POL30

Functionⁱ

This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.2 Publications

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
DNA bindingⁱ	61 – 80	Sequence analysisAdd BLAST		20

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chromatin silencing at silent mating-type cassette
Source: SGD
Inferred from mutant phenotypeⁱ
- 16157874
chromatin silencing at telomere
Source: SGD
Inferred from mutant phenotypeⁱ
- 16157874
error-free translesion synthesis
Source: SGD
Inferred from genetic interactionⁱ
- 19264809
establishment of mitotic sister chromatid cohesion
Source: SGD
Inferred from genetic interactionⁱ
- 16934511
lagging strand elongation
Source: SGD
Inferred from direct assayⁱ
- 7673186
leading strand elongation
Source: SGD
Inferred from direct assayⁱ
- 1682321
maintenance of DNA trinucleotide repeats
Source: SGD
Inferred from mutant phenotypeⁱ
- 16079237
meiotic mismatch repair
Source: SGD
Inferred from mutant phenotypeⁱ
- 18245822
mismatch repair
Source: SGD
Inferred from mutant phenotypeⁱ
- 8858149
mitotic cell cycle
Source: SGD
Inferred from genetic interactionⁱ
- 7516465
mitotic sister chromatid cohesion
Source: SGD
Inferred from genetic interactionⁱ
- 16934511
nucleotide-excision repair
Source: SGD
Inferred from mutant phenotypeⁱ
- 9806417
positive regulation of exodeoxyribonuclease activity
Source: SGD
Inferred from direct assayⁱ
- 12192046
positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands
Source: SGD
Inferred from direct assayⁱ
- 12192046
postreplication repair
Source: SGD
Inferred from mutant phenotypeⁱ
- 8790390
regulation of DNA replication Source: InterPro
translesion synthesis
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding
Biological process	DNA damage, DNA repair, DNA replication

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-29055-MONOMER
Reactomeⁱ	R-SCE-110312 Translesion synthesis by REV1 R-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex R-SCE-110320 Translesion Synthesis by POLH R-SCE-174411 Polymerase switching on the C-strand of the telomere R-SCE-4615885 SUMOylation of DNA replication proteins R-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-SCE-5651801 PCNA-Dependent Long Patch Base Excision Repair R-SCE-5655862 Translesion synthesis by POLK R-SCE-5656121 Translesion synthesis by POLI R-SCE-5656169 Termination of translesion DNA synthesis R-SCE-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER R-SCE-5696400 Dual Incision in GG-NER R-SCE-6782135 Dual incision in TC-NER R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER R-SCE-69091 Polymerase switching R-SCE-69166 Removal of the Flap Intermediate R-SCE-69183 Processive synthesis on the lagging strand R-SCE-8866654 E3 ubiquitin ligases ubiquitinate target proteins

BioCycⁱ

YEAST:G3O-29055-MONOMER

Reactomeⁱ

R-SCE-110312 Translesion synthesis by REV1
R-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex
R-SCE-110320 Translesion Synthesis by POLH
R-SCE-174411 Polymerase switching on the C-strand of the telomere
R-SCE-4615885 SUMOylation of DNA replication proteins
R-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-SCE-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-SCE-5655862 Translesion synthesis by POLK
R-SCE-5656121 Translesion synthesis by POLI
R-SCE-5656169 Termination of translesion DNA synthesis
R-SCE-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-SCE-5696400 Dual Incision in GG-NER
R-SCE-6782135 Dual incision in TC-NER
R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-69091 Polymerase switching
R-SCE-69166 Removal of the Flap Intermediate
R-SCE-69183 Processive synthesis on the lagging strand
R-SCE-8866654 E3 ubiquitin ligases ubiquitinate target proteins

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Proliferating cell nuclear antigen Short name: PCNA
Gene namesⁱ	Name:POL30 Ordered Locus Names:YBR088C ORF Names:YBR0811
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome II

Organism-specific databases

Saccharomyces Genome Database More...SGDⁱ	S000000292 POL30

SGDⁱ

S000000292 POL30

Keywords - Cellular componentⁱ

Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000149176	1 – 258	Proliferating cell nuclear antigenAdd BLAST		258

Amino acid modifications

Feature key	Position(s)	DescriptionActions
Cross-linkⁱ	127	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linkⁱ	164	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate2 Publications
Cross-linkⁱ	164	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication

Post-translational modificationⁱ

Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and function in DNA repair.3 Publications

Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA damage, and then polyubiquitinated through 'Lys-63'-linkage by UBC13/MMS2. Ubiquitination is required for UBC2-mediated DNA repair.1 Publication

Lys-164 is deubiquitinated by UBP10 (PubMed:22829782).1 Publication

Keywords - PTMⁱ

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P15873
PaxDbⁱ	P15873
PRIDEⁱ	P15873
TopDownProteomicsⁱ	P15873

PTM databases

iPTMnetⁱ	P15873

iPTMnetⁱ

P15873

Interactionⁱ

Subunit structureⁱ

Homotrimer (PubMed:15201901). Interacts with RAD30 (PubMed:11545742). Interacts with MCM10 (PubMed:16782870). Interacts with UBP10 (PubMed:22829782).4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		10	EBI-12993,EBI-12993
ECO1	P43605	2	EBI-12993,EBI-22988
ELG1	Q12050	9	EBI-12993,EBI-32195
MCM10	P32354	4	EBI-12993,EBI-5965
MSH6	Q03834	5	EBI-12993,EBI-11383
POL32	P47110	4	EBI-12993,EBI-6084
RAD27	P26793	7	EBI-12993,EBI-14693
RAD30	Q04049	7	EBI-12993,EBI-36214
RLF2	Q12495	3	EBI-12993,EBI-3913
SMT3	Q12306	6	EBI-12993,EBI-17490
SRS2	P12954	10	EBI-12993,EBI-18110
UNG1	P12887	4	EBI-12993,EBI-2097931

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	32794, 460 interactors
ComplexPortalⁱ	CPX-544 PCNA homotrimer
Database of interacting proteins More...DIPⁱ	DIP-2417N
IntActⁱ	P15873, 37 interactors
Molecular INTeraction database More...MINTⁱ	P15873
STRINGⁱ	4932.YBR088C

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	2 – 7	Combined sources	6
Helixⁱ	9 – 17	Combined sources	9
Turnⁱ	18 – 22	Combined sources	5
Beta strandⁱ	24 – 31	Combined sources	8
Beta strandⁱ	34 – 40	Combined sources	7
Beta strandⁱ	42 – 44	Combined sources	3
Beta strandⁱ	46 – 53	Combined sources	8
Helixⁱ	54 – 56	Combined sources	3
Beta strandⁱ	57 – 64	Combined sources	8
Beta strandⁱ	66 – 71	Combined sources	6
Helixⁱ	72 – 79	Combined sources	8
Beta strandⁱ	80 – 82	Combined sources	3
Beta strandⁱ	84 – 92	Combined sources	9
Beta strandⁱ	97 – 104	Combined sources	8
Beta strandⁱ	106 – 109	Combined sources	4
Beta strandⁱ	111 – 117	Combined sources	7
Helixⁱ	122 – 124	Combined sources	3
Beta strandⁱ	134 – 140	Combined sources	7
Helixⁱ	141 – 152	Combined sources	12
Beta strandⁱ	156 – 163	Combined sources	8
Beta strandⁱ	166 – 173	Combined sources	8
Beta strandⁱ	176 – 182	Combined sources	7
Beta strandⁱ	185 – 187	Combined sources	3
Beta strandⁱ	188 – 190	Combined sources	3
Helixⁱ	191 – 193	Combined sources	3
Beta strandⁱ	195 – 201	Combined sources	7
Beta strandⁱ	203 – 208	Combined sources	6
Helixⁱ	209 – 215	Combined sources	7
Helixⁱ	216 – 220	Combined sources	5
Beta strandⁱ	223 – 229	Combined sources	7
Beta strandⁱ	231 – 233	Combined sources	3
Beta strandⁱ	235 – 241	Combined sources	7
Beta strandⁱ	244 – 250	Combined sources	7
Beta strandⁱ	254 – 256	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P15873
SMRⁱ	P15873
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P15873

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the PCNA family.Curated

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000004965
HOGENOMⁱ	HOG000211098
InParanoidⁱ	P15873
KEGG Orthology (KO) More...KOⁱ	K04802
OMAⁱ	KILRCAG
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C4AWZ

Family and domain databases

HAMAPⁱ	MF_00317 DNApol_clamp_arch, 1 hit
InterProⁱ	View protein in InterPro IPR000730 Pr_cel_nuc_antig IPR022649 Pr_cel_nuc_antig_C IPR022659 Pr_cel_nuc_antig_CS IPR022648 Pr_cel_nuc_antig_N
PANTHERⁱ	PTHR11352:SF0 PTHR11352:SF0, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02747 PCNA_C, 1 hit PF00705 PCNA_N, 1 hit
PRINTSⁱ	PR00339 PCNACYCLIN
TIGRFAMsⁱ	TIGR00590 pcna, 1 hit
PROSITEⁱ	View protein in PROSITE PS01251 PCNA_1, 1 hit PS00293 PCNA_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P15873-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLEAKFEEAS LFKRIIDGFK DCVQLVNFQC KEDGIIAQAV DDSRVLLVSL 
        60         70         80         90        100
EIGVEAFQEY RCDHPVTLGM DLTSLSKILR CGNNTDTLTL IADNTPDSII 
       110        120        130        140        150
LLFEDTKKDR IAEYSLKLMD IDADFLKIEE LQYDSTLSLP SSEFSKIVRD 
       160        170        180        190        200
LSQLSDSINI MITKETIKFV ADGDIGSGSV IIKPFVDMEH PETSIKLEMD 
       210        220        230        240        250
QPVDLTFGAK YLLDIIKGSS LSDRVGIRLS SEAPALFQFD LKSGFLQFFL 

APKFNDEE

Length:258

Mass (Da):28,916

Last modified:April 1, 1990 - v1

Checksum:ⁱ9B56C5851621DDDC

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X16676 Genomic DNA Translation: CAA34664.1 X78993 Genomic DNA Translation: CAA55594.1 Z35957 Genomic DNA Translation: CAA85038.1 AY557715 Genomic DNA Translation: AAS56041.1 BK006936 Genomic DNA Translation: DAA07209.1
PIRⁱ	S22851 WMBYET
NCBI Reference Sequences More...RefSeqⁱ	NP_009645.1, NM_001178436.1

Genome annotation databases

EnsemblFungiⁱ	YBR088C; YBR088C; YBR088C
GeneIDⁱ	852385
KEGGⁱ	sce:YBR088C

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P15873	Proliferating cell nuclear antigen		YEASB		258	UniRef100_P15873
Proliferating cell nuclear antigen		SACAR		258
Proliferating cell nuclear antigen		YEAS1		258
Proliferating cell nuclear antigen		YEASK		258
Proliferating cell nuclear antigen		YEASA		258
+10

Protein	Similar proteins		Species	Score	Length	Source
P15873	Proliferating cell nuclear antigen		YEASB		258	UniRef90_P15873
Proliferating cell nuclear antigen		SACAR		258
Proliferating cell nuclear antigen		YEAS1		258
Proliferating cell nuclear antigen		YEASK		258
Proliferating cell nuclear antigen		YEASA		258
+36

Protein	Similar proteins		Species	Score	Length	Source
P15873	Proliferating cell nuclear antigen		YEASB		258	UniRef50_P15873
Proliferating cell nuclear antigen		SACAR		258
Proliferating cell nuclear antigen		YEAS1		258
Proliferating cell nuclear antigen		YEASK		258
Proliferating cell nuclear antigen		YEASA		258
+36

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X16676 Genomic DNA Translation: CAA34664.1 X78993 Genomic DNA Translation: CAA55594.1 Z35957 Genomic DNA Translation: CAA85038.1 AY557715 Genomic DNA Translation: AAS56041.1 BK006936 Genomic DNA Translation: DAA07209.1
PIRⁱ	S22851 WMBYET
RefSeqⁱ	NP_009645.1, NM_001178436.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1PLQ	X-ray	2.30	A	1-258	[»]
	1PLR	X-ray	3.00	A	1-258	[»]
	1SXJ	X-ray	2.85	F/G/H	1-258	[»]
	2OD8	X-ray	2.80	A	1-258	[»]
	3F1W	X-ray	2.90	A	1-258	[»]
	3GPM	X-ray	3.80	A	1-258	[»]
	3GPN	X-ray	2.50	A	1-258	[»]
	3L0W	X-ray	2.80	A	1-163	[»]
	3L0X	X-ray	3.00	A	1-163	[»]
				B	165-258	[»]
	3L10	X-ray	2.80	A	1-163	[»]
	3PGE	X-ray	2.80	A	165-258	[»]
				B	1-163	[»]
	3V60	X-ray	2.60	B	1-258	[»]
	3V61	X-ray	2.80	B	1-258	[»]
	3V62	X-ray	2.90	B/E	1-258	[»]
	4L60	X-ray	3.00	A	1-256	[»]
	4L6P	X-ray	2.68	A/B/C	1-258	[»]
	4YHR	X-ray	2.95	A	1-258	[»]
	5JNE	X-ray	2.85	D/H	1-258	[»]
	5T9D	X-ray	3.27	A/B/C	2-258	[»]
	5V7K	X-ray	3.05	A	1-258	[»]
	5V7L	X-ray	3.20	A	1-258	[»]
	5V7M	X-ray	1.93	A	1-258	[»]
	5ZUT	X-ray	2.82	A	1-258	[»]
	6CX2	X-ray	3.10	A	1-258	[»]
	6CX3	X-ray	3.10	A	1-258	[»]
	6CX4	X-ray	3.08	A	1-258	[»]
	6E49	X-ray	2.90	A/B/C	1-258	[»]
ProteinModelPortalⁱ	P15873
SMRⁱ	P15873
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	32794, 460 interactors
ComplexPortalⁱ	CPX-544 PCNA homotrimer
DIPⁱ	DIP-2417N
IntActⁱ	P15873, 37 interactors
MINTⁱ	P15873
STRINGⁱ	4932.YBR088C

PTM databases

iPTMnetⁱ	P15873

iPTMnetⁱ

P15873

Proteomic databases

MaxQBⁱ	P15873
PaxDbⁱ	P15873
PRIDEⁱ	P15873
TopDownProteomicsⁱ	P15873

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	YBR088C; YBR088C; YBR088C
GeneIDⁱ	852385
KEGGⁱ	sce:YBR088C

Organism-specific databases

SGDⁱ	S000000292 POL30

Phylogenomic databases

GeneTreeⁱ	ENSGT00390000004965
HOGENOMⁱ	HOG000211098
InParanoidⁱ	P15873
KOⁱ	K04802
OMAⁱ	KILRCAG
OrthoDBⁱ	EOG092C4AWZ

Enzyme and pathway databases

BioCycⁱ	YEAST:G3O-29055-MONOMER
Reactomeⁱ	R-SCE-110312 Translesion synthesis by REV1 R-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex R-SCE-110320 Translesion Synthesis by POLH R-SCE-174411 Polymerase switching on the C-strand of the telomere R-SCE-4615885 SUMOylation of DNA replication proteins R-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) R-SCE-5651801 PCNA-Dependent Long Patch Base Excision Repair R-SCE-5655862 Translesion synthesis by POLK R-SCE-5656121 Translesion synthesis by POLI R-SCE-5656169 Termination of translesion DNA synthesis R-SCE-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER R-SCE-5696400 Dual Incision in GG-NER R-SCE-6782135 Dual incision in TC-NER R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER R-SCE-69091 Polymerase switching R-SCE-69166 Removal of the Flap Intermediate R-SCE-69183 Processive synthesis on the lagging strand R-SCE-8866654 E3 ubiquitin ligases ubiquitinate target proteins

BioCycⁱ

YEAST:G3O-29055-MONOMER

Reactomeⁱ

R-SCE-110312 Translesion synthesis by REV1
R-SCE-110314 Recognition of DNA damage by PCNA-containing replication complex
R-SCE-110320 Translesion Synthesis by POLH
R-SCE-174411 Polymerase switching on the C-strand of the telomere
R-SCE-4615885 SUMOylation of DNA replication proteins
R-SCE-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-SCE-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-SCE-5655862 Translesion synthesis by POLK
R-SCE-5656121 Translesion synthesis by POLI
R-SCE-5656169 Termination of translesion DNA synthesis
R-SCE-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-SCE-5696400 Dual Incision in GG-NER
R-SCE-6782135 Dual incision in TC-NER
R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-69091 Polymerase switching
R-SCE-69166 Removal of the Flap Intermediate
R-SCE-69183 Processive synthesis on the lagging strand
R-SCE-8866654 E3 ubiquitin ligases ubiquitinate target proteins

Miscellaneous databases

EvolutionaryTraceⁱ	P15873
Protein Ontology More...PROⁱ	PR:P15873

Family and domain databases

HAMAPⁱ	MF_00317 DNApol_clamp_arch, 1 hit
InterProⁱ	View protein in InterPro IPR000730 Pr_cel_nuc_antig IPR022649 Pr_cel_nuc_antig_C IPR022659 Pr_cel_nuc_antig_CS IPR022648 Pr_cel_nuc_antig_N
PANTHERⁱ	PTHR11352:SF0 PTHR11352:SF0, 1 hit
Pfamⁱ	View protein in Pfam PF02747 PCNA_C, 1 hit PF00705 PCNA_N, 1 hit
PRINTSⁱ	PR00339 PCNACYCLIN
TIGRFAMsⁱ	TIGR00590 pcna, 1 hit
PROSITEⁱ	View protein in PROSITE PS01251 PCNA_1, 1 hit PS00293 PCNA_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PCNA_YEAST
Accessionⁱ	P15873Primary (citable) accession number: P15873 Secondary accession number(s): D6VQ89
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
	Last sequence update:	April 1, 1990
	Last modified:	November 7, 2018
	This is version 184 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
Yeast chromosome II
Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P15873 (PCNA_YEAST)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Proliferating cell nuclear antigen

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ