Domains within Homo sapiens protein PARP1_HUMAN (P09874)

Poly [ADP-ribose] polymerase 1

Alternative representations: 1 /

Protein length1014 aa
Source databaseUniProt
Identifiers PARP1_HUMAN, P09874, ENSP00000355759.5, ENSP00000355759, B1ANJ4, Q8IUZ9, A0A024R3T8_HUMAN, A0A024R3T8
Source gene ENSG00000143799
Alternative splicing PARP1_HUMAN, Q5VX84_HUMAN, Q5VX85_HUMAN

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

Predicted functional partners

PARP1_HUMAN is shown as PARP1 in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for PARP1

Protein PARP1_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map03410Base excision repair
map05415Diabetic cardiomyopathy

KEGG orthologous groups

KONameDescription
K10798PARP3_4protein mono-ADP-ribosyltransferase 3/4 [EC:2.4.2.-]
K24070PARP1poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]

Post-translational modifications

PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 106 PTMs annotated in this protein:

PTMCount
Ubiquitination43
Phosphorylation22
Acetylation19
ADP ribosylation15
Proteolytic cleavage3
Methylation2
SUMOylation2

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein PARP1.

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 9606.ENSP00000355759 in eggNOG.

OGTaxonomic classDescription
LKOG1037All organisms (root)poly [ADP-ribose] polymerase 2/3/4 [EC:2.4.2.30],poly [ADP-ribose] polymerase 1 [EC:2.4.2.30],von Willebrand factor A domain-containing protein 5
KOG1037Eukaryota (superkingdom)poly [ADP-ribose] polymerase 2/3/4 [EC:2.4.2.30],poly [ADP-ribose] polymerase 1 [EC:2.4.2.30],von Willebrand factor A domain-containing protein 5
HWAGUMetazoa (kingdom)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30],poly [ADP-ribose] polymerase 2/3/4 [EC:2.4.2.30],uncharacterized protein
946BNChordata (phylum)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
5QC8MSarcopterygii (superclass)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
8ZGUEMammalia (class)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
4R28XEuarchontoglires (superorder)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
4ZSAVPrimates (order)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
98KS4Haplorrhini (suborder)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
BVF5QSimiiformes (infraorder)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
9EUUPCatarrhini (parvorder)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
9GU88Vertebrata (clade)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
7JSVBOpisthokonta (clade)poly [ADP-ribose] polymerase 2/3/4 [EC:2.4.2.30],poly [ADP-ribose] polymerase 1 [EC:2.4.2.30],centrosomal protein CEP128
H4Y90Bilateria (clade)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30],poly [ADP-ribose] polymerase 2/3/4 [EC:2.4.2.30],uncharacterized protein
FXEKUHominoidea (superfamily)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
5MZKMHominidae (family)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]
5Y6IXHomininae (subfamily)poly [ADP-ribose] polymerase 1 [EC:2.4.2.30]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: