360

78

PAH 3

Region

52 – 98

47

Interaction with REST

Region

275 – 499

225

Interaction with NCOR1

Region

383 – 550

168

Interaction with SDS3 and HDAC1

Natural variations

Alternative sequence

275 – 302

28

KKMKL…EFSFF → VLVHVWVLPAHGRSGVEAQA AGEPEARA in isoform 3.

VSP_008227

Alternative sequence

275 – 293

19

KKMKL…AVGKY → VGLQLKCAVVWFGYCTAEE in isoform 2.

VSP_008225

Alternative sequence

294 – 954

661

Missing in isoform 2.

VSP_008226

Alternative sequence

303 – 954

652

Missing in isoform 3.

VSP_008228

Alternative sequence

955 – 1098

144

Missing in isoform 1, isoform 2 and isoform 3.

VSP_014187

Experimental info

Sequence conflict

230

1

A → G in AAC04821. Ref.2

Sequence conflict

233

1

S → P in AAC04821. Ref.2

Secondary structure

1

.

1098

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 4 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: A73F6DFC11EBA256 Show »	FASTA	1,098	126,405
10 20 30 40 50 60 MAHAGSGGSA GRGFGGSRWG RSGSGGHEKL PVHVEDALTY LDQVKIRFGS DPATYNGFLE 70 80 90 100 110 120 IMKEFKSQSI DTPGVIRRVS QLFHEHPDLI VGFNAFLPLG YRIDIPKNGK LNIQSPLSSQ 130 140 150 160 170 180 DNSHSHGDCG EDFKQMSYKE DRGQVPLESD SVEFNNAISY VNKIKTRFLD HPEIYRSFLE 190 200 210 220 230 240 ILHTYQKEQL HTKGRPFRGM SEEEVFTEVA NLFRGQEDLL SEFGQFLPEA KRSLFTGNGS 250 260 270 280 290 300 CEMNSGQKNE EKSLEHNKKR SRPSLLRPVS APAKKKMKLR GTKDLSIAAV GKYGTLQEFS 310 320 330 340 350 360 FFDKVRRVLK SQEVYENFLR CIALFNQELV SGSELLQLVS PFLGKFPELF AQFKSFLGVK 370 380 390 400 410 420 ELSFAPPMSD RSGDGISREI DYASCKRIGS SYRALPKTYQ QPKCSGRTAI CKEVLNDTWV 430 440 450 460 470 480 SFPSWSEDST FVSSKKTPYE EQLHRCEDER FELDVVLETN LATIRVLESV QKKLSRMAPE 490 500 510 520 530 540 DQEKLRLDDC LGGTSEVIQR RAIHRIYGDK APEVIESLKR NPATAVPVVL KRLKAKEEEW 550 560 570 580 590 600 REAQQGFNKI WREQYEKAYL KSLDHQAVNF KQNDTKALRS KSLLNEIESV YDEHQEQHSE 610 620 630 640 650 660 GRSAPSSEPH LIFVYEDRQI LEDAAALISY YVKRQPAIQK EDQGTIRQLL HRFLPSLFFS 670 680 690 700 710 720 QQCPGTSDDS ADERDRDRDS AEPERRRPTD EKPPADASPE PPKVLDDVYS LFFANNNWYF 730 740 750 760 770 780 FLRLHQTLCA RLLKIYRQAQ KQLLEHRREQ EREQLLCEGR REKAADPAME LRLKQPSEVE 790 800 810 820 830 840 LEEYYPAFLD MVRSLLEGSI DPTQYEDTLR EMFTIHAYIG FTMDKLVQNI ARQLHHLVSD 850 860 870 880 890 900 DVCLKVVELY LNEQQRGAAG GNLSSRCVRA ARETSYQWKA ERCMADENCF KVMFLQRRGQ 910 920 930 940 950 960 VIMTIELLDT EEAQTEDPVE VQHLARYVEQ YVGSEGASSS STEGFLLKPV FLQRNLKKFR 970 980 990 1000 1010 1020 RWQCEQVRAM RGEAKSSWKR LMGVESACDV DCRFRLGTHK MVFIVNSEDY MYRRGTLCRA 1030 1040 1050 1060 1070 1080 KQVQPLVLLR HHRHFEEWHG RWLEDNVTVA AAGLVQDWLM GEEEEDMVPC KTLCETAHVH 1090 GLPVTRYRVQ YSRRPASP « Hide
Isoform 1 [UniParc]. Checksum: 31F4BE14523EA213 Show »	FASTA	954	109,393
10 20 30 40 50 60 MAHAGSGGSA GRGFGGSRWG RSGSGGHEKL PVHVEDALTY LDQVKIRFGS DPATYNGFLE 70 80 90 100 110 120 IMKEFKSQSI DTPGVIRRVS QLFHEHPDLI VGFNAFLPLG YRIDIPKNGK LNIQSPLSSQ 130 140 150 160 170 180 DNSHSHGDCG EDFKQMSYKE DRGQVPLESD SVEFNNAISY VNKIKTRFLD HPEIYRSFLE 190 200 210 220 230 240 ILHTYQKEQL HTKGRPFRGM SEEEVFTEVA NLFRGQEDLL SEFGQFLPEA KRSLFTGNGS 250 260 270 280 290 300 CEMNSGQKNE EKSLEHNKKR SRPSLLRPVS APAKKKMKLR GTKDLSIAAV GKYGTLQEFS 310 320 330 340 350 360 FFDKVRRVLK SQEVYENFLR CIALFNQELV SGSELLQLVS PFLGKFPELF AQFKSFLGVK 370 380 390 400 410 420 ELSFAPPMSD RSGDGISREI DYASCKRIGS SYRALPKTYQ QPKCSGRTAI CKEVLNDTWV 430 440 450 460 470 480 SFPSWSEDST FVSSKKTPYE EQLHRCEDER FELDVVLETN LATIRVLESV QKKLSRMAPE 490 500 510 520 530 540 DQEKLRLDDC LGGTSEVIQR RAIHRIYGDK APEVIESLKR NPATAVPVVL KRLKAKEEEW 550 560 570 580 590 600 REAQQGFNKI WREQYEKAYL KSLDHQAVNF KQNDTKALRS KSLLNEIESV YDEHQEQHSE 610 620 630 640 650 660 GRSAPSSEPH LIFVYEDRQI LEDAAALISY YVKRQPAIQK EDQGTIRQLL HRFLPSLFFS 670 680 690 700 710 720 QQCPGTSDDS ADERDRDRDS AEPERRRPTD EKPPADASPE PPKVLDDVYS LFFANNNWYF 730 740 750 760 770 780 FLRLHQTLCA RLLKIYRQAQ KQLLEHRREQ EREQLLCEGR REKAADPAME LRLKQPSEVE 790 800 810 820 830 840 LEEYYPAFLD MVRSLLEGSI DPTQYEDTLR EMFTIHAYIG FTMDKLVQNI ARQLHHLVSD 850 860 870 880 890 900 DVCLKVVELY LNEQQRGAAG GNLSSRCVRA ARETSYQWKA ERCMADENCF KVMFLQRRGQ 910 920 930 940 950 VIMTIELLDT EEAQTEDPVE VQHLARYVEQ YVGSEGASSS STEGFLLKPV FLQR « Hide
Isoform 2 [UniParc]. Checksum: 11A75E8F67C818AE Show »	FASTA	293	32,846
10 20 30 40 50 60 MAHAGSGGSA GRGFGGSRWG RSGSGGHEKL PVHVEDALTY LDQVKIRFGS DPATYNGFLE 70 80 90 100 110 120 IMKEFKSQSI DTPGVIRRVS QLFHEHPDLI VGFNAFLPLG YRIDIPKNGK LNIQSPLSSQ 130 140 150 160 170 180 DNSHSHGDCG EDFKQMSYKE DRGQVPLESD SVEFNNAISY VNKIKTRFLD HPEIYRSFLE 190 200 210 220 230 240 ILHTYQKEQL HTKGRPFRGM SEEEVFTEVA NLFRGQEDLL SEFGQFLPEA KRSLFTGNGS 250 260 270 280 290 CEMNSGQKNE EKSLEHNKKR SRPSLLRPVS APAKVGLQLK CAVVWFGYCT AEE « Hide
Isoform 3 [UniParc]. Checksum: 421131CCD87C88F8 Show »	FASTA	302	33,637
10 20 30 40 50 60 MAHAGSGGSA GRGFGGSRWG RSGSGGHEKL PVHVEDALTY LDQVKIRFGS DPATYNGFLE 70 80 90 100 110 120 IMKEFKSQSI DTPGVIRRVS QLFHEHPDLI VGFNAFLPLG YRIDIPKNGK LNIQSPLSSQ 130 140 150 160 170 180 DNSHSHGDCG EDFKQMSYKE DRGQVPLESD SVEFNNAISY VNKIKTRFLD HPEIYRSFLE 190 200 210 220 230 240 ILHTYQKEQL HTKGRPFRGM SEEEVFTEVA NLFRGQEDLL SEFGQFLPEA KRSLFTGNGS 250 260 270 280 290 300 CEMNSGQKNE EKSLEHNKKR SRPSLLRPVS APAKVLVHVW VLPAHGRSGV EAQAAGEPEA RA « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3." Ayer D.E., Lawrence Q.A., Eisenman R.N. Cell 80:767-776(1995) [PubMed: 7889570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION. Tissue: Embryonic kidney.
[2]	"The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) forms a co-repressor complex with mammalian Sin3B." Yang Q., Kong Y., Rothermel B., Garry D.J., Bassel-Duby R., Williams R.S. Biochem. J. 345:335-343(2000) [PubMed: 10620510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH FOXK1. Tissue: Heart.
[3]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Brain.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Mammary gland and Salivary gland.
[5]	"Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation." Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N. EMBO J. 14:5646-5659(1995) [PubMed: 8521822] [Abstract] Cited for: INTERACTION WITH MAD3 AND MAD4.
[6]	Erratum Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N. EMBO J. 15:2030-2030(1996) [PubMed: 8617250] [Abstract]
[7]	"A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression." Heinzel T., Lavinsky R.M., Mullen T.-M., Soederstroem M., Laherty C.D., Torchia J., Yang W.M., Brard G., Ngo S.D., Davie J.R., Seto E., Eisenman R.N., Rose D.W., Glass C.K., Rosenfeld M.G. Nature 387:43-48(1997) [PubMed: 9139820] [Abstract] Cited for: INTERACTION WITH NCOR1.
[8]	"SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors." Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N. Mol. Cell 2:33-42(1998) [PubMed: 9702189] [Abstract] Cited for: INTERACTION WITH SAP30.
[9]	"Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex." Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., Chen K., DePinho R.A. Mol. Cell. Biol. 22:2743-2750(2002) [PubMed: 11909966] [Abstract] Cited for: INTERACTION WITH SDS3 AND HDAC1.
[10]	"An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B." Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A. Biochem. J. 369:651-657(2003) [PubMed: 12398767] [Abstract] Cited for: INTERACTION WITH SETDB1.
[11]	"Mouse MAELSTROM: the link between meiotic silencing of unsynapsed chromatin and microRNA pathway?" Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A., Cooke H.J. Hum. Mol. Genet. 15:2324-2334(2006) [PubMed: 16787967] [Abstract] Cited for: INTERACTION WITH MAEL.
[12]	"RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination." Kong Q., Zeng W., Wu J., Hu W., Li C., Mao B. Biochem. Biophys. Res. Commun. 393:708-713(2010) [PubMed: 20170641] [Abstract] Cited for: INTERACTION WITH RNF220, SUBCELLULAR LOCATION, UBIQUITINATION.
[13]	"The Mad1-Sin3B interaction involves a novel helical fold." Spronk C.A.E., Tessari M., Kaan A.M., Jansen J.F.A., Vermeulen M., Stunnenberg H.G., Vuister G.W. Nat. Struct. Biol. 7:1100-1104(2000) [PubMed: 11101889] [Abstract] Cited for: STRUCTURE BY NMR OF 148-232 IN COMPLEX WITH MAD1.
[14]	"The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix." Nomura M., Uda-Tochio H., Murai K., Mori N., Nishimura Y. J. Mol. Biol. 354:903-915(2005) [PubMed: 16288918] [Abstract] Cited for: STRUCTURE BY NMR OF 31-107 IN COMPLEX WITH REST, INTERACTION WITH REST.
[15]	"Solution structure of the first PAH domain of the mouse transcriptional repressor SIN3B." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 32-100.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L38622 mRNA. Translation: AAA69774.1.
AF038848 mRNA. Translation: AAC04821.1.
AK173005 mRNA. Translation: BAD32283.1. Different initiation.
BC020049 mRNA. Translation: AAH20049.1.
BC021160 mRNA. Translation: AAH21160.1.

IPI

IPI00121971.
IPI00124066.
IPI00338793.
IPI00608092.

PIR

I61714.

RefSeq

NP_001106719.1. NM_001113248.1.
NP_033214.2. NM_009188.3.

UniGene

Mm.2137.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E91	NMR	-	A	148-232	[»]
1PD7	NMR	-	A	148-232	[»]
2CR7	NMR	-	A	32-98	[»]
2CZY	NMR	-	A	31-107	[»]
2F05	NMR	-	A	148-252	[»]

ProteinModelPortal

Q62141.

SMR

Q62141. Positions 31-107, 148-232, 292-361.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-470N.

IntAct

Q62141. 6 interactions.

STRING

Q62141.

PTM databases

PhosphoSite

Q62141.

Proteomic databases

PRIDE

Q62141.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000004494; ENSMUSP00000004494; ENSMUSG00000031622.
ENSMUST00000109950; ENSMUSP00000105576; ENSMUSG00000031622.

GeneID

20467.

KEGG

mmu:20467.

UCSC

uc009mgp.2. mouse.
uc009mgq.3. mouse.

Organism-specific databases

CTD

23309.

MGI

MGI:107158. Sin3b.

Rouge

Search...

Phylogenomic databases

eggNOG

roNOG07303.

GeneTree

ENSGT00390000007239.

HOGENOM

HBG738583.

HOVERGEN

HBG060425.

InParanoid

Q62141.

OMA

DVYSLFF.

OrthoDB

EOG4ZGPBH.

PhylomeDB

Q62141.

Gene expression databases

ArrayExpress

Q62141.

Bgee

Q62141.

CleanEx

MM_SIN3B.

Genevestigator

Q62141.

GermOnline

ENSMUSG00000031622. Mus musculus.

Family and domain databases

InterPro

IPR013194. HDAC_interact.
IPR003822. PAH.
[Graphical view]

Gene3D

G3DSA:1.20.1160.11. PAH. 3 hits.

Pfam

PF08295. HDAC_interact. 1 hit.
PF02671. PAH. 3 hits.
[Graphical view]

SMART

SM00761. HDAC_interact. 1 hit.
[Graphical view]

SUPFAM

SSF47762. PAH. 3 hits.

PROSITE

PS51477. PAH. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

298571.

SOURCE

Search...

Entry information

Entry name

SIN3B_MOUSE

Accession

Primary (citable) accession number: Q62141
Secondary accession number(s): O54976

Q8VDZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents