wanglab/gogpt-training-data huggingface dataset:
Protein: Hsp90-related protein TRAP1 (Q7KNF3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGVLGQACRLGRCAQVLRQSHRSAPAAFNITIGSQHSPGALSLRRYSTETKQASGSVVDKHEFQAETRQLLDIVARSLYSDHEVFVRELISNASDALEKFRYTSLSAGGENLAGKDRPLEIRITTDKPLMQLIIQDTGIGMTKEELVSNLGTIARSGSKKFLEQMKGTQQGASSEASSNIIGQFGVGFYSSFIVANKVEVFTRAAVPNAPGLRWSTDGSGTYEIEEVPDVELGTRIVLHLKTDCREYADEERIKAVIKKYSNFVGSPILLNGKQANEIKPLWLLEPQSISKEQHHDFYRFISNSFDVPRFTLHYNADVPLSIHALLYFPEGKPGLFEMSRDGNTGVALYTRKVLIQSKTEHLLPKWLRFVKGVVDSEDIPLNLSRELLQNSSLIRKLSSVISTRVIRFLQERSKKQPEEYEAFYRDYGLFLKEGIVTSSDASEKEEIAKLLRFESSKSETASGRMSLEEYYNAVPAEQQNIYYLAAPNRVLAESSPYYESLKKRNELVLFCYEPYDELVLMQLGKFKSKKLVSVEKEMREESKETTATTDFGEGSLLRSELDTLIPWLEEELRGQVIKVKATTRLDTHPCVITVEEMAAARHFIRTQSHQVPEQNRFALLQPELEINPKHPIIKKLNKLRESDKDLAQLIAKQLFANAMVGAGLAEDPRMLLTNMNTLLSRALEKY
Protein: Tegument protein VP16 homolog (Alpha trans-inducing protein) (Alpha-TIF) (ORF10 protein) (Tegument protein 10) (P09265)
Organism: Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3)
Function: Transcriptional activator of immediate-early (IE) gene products (alpha genes). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F1. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection (By similarity).
Subcellular location: Virion tegument {ECO:0000250|UniProtKB:P04486}. Host nucleus {ECO:0000250|UniProtKB:P04486}.
Interaction partners:
Sequence:
MECNLGTEHPSTDTWNRSKTEQAVVDAFDESLFGDVASDIGFETSLYSHAVKTAPSPPWVASPKILYQQLIRDLDFSEGPRLLSCLETWNEDLFSCFPINEDLYSDMMVLSPDPDDVISTVSTKDHVEMFNLTTRGSVRLPSPPKQPTGLPAYVQEVQDSFTVELRAREEAYTKLLVTYCKSIIRYLQGTAKRTTIGLNIQNPDQKAYTQLRQSILLRYYREVASLARLLYLHLYLTVTREFSWRLYASQSAHPDVFAALKFTWTERRQFTCAFHPVLCNHGIVLLEGKPLTASALREINYRRRELGLPLVRCGLVEENKSPLVQQPSFSVHLPRSVGFLTHHIKRKLDAYAVKHPQEPRHVRADHPYAKVVENRNYGSSIEAMILAPPSPSEILPGDPPRPPTCGFLTR
Protein: Cation channel sperm-associated targeting subunit tau (CatSper-tau) (C2 calcium-dependent domain-containing 6) (A0A5F8MPU3)
Organism: Mus musculus (Mouse)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Required for CatSper complex targeting and trafficking into the quadrilinear nanodomains. Targets the preassembled CatSper complexes to elongating flagella, where it links the channel-carrying vesicles and motor proteins.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:34998468}. Note=Specifically located in the principal piece of the sperm tail. {ECO:0000269|PubMed:34998468}.
Interaction partners:
Sequence:
MELPPPGNRRVSINNPQETSGRVPTTSAGFPTQSSKISLKRSTYAYRPSMMSNRSSGGQSLLPSSILQKTSLNPPGSLQSKPSNLSSVHYADEEGKPLTDKNKDKDKGRGKGKGTGTRLLTMLRKTLQGSQSDEMAIANQTPNLIPFGDVVGCLAIHIKSCRQFSQRFLGQQRFNLFMRVSINNIVKCTKIRHLKAVNNEKNLVLRFGEMKYFSVQVPRRQDDERNFIYLELMHDGGDPESPPIPLGGAESHLYEVIQKGCFTEVMHLMHKNSSICRVEVEFMFSYGNFGYGFSHQLKPLQKAIEPSMFMNIAPPPERTDPVTNVITPQRVEYPAFLSPEFNVSIGVPEASHATVVQLEKLREKPRERLERMKEEYKNMSTWIEKADYLRNLINPKMTKRDNKGSSIPSESNSSALEELERTTYDIHHRKYEAISNEYGDKEGRVIPVLKVLDQNYSEVFLPKSSDSTPLEDVLLPPIHSLQIVEENEMPHLPKTSEPEDRPHEERKSIVFSSDEELMPKHPSILKISSSQQENRRKMEKSPHFSDVLIIPDKPFEDLNTNKKGRPPIELRKSWERHPTDVACSLRKVAFAQKDYTIPVCKAETTEFKPKHQFQKLSKSGLDPFLRNINSKMSFRKKKDHDDGYRNLSTSSAEILEHEDQDPPYPGHSGSAGSDATWAENPSPVTVQMVNRDSLPPDLITATIVISDRKNKLSLDSVFNSANSLNTKSIFASDNPVVSLTKLSDSDNKLITDSSFNTTKPSNRRLSKDSNFNTTKPSDRKLSSDPSSNTTKPSDTKLFSDPSSNKLSQGPSSNASQLSGSNRLSHNPSINGNKSSYTSDLNKVSRDPSIVSTISSDPNKLSRDPSFVLAKSSDPNKLSHYPSIISAKSSDPNKLSHDPSFVSARSSDPNKLSHDPSIISARSSDPIKLSRDPSFVSARSSDPNKLSHDPSIISARSSDPNKLSRDPSINSTKLSDPSKLSRDPSIFSTKSSDPNKLYRVPSIISGMSSNPKLSRDPSIISGMSSDPKLSRDPSIISAKSSDPNKLSHDPSIISGMSSNPNKLSHDPSIISMKLSDMSKLSRESSINASKSSDTNQLSYDPNIISAKSLDSNNSSASSSPTVNSDTTTNAAEPSGTKNMLDPVVSTIDSSDKQSKLEWLPNVQGASSVTENINTHRSSNSVNFTSDIDILKQSIVLKSILSKNLQDLSDELFSKSELYTNDEGYSPPPSVHSRPSDSTDDRVLGKVQDLNSWRSSKDLLNSQVLLSPVVKNSPQDLLPEGEPGKSSDIEDYVSEKLLEAAGRNFPMNRKSSFKKKHLVSEESSSEHVLSGSIYEYVIKQIFTAPIFSQLGIGIKSSSEARMDSQNQLLTPWERSVTSHIINYEEKDSDVNLSQSKSIISQIIQSFPVNTLLESGVIKVIELDKEHQNSLLDSQTTSSTEQYSDSRSQIKLLSRQNTSSINPLDSSVSGAEYTEDCQSISTQESKYPVRDTKSDSPNDTEEMELDSNLESSSSSLDKVKDTDTAKLKNILKNIFSIFFKYNQSERRQQPEKDSESLIKHSSSSGSEHLEKTQENFNKADKKVDRKPILNPKLRMFLEKLSETEVKNLKSELSKHIQHYLVERLTESGHITKEDLPTIYHKLYLMNEKVELKEQTPFQEKYSETVKEIMSFVNNFNHHFIDKHLETKLRGFLSEILQNYFLKNLSVSNLFNETDAMALHASMSPVRSKSELGQDIADGNFGSSLKINMQYPVTKSLQHYLQDLSENELLSLKTDLSKYLQVLFIEKLYKSGLVSERQLKGISQEIISLHSPSIPLKHIKTNLPFRNESYFMREDSEEQMKYLKNGQNAALHVLLKDKCGETELSRKKERESSFSQILKENLPAIWEQKNIYTREEETLNLIQMQSFLNKNNQANPLTRSPERPSDISLKKQKKDHGFMQFTQVEGSVYKTEIQDPYSWDSRSKTIQSKPCLEKTLKMKLLDKRENNNFYKLTAQEKLDTEFSSYLKLPNCKIPKEKEPISRLSFPTWKTNTFIHVKPEIGEQSKLDHYYQRLKGNNNNNKKHLVTFAQFKNEMETLYRNPYEACNEKRAKISESQSFKYKEKEKSSRPFFFPEVLKRENTKSKRKERDHATKPKKSFHKIVRLLPATLPTTRPHLRKSAPRNLLHWTARRTIHDCLDRFDDLHAPTVKCPKKSKSGARLLGKSPEDSHNQAKHCARPYTAPEPNKRRESAAWKFASPRMVSAGLLHLYVTPAYGIRKVRSKRKLKEDIEKRPLISEIIQMLDNAE
Protein: Assembly factor CBP4 (Cytochrome b mRNA-processing protein 4) (P37267)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein CBP3
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Mitochondrial chaperone BCS1
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b
Sequence:
MERPLWVRWLKVYAIGGAIIGSGFLLFKYTTPTDQQLISQLSPELRLQYEREKKLRQSEQQALMKIVKETSQSDDPIWKTGPLQSPWERNGDNVQSRDHFAKVRAEEVQKEELARIRNELSQLRSETEEKTKEIVQDKQVKSWWRFW
Protein: Fork head transcription factor long isoform (Forkhead box K, isoform K) (Q0E8F8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MAATTTTTTTTLATTTGNSSSTNNSSSNNNNSIASSHNNNNNIVTVHTVLNNPPTNTAGGGVADAATVAIAKDMLQLHHGAAAAATAALNNYNNSSNNNNNSADQLTGNSNNSANHPPATSSTTNSSSSSTTSANTNNPSANAASTLTSSSPPYGELRFNQEVLPITDAVTVIGRNSSTSLVHFNVAENNLVSRKHFQVLYDVELRAFFVQCLSKNGIFVDDFLQRRNVDPLRLPQRCYFRFPSTEIRIEFESYVPATSSDAIDGHSPSLVVGGGGGVAGGGAHVIITPLPRDELHQQQLHHHQQQPHLQQQQHPHHPPAHHLPLQQQQQQQQPAHHPLPHTPHHPLHHTALHQQQQRSGSIVVAPPAGAAAHLIAGDGPGIYSPLKISIPKKEQKSPYLSPTGNCPASPRQGFIQNQPNNYNNYGNNNTQDLFQTPSTASYNHNEKPPYSYAQLIVQAISAAPDKQLTLSGIYSFIVKHYPYYRKETNKGWQNSIRHNLSLNRYFIKVARSQDEPGKGSFWRIDPDSGAKLIDHSYKKRRQRSSQGFRPPYGMPRSAPVSPSHMDNSRESSPLQDIVLQSAPGSPGMSLEQRAADPEIIYNSQNAHQQQQQQQQQQQQQTLSNNSNQYSSGSPYYVTNQSSGVATPQTHVEGSAASGGGGGGGVGALLALKRNHVMGGGASQHTLHQQQAVAQQQHSEIIYEELPTDYSGHIEASEEECVTTATDATVAKRPKYVSEVL
Protein: Glucosyl-3-phosphoglycerate synthase (GpgS) (EC 2.4.1.266) (Retaining glucosyltransferase) (P9WMW9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of 6-O-methylglucose lipopolysaccarides (MGLPs). Catalyzes the transfer of the glucose moiety from UDP-alpha-D-glucose (UDP-Glc) to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG).
Interaction partners:
- Glucosyl-3-phosphoglycerate phosphatase
- Probable S-adenosylmethionine-dependent methyltransferase Rv3030
- Inactive dihydropteroate synthase 2
- Glycogen synthase
- Probable acetyltransferase Rv3034c
- Uncharacterized S-adenosylmethionine-dependent methyltransferase Rv3037c
- Cytokinin riboside 5'-monophosphate phosphoribohydrolase
- Probable DNA-3-methyladenine glycosylase I TagA
- Conserved protein
- Medium/long-chain-fatty-acid--CoA ligase FadD6
Sequence:
MTASELVAGDLAGGRAPGALPLDTTWHRPGWTIGELEAAKAGRTISVVLPALNEEATIESVIDSISPLVDGLVDELIVLDSGSTDDTEIRAIASGARVVSREQALPEVPVRPGKGEALWRSLAATSGDIVVFIDSDLINPHPLFVPWLVGPLLTGEGIQLVKSFYRRPLQVSDVTSGVCATGGGRVTELVARPLLAALRPELGCVLQPLSGEYAASRELLTSLPFAPGYGVEIGLLIDTFDRLGLDAIAQVNLGVRAHRNRPLDELGAMSRQVIATLLSRCGIPDSGVGLTQFLPGGPDDSDYTRHTWPVSLVDRPPMKVMRPR
Protein: Iron sulfur cluster assembly protein 2, mitochondrial (Iron sulfur cluster scaffold protein 2) (Q12056)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. First, a [2Fe-2S] cluster is transiently assembled on the scaffold proteins ISU1 and ISU2. In a second step, the cluster is released from ISU1/ISU2, transferred to glutaredoxin GRX5, followed by the formation of mitochondrial [2Fe-2S] proteins, the synthesis of [4Fe-4S] clusters and their target-specific insertion into the recipient apoproteins. Cluster assembly on ISU1/ISU2 depends on the function of the cysteine desulfurase complex NFS1-ISD11, which serves as the sulfur donor for cluster synthesis, the iron-binding protein frataxin (YFH1) as the putative iron donor, and the electron transfer chain comprised of ferredoxin reductase ARH1 and ferredoxin YAH1, which receive their electrons from NADH. Fe-S cluster release from ISU1/ISU2 is achieved by interaction with the Hsp70 chaperone SSQ1, assisted by the DnaJ-like co-chaperone JAC1 and the nucleotide exchange factor MGE1. ISU1 is the major isoform in yeast, while ISU2 is not detectable in cells grown to stationary phase (By similarity). ISU2 is the minor isoform in yeast and is not detectable in cells grown to stationary phase. Also involved in production of a sulfur precursor required for thiolation of cytoplasmic tRNAs.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:10468587, ECO:0000269|PubMed:10588895}.
Interaction partners:
- Cysteine desulfurase, mitochondrial
- Frataxin homolog, mitochondrial
- Protein ISD11
- J-type co-chaperone JAC1, mitochondrial
- NifU-like protein
- Adrenodoxin homolog, mitochondrial
- Iron-sulfur assembly protein 2
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Iron-sulfur assembly protein 1
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
Sequence:
MFARLANPAHFKPLTGSHITRAAKRLYHPKVIDHYTNPRNVGSMDKSLANVGTGIVGAPACGDVIKLQIQVNDKSGIIENVKFKTFGCGSAIASSSYMTELVRGMSLDEAVKIKNTEIAKELSLPPVKLHCSMLAEDAIKAAIKDYKTKRNPSVLH
Protein: Mitochondrial import receptor subunit TOM20 homolog (Mitochondrial 20 kDa outer membrane protein) (Outer mitochondrial membrane receptor Tom20) (Q9DCC8)
Organism: Mus musculus (Mouse)
Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q15388}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM7 homolog
- Mitochondrial import receptor subunit TOM5 homolog
- Mitochondrial import receptor subunit TOM6 homolog
- Alpha-synuclein
- Serine/threonine-protein kinase PINK1, mitochondrial
- Non-selective voltage-gated ion channel VDAC1
- Mitofusin-1
Sequence:
MVGRNSAIAAGVCGALFIGYCIYFDRKRRSDPNFKNRLRERRKKQKLAKERAGLSKLPDLKDAEAVQKFFLEEIQLGEELLAQGDYEKGVDHLTNAIAVCGQPQQLLQVLQQTLPPPVFQMLLTKLPTISQRIVSAQSLAEDDVE
Protein: WPP domain-containing protein 2 (MFP1 attachment factor 2) (Q9C500)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates the mitotic activity in roots. Plays a role with HSP70-1 in facilitating WIT1 nuclear envelope targeting.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:15548735}. Cytoplasm {ECO:0000269|PubMed:15548735}. Nucleus {ECO:0000269|PubMed:15548735}. Golgi apparatus {ECO:0000250}. Note=Associated to the nuclear envelope (NE) in undifferentiated cells of the root tip. Associated with the outer NE and the nuclear pores in interphase cells and with the immature cell plate during cytokinesis. In differentiated cells, localized in both cytoplasm and nucleus. Accumulate in speckles of the cytoplasm belonging to the Golgi apparatus (By similarity). Appears at the NE as cells reenter the cell cycle during dedifferentiation. {ECO:0000250}.
Interaction partners:
- WPP domain-interacting tail-anchored protein 1
- WPP domain-associated protein
- WPP domain-interacting tail-anchored protein 2
- Heat shock 70 kDa protein 1
- Spindle pole body component
- Probable histone-arginine methyltransferase 1.3
- FRIGIDA-like protein 4a
Sequence:
MAETAETINTTISSPPPESESSTTISAMTDPTSQEAASKDTDLTKEAESEKKPGGISLRIWPPTQKTRDAVLNRLIETLSTESILSKRYGTLKSDDATTVAKLIEEEAYGVASNAVSSDDDGIKILELYSKEISKRMLESVKARSNASVGNGSVEDANTDASEVSKDDAGPASEEEKSEA
Protein: Perilipin (Q9MZE5)
Organism: Sus scrofa (Pig)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MASVAVESQPSVVTRVANLPLVSSTYGLVSSAYISTKDQYPYLKSLCEMAEKGVKTITSVAMSGALPIIQKLEPQIAIANTYACKGLDRIEEKLPILNQPTNQVVANAKGAVTGAKDAMTTTVTGAKDCVASTITEVVDKTKEAVTGSVEKTKSVVNGSINTVLGSRMMQLVSSGVEKAFTKSELLVDQYLPLTEEELEKEAKKVEGFDMVQKPSYYIRLGSLSTKLRSRAYQQALTRVKEVKQKSQETISQLHSTVNLIEFARKNVHNANQKIQGTQDKLYLSWVEWKRSIGYDDTDESHRAEHIESRTLAIARNLTQQLQTTCHTLVSNIRGLPQNIHDQANHLGVMAGDIYSVFHNASSFKEMSDGLLSSSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQLTESQDAQSRGAENTTSPETQQPETKRIKPAPASSAWGSQSGDTSCTVATC
Protein: Lysophospholipid acyltransferase 6 (LPLAT 6) (EC 2.3.1.-) (EC 2.3.1.23) (EC 2.3.1.n6) (EC 2.3.1.n7) (Membrane-bound acyltransferase 6) (MBOA 6) (Oysgedart) (Oys) (Q6NN55)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acyltransferase with broad-specificity, that mediates the acylation of lysophospholipids to produce phospholipids (glycerophospholipids). Converts lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) to phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity), lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity), also lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphochethanolamine or LPE) to phosphatidylchethanolamine (LPEAT activity) and lysophosphatidylglycerol (1-acyl-2-hydroxy-sn-glycero-3-phospho-(1'-sn-glycerol) or LPG) to phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) or PG) (LPGAT activity). Has a preference for unsaturated fatty acids of at least 16 carbons such as oleoyl-CoA ((9Z)-octadecenoyl-CoA) and palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA). Glycerophospholipids are important structural and functional components of cellular membrane, acyl-chain remodeling regulates the molecular species distribution of glycerophospholipids which can affect membrane fluidity and curvature. Essential for fertility and viability together with Nessy protein (Nes).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:19864461}. Membrane {ECO:0000269|PubMed:19864461}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
Sequence:
MLEPPKFIENDCYNGSRTFTWLADMVGLSVDLVNFLICQISALFLASLFRSMLHPSKVSSKLRHTFALSIGLAFGYFCFGQQAIHIAGLPAICYIVIRTQDPRIVQRAVLLVAMSYLLCVHLMRQLYDYGSYALDITGPLMIITQKVTSLAFSIHDGFVRGDEELTKAQQYHAIRKMPSALEYFSYVWHFQSILAGPLVFYKDYIEFVEGYNLLSTPPGNGNLDSSKREVVLEPSPTKAVIRKVVGSLVCAFIFMKFVKIYPVKDMKEDDFMNNTSMVYKYWYAMMATTCIRFKYYHAWLLADAICNNSGLGFTGYDKDGNSKWDLISNINVLSFEFSTNMRDAINNWNCGTNRWLRTLVYERVPQQYGTLLTFALSAVWHGFYPGYYLTFATGAVVVTAARTGRRLFRHRFQSTQVTRMFYDILTCLITRVVLGYATFPFVLLEFMGSIKLYLRFYLCLHIISLVTIFILPKFIRGERRLRTSNGNGNVRLSGSGNTKDAVTTSVESTAALTAGNDLNEDKEEDKHAQCKVHTPTQQQPAAGPHKTTVEQPTEQPNNVNLRSRPQQQQPHLEKKAMPPTCARDAVSVPHDQCEMDQLSSKLKEKIEAETKNIEEFIDKTVTETVSGIVEFKNDLMRDIEFPKLKLPGSNGAISLDSSNGGGLRKRNISSVHDNGTDPGHATADLHPPLEENGAAFLKKEIEVINAVVQQAVPAVLSNGHAK
Protein: Inositol-trisphosphate 3-kinase C (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase C) (IP3 3-kinase C) (IP3K C) (InsP 3-kinase C) (Q80ZG2)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis. Can phosphorylate inositol 2,4,5-triphosphate to inositol 2,4,5,6-tetraphosphate.
Subcellular location: Nucleus {ECO:0000269|PubMed:12649294}. Cytoplasm {ECO:0000269|PubMed:12649294}. Note=Shuttles actively between nucleus and cytoplasm with both nuclear import and nuclear export activity.
Interaction partners:
- Inositol polyphosphate multikinase
- Inositol polyphosphate-5-phosphatase A
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- Multiple inositol polyphosphate phosphatase 1
- Calmodulin-1
- Inositol polyphosphate 5-phosphatase K
- Inositol-trisphosphate 3-kinase B
- Inositol-trisphosphate 3-kinase A
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
Sequence:
MRRCPCRGSLSEAEAGALPAEARMGLEALRGGRRRQPGLQRPGPGAGGPTGRPEGGGPRAWIEGFSLHSEAERTDFGPAPCPDGPQAEPCGDEHEECEAAGLGVASEKPSQNKELDGSNLQTHPKLSSPLAEMEMAGSWTDGFRTDLHRPDLQARPKRASLCTQPGFDESWTELDRSELWQTLPERDKPWVDHLRTHQDMSRLQNHPACPSPEPSAGTSCKELSADGSRTPHDTDGFWIESQTDGSLIGPSTQTACRQPANDGFSAQDTDGTLIQPGTDDGPWVDSVLEKSNGDDPLMEPEPRDLVTNLCSHLECSSLCPVPRLIITSESPEPGAQPLGPQARIEGGTGGFSSASSFDESEDDLVAGGGGTSDPEDRSGSKPWKKLKTVLKYSPFVVSFHKHYYPWVQLSGHAGNFQAGEDGRILKRFCQCEQRSLELLMGDPLRPFVPTYYGMVQRDGQAFNQMEDLLADFEGPSIMDCKMGSRTYLEEELVKARERPKPRKDMYEKMVAVDPGAPTPEEHAQGAVTKPRYMQWRETLSSTSTLGFRIEGIKKADGTCNTNFKKTQALEQVTKVLEDFVNGDVGILRKYVARLEDLRDTLENSPFFKTHEVVGSSLLFVHDHTGLAKVWMIDFGKTVALPDHQMLSHRLPWAEGNREDGYLWGLDNLICLLQGLAQS
Protein: Homeotic protein labial (F24) (F90-2) (P10105)
Organism: Drosophila melanogaster (Fruit fly)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Required for proper head development.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein extradenticle
Sequence:
MMDVSSMYGNHPHHHHPHANAYDGYSTTTASAANASSYFAPQQHQPHLQLQQQQQHQHLQQPQQHLTYNGYESSSPGNYYPQQQAQLTPPPTSSHQVVQQHQQQQQAQQQQLYPHSHLFSPSAAEYGITTSTTTGNPGTPLHPSSHSPADSYYESDSVHSYYATAAVATVAPPSNSSPITAANASATSNTQQQQQQAAIISSENGMMYTNLDCMYPTAQAQAPVHGYAGQIEEKYAAVLHASYAPGMVLEDQDPMMQQATQSQMWHHQQHLAGSYALDAMDSLGMHAHMHHGLPHGHLGNLANNPHQQQPQVQQQQQQPHQQPQHPQNQSPAAHQQHHQNSVSPNGGMNRQQRGGVISPGSSTSSSTSASNGAHPASTQSKSPNHSSSIPTYKWMQLKRNVPKPQAPSYLPAPKLPASGIASMHDYQMNGQLDMCRGGGGGGSGVGNGPVGVGGNGSPGIGGVLSVQNSLIMANSAAAAGSAHPNGMGVGLGSGSGLSSCSLSSNTNNSGRTNFTNKQLTELEKEFHFNRYLTRARRIEIANTLQLNETQVKIWFQNRRMKQKKRVKEGLIPADILTQHSTSVISEKPPQQQQPQPPELQLKSQGSDLGGNELATGAPSTPTTAMTLTAPTSKQS
Protein: Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Phosphopyruvate hydratase) (P51913)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm.
Interaction partners:
- Pyruvate kinase PKM
- Phosphoglycerate mutase 1
- Triosephosphate isomerase
- Glucose-6-phosphate isomerase
- Phosphoglycerate kinase
- Phosphoglycerate mutase
- Phosphoenolpyruvate carboxykinase, mitochondrial
- Phosphoenolpyruvate carboxykinase, cytosolic
- Transketolase
- Glycerate kinase
Sequence:
MSILKIHAREIFDSRGNPTVEVDLYTNKGLFRAAVPSGASTGIYEALELRDNDKTRYLGKGVSKAVEHVNKTIAPALISKNVNVVEQEKIDKLMLEMDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGADTFKEAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEALELLKTAIGKAGYSDKVVIGMDVAASEFYRDGKYDLDFKSPDDPSRYISPDQLADLYLGFVKNYPVVSIEDPFDQDDWAAWKKFTASVGIQVVGDDLTVTNPKRIAKAVEEKSCNCLLLKVNQIGSVTESLQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKARFAGRNFRNPRIN
Protein: ADAM DEC1 (EC 3.4.24.-) (A disintegrin and metalloproteinase domain-like protein decysin-1) (ADAM-like protein decysin-1) (O15204)
Organism: Homo sapiens (Human)
Function: May play an important role in the control of the immune response and during pregnancy.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MLRGISQLPAVATMSWVLLPVLWLIVQTQAIAIKQTPELTLHEIVCPKKLHILHKREIKNNQTEKHGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENMEHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHAVFTSNQEEQDPANHTCGVKSTDGKQGPIRISRSLKSPEKEDFLRAQKYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLLSGISFNNRRVGLAASNSLCSPSSVAVIEAKKKNNVALVGVMSHELGHVLGMPDVPFNTKCPSGSCVMNQYLSSKFPKDFSTSCRAHFERYLLSQKPKCLLQAPIPTNIMTTPVCGNHLLEVGEDCDCGSPKECTNLCCEALTCKLKPGTDCGGDAPNHTTE
Protein: Transcriptional activator II (P03042)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Acts as a transcriptional activator that allows virus to initiate a latent state. Following infection, participates, together with cIII, in activation of the Pe and Pi promoters, which are responsible for the transcription of the cI (repressor) and int (integrase) genes, respectively. Both of these gene products are required for the establishment of latency.
Interaction partners:
Sequence:
MVRANKRNEALRIESALLNKIAMLGTEKTAEAVGVDKSQISRWKRDWIPKFSMLLAVLEWGVVDDDMARLARQVAAILTNKKRPAATERSEQIQMEF
Protein: Trissin receptor (Q9VML9)
Organism: Drosophila melanogaster (Fruit fly)
Function: G-protein coupled receptor which is activated by the Trissin peptide in vitro, leading to increased intracellular calcium ion levels.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21939639}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Trissin
Sequence:
MIMTMMQTVRAWQQESDVEHRKQHKQRWRPDGAHISAAYDLNSDNDDGHHRVVHNQNNGSPNSSPNQSTSAFRQRQPHHPPTGQQPPRLPCTVTHFSAHWKTLLILLTLLSASTLTASANVTSTISPPINGSSTDYILLYGESTTSLVPALTTGLSGDGSGAVIEDEEDAEKASEYIFDRTDVRIIFITLYTLVFCCCFFGNLLVILVVTLSRRLRSITNFFLANLAFADFCVGLFCVMQNLSIYLIESWVFGEFLCRMYQFVHSLSYTASIFILVVICMERYFAIVHPITCKQILTAARLRMVIVTVWITSAVYSTPKFVFSKTIKNIHTQDGQEEEICVLDREMFNSKLLDMINFVLLYVMPLLVMTVLYSKIAIALWRSSRGLTPHVVQHQHQQPQQPSCQDIGMGMHNSMYHHHPHHHHHHHQHHQLQSAASSAGVVGVGLGGGGGGGPGPSLASGGSSTTSLSRKQSSKYEKRGVSITESQLDNCKVSLEADRPIVSACRKTSFYHHGHAHHQRAGNASVGGGSGGAGAGATHMSHSSSNVLRARRGVVRMLIIFVLTFALCNLPYHARKMWQYWSRSYRGDSNFNALLTPLTFLVTYFNSGVNPLLYAFLSRNFRKGMKELLLCSWKKGKGKSSSNSSMHHKRKALQTHSLPTDTTHIGNEQL
Protein: Protein-cysteine N-palmitoyltransferase HHAT-like protein (Glycerol uptake/transporter homolog) (Hedgehog acyltransferase-like protein) (Q9D1G3)
Organism: Mus musculus (Mouse)
Function: Negatively regulates N-terminal palmitoylation of SHH by HHAT/SKN.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18081866}; Multi-pass membrane protein {ECO:0000269|PubMed:18081866}.
Interaction partners:
- Beta-alanine-activating enzyme
- Acyl carrier protein, mitochondrial
- Partner and localizer of BRCA2
Sequence:
MGIKTALPAAELGLYSLVLSGALAYAGRGLLEASQDGAHRKAFRESVRPGWEYLGRKMDVADFEWVMWFTNFRNVIVFALSGHVLFAKLCTMVAPQLRSWMYAVYGVLAVVGTMGPWYLLLLLGHCMVLYVASLLGQRWLCLALGLASLASFKVDPGISWQSGFVTGTFDLQDVLFHGGSSFTVLRCTSFALESCAHPDRRYSLADLLKYNFYLPFFFFGPIMTFDRFHAQVSQEPVRPEGELWHIQAQAGLSAAAIVAVDVFFHFFYILTIPSDLKFASRLPDSALAGLAYSNLVYDWVKAAVLFGVVNTVARLDHLDPPQPPKCITALYVFGETHFDRGINDWLCKYVYDHIGGDHSTVIPELAASVATFVVTTLWLGPCDIVYLWSVLNCFGLNFELWVQKLAERGPLAQIEARLSEQMSRRVRALCGAVNFWAIIMYNLVSLNSLEFTELVARRLILTGFPQTTLAVLFVTYCGVQLVKERERSLALEEEQRQDREKLE