DNA mismatch repair protein MLH1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38920 (MLH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
DNA mismatch repair protein MLH1

Alternative name(s):
MutL protein homolog 1
Post meiotic segregation protein 2

Gene names

Name:	MLH1
Synonyms:	PMS2
Ordered Locus Names:	YMR167W
ORF Names:	YM8520.16

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	769 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of different MutL heterodimers that form a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats, the repair of heteroduplex sites present in meiotic recombination intermediates, and the promotion of meiotic crossing-over. Ref.7 Ref.8 Ref.12
Subunit structure	Heterodimer of MLH1 and PMS1, called MutLalpha, which is the major MMR MutL activity correcting base-base mismatches as well as IDLs. The heterodimer binds double strand DNA independently of a mismatch with positive cooperativity and has more than one DNA binding site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to mismatch DNA. Ternary complex formation is promoted by ATP binding. Heterodimer of MLH1 and MLH3, called MutLbeta, which is involved in correction of a specific subset of IDLs when associated with MutSbeta. Heterodimer of MLH1 and MLH2. Ref.7
Subcellular location	Nucleus Ref.13.
Miscellaneous	Present with 319 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DNA mismatch repair MutL/HexB family.
Biophysicochemical properties	Kinetic parameters: K_M=69 µM for ATP Ref.11

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	meiotic heteroduplex formation Inferred from mutant phenotype PubMed 15654114. Source: SGD meiotic mismatch repair Inferred from mutant phenotype PubMed 16702432. Source: SGD reciprocal meiotic recombination Inferred from mutant phenotype Ref.8. Source: SGD
Cellular_component	MutLalpha complex Inferred from physical interaction Ref.8. Source: SGD MutLbeta complex Inferred from physical interaction PubMed 9770499. Source: SGD chiasma Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrion Inferred from direct assay PubMed 14576278 PubMed 16823961. Source: SGD synaptonemal complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	ATP binding Inferred from mutant phenotype Ref.9. Source: SGD ATPase activity Inferred from direct assay Ref.11. Source: SGD mismatched DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
MLH2	Q07980	5	EBI-11003,EBI-33369
MLH3	Q12083	4	EBI-11003,EBI-31634
PMS1	P14242	7	EBI-11003,EBI-13561

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 769

769

DNA mismatch repair protein MLH1

PRO_0000178008

Regions

Region

1 – 335

335

DNA- and ATP-binding

Region

501 – 756

256

Interaction with PMS1

Amino acid modifications

Modified residue

439

Phosphoserine Ref.17

Modified residue

441

Phosphoserine; by ATM or ATR Ref.16 Ref.17

Natural variations

Natural variant

240

S → R in strain: SK1. Ref.2

Natural variant

242

D → E in strain: YJM326 and YJM339. Ref.2

Natural variant

271

L → P in strain: EAY1066, EAY1068, M2-8, M7-8, M5-7, SK1, YJM269, YJM280, YJM320, YJM326, YJM339 and YJM627. Ref.2

Natural variant

309

P → L in strain: M2-8. Ref.2

Natural variant

321

E → D in strain: EAY1066. Ref.2

Natural variant

333

E → K in strain: SK1. Ref.2

Natural variant

375

A → T in strain: YJM339. Ref.2

Natural variant

452

S → G in strain: EAY1068, M2-8, M7-8, M5-7, YJM269 and YJM627. Ref.2

Natural variant

465

D → N in strain: EAY1066 and YJM280. Ref.2

Natural variant

470

P → S in strain: YJM339. Ref.2

Natural variant

607

L → F in strain: EAY1068, M2-8, M7-8, M5-7 and YJM627. Ref.2

Natural variant

678

D → N in strain: SK1, YJM320 and YJM339. Ref.2

Natural variant

703

P → L in strain: SK1, YJM320 and YJM339. Ref.2

Natural variant

761

D → G in strain: EAY1066, EAY1068, M2-8, M7-8, M5-7, SK1, YJM145, YJM269, YJM320, YJM339 and YJM627; forms a non-functional heterodimer with PMS1 from strain S288c, resulting in an accumulation of mutations in spore progeny of crosses between these strains. Ref.2

Experimental info

Mutagenesis

E → A: Reduces ATPase activity by 98%. Displays 3300-fold increase in spontaneous mutation accumulation. Ref.9 Ref.11

Mutagenesis

N → A: Abolishes ATP binding, reducing ATPase activity by 95%. Displays 9800-fold increase in spontaneous mutation accumulation. Ref.11

Mutagenesis

A → F: Defective in a mismatch repair assay. Abolishes heterodimer formation. Displays an increases spontaneous mutation accumulation. Ref.5 Ref.6

Mutagenesis

A → G: Reduces heterodimer formation. Displays an weak increase in spontaneous mutation accumulation. Ref.5 Ref.6

Mutagenesis

A → S: Fully functional in a mismatch repair assay. Ref.5 Ref.6

Mutagenesis

G → R: Defective in a mismatch repair assay. Ref.5

Mutagenesis

I → N: Defective in a mismatch repair assay. Ref.5

Mutagenesis

F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.6

Mutagenesis

R → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.6

Mutagenesis

G → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.6 Ref.9

Mutagenesis

G → V: Abolishes heterodimer formation. Displays an increase in spontaneous mutation accumulation. Ref.6 Ref.9

Mutagenesis

E → K: Defective in a mismatch repair assay. Ref.5

Mutagenesis

104

I → R: Defective in a mismatch repair assay. Ref.5

Mutagenesis

114

T → R: Defective in a mismatch repair assay. Ref.5

Mutagenesis

214

R → C: Partially defective in a mismatch repair assay. Ref.5

Mutagenesis

216

V → I: Fully functional in a mismatch repair assay. Ref.5

Mutagenesis

265

R → C: Partially defective in a mismatch repair assay. Ref.5

Mutagenesis

265

R → H: Partially defective in a mismatch repair assay. Ref.5

Mutagenesis

273

R → E: Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation; when associated with E-274. Ref.15

Mutagenesis

274

R → E: Reduces DNA-binding and displays a 1700-fold increase in spontaneous mutation accumulation. Strongly reduces DNA-binding and displays 12000-fold increase in spontaneous mutation accumulation; when associated with E-273. Ref.15

Mutagenesis

326

I → A: Partially defective in a mismatch repair assay. Ref.5

Mutagenesis

326

I → V: Fully functional in a mismatch repair assay. Ref.5

Mutagenesis

552

Q → L: Defective in a mismatch repair assay. Ref.5

Mutagenesis

672

R → P: Defective in a mismatch repair assay. Ref.5

Mutagenesis

694

A → T: Fully functional in a mismatch repair assay. Ref.5

Mutagenesis

764

K → E: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.6

Mutagenesis

764

K → R: No effect. Ref.6

Mutagenesis

766

F → A: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.6

Mutagenesis

767

E → D: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.6

Mutagenesis

769

C → A: No effect. Ref.6

Mutagenesis

769

C → S: Displays an increase in spontaneous mutation accumulation. Does not impair heterodimer formation. Ref.6

Sequence conflict

258

P → L in AAA16835. Ref.1

Sequence conflict

288

N → F in AAA16835. Ref.1

Sequence conflict

708

S → L in AAA16835. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P38920 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: B2DBB31DE3943171
Show »

FASTA

769

87,062

        10         20         30         40         50         60 
MSLRIKALDA SVVNKIAAGE IIISPVNALK EMMENSIDAN ATMIDILVKE GGIKVLQITD 

        70         80         90        100        110        120 
NGSGINKADL PILCERFTTS KLQKFEDLSQ IQTYGFRGEA LASISHVARV TVTTKVKEDR 

       130        140        150        160        170        180 
CAWRVSYAEG KMLESPKPVA GKDGTTILVE DLFFNIPSRL RALRSHNDEY SKILDVVGRY 

       190        200        210        220        230        240 
AIHSKDIGFS CKKFGDSNYS LSVKPSYTVQ DRIRTVFNKS VASNLITFHI SKVEDLNLES 

       250        260        270        280        290        300 
VDGKVCNLNF ISKKSISPIF FINNRLVTCD LLRRALNSVY SNYLPKGNRP FIYLGIVIDP 

       310        320        330        340        350        360 
AAVDVNVHPT KREVRFLSQD EIIEKIANQL HAELSAIDTS RTFKASSIST NKPESLIPFN 

       370        380        390        400        410        420 
DTIESDRNRK SLRQAQVVEN SYTTANSQLR KAKRQENKLV RIDASQAKIT SFLSSSQQFN 

       430        440        450        460        470        480 
FEGSSTKRQL SEPKVTNVSH SQEAEKLTLN ESEQPRDANT INDNDLKDQP KKKQKLGDYK 

       490        500        510        520        530        540 
VPSIADDEKN ALPISKDGYI RVPKERVNVN LTSIKKLREK VDDSIHRELT DIFANLNYVG 

       550        560        570        580        590        600 
VVDEERRLAA IQHDLKLFLI DYGSVCYELF YQIGLTDFAN FGKINLQSTN VSDDIVLYNL 

       610        620        630        640        650        660 
LSEFDELNDD ASKEKIISKI WDMSSMLNEY YSIELVNDGL DNDLKSVKLK SLPLLLKGYI 

       670        680        690        700        710        720 
PSLVKLPFFI YRLGKEVDWE DEQECLDGIL REIALLYIPD MVPKVDTSDA SLSEDEKAQF 

       730        740        750        760 
INRKEHISSL LEHVLFPCIK RRFLAPRHIL KDVVEIANLP DLYKVFERC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dual requirement in yeast DNA mismatch repair for MLH1 and PMS1, two homologs of the bacterial mutL gene." Prolla T.A., Christie D.-M., Liskay R.M. Mol. Cell. Biol. 14:407-415(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Negative epistasis between natural variants of the Saccharomyces cerevisiae MLH1 and PMS1 genes results in a defect in mismatch repair." Heck J.A., Argueso J.L., Gemici Z., Reeves R.G., Bernard A., Aquadro C.F., Alani E. Proc. Natl. Acad. Sci. U.S.A. 103:3256-3261(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-240; GLU-242; PRO-271; LEU-309; ASP-321; LYS-333; THR-375; GLY-452; ASN-465; SER-470; PHE-607; ASN-678; LEU-703 AND GLY-761. Strain: ATCC 200060 / W303, EAY1066, EAY1068, M2-8, M5-7, M7-8, SK1, YJM 145, YJM 269, YJM 280, YJM 320, YJM 326, YJM 339 and YJM 627.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Functional analysis of human MLH1 and MSH2 missense variants and hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae." Ellison A.R., Lofing J., Bitter G.A. Hum. Mol. Genet. 10:1889-1900(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ALA-41; GLY-64; ILE-65; GLU-99; ILE-104; THR-114; ARG-214; VAL-216; ARG-265; ILE-326; GLN-552; ARG-672 AND ALA-694.
[6]	"Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations." Pang Q., Prolla T.A., Liskay R.M. Mol. Cell. Biol. 17:4465-4473(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PMS1, MUTAGENESIS OF ALA-41; PHE-96; ARG-97; GLY-98; LYS-764; PHE-766; GLU-767 AND CYS-769.
[7]	"ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes." Habraken Y., Sung P., Prakash L., Prakash S. J. Biol. Chem. 273:9837-9841(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[8]	"Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction." Wang T.-F., Kleckner N., Hunter N. Proc. Natl. Acad. Sci. U.S.A. 96:13914-13919(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MLH2; MLH3 AND PMS1.
[9]	"Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha." Tran P.T., Liskay R.M. Mol. Cell. Biol. 20:6390-6398(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PMS1, ATP-BINDING, MUTAGENESIS OF GLU-31 AND GLY-98.
[10]	"DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers." Drotschmann K., Hall M.C., Shcherbakova P.V., Wang H., Erie D.A., Brownewell F.R., Kool E.T., Kunkel T.A. Biol. Chem. 383:969-975(2002) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[11]	"Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins." Hall M.C., Shcherbakova P.V., Kunkel T.A. J. Biol. Chem. 277:3673-3679(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ATP-BINDING, MUTAGENESIS OF GLU-31 AND ASN-35, BIOPHYSICOCHEMICAL PROPERTIES.
[12]	"Systematic mutagenesis of the Saccharomyces cerevisiae MLH1 gene reveals distinct roles for Mlh1p in meiotic crossing over and in vegetative and meiotic mismatch repair." Argueso J.L., Kijas A.W., Sarin S., Heck J.A., Waase M., Alani E. Mol. Cell. Biol. 23:873-886(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS.
[13]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[14]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[15]	"DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair." Hall M.C., Shcherbakova P.V., Fortune J.M., Borchers C.H., Dial J.M., Tomer K.B., Kunkel T.A. Nucleic Acids Res. 31:2025-2034(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, MUTAGENESIS OF ARG-273 AND ARG-274.
[16]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, MASS SPECTROMETRY.
[17]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-441, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U07187 Unassigned DNA. Translation: AAA16835.1.
DQ356633 Genomic DNA. Translation: ABC86937.1.
DQ356634 Genomic DNA. Translation: ABC86938.1.
DQ356635 Genomic DNA. Translation: ABC86939.1.
DQ356636 Genomic DNA. Translation: ABC86940.1.
DQ356637 Genomic DNA. Translation: ABC86941.1.
DQ356638 Genomic DNA. Translation: ABC86942.1.
DQ356639 Genomic DNA. Translation: ABC86943.1.
DQ356640 Genomic DNA. Translation: ABC86944.1.
DQ356641 Genomic DNA. Translation: ABC86945.1.
DQ356642 Genomic DNA. Translation: ABC86946.1.
DQ356643 Genomic DNA. Translation: ABC86947.1.
DQ356644 Genomic DNA. Translation: ABC86948.1.
DQ356645 Genomic DNA. Translation: ABC86949.1.
DQ356646 Genomic DNA. Translation: ABC86950.1.
Z49705 Genomic DNA. Translation: CAA89803.1.
BK006946 Genomic DNA. Translation: DAA10063.1.

PIR

S54525.

RefSeq

NP_013890.1. NM_001182671.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4E4W	X-ray	2.50	A	485-769	[»]
4FMN	X-ray	2.69	A	485-769	[»]
4FMO	X-ray	3.04	A	485-769	[»]

ProteinModelPortal

P38920.

SMR

P38920. Positions 5-298.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2412N.

IntAct

P38920. 10 interactions.

MINT

MINT-625234.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YMR167W; YMR167W; YMR167W.

GeneID

855203.

KEGG

sce:YMR167W.

Organism-specific databases

CYGD

YMR167w.

SGD

S000004777. MLH1.

Phylogenomic databases

GeneTree

ENSGT00550000074923.

K08734.

OMA

SIQVVVK.

OrthoDB

EOG43XZBN.

Gene expression databases

Genevestigator

P38920.

GermOnline

YMR167W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.230.10. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR002099. DNA_mismatch_repair.
IPR013507. DNA_mismatch_repair_C.
IPR014762. DNA_mismatch_repair_CS.
IPR011186. DNA_mismatch_repair_MLH1.
IPR014763. DNA_mismatch_repair_N.
IPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]

PANTHER

PTHR10073. PTHR10073. 1 hit.
PTHR10073:SF11. PTHR10073:SF11. 1 hit.

Pfam

PF01119. DNA_mis_repair. 1 hit.
[Graphical view]

SMART

SM00387. HATPase_c. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.

TIGRFAMs

TIGR00585. mutl. 1 hit.

PROSITE

PS00058. DNA_MISMATCH_REPAIR_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

978693.

Entry information

Entry name

MLH1_YEAST

Accession

Primary (citable) accession number: P38920
Secondary accession number(s): D6VZY9

Q2I041

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

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

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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