wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized alpha-1,2-galactosyltransferase C8D2.17 (EC 2.4.1.-) (O13640)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized alpha-1,2-galactosyltransferase C637.06
- Mannan polymerase II complex anp1 subunit
- Mannan polymerase complex subunit mnn9
- Alpha-1,2-galactosyltransferase
Sequence:
MFNFRLFSRRGKSLGLLAIVLLLFGFYSLKSSMPVYSNSIGSPSAHSSSYKGVSKAKTSPQDPDSVVMLIVSFDDHYDSSRSDSSSVFLDKVLSDRTEYALRHGYTLVHKKARDIQARYGVYGTWSIIPALRETLAEYPDAGWIWLLDAKAVIMNPSESLKDRVLKPEKLSQHLLLNSPIDPLKNYIRTRRKMDPSDVFVITTSDYNGISTRSLLIKNNNFAPFLLDAWNEPLLKSAGFDQAERSALSHLLEAHNTILDHVALVSPKVLNSYTNSAVDLNYEEGDFLVILQDCENAAACERIFDNYYQQRKLPAIKKQLSEETVDEQS
Protein: Outer envelope pore protein 24, chloroplastic (Chloroplastic outer envelope pore protein of 24 kDa) (O49929)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: High-conductance voltage-dependent solute channel with a slight selectivity for cations transporting triosephosphates, dicarboxylic acids, ATP, inorganic phosphate (Pi), sugars, and positively or negatively charged amino acids.
Subcellular location: Plastid, etioplast membrane {ECO:0000305|PubMed:9668138}; Multi-pass membrane protein. Plastid, chloroplast outer membrane {ECO:0000269|PubMed:9668138}; Multi-pass membrane protein. Note=Present in non-green root plastids.
Interaction partners:
Sequence:
MKAALKGKYDLDHNSSGAATVAFNAGDVKLRASITDATFKNSPSLTGLVLAVEKPGSFSVDYNVPKKDFRFQFMNTVRVAEKPLNLAYIHSKGDNRTILDGTLVWDPSNKVSANYAVESGNCKLKYSYNHKGLTTIEPTYDVAKNSWDFAVSGKVYGDDSLKASYQTSSKVLGLEWTRNSKQTGCFKVVASVNLAEEKKIPKLSVESTLNFEM
Protein: mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) (Q9I1N7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PslA
- PslD
- PslH
- dTDP-Rha:alpha-D-Gal-diphosphoundecaprenol alpha-1,3-rhamnosyltransferase
- PslE
- PslF
- GDP-mannose 6-dehydrogenase
- PslG
- Phosphomannomutase/phosphoglucomutase
- GDP-mannose 4,6-dehydratase
Sequence:
MNAVAPLIPCIVSGGSGTRLWPVSRESMPKPFMRLADDQSLLQKTFLRIAGLPDVARLLTVTNRDLLFRTLDDYRAVNRSGLAQDLLLEPVGRNTAPAIAAAALHVQEHFGDQAQLLILPADHLIRDEQAFAAAVAEARGLAAQGYLVTFGITPERAETGFGYIEQGAPLGNGFRVARFVEKPDQATAQSYLDSGKYLWNAGMFCFQAATVLQELERHAPEVLIAARAALADGSSLENGQCRQRELAAGAFAEAPDISVDYALMERSDKVAVVPCSIGWSDIGSWQALRELSAADENGNQVRGESVLHDVSNCYIDSPKRLVGAVGVHDLIIVDTPDALLVADAARSQDVKFVAQELKRRGHDAFRLHRTVSRPWGTYTVLEEGRRFKIKRIVVRPKASLSLQMHHHRSEHWIVVSGMALVENGEREFLLNTNESTFIPAGHSHRLSNPGIIDLVMIEVQSGEYLGEDDIVRFNDIYGRAPASDEKKA
Protein: Probable indole-3-acetic acid-amido synthetase GH3.13 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 13) (OsGH3-13) (OsGH3-14) (Q2R3B4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May catalyze the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin.
Interaction partners:
- Indole-3-acetic acid-amido synthetase GH3.8
Sequence:
MTSTSSENAPDHDHDHDASSPAPATATAAALPPMIPACDPHDGPACLELIEVLTTRAAAVQRRVLAEVLAMNTGTDYLRRFLGDEVVAAAGGEDELAAAFKERVPVVEYEDVKPYIERIANGAPSSLISSKPITELLTSSGTSGGQPKLMPATEEELDRKTFLYNLLVPVMNKYVEGLDEGRGMYLLFVKPEITTASGMVARPVLTSYYKSRHFRRRPDSPYTRYTSPDAAILCPDSRQSMYAQLLCGLARRGEVLRVGAVFASAFLRAVKFLEGHWRALCADIRAGRADPAVVTDAACRGAVDAVLAARADPDLADAIAAECGGASWRGIVRRLWPRTKYIDVIVTGSMAQYIPLLEFYGGGLPLVSTMYASSESYFGINLRPLDPPEEVVYTLLPNMCYYEFIKVEKDGDGEKVRDGEVVDLVGVEVGAYYELVVTTFTGERVCSPFDFFPTSCMGLSTPSDRKING
Protein: High mobility group nucleosome binding domain 5 (Q5JSK9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPKRKMLVPVTPEVKPKRTSSSRKMKTKSDMMEENIDTSAQAVAETKQEAVVEEDYNENAKNGEAKITEAPASEKEIVEVKEENIEDATEKGGEKKEAVAAEVKNEEEDQKEDEEDQNEEKGEAGKEDKDEKGEEDGKEDKNGNEKGEDAKEKEDGKKGEDGKGNGEDGKEKGEDEKEEEDRKETGDGKENEDGKEKGDKK
Protein: Accessory gland protein Acp36DE (Q9V3R1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for physiological and behavioral changes in mated female flies. Associates with sperm and localizes to specific regions of the female reproductive tract, including the sperm storage organs. It accelerates sperm accumulation into storage but does not mediate the entry of the first sperm into storage. Once sperm storage has initiated it seems to act as a guidance factor helping subsequent sperm move into storage, a corral concentrating sperm around the SSO entrances and/or a trigger for responses within the female that accelerate storage of sperm.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Accessory gland-specific peptide 26Aa
- ACP53C14A
- Accessory gland protein Acp62F
- Accessory gland-specific peptide 70A
- Accessory gland protein Acp29AB
- Accessory gland protein Acp53Ea
- Accessory gland protein Acp76A
- Accessory gland protein Acp63F
- Serpin 38F, isoform A
- Uncharacterized protein, isoform A
Sequence:
MWTLTCQQFIALILLGTLVPSESFLCKHCFRKNLEKVHESFRDILSPPIFGVNPQPLIEVQQPKVTPKPESSQVIHVHQPQVILKPIYYPKVDTISTKNQIGIHGPYSQYPSLLPSANLLGIPNQQLINAQDVLSDKDQKQTQVQNNNLHIRFGVSALREGRNNPSLETISRDKVDKISPALQLQLLRYADSQSQSQTQSQSASQSESNASSQFQAQEQSNRLLENPPVSESQSQSESQSQSESQKQSQSQSQRQQQIQTQLQILRQLQQKSNEQSAAQSASQIQSQRQSDSQSNLQLQEQSQSQSEQGKPIQSQIQILQGLQQKELDDKSASQSQSESKTRQEQQKQLNLQQLEELSSSLSQSRLGLGQQIQSQLQKNQLDKQFASQFQSQSKSQLEQQMQLQLQSLRQLQQKQLDEQSASQSQPQSQVAQQIQSHLQLLRLLQSRLKTQSALKSDLEQQILLQLKKLTEVQQKQLAEQPTLRPSSKSQSPGQLEQQILLQLQNLLQFQQNQLKSDTQTQSQLQESKSNSLSQSQSQSQEQLQLQRDQNLRQLEQIKLEMQNIRELLQKGKSELQTQSDSQRRIHELYQNILQLNKEKLSYQLKQLKLKELEDQKKSQAEISKGSNPSNLFIIGQLPSEGKPAPGNQGPSIEPKLVPQPGSLDKLPSGGGLIGKPASTGLYILSPDFNDLSDYRDQFRLQQELKKHQNILSLLQRRQNDIKKQQNAQLLLGQQQKEQQAQESINKQQSSSAGSSSQTKLQQDIQSTGAQGSQQGLQAGSTGLQTSSLQGTESSASQSAALQRLKEQEQLRIQTENDQKTSSSSSHSNSQNSQSSSSQSSQASQSEAQRQEAGNRNTLLLDQSSSKTQSESKSESSSQSSSHSSSQSTSNSSSNVQSKLQGESQALLNNLSG
Protein: Syntrophin beta 2 (H0YCS0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
XGRENRMPILISKIFPGLAADQSRALRLGDAILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGAAPQSPSFSGSEDSGSPKHQNSTKDRKIIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWQN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q86BR9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQRRERQASGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCDGHPEEFATYLRYVRRLDFFETPDYDFLRRLFQDLFDRKGYTDEGEFDWTGKTMSTPVGSLQTGHEVIISPNKDRHNVTAKTNAKGGVAAWPDVPKPGATLGNLTPADRHGSVQVVSSTNGELNPDDPTAGHSNTPITQQPEVEVVDETKCCCFFKRKKKKSTRQK
Protein: Protein phosphatase 1F (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase) (CaM-kinase phosphatase) (CaMKPase) (Partner of PIX 2) (Protein fem-2 homolog) (hFem-2) (P49593)
Organism: Homo sapiens (Human)
Function: Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type 1
- Calmodulin-1
- Cullin-2
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
Sequence:
MSSGAPQKSSPMASGAEETPGFLDTLLQDFPALLNPEDPLPWKAPGTVLSQEEVEGELAELAMGFLGSRKAPPPLAAALAHEAVSQLLQTDLSEFRKLPREEEEEEEDDDEEEKAPVTLLDAQSLAQSFFNRLWEVAGQWQKQVPLAARASQRQWLVSIHAIRNTRRKMEDRHVSLPSFNQLFGLSDPVNRAYFAVFDGHGGVDAARYAAVHVHTNAARQPELPTDPEGALREAFRRTDQMFLRKAKRERLQSGTTGVCALIAGATLHVAWLGDSQVILVQQGQVVKLMEPHRPERQDEKARIEALGGFVSHMDCWRVNGTLAVSRAIGDVFQKPYVSGEADAASRALTGSEDYLLLACDGFFDVVPHQEVVGLVQSHLTRQQGSGLRVAEELVAAARERGSHDNITVMVVFLRDPQELLEGGNQGEGDPQAEGRRQDLPSSLPEPETQAPPRS
Protein: Taste receptor type 2 member 5 (T2R5) (Q9NYW4)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Taste receptor type 1 member 2
- Taste receptor type 1 member 3
- Taste receptor type 1 member 1
Sequence:
MLSAGLGLLMLVAVVEFLIGLIGNGSLVVWSFREWIRKFNWSSYNLIILGLAGCRFLLQWLIILDLSLFPLFQSSRWLRYLSIFWVLVSQASLWFATFLSVFYCKKITTFDRPAYLWLKQRAYNLSLWCLLGYFIINLLLTVQIGLTFYHPPQGNSSIRYPFESWQYLYAFQLNSGSYLPLVVFLVSSGMLIVSLYTHHKKMKVHSAGRRDVRAKAHITALKSLGCFLLLHLVYIMASPFSITSKTYPPDLTSVFIWETLMAAYPSLHSLILIMGIPRVKQTCQKILWKTVCARRCWGP
Protein: Luciferin 4-monooxygenase (EC 1.13.12.7) (Q9VCC6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Acyl-coenzyme A oxidase
Sequence:
MTSKLLPGNIVYGGPVTERQAQDSRSLGQYILDKYKSFGDRTVLVDAVNGVEYSASFMHKSIVRLAYILQKLGVKQNDVVGLSSENSVNFALAMFAGLAVGATVAPLNVTYSDREVDHAINLSKPKIIFASKITIDRVAKVASKNKFVKGIIALSGTSKKFKNIYDLKELMEDEKFKTQPDFTSPAANKDEDVSLIVCSSGTTGLPKGVQLTQMNLLATLDSQIQPTVIPMEEVTLLTVIPWFHAFGCLTLITTACVGARLVYLPKFEEKLFLSAIEKYRVMMAFMVPPLMVFLAKHPIVDKYDLSSLMVLLCGAAPLSRETEDQIKERIGVPFIRQGYGLSESTLSVLVQNDEFCKPGSVGVLKVGIYAKVIDPDTGKLLGANERGELCFKGDGIMKGYIGDTKSTQTAIKDGWLHTGDIGYYDDDFEFFIVDRIKELIKYKGYQVPPAEIEALLLTNDKIKDAAVIGKPDEEAGELPLAFVVKQANVQLTENEVIQFVNDNASPAKRLRGGVIFVDEIPKNPSGKILRRILREMLKKQKSKL
Protein: Ninein (H9KV85)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
XVLAEKFGDLDPSSAEFFLQEERLTQMRNEYERQCRVLQDQVDELQSELEEYRAQGRVLRLPLKNSPSEEVEANSGGIEPEHGLGSEECNPLNMSIEAELVIEQMKEQHHRDICCLRLELEDKVRHYEKQLDETVVSCKKAQENMKQRHENETHTLEKQISDLKNEIAELQGQAAVLKEAHHEATCRHEEEKKQLQVKLEEEKTHLQEKLRLQHEMELKARLTQAQASFEREREGLQSSAWTEEKVRGLTQELEQFHQEQLTSLVEKHTLEKEELRKELLEKHQRELQEGREKMETECNRRTSQIEAQFQSDCQKVTERCESALQSLEGRYRQELKDLQEQQREEKSQWEFEKDELTQECAEAQELLKETLKREKTTSLVLTQEREMLEKTYKEHLNSMVVERQQLLQDLEDLRNVSETQQSLLSDQILELKSSHKRELREREEVLCQAGASEQLASQRLERLEMEHDQERQEMMSKLLAMENIHKATCETADRERAEMSTEISRLQSKIKEMQQATSPLSMLQSGCQVIGEEEVEGDGALSLLQQGEQLLEENGDVLLSLQRAHEQAVKENVKMATEISRLQQRLQKLEPGLVMSSCLDEPATEFFGNTAEQTEQFLQQNRTKQVEGVTRRHVLSDLEDDEVRDLGSTGTSSVQRQEVKIEESEASVEGFSELENSEETRTESWELKNQISQLQEQLMMLCADCDRASEKKQDLLFDVSVLKKKLKMLERIPEASPKYKLLYEDVSRENDCLQEELRMMETRYDEALENNKELTAEVFRLQDELKKMEEVTETFLSLEKSYDEVKIENEGLNVLVLRLQGKIEKLQESVVQRCDCCLWEASLENLEIEPDGNILQLNQTLEECVPRVRSVHHVIEECKQENQYLEGNTQLLEKVKAHEIAWLHGTIQTHQERPRVQNQVILEENTTLLGFQDKHFQHQATIAELELEKTKLQELTRKLKERVTILVKQKDVLSHGEKEEELKAMMHDLQITCSEMQQKVELLRYESEKLQQENSILRNEITTLNEEDSISNLKLGTLNGSQEEMWQKTETVKQENAAVQKMVENLKKQISELKIKNQQLDLENTELSQKNSQNQEKLQELNQRLTEMLCQKEKEPGNSALEEREQEKFNLKEELERCKVQSSTLVSSLEAELSEVKIQTHIVQQENHLLKDELEKMKQLHRCPDLSDFQQKISSVLSYNEKLLKEKEALSEELNSCVDKLAKSSLLEHRIATMKQEQKSWEHQSASLKSQLVASQEKVQNLEDTVQNVNLQMSRMKSDLRVTQQEKEALKQEVMSLHKQLQNAGGKSWAPEIATHPSGLHNQQKRLSWDKLDHLMNEEQQLLWQENERLQTMVQNTKAELTHSREKVRQLESNLLPKHQKHLNPSGTMNPTEQEKLSLKRECDQFQKEQSPANRKVSQMNSLEQELETIHLENEGLKKKQVKLDEQLMEMQHLRSTATPSPSPHAWDLQLLQQQACPMVPREQFLQLQRQLLQAERINQHLQEELENRTSETNTPQGNQEQLVTVMEERMIEVEQKLKLVKRLLQEKVNQLKEQVSLPGHLCSPTSHSSFNSSFTSLYCH
Protein: Exportin-1 (Exp1) (Chromosome region maintenance 1 protein homolog) (Q80U96)
Organism: Rattus norvegicus (Rat)
Function: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm (By similarity). {ECO:0000250}.
Interaction partners:
- GTP-binding nuclear protein Ran
- Snurportin-1
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup88
- Ran-specific GTPase-activating protein
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran, testis-specific isoform
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup98-Nup96
- E3 SUMO-protein ligase RanBP2
Sequence:
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTKKLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTPLNPGSPVSNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD
Protein: Alkaline ceramidase 1 (AlkCDase 1) (Alkaline CDase 1) (EC 3.5.1.-) (EC 3.5.1.23) (Acylsphingosine deacylase 3) (N-acylsphingosine amidohydrolase 3) (Q8TDN7)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum ceramidase that catalyzes the hydrolysis of ceramides into sphingosine and free fatty acids at alkaline pH. 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. Exhibits a strong substrate specificity towards the natural stereoisomer of ceramides with D-erythro-sphingosine as a backbone and has a higher activity towards very long-chain unsaturated fatty acids like the C24:1-ceramide. May also hydrolyze dihydroceramides to produce dihydrosphingosine. ACER1 is a skin-specific ceramidase that regulates the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes and more generally plays an important role in skin homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17713573}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neutral ceramidase
- Acid ceramidase
- Ceramide kinase
- Sphingosine kinase 2
- Sphingosine kinase 1
- Ceramide synthase 4
- Ceramide synthase 3
- Ceramide synthase 6
- Ceramide glucosyltransferase
- Ceramide synthase 2
Sequence:
MPSIFAYQSSEVDWCESNFQYSELVAEFYNTFSNIPFFIFGPLMMLLMHPYAQKRSRYIYVVWVLFMIIGLFSMYFHMTLSFLGQLLDEIAILWLLGSGYSIWMPRCYFPSFLGGNRSQFIRLVFITTVVSTLLSFLRPTVNAYALNSIALHILYIVCQEYRKTSNKELRHLIEVSVVLWAVALTSWISDRLLCSFWQRIHFFYLHSIWHVLISITFPYGMVTMALVDANYEMPGETLKVRYWPRDSWPVGLPYVEIRGDDKDC
Protein: Scaffold protein salvador (Shar-pei) (Q9VCR6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Required for cell cycle exit in eye imaginal disk and hid-induced apoptotic cell deaths that are part of normal retinal development. Activation of Drice in eye imaginal disk by either Hid or Rpr is almost completely blocked by Sav expression.
Interaction partners:
- Serine/threonine-protein kinase hippo
- Serine/threonine-protein kinase Warts
- MOB kinase activator-like 1
- Transcriptional coactivator yorkie
- Moesin/ezrin/radixin homolog 2
- Protein kibra
- LIM domain-containing protein jub
- LD40758p
- Scalloped, isoform Q
- Tondu-domain-containing growth inhibitor, isoform A
Sequence:
MNYLTILLCNRKPTMLSRRNKEKSQHKEGVVGKYMKKDTPPDISVINVWSDQRAKKKSLQRCASTSPSCEFHPRSSSTSRNTYSCTDSQPDYYHARRAQSQMPLQQHSHSHPHSLPHPSHPHVRSHPPLPPHQFRASSNQLSQNSSNYVNFEQIERMRRQQSSPLLQTTSSPAPGAGGFQRSYSTTQRQHHPHLGGDSYDADQGLLSASYANMLQLPQRPHSPAHYAVPPQQQQHPQIHQQHASTPFGSTLRFDRAAMSIRERQPRYQPTSSPMQQQQQQQQQQQQQLQHTQLAAHLGGSYSSDSYPIYENPSRVISMRATQSQRSESPIYSNTTASSATLAVVPQHHHQGHLAVPSGSGGGSLSGSGRGGSSGSVRGASTSVQSLYVPPRTPPSAVAGAGGSANGSLQKVPSQQSLTEPEELPLPPGWATQYTLHGRKYYIDHNAHTTHWNHPLEREGLPVGWRRVVSKMHGTYYENQYTGQSQRQHPCLTSYYVYTTSAEPPKAIRPEASLYAPPTHTHNALVPANPYLLEEIPKWLAVYSEADSSKDHLLQFNMFSLPELEGFDSMLVRLFKQELGTIVGFYERYRRALILEKNRRAGQNQNQNQ
Protein: WD repeat-containing protein PCN (Protein POPCORN) (Q8RXU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in auxin signaling pathway. Required for embryo development and meristem organization. Functions in the auxin pathway, integrating auxin signaling in the organization and maintenance of the shoot apical meristem (SAM) and root apical meristem (RAM).
Subcellular location: Nucleus {ECO:0000269|PubMed:22158464}.
Interaction partners:
- Protein TORMOZ EMBRYO DEFECTIVE
- Periodic tryptophan protein 2
- Putative WD-repeat membrane protein
- U3 small nucleolar RNA-associated protein 18 homolog
- Uncharacterized protein At3g06530
- Transducin family protein / WD-40 repeat family protein
- F18K10.11 protein
- rRNA biogenesis protein RRP5
- Protein SLOW WALKER 1
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
Sequence:
MLEYRCSSVDWKPSPVVALANSSDDSQVAAAREDGSLEIWLVSPGAVGWHCQLTIHGDPNSRISSLAWCCSPSIGLPSGRLFSSSIDGSISEWDLFDLKQKIVLESIGISIWQMALAPISGFSSDVEGIKNGYLSEKSNDEEEIGSEEDGSDSDEFHEKSEEEIDRILAAACDDGCVRLYRISNLEKLTYYRSLPRVSGRALSVTWSPDAKRIFSGSSDGLIRCWDATSCHEVYRITAGLGGLGSSSEICVWSLLSLRCSVLVSGDSTGTVQFWDSEHGTLLEAHSNHKGDVNTLAAAPSHNRVFSAGADGQVILYKLSGSTNGSQDLKPSSSQKWDYIGYVKAHTHDIRALTVAVPISREDPFPDDILPDKASRKHRKKGKPVDFTYHKWAHLGVPMLISAGDDAKLFAYSIQEFTKFSPHDICPAPQRIPMQMVHNSMFNKTSLLLVQGISTLDILRLNISSDSSGRASTKSLVRVKSRDARKIICSAISNTGSHFAYSDQIGPSLFELKKNEFTKCPWSVSRRRLPELPFAHSMIFSSDCSRLIIAGHDRRIYTIDISSLELVYAFTPSREEHEGEAPTPKEPPITKLFTSSDGQWLAAINCFGDIYVFNLETQRQHWFISRLDGASVTAAGFHPWNNNALVISTSSNQVFAFDVEARQLGKWSLLNTYVLPKRYQEFPGEVLGLSFSPSPNSSSVIVYSSRAKCLIDFGKPVEEDEEYDLPNGNLSKTLEGKLVNLGLKKGKGTNRKRRLDEYQLEGKSNERKNFEILPSNHPVLFVGHLSKNSILVIEKPWMDVVKSLDNQPVDRHIFGT
Protein: Stathmin (E7FE68)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAKTAIAYKEKMKELSMLSLICSCFSPQTRNNIVCEFEDMEVKPINKRASGQAFEVILKPPSPVSDAAHSITSPPKKRDMSLDDIQKKLEAAEDRRRSQEAQVLKALAEKREHERDVLLKAMEENSNFSKMAEEKLILKMEQNKENREAHLAAMIDRLHEKERHAAIVRRNKELREQIVE
Protein: candidapepsin (EC 3.4.23.24) (G8B6X1)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVAIVTLTRQVLLTIALALFAQGAAIPEEAAKRDDNPGFVALDFDVLRKPLNLTEALLREKRDSISLSLINEGPSYASKVSVGSNKQQQTVIIDTGSSDFWVVDSNAQCGKGVDCKSSGTFTPSSSSSYKNLGAAFTIRYGDGSTSQGTWGKDTVTINGVSITGQQIADVTQTSVDQGILGIGYTSNEAVYDTSGRQTTPNYDNVPVTLKKQGKIRTNAYSLYLNSPSAETGTIIFGGVDNAKYSGKLVAEQVTSSQALTISLASVNLKGSSFSFGDGALLDSGTTLTYFPSDFAAQLADKAGARLVQVARDQYLYFIDCNTDTSGTTVFNFGNGAKITVPNTEYVYQNGDGTCLWGIQPSDDTILGDNFLRHAYLLYNLDANTISIAQVKYTTDSSISAV
Protein: Uncharacterized protein (Q386Z0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGQRNSLRDAPVEAVSRRPRTNDIVDNNQGEREVLYVKAPLTFTDPTPRVLPQSGYNQQYQSPPRVQRRRRGGGTKTLYVRTDDSESEKEGSSDGRNGMRQLVTAAEQPEGDSDVGEEEDSSSFMGKLAACGDAFLRVANSIPGTVFGVCQKWHVTGILIFLFFFLCFMFFLMLSAKQAQYAAKVIEHDNRQSLLFTASLVDQHLMAANEARKLMGSDSQRSAAALKEAKLHVEELAELCDGSIKQLHSRILYPGPVEDIKFLLEEHVAYEANLVRLIKEEVEWFERHVHDHKKVTTGPQTGVGNASSKKKERTPKHRQGQKFTLTKTGFYLGAGDGPEANSKDLLPFFRVFLGGLLGNRVIVAVALLALVVLYRRLS
Protein: Endochitinase At2g43580 (EC 3.2.1.14) (O24598)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- PLC-like phosphodiesterases superfamily protein
- RING-type E3 ubiquitin transferase
- Metalloendoproteinase 3-MMP
- Lectin-like protein At3g16530
- Regulator of Vps4 activity in the MVB pathway protein
- At1g25420/F2J7_16
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
Sequence:
MALTKIFLILLLSLLGLYSETVKSQNCDCAPNLCCSQFGYCGTTADYCGSTCQSGPCRVGGPPTGAGLVGNIVTQIFFNNIINQAGNGCAGKSFYTRDSFINATNTFPSFANTVTRREIATMFAHFTYETGHFCYIEEINGASRVMCDQNNRQYPCAPAKSYHGRGPLLLSWNFNYGACGQSLGLDLLRQPELVSSNPVVAFRTALWFWMKSVRPVLNQGFGATIRAISGFDCDGRNLGGVNARIGYYRDYCGQLGLDPGANITC
Protein: 2S seed storage albumin protein (2S albumin) (2S albumin seed storage protein) (Allergen Jug r 1) (allergen Jug r 1.0101) [Cleaved into: 2S albumin seed storage protein small subunit; 2S albumin seed storage protein large subunit] (P93198)
Organism: Juglans regia (English walnut)
Function: Seed storage protein.
Interaction partners:
Sequence:
AALLVALLFVANAAAFRTTITTMEIDEDIDNPRRRGEGCREQIQRQQNLNHCQYYLRQQSRSGGYDEDNQRQHFRQCCQQLSQMDEQCQCEGLRQVVRRQQQQQGLRGEEMEEMVQSARDLPNECGISSQRCEIRRSWF