| IED ID |
IndEnz0002009565 |
| Enzyme Type ID |
protease009565 |
| Protein Name |
Spermatogenesis-associated protein 2
|
| Gene Name |
SPATA2 KIAA0757 PD1 |
| Organism |
Homo sapiens (Human) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Euarchontoglires
Primates
Haplorrhini
Simiiformes
Catarrhini
Hominoidea (apes)
Hominidae (great apes)
Homininae
Homo
Homo sapiens (Human)
|
| Enzyme Sequence |
MGKPSSMDTKFKDDLFRKYVQFHESKVDTTTSRQRPGSDECLRVAASTLLSLHKVDPFYRFRLIQFYEVVESSLRSLSSSSLRALHGAFSMLETVGINLFLYPWKKEFRSIKTYTGPFVYYVKSTLLEEDIRAILSCMGYTPELGTAYKLRELVETLQVKMVSFELFLAKVECEQMLEIHSQVKDKGYSELDIVSERKSSAEDVRGCSDALRRRAEGREHLTASMSRVALQKSASERAAKDYYKPRVTKPSRSVDAYDSYWESRKPPLKASLSLRKEPVATDVGDDLKDEIIRPSPSLLTMASSPHGSPDVLPPASPSNGPALLRGTYFSTQDDVDLYTDSEPRATYRRQDALRPDVWLLRNDAHSLYHKRSPPAKESALSKCQSCGLSCSSSLCQRCDSLLTCPPASKPSAFPSKASTHDSLAHGASLREKYPGQTQGLDRLPHLHSKSKPSTTPTSRCGFCNRPGATNTCTQCSKVSCDACLSAYHYDPCYKKSELHKFMPNNQLNYKSTQLSHLVYR |
| Enzyme Length |
520 |
| Uniprot Accession Number |
Q9UM82 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Bridging factor that mediates the recruitment of CYLD to the LUBAC complex, thereby regulating TNF-alpha-induced necroptosis (PubMed:27307491, PubMed:27458237, PubMed:27545878, PubMed:27591049). Acts as a direct binding intermediate that bridges RNF31/HOIP, the catalytic subunit of the LUBAC complex, and the deubiquitinase (CYLD), thereby recruiting CYLD to the TNF-R1 signaling complex (TNF-RSC) (PubMed:27458237, PubMed:27545878, PubMed:27591049). Required to activate the 'Met-1'- (linear) and 'Lys-63'-linked deubiquitinase activities of CYLD (PubMed:27458237, PubMed:27591049). Controls the kinase activity of RIPK1 and TNF-alpha-induced necroptosis by promoting 'Met-1'-linked deubiquitination of RIPK1 by CYLD (By similarity). {ECO:0000250|UniProtKB:Q8K004, ECO:0000269|PubMed:27307491, ECO:0000269|PubMed:27458237, ECO:0000269|PubMed:27545878, ECO:0000269|PubMed:27591049}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (4); Chain (1); Domain (1); Erroneous initiation (1); Helix (12); Modified residue (1); Motif (1); Mutagenesis (6); Natural variant (1); Region (2); Sequence conflict (1); Turn (2) |
| Keywords |
3D-structure;Cytoplasm;Developmental protein;Necrosis;Nucleus;Phosphoprotein;Reference proteome |
| Interact With |
X5D778; Q9UI12; Q53TS8; Q68D86; Q9NQC7; Q5JVL4; P14136; Q08379; O95872; Q92993; Q9BVG8-5; Q96BZ8; Q9BRK4; Q9Y6D9; Q9NU19; Q15025; P14373; Q9Y2P0 |
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10222154, ECO:0000269|PubMed:11079456}. Nucleus {ECO:0000250|UniProtKB:Q66HP6}. Note=Detected in the tubular compartment of the testis and, in the cytoplasm of the Sertoli cells. {ECO:0000269|PubMed:11079456}. |
| Modified Residue |
MOD_RES 253; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" |
| Post Translational Modification |
|
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (2) |
| Cross Reference PDB |
5LJM;
5LJN;
|
| Mapped Pubmed ID |
12531478;
16189514;
18364390;
19389623;
19605492;
19615732;
20385810;
25093496;
25264125;
25416956;
26638075;
30697874;
|
| Motif |
MOTIF 327..344; /note="PIM motif"; /evidence="ECO:0000305|PubMed:27458237, ECO:0000305|PubMed:27545878" |
| Gene Encoded By |
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| Mass |
58,427 |
| Kinetics |
|
| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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