O60336 · MABP1_HUMAN
- ProteinMitogen-activated protein kinase-binding protein 1
- GeneMAPKBP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1514 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in JNK signaling pathway (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitotic spindle pole | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Biological Process | negative regulation of canonical NF-kappaB signal transduction | |
Biological Process | negative regulation of defense response to bacterium | |
Biological Process | negative regulation of interleukin-8 production | |
Biological Process | positive regulation of JNK cascade |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase-binding protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60336
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Nephronophthisis 20 (NPHP20)
- Note
- DescriptionA form of nephronophthisis, an autosomal recessive chronic tubulo-interstitial nephritis that progresses to end-stage renal failure. Some patients have cystic kidneys of normal size and no extrarenal manifestations, whereas others have enlarged renal size and severe extrarenal defects, including hypertrophic obstructive cardiomyopathy, aortic stenosis, pulmonary stenosis, patent ductus arteriosus, situs inversus, and periportal liver fibrosis. NPHP20 patients do not show extrarenal manifestations or evidence of a ciliopathy, such as situs inversus or polydactyly.
- See alsoMIM:617271
Natural variants in NPHP20
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_077958 | 544 | R>Q | in NPHP20; uncertain significance; no effect on localization at the spindle pole; no effect on interaction with WDR62; no effect on interaction with MAPK9; dbSNP:rs1057519305 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_043343 | 204 | in dbSNP:rs4354909 | |||
Sequence: Y → S | ||||||
Natural variant | VAR_043344 | 313 | in dbSNP:rs1201689 | |||
Sequence: L → V | ||||||
Natural variant | VAR_077958 | 544 | in NPHP20; uncertain significance; no effect on localization at the spindle pole; no effect on interaction with WDR62; no effect on interaction with MAPK9; dbSNP:rs1057519305 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_043345 | 1240 | in dbSNP:rs3959569 | |||
Sequence: R → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,487 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000334158 | 2-1514 | UniProt | Mitogen-activated protein kinase-binding protein 1 | |||
Sequence: AVEGSTITSRIKNLLRSPSIKLRRSKAGNRREDLSSKVTLEKVLGITVSGGRGLACDPRSGLVAYPAGCVVVLFNPRKHKQHHILNSSRKTITALAFSPDGKYLVTGESGHMPAVRVWDVAEHSQVAELQEHKYGVACVAFSPSAKYIVSVGYQHDMIVNVWAWKKNIVVASNKVSSRVTAVSFSEDCSYFVTAGNRHIKFWYLDDSKTSKVNATVPLLGRSGLLGELRNNLFTDVACGRGKKADSTFCITSSGLLCEFSDRRLLDKWVELRNIDSFTTTVAHCISVSQDYIFCGCADGTVRLFNPSNLHFLSTLPRPHALGTDIASVTEASRLFSGVANARYPDTIALTFDPTNQWLSCVYNDHSIYVWDVRDPKKVGKVYSALYHSSCVWSVEVYPEVKDSNQACLPPSSFITCSSDNTIRLWNTESSGVHGSTLHRNILSSDLIKIIYVDGNTQALLDTELPGGDKADASLLDPRVGIRSVCVSPNGQHLASGDRMGTLRVHELQSLSEMLKVEAHDSEILCLEYSKPDTGLKLLASASRDRLIHVLDAGREYSLQQTLDEHSSSITAVKFAASDGQVRMISCGADKSIYFRTAQKSGDGVQFTRTHHVVRKTTLYDMDVEPSWKYTAIGCQDRNIRIFNISSGKQKKLFKGSQGEDGTLIKVQTDPSGIYIATSCSDKNLSIFDFSSGECVATMFGHSEIVTGMKFSNDCKHLISVSGDSCIFVWRLSSEMTISMRQRLAELRQRQRGGKQQGPSSPQRASGPNRHQAPSMLSPGPALSSDSDKEGEDEGTEEELPALPVLAKSTKKALASVPSPALPRSLSHWEMSRAQESVGFLDPAPAANPGPRRRGRWVQPGVELSVRSMLDLRQLETLAPSLQDPSQDSLAIIPSGPRKHGQEALETSLTSQNEKPPRPQASQPCSYPHIIRLLSQEEGVFAQDLEPAPIEDGIVYPEPSDNPTMDTSEFQVQAPARGTLGRVYPGSRSSEKHSPDSACSVDYSSSCLSSPEHPTEDSESTEPLSVDGISSDLEEPAEGDEEEEEEEGGMGPYGLQEGSPQTPDQEQFLKQHFETLASGAAPGAPVQVPERSESRSISSRFLLQVQTRPLREPSPSSSSLALMSRPAQVPQASGEQPRGNGANPPGAPPEVEPSSGNPSPQQAASVLLPRCRLNPDSSWAPKRVATASPFSGLQKAQSVHSLVPQERHEASLQAPSPGALLSREIEAQDGLGSLPPADGRPSRPHSYQNPTTSSMAKISRSISVGENLGLVAEPQAHAPIRVSPLSKLALPSRAHLVLDIPKPLPDRPTLAAFSPVTKGRAPGEAEKPGFPVGLGKAHSTTERWACLGEGTTPKPRTECQAHPGPSSPCAQQLPVSSLFQGPENLQPPPPEKTPNPMECTKPGAALSQDSEPAVSLEQCEQLVAELRGSVRQAVRLYHSVAGCKMPSAEQSRIAQLLRDTFSSVRQELEAVAGAVLSSPGSSPGAVGAEQTQALLEQYSELLLRAVERRMERKL | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 488 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 761 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 785 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 787 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 796 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 819 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 827 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1198 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1263 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1309 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1314 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1357 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via C-terminus) with WDR62 (via C-terminus) (PubMed:23341463, PubMed:28089251).
Interacts with MAPK9 (PubMed:28089251).
Interacts (via N-terminus) with NOD2; the interaction is enhanced in presence of muramyl dipeptide (MDP) (PubMed:22700971).
Interacts with MAPK10 (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 88-129 | WD 1 | ||||
Sequence: SSRKTITALAFSPDGKYLVTGESGHMPAVRVWDVAEHSQVAE | ||||||
Repeat | 132-173 | WD 2 | ||||
Sequence: EHKYGVACVAFSPSAKYIVSVGYQHDMIVNVWAWKKNIVVAS | ||||||
Repeat | 175-213 | WD 3 | ||||
Sequence: KVSSRVTAVSFSEDCSYFVTAGNRHIKFWYLDDSKTSKV | ||||||
Repeat | 276-315 | WD 4 | ||||
Sequence: DSFTTTVAHCISVSQDYIFCGCADGTVRLFNPSNLHFLST | ||||||
Repeat | 342-381 | WD 5 | ||||
Sequence: ARYPDTIALTFDPTNQWLSCVYNDHSIYVWDVRDPKKVGK | ||||||
Repeat | 387-436 | WD 6 | ||||
Sequence: YHSSCVWSVEVYPEVKDSNQACLPPSSFITCSSDNTIRLWNTESSGVHGS | ||||||
Repeat | 477-516 | WD 7 | ||||
Sequence: DPRVGIRSVCVSPNGQHLASGDRMGTLRVHELQSLSEMLK | ||||||
Repeat | 519-561 | WD 8 | ||||
Sequence: AHDSEILCLEYSKPDTGLKLLASASRDRLIHVLDAGREYSLQQ | ||||||
Repeat | 565-606 | WD 9 | ||||
Sequence: EHSSSITAVKFAASDGQVRMISCGADKSIYFRTAQKSGDGVQ | ||||||
Repeat | 614-653 | WD 10 | ||||
Sequence: VRKTTLYDMDVEPSWKYTAIGCQDRNIRIFNISSGKQKKL | ||||||
Repeat | 659-698 | WD 11 | ||||
Sequence: GEDGTLIKVQTDPSGIYIATSCSDKNLSIFDFSSGECVAT | ||||||
Repeat | 701-740 | WD 12 | ||||
Sequence: GHSEIVTGMKFSNDCKHLISVSGDSCIFVWRLSSEMTISM | ||||||
Region | 748-804 | Disordered | ||||
Sequence: RQRQRGGKQQGPSSPQRASGPNRHQAPSMLSPGPALSSDSDKEGEDEGTEEELPALP | ||||||
Compositional bias | 753-782 | Polar residues | ||||
Sequence: GGKQQGPSSPQRASGPNRHQAPSMLSPGPA | ||||||
Region | 880-925 | Disordered | ||||
Sequence: PSLQDPSQDSLAIIPSGPRKHGQEALETSLTSQNEKPPRPQASQPC | ||||||
Compositional bias | 904-920 | Polar residues | ||||
Sequence: ALETSLTSQNEKPPRPQ | ||||||
Region | 951-1256 | Disordered | ||||
Sequence: EDGIVYPEPSDNPTMDTSEFQVQAPARGTLGRVYPGSRSSEKHSPDSACSVDYSSSCLSSPEHPTEDSESTEPLSVDGISSDLEEPAEGDEEEEEEEGGMGPYGLQEGSPQTPDQEQFLKQHFETLASGAAPGAPVQVPERSESRSISSRFLLQVQTRPLREPSPSSSSLALMSRPAQVPQASGEQPRGNGANPPGAPPEVEPSSGNPSPQQAASVLLPRCRLNPDSSWAPKRVATASPFSGLQKAQSVHSLVPQERHEASLQAPSPGALLSREIEAQDGLGSLPPADGRPSRPHSYQNPTTSSMA | ||||||
Compositional bias | 990-1014 | Polar residues | ||||
Sequence: SEKHSPDSACSVDYSSSCLSSPEHP | ||||||
Compositional bias | 1033-1050 | Acidic residues | ||||
Sequence: LEEPAEGDEEEEEEEGGM | ||||||
Compositional bias | 1058-1072 | Polar residues | ||||
Sequence: GSPQTPDQEQFLKQH | ||||||
Compositional bias | 1091-1138 | Polar residues | ||||
Sequence: RSESRSISSRFLLQVQTRPLREPSPSSSSLALMSRPAQVPQASGEQPR | ||||||
Region | 1299-1336 | Disordered | ||||
Sequence: DIPKPLPDRPTLAAFSPVTKGRAPGEAEKPGFPVGLGK |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 6 isoforms produced by Alternative splicing.
O60336-1
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.
- Name1
- Length1,514
- Mass (Da)163,818
- Last updated2008-11-25 v4
- Checksum13FD125E44CABBFD
O60336-2
- Name2
- Differences from canonical
- 274-279: Missing
- 1134-1410: Missing
O60336-3
- Name3
- Differences from canonical
- 274-396: Missing
- 1411-1412: Missing
O60336-4
- Name4
- Differences from canonical
- 1-499: Missing
O60336-5
- Name5
O60336-6
- Name6
- Differences from canonical
- 274-279: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_033629 | 1-499 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_033630 | 214-215 | in isoform 5 | |||
Sequence: NA → RC | ||||||
Alternative sequence | VSP_033631 | 216-1514 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_033633 | 274-279 | in isoform 2 and isoform 6 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_033632 | 274-396 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 753-782 | Polar residues | ||||
Sequence: GGKQQGPSSPQRASGPNRHQAPSMLSPGPA | ||||||
Sequence conflict | 843 | in Ref. 8; AAH36660 | ||||
Sequence: P → S | ||||||
Compositional bias | 904-920 | Polar residues | ||||
Sequence: ALETSLTSQNEKPPRPQ | ||||||
Compositional bias | 990-1014 | Polar residues | ||||
Sequence: SEKHSPDSACSVDYSSSCLSSPEHP | ||||||
Compositional bias | 1033-1050 | Acidic residues | ||||
Sequence: LEEPAEGDEEEEEEEGGM | ||||||
Compositional bias | 1058-1072 | Polar residues | ||||
Sequence: GSPQTPDQEQFLKQH | ||||||
Compositional bias | 1091-1138 | Polar residues | ||||
Sequence: RSESRSISSRFLLQVQTRPLREPSPSSSSLALMSRPAQVPQASGEQPR | ||||||
Alternative sequence | VSP_033634 | 1134-1410 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_033635 | 1411-1412 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1444 | in Ref. 5; AL833267 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB177850 EMBL· GenBank· DDBJ | BAD66828.1 EMBL· GenBank· DDBJ | mRNA | ||
AB011168 EMBL· GenBank· DDBJ | BAA25522.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK292414 EMBL· GenBank· DDBJ | BAF85103.1 EMBL· GenBank· DDBJ | mRNA | ||
AL833267 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AC020659 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC073657 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471125 EMBL· GenBank· DDBJ | EAW92516.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC036660 EMBL· GenBank· DDBJ | AAH36660.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113983 EMBL· GenBank· DDBJ | AAI13984.1 EMBL· GenBank· DDBJ | mRNA | ||
BC114493 EMBL· GenBank· DDBJ | AAI14494.1 EMBL· GenBank· DDBJ | mRNA |