wanglab/gogpt-training-data huggingface dataset:
Protein: Deformed epidermal autoregulatory factor 1 (Protein DEAF-1) (Q24180)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription factor that binds the homeotic Deformed (Dfd) response element. High affinity binding sites contain at least 1 TTCG motif surrounded by additional TCG sequences. May be involved in the selective action of Dfd on these sites without binding directly to the Dfd protein. Requirement of DEAF1 activity may be a common feature of enhancers targeted by Dfd.
Subcellular location: Nucleus.
Interaction partners:
- Homeotic protein deformed
Sequence:
MEQVDSSTELHLNRKDLAALAEDVVKEEVILESSSHHHHHHHHQLDTKVRMVTSSSNDNSGSGGASGGTSGAGGGNGGGGVVSVPVSLPIGSMITGTTFNVITPDQLPPHFKPMLCVDNNGYLSGSTVSMGNDLKTIVIQQQQTQPGGGGGGANNAGTNTTATNTIGLNHDGSGSNNSHDSLATLEHAAGGASGVGGGGGGTGGGSSGWSENPSTQHNEVFQIRCKTTCAELYRSKLGSGGRGRCVKYKDKWHTPSEFEHVCGRGSSKDWKRSIKYGGKSLQSLIDEGTLTPHATNCSCTVCCDDEAGESASGPVRLFTPYKRRKRNQTDLDMESGPKRKRNTHHSNNNNSNTNNNNTSGSGANNCVDVTAAVAAATASVVDENNMFLSEENITSKDEPWAALNDSLDTSTELVDQSQMGNTYERETFVVNINDGSSIAVLDTSQSMKNIEHVYCTMVKATNDFKRMLNDMKQSFERRIEVLQKERDAAVSAMRVQVHADIDDPNISGSLHGNEIISAKKCANCNREALAECSLCRKTPYCSEFCQRKDWNAHQVECTRNPQTTTQQVMLLIDDQS
Protein: CCN family member 2 (Cellular communication network factor 2) (Connective tissue growth factor) (Hypertrophic chondrocyte-specific protein 24) (Insulin-like growth factor-binding protein 8) (IBP-8) (IGF-binding protein 8) (IGFBP-8) (P29279)
Organism: Homo sapiens (Human)
Function: Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes. Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P29268}. Secreted {ECO:0000250|UniProtKB:P29268}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Fibronectin
- High affinity nerve growth factor receptor
- Decorin
- Insulin-like growth factor-binding protein 7
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Transcriptional coactivator YAP1
- von Willebrand factor
- Collagen alpha-1
- Bone morphogenetic protein 2
Sequence:
MTAASMGPVRVAFVVLLALCSRPAVGQNCSGPCRCPDEPAPRCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDPHKGLFCHFGSPANRKIGVCTAKDGAPCIFGGTVYRSGESFQSSCKYQCTCLDGAVGCMPLCSMDVRLPSPDCPFPRRVKLPGKCCEEWVCDEPKDQTVVGPALAAYRLEDTFGPDPTMIRANCLVQTTEWSACSKTCGMGISTRVTNDNASCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSMKTYRAKFCGVCTDGRCCTPHRTTTLPVEFKCPDGEVMKKNMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA
Protein: Dicarboxylate transporter 2.1, chloroplastic (AtpDCT1) (Glutamate/malate translocator) (Q9FMF7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glutamate/malate translocator involved with DIT1 in primary ammonia assimilation and in the re-assimilation of ammonia generated by the photorespiratory pathway. Exports the end product of ammonia assimilation, glutamate, from plastids to the cytosol. The precursor for ammonia assimilation, 2-oxoglutarate, is imported from the cytosol by DIT1.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Plastidal glycolate/glycerate translocator 1, chloroplastic
- Malate dehydrogenase, chloroplastic
- Sodium/pyruvate cotransporter BASS2, chloroplastic
- D-glycerate 3-kinase, chloroplastic
- Mitochondrial carnitine/acylcarnitine carrier-like protein
- AT5g24690/MXC17_8)
- Phosphoenolpyruvate/phosphate translocator 1, chloroplastic
- Sodium/proton antiporter 1
- Nucleotide-sugar transporter family protein
- Sodium/proton antiporter 2
Sequence:
MESFALHSLSTTATSTLLSHHHHHHPSRLSLLRRTSSRSPPSTISLRSLSVQPLSFPLLKPIPRFSTRIAAAPQDNAPPPPPPSPSPSPSPQGAKLIPLILSISVGLILRFAVPVPEGVTPQGWQLLSIFLSTIAGLVLSPLPVGAWAFIGLTASIVTKTLSFSAAFSAFTSEVIWLIVISFFFARGFVKTGLGDRIATYFVKWLGKSTLGLSYGLTLSEALIAPAMPSTTARAGGIFLPIIKSLSLSAGSKPNDSSSRKLGSYLIQSQFQCAGNSSALFLTAAAQNLLCLKLAEELGVVISNPWVSWFKAASLPAIISLLCTPLILYKLYPPETKDTPEAPGIAATKLKQMGPVTKNEWIMVGTMLLAVTLWICGETLGIPSVVAAMIGLSILLVLGVLNWDDCLSEKSAWDTLAWFAVLVGMAGQLTNLGVVTWMSDCVAKVLQSLSLSWPAAFGLLQAAYFFIHYLFASQTGHVGALFSAFLAMHIAAGVPGILAALALAYNTNLFGALTHYSSGQAAVYYGAGYVDLPDVFKIGFVMATINAIIWGVVGTFWWKFLGLY
Protein: cAMP-dependent protein kinase type II-alpha regulatory subunit (P12367)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- A-kinase anchor protein 10, mitochondrial
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase type II-beta regulatory subunit
- cAMP-dependent protein kinase type I-beta regulatory subunit
- A-kinase anchor protein 7 isoform gamma
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- Hormone-sensitive lipase
- A kinase
- A-kinase anchor protein 1, mitochondrial
Sequence:
MSHIQIPPGLTELLQGYTVEVGQQPPDLVDFAVEYFTRLREARRQESDTFIVSPTTFHTQESSAVPVIEEDGESDSDSEDADLEVPVPSKFTRRVSVCAETFNPDEEEEDNDPRVVHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFEKIVKTDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIIATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLFKSLEMSERMKIVDVIGEKIYKDGERIIAQGEKADSFYIIESGEVSILIRSKTKSNKNGGNQEVEIAHCHKGQYFGELALVTNKPRAASAYGVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSNLDLMDPGQ
Protein: Nucleoprotein (Ebola NP) (eNP) (Nucleocapsid protein) (Protein N) (P18272)
Organism: Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Function: Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response. VP35 binds to and stabilizes monomeric NP, keeping it soluble. Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm. Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid. Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription. Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1.
Subcellular location: Virion {ECO:0000269|PubMed:16719918}. Host cytoplasm {ECO:0000269|PubMed:28794491, ECO:0000269|PubMed:29290611, ECO:0000269|PubMed:32528005}.
Interaction partners:
Sequence:
MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAPDDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHASAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNRTPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQGPFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQFYWPVMNHKNKFMAILQHHQ
Protein: WD repeat-containing protein 20 (Protein DMR) (Q8TBZ3)
Organism: Homo sapiens (Human)
Function: Regulator of deubiquitinating complexes. Activates deubiquitinating activity of complexes containing USP12. Anchors at the base of the ubiquitin-contacting loop of USP12 and remotely modulates the catalytic center of the enzyme.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30466959, ECO:0000269|PubMed:33844468}. Nucleus {ECO:0000269|PubMed:30466959, ECO:0000269|PubMed:33844468}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 12
- WD repeat-containing protein 48
- Ubiquitin carboxyl-terminal hydrolase 46
- PH domain leucine-rich repeat-containing protein phosphatase 2
- PH domain leucine-rich repeat-containing protein phosphatase 1
- BRCA1-associated protein
- Ubiquitin carboxyl-terminal hydrolase 1
Sequence:
MATEGGGKEMNEIKTQFTTREGLYKLLPHSEYSRPNRVPFNSQGSNPVRVSFVNLNDQSGNGDRLCFNVGRELYFYIYKGVRKAADLSKPIDKRIYKGTQPTCHDFNHLTATAESVSLLVGFSAGQVQLIDPIKKETSKLFNEERLIDKSRVTCVKWVPGSESLFLVAHSSGNMYLYNVEHTCGTTAPHYQLLKQGESFAVHTCKSKSTRNPLLKWTVGEGALNEFAFSPDGKFLACVSQDGFLRVFNFDSVELHGTMKSYFGGLLCVCWSPDGKYIVTGGEDDLVTVWSFVDCRVIARGHGHKSWVSVVAFDPYTTSVEEGDPMEFSGSDEDFQDLLHFGRDRANSTQSRLSKRNSTDSRPVSVTYRFGSVGQDTQLCLWDLTEDILFPHQPLSRARTHTNVMNATSPPAGSNGNSVTTPGNSVPPPLPRSNSLPHSAVSNAGSKSSVMDGAIASGVSKFATLSLHDRKERHHEKDHKRNHSMGHISSKSSDKLNLVTKTKTDPAKTLGTPLCPRMEDVPLLEPLICKKIAHERLTVLIFLEDCIVTACQEGFICTWGRPGKVVSFNP
Protein: Beta-glucosidase (O93785)
Organism: Hypocrea jecorina (Trichoderma reesei)
Interaction partners:
Sequence:
MLPKDFQWGFATAAYQIEGAVDQDGRGPSIWDTFCAQPGKIADGSSGVTACDSYNRTAEDIALLKSLGAKSYRFSISWSRIIPEGGRGDAVNQAGIDHYVKFVDDLLDAGITPFITLFHWDLPEGLHQRYGGLLNRTEFPLDFENYARVMFRALPKVRNWITFNEPLCSAIPGYGSGTFAPGRQSTSEPWTVGHNILVAHGRAVKAYRDDFKPASGDGQIGIVLNGDFTYPWDAADPADKEAAERRLEFFTAWFADPIYLGDYPASMRKQLGDRLPTFTPEERALVHGSNDFYGMNHYTSNYIRHRSSPASADDTVGNVDVLFTNKQGNCIGPETQSPWLRPCAAGFRDFLVWISKRYGYPPIYVTENGTSIKGESDLPKEKILEDDFRVKYYNEYIRAMVTAVELDGVNVKGYFAWSLMDNFEWADGYVTRFGVTYVDYENGQKRFPKKSAKSLKPLFDELIAAA
Protein: Anion exchange protein (M9PC95)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MAEKNEYIELPWTMNSSSGDDEAPKDPRTGGEDFTQQFTENDFEVTPPAQRVQFILGEDVDDGTHVSHPLFSEMGMLVKEGDEIEWKETARWIKFEEDVEEGGNRWSKPHVATLSLHSLFELRRLLVNGSVMLDMEAQNLEVMADLVCDHMVSAGTLPPGVKDKVKDALLRRHRHQHEYAKKTRLPIIRSLADMRNHSSSKIEEHSASILGATTPISLTASEPGPPGSNGNSNLSTAAGAMGRFLTVPSGKPSNRTLEKKSNSKHSRPAQNLSSITEDMVKSPSNQSMARPGSGTELSEQQHKGNTHFMRKIPPGAEASNILVGEVDFLERTLSCFIRLSQAVVLGDLTEVPVPTRFVFILLGPPGSQSNFHEIGRAMATLMSDEIFHEVAYRARKRDHLLSGVDEFLDAVTVLPPGEWDPTIRIEPPAAIPSQEVRKRPPELPKEEVDEEEEEARLREENGLSRTGRLFGGLINDIKRKAPWYISDYKDALSMQCVASWIFLYFACLSPIITFGGLLAEATGKHMAAMESLVSGFVCGMGYGFFSGQPLTILGSTGPVLVFESIIYEFCLKMGWDYMTFRFWIGMWVAGICIVLTAIDASALVCYITRFTEENFATLIAFIFIYKAIENVMVIGKNFPVNQGIYDCVCTPPIGSNASVIDYAKYNWDSCESYNGTLVGGDCGTPPTENVFLMSVVLCAGTFLISTVLKEFKNALFFPSIVRQYISDFSVLIAIFAMSFFDYSLGVPTQKLEVPNELKPTLSTRGWLIPPFVEKNPWWSAIIAVFPALLGTILIFMDQQITAVIVNRKENKLKKGCGYHLDLFILSILIAICSMMGLPWFVAATVLSINHVNSLKLESECSAPGEKPQFLGVREQRVTHILIFLTIGVSVLLTPLLGNIPMPVLFGVFLYMGVASLKGLQFFDRILIMFMPAKYQPDYMFLRQVPIKRVHLFTMIQLACLIILWLIKSFSQTSILFPLMLVVMIGIRKALDLVFTRRELKILDDIMPEMTKRAAADDLHKLDAENPKFNTSKQLWRGYLTPTETSV
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (K7EPJ2)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFK
Protein: Small ribosomal subunit protein uS3m (28S ribosomal protein S24, mitochondrial) (MRP-S24) (S24mt) (Q9VCC3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q2M2T7}.
Interaction partners:
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS33
- LD06441p
- Small ribosomal subunit protein uS15m
- 28S ribosomal protein S14
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS12m
- GEO10172p1
Sequence:
MNFLKKLLPQVATEVQQLSRSGFHTSSVCCRVQSGRYRITTKRNRPLTYEMANPPHFIGHRKSWNSWNTSTMKDALRPSQTAIEDVFIRKFVTGTWHALVCSEVIIKRQHNTIRIAALIRQAITPRKMYFLIGYTEELLSYWMQCPVTLELQTVGDKKDVVFKYI
Protein: Eukaryotic translation initiation factor 2 subunit alpha (eIF-2-alpha) (eIF-2A) (eIF-2alpha) (eIF2-alpha) (Q9FE78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56286}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit beta
- eIF-2-alpha kinase GCN2
- protein-synthesizing GTPase
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 3 subunit C
- Translation initiation factor eIF2B subunit gamma
- Eukaryotic translation initiation factor 3 subunit A
- protein-synthesizing GTPase
Sequence:
MANPAPNLECRMYESRYPDVDMAVMIQVKTIADMGAYVSLLEYNNIEGMILFSELSRRRIRSISSLIKVGRTEPVMVLRVDRERGYIDLSKRRVSDEDKEACEERYNKSKLVHSIMRHVAETVGVDLEELYVNIGWPLYKKHGHAFEAFKIVVTDPDSVFDALTREVKETGPDGVEVTKVVPAVSEELKDAFLKDIRRRMTPQPMKIRADIELKCFQFDGVLHIKEAMKKAEAVGTDDCPVKIKLVAPPLYVLTTHTHYKEKGIVTLNKAIEACITAIEEHKGKLVVKEGARAVSERDDKLLAEHMAKLRMDNEEMSGDEGSEDEEEDTGMGEVDIDGGSGIIE
Protein: Sperm protein (Q24403)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCSPCGPCSPCDPCCGPFESSPKCYNAAQLEALPQCAPRIPPPFPKCITVQQPPRMICKKRVVFTEKIVPEPMVVNRCRQITIPKVVDATRVIKVPKLIWVSQMVREPRVIYYPSMIPDPYVVCYPKRVCEPREVCQSILCQPKPQTIDIPPPREYCCYPNGPINYKPSAACPPCPIGPCAPGGPCCPLPCFSTNQYPVAEGRCGPCGPCGPGCGPCGPRCGPCGPGPCGPCGPRCGPGGPCAVPNCGPCGLTMPSGPFVPAPCGPCAPCGPCGPLGNSPCGPCGPCGPCSPPCPYESPECGPCYPCAPTPWNTHCGPVGPCGPQVPCGPSGPC
Protein: Lysine-specific demethylase 5B (EC 1.14.11.67) (Histone demethylase JARID1B) (Jumonji/ARID domain-containing protein 1B) (PLU-1) ([histone H3]-trimethyl-L-lysine(4) demethylase 5B) (Q80Y84)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Represses the CLOCK-BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:14579128}.
Interaction partners:
- Lysine-specific histone demethylase 1A
- Histone deacetylase 1
- Polycomb protein Suz12
- Myc proto-oncogene protein
- Histone-lysine N-methyltransferase EZH2
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
Sequence:
MEPATTLPPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTSDTKDKEYKPHDIPQRQSVQPAETCPPARRAKRMRAEAMNIKIEPEEATEARTHNLRRRMGCTTPKWENEKEMKSTIKQEPTEKKDCELESEKEKPKSRAKKTATAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLVPPLHDVPKGDWRCPKCLAQECNKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKISPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCIKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYNLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQQSQKLLSEEMPSAAELQELLDVSFEFDVELPQLTEMRIRLEQARWLEEVQQACLDSSSLSLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLRARPRHSLSSLATAVKEMEEIPAYLPNGTVLKDSVQRARDWVQDVDALQAGGRVPVLETLIELVARGRSIPVHLNSLPRLEMLVAEVHAWKECAAKTFLPENSTYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPSGKKRSTKLESLSDLERALMESKETAAAMATLGEARLREMEALQSLRFANEEKLLSPVQDLEMKVCLCQKTPATPMIQCELCRDAFHTSCVAAPSISQSSRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKLVQDQVGSGLLSSRWPASAGQASATDKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGQSCLPLHGLSPEVNELLMEAQLLQVSLPEIQELYQTLLTKPSSVQQADRSSPVRSSSEKNDCLRGKRDAINSPERKLKRRPEREGLPSERWDRVKHMRTPQKKKIKLSHPKDMDSFKLERERSYDLVRNAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTGKDAPSRK
Protein: Helix-loop-helix DNA-binding domain containing protein, expressed (Os11g0523700 protein) (Q2R3F6)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Os03g0737200 protein
Sequence:
MLPRFHGAMWMQDDGGGDQEHGQAAPPGQEQHHHDQHLMALAAAAAGGAGFGAAQAPAPLLDEDWYFDAAGGGGGGAHGSMMLGLSSVHGGIGAGTSGGGHGQQFSLLNMGAAAAPFDVSGFDLGIACGGVGGGGDVVSFLGGGNASNTALLPVGNAGFLGTFGGFGTAASQMPEFGGLAGFDMFDAGAVNTGGSSSSSSAAAAAASASAHVSNTAPFSGRGKAAVLRPLDIVPPVGAQPTLFQKRALRRNAGEDDDDKKRKAAAGAGAGALSADGADMVLDDGDDDGLSIDASGGLNYDSEDARGGEDSGAKKESNANSTVTGDGKGKKKGMPAKNLMAERRRRKKLNDRLYMLRSVVPKISKMDRASILGDAIEYLKELLQKINDLQNELESSPATSSLPPTPTSFHPLTPTLPTLPSRIKEEICPSALPSPTGQQPRVEVRLREGRAVNIHMFCARRPGLLLSAMRAVEGLGLDVQQAVISCFNGFTLDIFKAEQCKDGPGLLPEEIKAVLMQSAGFHTMI
Protein: RH44771p (Succinate dehydrogenase, subunit C, isoform A (EC 1.3.-.-)) (Succinate dehydrogenase, subunit C, isoform B) (Q9VGS3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- NADH dehydrogenase 23 kDa subunit
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- Cytochrome b-c1 complex subunit 8
- NADH dehydrogenase 24 kDa subunit, isoform A
Sequence:
MYALSSSLIRSPALRQGLQMAAASRPVSMKVVSVAETQKDESFFEKNERLGRELSPHLTIYQPQLTSMLSICHRGTGLALGVGVWGLGLGALISSHDISHYVTMVEGLQLSGATLTALKFIIAYPAGYHTANGIRHLLWDTGRFLKIKEVYSTGYAMVATSFVLSAILALL
Protein: Lysine-specific demethylase 5D (EC 1.14.11.67) (Histocompatibility Y antigen) (H-Y) (Histone demethylase JARID1D) (Jumonji/ARID domain-containing protein 1D) (Protein SmcY) ([histone H3]-trimethyl-L-lysine(4) demethylase 5D) (Q9BY66)
Organism: Homo sapiens (Human)
Function: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May play a role in spermatogenesis. Involved in transcriptional repression of diverse metastasis-associated genes; in this function seems to cooperate with ZMYND8. Suppresses prostate cancer cell invasion. Regulates androgen receptor (AR) transcriptional activity by demethylating H3K4me3 active transcription marks.
Subcellular location: Nucleus {ECO:0000269|PubMed:27185910, ECO:0000269|PubMed:27477906, ECO:0000305}.
Interaction partners:
- ATP-dependent RNA helicase DDX3Y
- Eukaryotic translation initiation factor 1A, Y-chromosomal
- Small ribosomal subunit protein eS4, Y isoform 1
- Ubiquitin carboxyl-terminal hydrolase 9Y
- Histone demethylase UTY demethylase UTY)
- Zinc finger Y-chromosomal protein
- Putative serine/threonine-protein kinase PRKY
- Thymosin beta-4, Y-chromosomal
- Small ribosomal subunit protein eS4, Y isoform 2
- ATP synthase F
Sequence:
MEPGCDEFLPPPECPVFEPSWAEFQDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRVQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERKILDLYSLSKIVIEEGGYEAICKDRRWARVAQRLHYPPGKNIGSLLRSHYERIIYPYEMFQSGANHVQCNTHPFDNEVKDKEYKPHSIPLRQSVQPSKFSSYSRRAKRLQPDPEPTEEDIEKHPELKKLQIYGPGPKMMGLGLMAKDKDKTVHKKVTCPPTVTVKDEQSGGGNVSSTLLKQHLSLEPCTKTTMQLRKNHSSAQFIDSYICQVCSRGDEDDKLLFCDGCDDNYHIFCLLPPLPEIPRGIWRCPKCILAECKQPPEAFGFEQATQEYSLQSFGEMADSFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVTVEYGADIHSKEFGSGFPVSNSKQNLSPEEKEYATSGWNLNVMPVLDQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKMLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAAFPETLDLNLAVAVHKEMFIMVQEERRLRKALLEKGVTEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPTMLHKLKIRAESFDTWANKVRVALEVEDGRKRSFEELRALESEARERRFPNSELLQRLKNCLSEVEACIAQVLGLVSGQVARMDTPQLTLTELRVLLEQMGSLPCAMHQIGDVKDVLEQVEAYQAEAREALATLPSSPGLLRSLLERGQQLGVEVPEAHQLQQQVEQAQWLDEVKQALAPSAHRGSLVIMQGLLVMGAKIASSPSVDKARAELQELLTIAERWEEKAHFCLEARQKHPPATLEAIIRETENIPVHLPNIQALKEALTKAQAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKALGLYQCDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLAPSLMASSPTSICVCGQVPAGVGVLQCDLCQDWFHGQCVSVPHLLTSPKPSLTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAIGWQDRARKALASEDVTALLRQLAELRQQLQAKPRPEEASVYTSATACDPIREGSGNNISKVQGLLENGDSVTSPENMAPGKGSDLELLSSLLPQLTGPVLELPEAIRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLDRIRTLLELEKFEHQGSRTRSRALERRRRRQKVDQGRNVENLVQQELQSKRARSSGIMSQVGREEEHYQEKADRENMFLTPSTDHSPFLKGNQNSLQHKDSGSSAACPSLMPLLQLSYSDEQQL
Protein: GH23983p (Vrille, isoform A) (Vrille, isoform D) (Vrille, isoform F) (Q9VMS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein cycle
- Circadian locomoter output cycles protein kaput
- Protein timeless
- Transcription factor cwo
- Cryptochrome-1
- Timeout
- Supernumerary limbs, isoform B
- Discs overgrown protein kinase
- Ecdysone-induced protein 75B, isoform B
- Protein PDF
Sequence:
MSIVCTLEQKVNFFKAAATTKNLLILKNNTDTNYINNYKQDNPSNNKFPRIQAQSNNSHLQHQQQLQQKLAQLHHYSQQKLSGSDFPYGPRPPTGGKEEKLLLLAPPGKLYPEASVSTAMPEVLSGTPTNSHNKANIAMMNNVRLSNISPTLSMNGSSNEASNLHPLSMYGGSISPQSNDSGMSDSLGKYVPGSGYGDGMMAQSPSQGGNGPQSALTAAQKELFSQRKQREFTPDNKKDESYWDRRRRNNEAAKRSREKRRYNDMVLEQRVIELTKENHVLKAQLDAIRDKFNISGENLVSVEKILASLPTSEQVLSNTKRAKMSGSGGSSSGSSPSGSGSGEGSPQGGHNGYPVGPPLSPLIYGPNGNARPEATVKSVHHIHHAGVAPPPTHLQQLVVPQSQTQHLYQPQPQQHQPHQQQQISQPPQQQQQQQEPSPSAGSSSPVISDPHNRPPSTTIANLQVQLQQALNRNVRPEDLDSLRKVVAAGALYNAAAVVGAPPPPPSAGLYVPAPSAYKDHLEAAAAWSHNVEAAVSSSAVDAVSSSSVSGSAASVLNLSRRACSPSYEHMLSSTTSSTLSSASSSGAVSGDDEQEHEPAHMAPLQLQRSSPQQGSDANNCLPLKLRHKSHLGDKDAAATALLSLQHIKQEPNCSRASPPAWNDGGDNSSDERDSGISIASAEWTAQLQRKLLAPKEANVVTSAERDQMLKSQLERLESEVASIKMILAE
Protein: Cdc13p (Q5AB98)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Telomere replication protein EST3
- Est1p
Sequence:
MCFIRKTRKINKQNRARLQKFFFFINTCQLLSLQLHTQLQYEMARDLIKIEDFPEIMDGQKQGPRVGFCGLVVRFYPSRRDYIGMDVTDFTSHPRVCQNQEYYNGGLLLARNELLTIPVKIEALKRIQVSYPGIFGEQYNLAEEYYSASGVLDVHDKLLVVKMTLRTRLYQGFYEPYSYDQEIVDYEYLGNKDRLVVDDLFRNIVSRKEYFSKVSHLAPRLMPAKFLISTGHSSEVSDKVQHLNAISSVPDTKIKSPPHNSQYIHPPDPNTIRSSPTQNLVPDIEHGDFDFCNSSTVGSPEEEQVFTISELKQLDMTIDNKTYMVSCKIIGCFPDDWMYLSGKEMDPKSNTAKDPIIRDLEWIIADANVDERTVLNSENTLSVISPAQDILEFSNYGSVEDFFIGCSGYRKKSNSIFNIPTKLEVRKIEIPINSSTTTVVWSPVESK