wanglab/gogpt-training-data huggingface dataset:
Protein: NOT1 (Q38C90)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cell differentiation protein, putative
- Uncharacterized protein
- NOT2/NOT3/NOT5 C-terminal domain-containing protein
- poly
- Probable eukaryotic initiation factor 4A
- Endonuclease/exonuclease/phosphatase domain-containing protein
- Endonuclease/exonuclease/phosphatase, putative
- CCR4-NOT transcription complex subunit 10
- Diphthine--ammonia ligase
- Transcription activator, putative
Sequence:
MLYEHTTDIGSSRGAAARYLIASATKSSLQTTLQALEKIAGQSVELYRFVVSAAVSSIWTPPQTEEKNLLVSKLVSTALEKSNALTLVSAAVDESPVTVTKESLVTLMTRDLKLTPPQQLQFAMGLLAGSKKGKEAAAEFLNGISVAQYTVKEDVASLWSYSVLARQLGDVQALETQLSAAAAGAAGGANDRVTVLPHDGVVDMHVSLSRIIDELGTACVATPADCRELLSLFPRPVTQVDVADVVGFFASQGSAPTDTNTYNALMASAGREPTKVQQNAAISPFPLLELLQERVQEPVDWDTVLRMLDKSNEGPFVRKHVSIVFDAYCKFKGTGTPGVYPPITIFLGRWSNVGRQRTVLEYILKHPEKVSMQGLSCDQMAPIELVEVDAADAASSPTTSGASASPSTVPESRAGEVELWRYFPFLEAAVHVASRDGAFDAETLRPAALRYPLLMLYSLLFGSFPGTMKNFSTAKLILRDSRLPLERVATTIIPEAERRGKLNTVISLLSELTIVVPSRTIDVMEAVLKTKNAVRAFLAVGGNPRLVTAIAMCMDESNEGGGGGANCGVSGGAGDSWISKALEGKLHFRAHAAENRFAVATSIVEVAEQLLDKQKYVPKATAALNTFLASSLKDLLRDVAEQARILLASTDSLFPTDVENDATEFYRRMYKAGDPTISASLAFIEQLLKSSKSRDKQLCACIVSIMFEECNAIGCYPHKELQLFATLYGQMIARELLPPNQQQRAWTLLLPVIVKPTDHLVEEYGIIALEQIKPRLAEWPQYGRALRHVKDLDIRIPGIMAAINRGIKAEEAARQSQSRAQNQEKTTQQQKEVESLLSDPAVLALSTERRDNMLAAEQQKDRVAAATLHQHDIGTLLSKKNITAPPRVIQEQINFIIGNTDLHNVENNARELAKQLRPEYYEFFAEYFVVKRAALEPNYHPTYLNLLNNLQSKQLEKAIRSATVSSIKLLLSSDKIRADPGERSLLKNLGYWLGLLTLAKNIPITAQELCFKDLIILGLREGKLMAVVSCIARVLHHCMDSRFFCPPNPWTMRQLCLLWEMYNLRNLRVTLRFEVDLLCKHMNVKLEEIEQYYNMHPIHSSTQLCISDVYREINIHQSADFRVDKMELQDVVQQPHKQVQQPQQAAQPQLQTQAARANRPLQANAEPFKPKDSMVPSGGALAFEAVGPRRPPIVITPETVRVSEEEASLFGERLAVYKGYLAKTLERVTQELKPTVQRSGTIAAVTACHITTKDFLFDRDIKAQLRAADAMARSLASNLCTVAIRDALPEPFNVQVGDLISRLIDVNVPSYTERRERLKGLIRENNMDLCVRALEWQAAEEGAKRLHEKLDKIIKEKIDQITAREPPRAPKEYHDVRDLLMHMGEVLRPPHNLPPLQRAVYEEFNNSVPVVGLLTAYVRTLEDATVQHYSTGDAKVLSLTSPEFANGHFGESHDVIRTRVIGISNIINAETAIYCVGPMLRKLFVLAGAMKRADSGTAASNDLTTARHRNVCNLLNEVYLFVLQTCYERGGDIIREELTQLYLQAEQRWSYTDLAVNLLRIKVLNVSRFDAALSKALLAEGMGRQGVVDFAGATLSRVIVNEKLLSAKELRDTVSQLESIASKQDNQTPRQQQNQPKQQRHQPQSQQLPASGQDSGAMGGAQMAPGGAAPTNAMRASPALSNLVEQHVRRLVVPTLAPQNQEDAEKIRGLFEEWLIVNARRMHSSSSESNQASGAATNAPSQEGATAPTTSSPASATAAPTSTTSAALPGNKPPPQYEYMMKLRDNKQLDGPQLRTFLTTSLRFCVEHYATKSLELERSNPAVLGRALTAEWKPGNAPPHRYQYDDGLFTHVDALSDLVTVLLYYCSLKNESRTLLTLLRRVLDAFQWALIDNHQAVVVRLQQAQNPNHLGNAKSELPAGTAYAPMFQQQPYVRFFSNLFTTLVRADSPKRETMEQITSAFADTLHNLPPLKYPAFTFGWLELVSHRIFLNRCLRSPVPWPSYVALLVQGLEFIERFTREGNISKNVLVFYKAFFKLMLVLTHDYSRFLITYHYQLCDAIPPYCVQLLNTVLCSFPSGVKLPEFFARVPDDGSEMRKHPATDNQVKCIEESFKQHHFDGNALSEKLQDDRPMSESYMQSIVEKLQSLHNWRLMNAIVLHVCIVYLQVNDHAVKPNFPESNAMRFYRHLAGSLDHEHRYYFICSCANHLRYPNCQTNFFVKVISNLFLPHRSIRNAVVQQCIQEQITRVAVEKTLIIQPHPWGVLSTFMELMRAPEYGFWEKSFICSTSFLESMFTKLRRSVESRNAQQQVQQSTGSASTSATQGKK
Protein: Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1) (O43806)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDGSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATD
Protein: KCNQ potassium channel, isoform H (A0A0B4KEI9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDPDNDIYAFYDIRGYKGKCRPGRPNSERILQPRMSLLGKPLNYNRGTRRDVRYRRLQSRLYNFLERPRGLHAIFYHVMVFLMVFTCLALSVFSTIKEYEEDAVYILFRMEILVVIWFTMEFGARLWSSGCRSRYQGCLGRLKFVKRPFCIIDIVTILASIVVLGMGTSGQVFATSALRGLRFFQILRMVRMDRRGGTWKLLGSVVYAHRQELITTMYIGFLGLIFASFLVYMWEKDVNDKFSNFAQALWWGVITLCTVGYGDMVPITWQGKLIASCCALLGISFFALPAGILGSGFALKVQQQQRQKHMIRRRQPAATLIQAVWRCYAADEHSVSVATWNIHRVALPSPPASSENWERLLKNITEYRRASSSFKHNTSFVARLPTIRRHKSQTIQTPGGGDGGGVSKPPGSSRASTRYTRTIRDINASVENLDEEDEPRCTQLTNRHKTAIRFIRKLKYFVARRKFKEALKPYDVKDVMEQYAAGHVDLLGRVKMLHLRLDQILGKQGSKAKDVYASKISLASRVVKVERQVADIEEKLDILIKAYMEDRDRFLALPLPAKPKIHSISPSHKPLHHAHNLAMIDVWKRTAALSVHPEQVTTTPLLNPSAPDSSELRSLTATQTPTTTTDAIATQTPMPPHVQHTATNTKSSVLNSYQLGSEKQQHNDVFMTELENRTKKRVTLSLHRSTSEPYSKQEQRITIPDEGADSLDSSAKPTPPDSSIILIDEYEDFEEEDLNCEGEMDHFPTWEIDSDIGVEVDVDADADGDCDESTEDTALLQCATRTAIVITPISPVSSAHNLQQLNDQTTTLNKSNLLPPDSG
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial (EC 7.1.1.2) (Complex I-23kD) (CI-23kD) (NADH-ubiquinone oxidoreductase 23 kDa subunit) (Q8K3J1)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (By similarity). Essential for the catalytic activity and assembly of complex I (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
Sequence:
MYRLSSSMLPRALAQAMRTGHLNGQSLHSSAVAATYKYVNKKEQESEVDMKSATDNAARILMWTELIRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR
Protein: Chitinase-like protein 3 (EC 3.2.1.52) (Beta-N-acetylhexosaminidase Ym1) (Chitinase-3-like protein 3) (ECF-L) (Eosinophil chemotactic cytokine) (Secreted protein Ym1) (O35744)
Organism: Mus musculus (Mouse)
Function: Lectin that binds saccharides with a free amino group, such as glucosamine or galactosamine. Binding to oligomeric saccharides is much stronger than binding to mono- or disaccharides. Also binds chitin and heparin. Has weak hexosaminidase activity but no chitinase activity. Has chemotactic activity for T-lymphocytes, bone marrow cells and eosinophils. May play a role in inflammation and allergy.
Subcellular location: Secreted. Rough endoplasmic reticulum lumen. Nucleus envelope. Cytoplasm. Cytoplasmic granule. Note=Predominantly localizes to the lumen of rough endoplasmic reticulum (rER) and nuclear envelope in alveolar macrophages. Localizes to the dilated lumen of rER in immature neutrophils in spleen and in cytoplasmic granules in peritoneal neutrophils. Detected in needle-shaped crystals present in the cytoplasm of bone marrow macrophages.
Interaction partners:
- Resistin-like alpha
- Arginase-1
- Macrophage mannose receptor 1
- Interleukin-4
- Chitinase-like protein 4
- Interleukin-10
- Interleukin-13
- Interleukin-1 beta
- Nitric oxide synthase, inducible
- Tumor necrosis factor
Sequence:
MAKLILVTGLAILLNVQLGSSYQLMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESVEKDIPRLLLTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSGSFCHQRHFPLTSTLKGDLNIHSASCKGPY
Protein: Proenkephalin-A [Cleaved into: Synenkephalin; Met-enkephalin (Opioid growth factor) (OGF); PENK(114-133); PENK(143-185); Met-enkephalin-Arg-Gly-Leu; Leu-enkephalin; PENK(239-260); Met-enkephalin-Arg-Phe] (P04094)
Organism: Rattus norvegicus (Rat)
Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
Subcellular location: Secreted {ECO:0000269|PubMed:19164277}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000250|UniProtKB:P01211}.
Interaction partners:
- Mu-type opioid receptor
- Delta-type opioid receptor
- Pro-opiomelanocortin
- Nociceptin receptor
- Kappa-type opioid receptor
- Proenkephalin-B
- Protachykinin-1
- Somatostatin
- Corticoliberin
- Neurotensin/neuromedin N
Sequence:
MAQFLRLCIWLLALGSCLLATVQADCSQDCAKCSYRLVRPGDINFLACTLECEGQLPSFKIWETCKDLLQVSKPEFPWDNIDMYKDSSKQDESHLLAKKYGGFMKRYGGFMKKMDELYPVEPEEEANGGEILAKRYGGFMKKDADEGDTLANSSDLLKELLGTGDNRAKDSHQQESTNNDEDSTSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAESLPSDEEGESYSKEVPEMEKRYGGFMRF
Protein: Protein RADIALIS-like 6 (AtRL6) (Protein RAD-like 6) (Protein RADIALIS-LIKE SANT/MYB 3) (Protein RSM3) (Q1A173)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- C2H2 and C2HC zinc fingers superfamily protein
- At2g21530
- C2H2 and C2HC zinc fingers superfamily protein
- Glycosyltransferase
- AAA-type ATPase family protein
- Zinc finger CCCH domain-containing protein 18
- Nuclear transcription factor Y subunit C-5
- 1-aminocyclopropane-1-carboxylate oxidase homolog 1
- Transcription factor bHLH96
Sequence:
MASNSRSSISPWTFSQNKMFERALAVYDKDTPDRWHNVAKAVGGKTVEEVKRHYDILVEDLINIETGRVPLPNYKTFESNSRSINDFDTRKMKNLKI
Protein: Large ribosomal subunit protein bL20m (39S ribosomal protein L20, mitochondrial) (L20mt) (MRP-L20) (Q9CQL4)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q2TBR2}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS3
Sequence:
MVFLTTRLWLRNRLTDRYWRVQEVLKHAQHFRGRKNRCYRLAVRAVTRAFVKCTKARRLKKRNLRTLWINRITAASQEHGLKYPAFIVNLIKCQVELNRKVLVDLAIYEPKTFKSLAALAKRRQQEGFAAALGDGKEPEGIFSRVVQYH
Protein: Cell adhesion molecule CEACAM8 (CD67 antigen) (Carcinoembryonic antigen CGM6) (Carcinoembryonic antigen-related cell adhesion molecule 8) (CEA cell adhesion molecule 8) (Non-specific cross-reacting antigen NCA-95) (CD antigen CD66b) (P31997)
Organism: Homo sapiens (Human)
Function: Cell surface glycoprotein that plays a role in cell adhesion in a calcium-independent manner. Mediates heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6. Heterophilic interaction with CEACAM8 occurs in activated neutrophils.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2208113}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2208113}. Cell surface {ECO:0000269|PubMed:8776764}.
Interaction partners:
- Defensin alpha 4
- Cell adhesion molecule CEACAM6
- Myeloperoxidase
- Neutrophil elastase
- B-lymphocyte antigen CD19
- Neutrophil collagenase
- Lactotransferrin
- Low affinity immunoglobulin gamma Fc region receptor III-B
- Cathelicidin antimicrobial peptide
- Integrin alpha-M
Sequence:
MGPISAPSCRWRIPWQGLLLTASLFTFWNPPTTAQLTIEAVPSNAAEGKEVLLLVHNLPQDPRGYNWYKGETVDANRRIIGYVISNQQITPGPAYSNRETIYPNASLLMRNVTRNDTGSYTLQVIKLNLMSEEVTGQFSVHPETPKPSISSNNSNPVEDKDAVAFTCEPETQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLLSVTRNDVGPYECEIQNPASANFSDPVTLNVLYGPDAPTISPSDTYYHAGVNLNLSCHAASNPPSQYSWSVNGTFQQYTQKLFIPNITTKNSGSYACHTTNSATGRNRTTVRMITVSDALVQGSSPGLSARATVSIMIGVLARVALI
Protein: Agglutinin (RCA) [Cleaved into: Agglutinin A chain (EC 3.2.2.22) (rRNA N-glycosidase); Agglutinin B chain] (P06750)
Organism: Ricinus communis (Castor bean)
Interaction partners:
Sequence:
MYAVATWLCFGSTSGWSFTLEDNNIFPKQYPIINFTTADATVESYTNFIRAVRSHLTTGADVRHEIPVLPNRVGLPISQRFILVELSNHAELSVTLALDVTNAYVVGCRAGNSAYFFHPDNQEDAEAITHLFTDVQNSFTFAFGGNYDRLEQLGGLRENIELGTGPLEDAISALYYYSTCGTQIPTLARSFMVCIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFNVYDVSILIPIIALMVYRCAPPPSSQFSLLIRPVVPNFNADVCMDPEPIVRIVGRNGLCVDVTGEEFFDGNPIQLWPCKSNTDWNQLWTLRKDSTIRSNGKCLTISKSSPRQQVVIYNCSTATVGATRWQIWDNRTIINPRSGLVLAATSGNSGTKLTVQTNIYAVSQGWLPTNNTQPFVTTIVGLYGMCLQANSGKVWLEDCTSEKAEQQWALYADGSIRPQQNRDNCLTTDANIKGTVVKILSCGPASSGQRWMFKNDGTILNLYNGLVLDVRRSDPSLKQIIVHPFHGNLNQIWLPLF
Protein: Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1) (PKU-beta) (Tousled-like kinase 1) (Q9UKI8)
Organism: Homo sapiens (Human)
Function: Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'.
Subcellular location: Nucleus {ECO:0000269|PubMed:10523312, ECO:0000269|PubMed:10588641, ECO:0000269|PubMed:11314006, ECO:0000269|PubMed:9427565}.
Interaction partners:
- Serine/threonine-protein kinase tousled-like 2
- Histone chaperone ASF1A
- Histone chaperone ASF1B
- Cell cycle checkpoint control protein RAD9A
- Serine/arginine-rich splicing factor 1
- Histone H3.1
- Histone H3.3
- Histone H3.2
- Histone H3.1t
- Histone H3-7
Sequence:
MSVQSSSGSLEGPPSWSQLSTSPTPGSAAAARSLLNHTPPSGRPREGAMDELHSLDPRRQELLEARFTGVASGSTGSTGSCSVGAKASTNNESSNHSFGSLGSLSDKESETPEKKQSESSRGRKRKAENQNESSQGKSIGGRGHKISDYFEYQGGNGSSPVRGIPPAIRSPQNSHSHSTPSSSVRPNSPSPTALAFGDHPIVQPKQLSFKIIQTDLTMLKLAALESNKIQDLEKKEGRIDDLLRANCDLRRQIDEQQKLLEKYKERLNKCISMSKKLLIEKSTQEKLSSREKSMQDRLRLGHFTTVRHGASFTEQWTDGFAFQNLVKQQEWVNQQREDIERQRKLLAKRKPPTANNSQAPSTNSEPKQRKNKAVNGAENDPFVRPNLPQLLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRINNEDNSQFKDHPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRSNSSGNLHMAGLTASPTPPSSSIITY
Protein: Acyl-CoA (8-3)-desaturase (EC 1.14.19.44) (Delta(5) fatty acid desaturase) (D5D) (Delta(5) desaturase) (Delta-5 desaturase) (Fatty acid desaturase 1) (O60427)
Organism: Homo sapiens (Human)
Function: Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively. As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, controls the metabolism of inflammatory lipids like prostaglandin E2, critical for efficient acute inflammatory response and maintenance of epithelium homeostasis. Contributes to membrane phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl chain esterified into phospholipids. In particular, regulates phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory cytokine production in T-cells (By similarity). Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6) (By similarity).
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A4UVI1}. Mitochondrion {ECO:0000269|PubMed:22619218}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A4UVI1}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A4UVI1}.
Interaction partners:
- Very long chain fatty acid elongase 2
- Lathosterol oxidase
- Stearoyl-CoA desaturase
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very long chain fatty acid elongase 5
Sequence:
MAPDPVAAETAAQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFHINKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFALGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKKWVDLAWMITFYVRFFLTYVPLLGLKAFLGLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKESGQLWLDAYLHQ
Protein: Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylethanolamine hydrolase ASAH1) (EC 3.5.1.-) (N-acylsphingosine amidohydrolase) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta] (Q6P7S1)
Organism: Rattus norvegicus (Rat)
Function: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (By similarity). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (By similarity). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (By similarity). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (By similarity). Has also an N-acylethanolamine hydrolase activity (By similarity). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (By similarity). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000250|UniProtKB:Q13510}.
Interaction partners:
- Alkaline ceramidase
- Neutral ceramidase
- Alkaline ceramidase
- Ceramide kinase
- RCG53912, isoform CRA_a.
- Sphingosine kinase 1
- Alkaline ceramidase
- Ceramide synthase 2
- Ceramide glucosyltransferase
- Ceramide synthase 5
Sequence:
MLGRSLLTWVLAAAVTCAQAQQVPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELLAHKAPVLRTLVNSISNLVNAFVPSGKIMQMVDEKLPGLIGSIPGPFGEEMRGIADVTGIPLGEIISFNIFYELFTMCTSIITEDGKGHLLHGRNMDFGIFLGWNINNNTWVVTEELKPLTVNLDFQRNNKTVFKATSFAGYVGMLTGFKPGLLSLTLNERFSLNGGYLGILEWMFGKKNAQWVGFITRSVLENSTSYEEAKNILTKTKITAPAYFILGGNQSGEGCVITRERKESLDVYELDPKHGRWYVVQTNYDRWKNTLFLDDRRTPAKKCLNHTTQKNLSFATIYDVLSTKPVLNKLTVFTTLIDVTKDQFESHLRDCPDPCIGW
Protein: Scaffold attachment factor B2 (SAF-B2) (Q80YR5)
Organism: Mus musculus (Mouse)
Function: Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MAEPGTGSGDPAFGPGASESGTRRLSDLRVIDLRAELKKRNLDTGGNKSVLMERLRKAFKEEGQEPEEVGISWGAVSKRAVKRNTKGSKMEEEGSEDNGLEEDSRYGQDGVVILQSSQDRDTMDTGVPDGMEAEDLSVPCLGKADTVNQILHAFDDSKEYVAAQLGQLPAQLLKHAVDEEVFKNTLEASVSDLKVTLADEEAPMEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEDQEEEQEEEGDLALASSSKSESPSTRCQWSEADAPLAVVKRELADAPGGGGGTRHRRKRKRRRKHQAQAEALGTGGGAGMNCEPVGLEEPVEQSSTAAQLPEATSQELVRAPTAALSPEPQDSKEDVKKFAFDACNDVPAPPKESSASEGADQKMSSVKEEQDIKPVIKDEKGRASCSSGRNLWVSGLSSSTRAADLKSLFSKHGKVIGAKVVTNARSPGARCYGFVTMSTSDEATKCISHLHRTELHGRMISVEKAKNEPSEKKSSDRRACDQKEKVPGPDRPHPVKIKTEKTVIKKEEKLERKEEKGPEDIKKEKDQDELTPGAAGHSRVTKSGSRGMERTVVMDKSKGEPVISVKATSRSKDRSSKSQDRKSEGREKRDILSFDKIKEQRERERQRQREREIRETERRREREQREREQRLDAFQERREKARLQRERMQLQCQRQRLERERLERERLERERMRVERERRKEQQRIMREREELRRQQEQLRAEQERRALRRPYDLDARRDDGYWPEGKRAALEDRYRDFPRPDHRFHDFDHRDRGHYQEHVIDRRDGSRTRVEERDGQYYPDDQHSHGRLLEHHAWDSGDGWHGYSSDKKLNEGQGLPPPPRVSREWAEHSSQLEEQQVPVWHSAVDTNMTGHEHIRWRGAERGLAGGPGHGHVAAGRGGMAGQGSFAHGGHSQGYIVPSGRLEGGGMASQDQGGRVPNPHPHPHFTRRY
Protein: alpha-amylase (EC 3.2.1.1) (Q8N0Q6)
Organism: Drosophila kikkawai (Fruit fly)
Interaction partners:
Sequence:
MFLTKSIVCLAILALASAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAANGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIAEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGRLKNLNTDHGFSSGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKSQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFNSDNSCSGGWVCEHRWRQIYNMVAFRNAVGSDAIQNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGTKNGSSCTGKTVTVGSDGRASIYLGNSEDDGVLAIHVNAKL
Protein: AP-4 complex subunit mu-1 (E2RED8)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system (By similarity). It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. Within AP-4, the mu-type subunit AP4M1 is directly involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos. The adaptor protein complex 4 (AP-4) may also recognize other types of sorting signal (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11802162}; Peripheral membrane protein {ECO:0000305}. Early endosome {ECO:0000269|PubMed:11802162}. Note=Found in soma and dendritic shafts of neuronal cells. {ECO:0000250|UniProtKB:Q2PWT8}.
Interaction partners:
- AP complex subunit beta
- AP complex subunit sigma
- Adaptor related protein complex 4 subunit epsilon 1.
- TEPSIN adaptor related protein complex 4 accessory protein.
- AP complex subunit beta.
- Autophagy-related protein 9
- AP complex subunit beta.
- AP complex subunit sigma
- AP complex subunit sigma
- DDB1- and CUL4-associated factor 11
Sequence:
MISQFFILSSKGDPLIYKDFRGDSGGRDVAELFYRKLTGLPGDESPVVMHHDDRHFIHIRHSGLYLVATTSENISPFSLLELLSRLATLLGDYCGSLSEGTISRNVALVYELLDEVLDYGYVQTTSMEMLRNFIQTEAVVSKPFSLFDLSSVGLFGAETQQSKVAPSTAASRPVLASRSDQSQKNEVFLDVVERLSVLIASNGSLLKVDVQGEIRLKSFLPSGSEMRIGLTEEFCVGKSELRGYGPGIRVDEVSFHSSVLLEEFESHRILRLQPPQGELTVMRYQLSDDLPSPLPFRLFPSVQWDRGSGRLQVYLKLRCDLPPKSQALNVRLHLPLPRGVVSLSQELSGPEQKAELGEGALRWDLPRVQGGSQLSGLFQMDVPGLPGPPGQGHSATAPLGLGPASLSFELPRHTCSGLQVRFLRLAFRPCGSTSPHKWVRHLSHSDAYVIRI