wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q1MT86)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTEVSEILMSVLSAIRVPRPGDRVHKDECAFSFSSPESEGGLYVCMNSFLGFGSKYVDRHHAKTGQRAYLHITRTRKTQKEDDPNSGSGDPPKKKPTRLAIGIEGGFDVEQEQYEEEVKVVLFPDRQEVTLDDLSSMPDVVRERVSLSVAELQAADSVSHTLQVQQWDGEVRQESKHAAELKQLDNGLKIPPSGWKCEVCELQENLWMNLTDGKVLCGRRYFDGSGGNNHALLYYQQTGYPLAVKLGTITPDGADVYSYDEDDMVLDSKLPEHLSHFGIDMMTMEKTERTMTELEIAVNQRVGEWEVIQESGTTLRPLWGPGLTGMKNLGNSCYLNSVMQVLFTIPDFQTKYVSNIDKIFDEAPSDPTQDFKTQVAKLGYGLLSGEYSKPAPDPADEPNTSAEPRGDQVGIAPRMFKALVGRGHPEFSTNRQQDAQEFLLHFINMVERNCRSGMNPSEAFRFLVEEKIVCQQSQKAKYTQRVDYIVQLPVPMDQATNMDELQEAERRREEAESSGAPPPVAPRAQIPFAACLAALSEPETLTDFWSSAVQAKTTATKTTRFASFPDHLVIQIKKFTFGLDWVPKKLDVSIDVPETLDLNALRAMGQQPGEELLPEVAPPPLMTPDVEVKGILGSHGNEEDDSLYSPLLSPVLDDSTVSQLCEMGFPLEACRKAVYYTGNTGIDAAMNWVMGHMDDPDFAAPLVLPGSSSAPGTTPTESLPEEHLATIVSMGFSRDQATRALRATNNVLERAVDWIFSHLDDLESMDVSEGGRSEGGSEASREPPPGPRVRDGTGKYELFAFISHMGSSTMCGHYVCHIKKDQQWVIFNDQKVCASEKPPKDLGYLYFYRRVVE
Protein: Immunoglobulin kappa variable 1D-39 (Ig kappa chain V-I region Daudi) (P04432)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVPAQLLGLLLLWLRGARCDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTP
Protein: 5-aminolevulinate synthase (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase) (Q5JAM2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU910713}; Peripheral membrane protein {ECO:0000256|RuleBase:RU910713}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000256|RuleBase:RU910713}.
Interaction partners:
Sequence:
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPERVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLELKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
Protein: Glucosidase II subunit alpha (Q20239)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Glucosidase 2 subunit beta
- Mannosyl-oligosaccharide glucosidase
- alpha-1,2-Mannosidase
- Glycoside hydrolase family 31 N-terminal domain-containing protein
- L-xylulose reductase
- Calnexin
- J domain-containing protein
- UDP-Glucose Glycoprotein glucosylTransferase
Sequence:
MTAGSSWIVPIILLATPLAVQMVKRDDFKTCEQSAFCKQHRAITVRRGSQNHHNWSLQEPTGYELLADSITHHGAVWTANVRNSQNTLKINVIGLADSTVRVQIDEPESAIRKRYVPNPALVSLPEELEFSSVENGDQEAKIIGGNKKLKVVVTYKPFLVSIFNEFDELVAQLNRDGKLKVEEFRTKEEGKEYPEGFWEERFKGFTDHKQHGSSSVGVDISFVNFKTAYGLPEHADAFALRNTVGNSDPYRLYNLDVFEYELNNPMALYVSIPYILAHRANRSVGALWFNAAETWVDTQSSVTSKGLFGKMLDKVTGSSDNVPHFDAHFISESGLVDVFFFVGPTVKDVQRQNSKLTGVTPLPPLFSIGYHQCRWNYNDEQDVATVNQGFDDHDMPMDVIWLDIEHTDGKKYFTWDKHKFPTPNDMVDKVAAKGRKMVTIVDPHIKKDDGYYVYKDAKDKGLFVKRVDGSDFEGHCWPGSSEYLDFWHPDTRSYWKDQFAFDRYTGSSSNLHIWNDMNEPSVFSGPEITMDKESIHYGGIEHREIHNMYGMMYTSATFDGMIARTGGKERPFLLSRAGFIGTQRTAAIWTGDNTADWGHLEIAAPMTLSLSIAGVPFVGADVGGFFGNPDEQLLSRWYQTAAFQPFFRAHAHIDTRRREPWLFSEQTQQIIREALRTRYALLPYWYTLFQQHTENGVPPMRPLFYEFENDDLLLEEQKQWMVGSGILARPVVEKDTFNVQVKLPRGEHKTERWFEWVSGNEVRGESIYVDAPITFTPIYQRGGTIIPTWQRIRRSATLMKDDPITLFVALDSNENSNGEIYLDDGNTHDYQSGQFVKASFKYTTLSKNSAMLEGEHLDGKYAAKNWIERVVVRGVESSPKKVEITRVSDPVQSLEFSYDHDSKVLVIRKPEALLTSSFKVHIEF
Protein: SAC3 domain-containing protein 1 (SAC3 homology domain-containing protein 1) (A6H687)
Organism: Mus musculus (Mouse)
Function: Involved in centrosome duplication and mitotic progression.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15322101}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15322101}. Note=Localizes on centrosomes in interphase cells and at spindles in mitosis.
Interaction partners:
- Transcription and mRNA export factor ENY2
- 26S proteasome complex subunit SEM1
- PCI domain-containing protein 2
- Transmembrane protein 160
Sequence:
MGRFKGENRSQARWIMGGVSKGRGSGKSRKPRQAAFGQTGARVCPSSPQQDAVPRFRWPGDAECASSTHTPTMSGCKLPMGLCPDMCPAAERARRERERRLHRLEVEPGGRGNAPRADPKRTVKEYSRPAAGKPRPPPSLLRPPPVLLATVRYLAGEVAGRGDVSCAEVASFVADRLRAVRLDLSLQGVDDADAATVLEAALATLLAVVARVRPEETRGAADPVLLQTQVQEGFGSLRRCYARGKGPYPRQAAFQGLFLLYNLGSVEALQEVLQLPAALRACPPLQAALAVDAAFREDNHARLFRLLRTLPYLQSCAVQEHIGYARRKALARLSRALSTPKGQTLPLDFIEHFLALDGLQEARDLCQAHGLTLDKDRVVFLRGQYSEEGLPPPGAYHILVGNKLQGHTLEDVVMAEEGDIHRPGSAA
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC 3.1.4.11) (PLC-154) (Phosphoinositide phospholipase C-beta-1) (Phospholipase C-beta-1) (PLC-beta-1) (Q9Z1B3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein-coupled receptors. Regulates the function of the endothelial barrier.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:18802028}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000269|PubMed:18802028}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Guanine nucleotide-binding protein subunit alpha-14
- Guanine nucleotide-binding protein G
- Protein kinase C beta type
- Protein kinase C alpha type
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Guanine nucleotide-binding protein subunit alpha-15
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKAPKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTASLAPKPPSQAPHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHNEIRQQILDEKPKLQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPPSLASDAAKVNLKSPSSEEIERENPGREFDTPL
Protein: Nuclear pore complex protein Nup54 (54 kDa nucleoporin) (Nucleoporin Nup54) (P70582)
Organism: Rattus norvegicus (Rat)
Function: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Cytoplasmic side {ECO:0000269|PubMed:8707840}. Nucleus membrane {ECO:0000269|PubMed:8707840}; Peripheral membrane protein {ECO:0000269|PubMed:8707840}; Nucleoplasmic side {ECO:0000269|PubMed:8707840}. Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter.
Interaction partners:
- Nucleoporin p58/p45
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup93
- Nucleoporin 205
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup107
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup153
Sequence:
MAFNFGAPSGTSGTSTATAAPAGGFGGFGTTTTTAGSAFSFSAPTNTGSTGLLGGTQNKGFGFGTGFGTSTGTGTGLGTGLGTGLGFGGFNTQQQQQQQQTSLGGLFSQPAQAPAQSNQLINTASALSAPTLLGDERDAILAKWNQLQAFWGTGKGYFNNNIPPVEFTQENPFCRFKAVGYSCMPNNKDEDGLVVLIFNKKETDIRSQQQQLVESLHKVLGGNQTLTVNVEGIKTLPDDQTEVVIYIVERSPNGTSRRVPATTLYAHFEQANIKTQLQQLGVTLSMTRTELSPAQIKQLLQNPPAGVDPIIWEQAKVDNPDSEKLIPVPMVGFKELLRRLKVQDQMTKQHQTRLDIISEDISELQKNQTTTMAKIAQYKRKLMDLSHRTLQVLIKQEIQRKSGYAIQAEEEQLRVQLDTIQGELNAPTQFKGRLNELMSQIRMQNHFGAVKSEEKYYIDADLLREIKQHLKQQQEGLSHLISIIKDDLEDIKLVEHGLNETIHSRGGVFS
Protein: Small RNA 2'-O-methyltransferase (EC 2.1.1.386) (HEN1 methyltransferase homolog) (P34283)
Organism: Caenorhabditis elegans
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of PIWI-interacting RNAs (piRNAs) and small interfering RNAs (siRNAs) which are classes of regulatory RNAs that are involved in gene silencing in endogenous RNA interference (RNAi) pathways. Methylation protects the 3'-end of small RNAs from tailing and trimming and could constitute a recognition signal for appropriate argonaute machineries (Probable). Methylates and stabilizes 26G-siRNAs (a class of 26 nucleotide siRNAs that possess a monophosphorylated guanine residue at the 5'-end) when they are bound by argonaute protein ergo-1. This occurs in the female germline and embryo, but not in the male germline. Does not methylate 26G-siRNAs bound by argonaute proteins alg-3 or alg-4. Methylates and stabilizes 21U-piRNAs, which are a class of 21 nucleotide piRNAs that possess a uracil residue at the 5'-end, in the male and female germline. In addition, may play a role in exogenous RNAi (exoRNAi) pathways in the germline.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22548001, ECO:0000269|PubMed:22829772}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22548001}. Cytoplasmic granule {ECO:0000269|PubMed:22829772}. Note=Nucleoplasm localization ceases following fertilization (PubMed:22548001). In embryos, diffusely localized in the cytoplasm (PubMed:22829772). In cells of the P-lineage (germ cell progenitor cells) in embryos, localizes to granules and at later postembryonic stages of development, localizes to perinuclear granules in the germ cells (PubMed:22829772). {ECO:0000269|PubMed:22548001, ECO:0000269|PubMed:22829772}.
Interaction partners:
- 3'-5' exoribonuclease parn-1
- Piwi-like protein ergo-1
- Piwi-like protein 1
- Argonaute
- Argonaute protein hrde-1
- Schlafen-like protein 1
- K Homology domain-containing protein
- Uncharacterized protein ZK1320.5
- C-type lectin domain-containing protein
- F-box C protein
Sequence:
MAHTSDGWGAPYDNQTYVEAYEQLEIALLEPLDRILETANVEEFRPKFKNHQDPNDRKNKKNNDEEWRDSIYNIATDESDTDDHEQRKNFFQPPLQVQRNSFVKNTLMEFKRSSQIDISRLAVMGCGEMSLEKGICEYLGSFGTINVLSVDIDEPSLSIGQQLLGKHLERNAEILAVETGLPVLMRSYVGDILEPDHRFADVDAIVSMEVVEHIPLPNAKKFVENVLGTLMPRIFIFSTPNHEYNAVFGMEPGEFRHGDHKFEMNRKEFSNWLEELSIRFPHYQIDPPHYIGMTRGYENLSGASQAAVCRLQVDLNTTLPQEVTPYEMVGHLPCRLGSRLIAYNLVKEAFLDWLEKIELQEHEPRTDGYSPYWIFNVQNILHHLKAPVSFALTIDEKVAIKYIQGMTSRKVHAEYSHGFNGIVILQMHSKEELIKTVQDNTL
Protein: Uncharacterized protein C106.07c (Q9URV4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSNLWRNLKSVRLPFRRAPTLPLYNVPVRRSISSSSSIPPSSSPPPRLTITQRVKELTKKYGWWSLGVYIGISVLDFSASFVLVRTLGAERIGYLEHSILNSIRRYFNWEIPESTASGEPEAYHSSIWTELAFAYGIHKALVVARVPLTAAIVPPLAKRFRGPRIRP
Protein: Mitogen-activated protein kinase 15 (EC 2.7.11.24) (Swimming-induced paralysis protein 13) (SWIP-13) (Q11179)
Organism: Caenorhabditis elegans
Function: Atypical MAPK protein. Regulates primary cilium formation in sensory neurons and the localization of ciliary proteins involved in cilium structure, transport, and signaling. Acts in dopamine (DA) neurons to support synaptic membrane dat-1 availability via activation of rho-1 thereby sustaining normal levels of DA clearance. Plays a role in male mating behavior, probably in part through regulating the localization of the polycystin pkd-2. Functions postembryonically in the URX sensory neurons to constrain URX dendrite growth throughout lifetime, probably by restricting expansion of the subcellular sensory compartment at the dendrite ending.
Subcellular location: Cell projection, dendrite {ECO:0000269|PubMed:29879119}. Note=Enriched localization at the URX dendrite ending. {ECO:0000269|PubMed:29879119}.; SUBCELLULAR LOCATION: [Isoform a]: Perikaryon {ECO:0000269|PubMed:28745435}. Cell projection, dendrite {ECO:0000269|PubMed:28745435}. Cell projection, cilium {ECO:0000269|PubMed:28745435, ECO:0000269|PubMed:29021280}. Cell projection, cilium membrane {ECO:0000269|PubMed:28745435}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29021280}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29021280}. Cell junction {ECO:0000269|PubMed:29021280}.; SUBCELLULAR LOCATION: [Isoform c]: Perikaryon {ECO:0000269|PubMed:28745435}. Cell projection, dendrite {ECO:0000269|PubMed:28745435}. Cell projection, cilium {ECO:0000269|PubMed:28745435, ECO:0000269|PubMed:29021280}. Cell projection, cilium membrane {ECO:0000269|PubMed:28745435}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29021280}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29021280}. Cell junction {ECO:0000269|PubMed:29021280}.
Interaction partners:
Sequence:
MTDDVDTHIHEKFDLQKRLGKGAYGIVWKAYDKRSRETVALKKIFDAFRNPTDSQRTFREVMFLQEFGKHPNVIKLYNIFRADNDRDIYLAFEFMEADLHNVIKKGSILKDVHKQYIMCQLFRAIRFLHSGNVLHRDLKPSNVLLDADCRVKLADFGLARSLSSLEDYPEGQKMPDLTEYVATRWYRSPEILLAAKRYTKGVDMWSLGCILAEMLIGRALFPGSSTINQIERIMNTIAKPSRADIASIGSHYAASVLEKMPQRPRKPLDLIITQSQTAAIDMVQRLLIFAPQKRLTVEQCLVHPYVVQFHNPSEEPVLNYEVYPPLPDHIQLSIDDYRDRLYEMIDEKKASFKRIQHEKIRPYGEDKSRAPIAQAECSDTDYDTARSLQRTTSMDKNNSSSHDSSSGTLRERAASAESRTSKDSNGEMRNGNGNTPSSIKQRRRSVERARLFANIKPSKILHPHKLISNY
Protein: p44-11 outer membrane protein (Q2GIB3)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MMSMAIVMAGNDVRAHDDVSALDTGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDKLTAALAKTSGKDIVQFAKTLGISHSEIDKKVCATKSGGSGSKYGEYAIETDNNSTGGNGKVAVCGGQNTSNSNGSTGQQFLRDFVKGSLEDGSKNWPTSKHKAGTPASETNDNAKAVAGDLTKLTSDEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGHITPKLAYRLKAGLSYQLSPEISAFAGGFYHRVVGDGV
Protein: CD209f antigen (D3Z1H5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAGEPEFHQSKNHEEEVTSGEQGFAEHDPEGLICSSKSLQGHLTQVPWLLLLLISLGLFLLMLATLVQVSRIRAYSQGQTQDQQGSSSLDKVAVPREQTHSGLEQIQQIQQQLTQFNASLGPRQKGEEKPATELSVCSVAGLCRPCPWDWELFQGSCYLFSRTLGSWETSASSCEDLGAHLVIVNSVSEQRFMKYWNVRKNQRSWIGLSDHIHEGSWQWVDGSALKFSFWKEGEPNNDGDEDCVELFMDDWNDNKCTEQNFWVCEQPSAPCPHH
Protein: Transcription initiation factor TFIID subunit 8 (TAFII-65) (TBP-associated factor 65 kDa) (TBP-associated factor 8) (Q03750)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor TFIID subunit 11
- SAGA complex/transcription factor TFIID complex subunit TAF9
- Transcription initiation factor TFIID subunit 14
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex/transcription factor TFIID complex subunit TAF10
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
- TATA-box-binding protein
Sequence:
MTSKTSESGTGTQSTIVQLRNLPDLTEISHLEIDAPVVEILKKTVLFQLNSLNICISNFALDELVNLVTVQMDGMFRNLHNLTLLQRRSQASQADLKLLLREFNLDAPSLYQQFQASEFIKSKHSTEYEKLMSWSSLAALPHNEEDEEDELNNIEEQQNEINVLLPPSNPLEKQIPSWLPNFPPDHTYKFTPEFNHPITDLKTIKKEIVKESQESEKALLNLNKSLSHISSASNTPQPPGLDDEDAIEQQLEIWGNALEERKPTITEKSFNENNIEQYAKYRVELARERVTKFEVNQLKRTKNPFLKISETLYLPESPHQSHKTIQKTIELQFRKSMTLFMHNLPKVQKLKKEKIRMAKEERAKSLKRRQEELISQRTKREQDEGHDLELLLNNEHARDAADDTTTPNALNNSTIVINTNAEDEDDDINLFGILGSSEDENEMSSMPAENLVAESEPPTMTAQDTTNTTPVAHNTTNIDATTSHSPHSTPNENAPTSPPADIATDHDITM
Protein: NAC domain-containing protein 2 (SlNAP2) (K4BNG7)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Transcription factor that binds DNA motifs 5'-CGT[AG](5N)NACG[ACT][AC][AT][ACG][ACT]-3' and 5'-CACG[ACT][AC][AT][AGT][CT]-3' in target genes promoters. Promotes leaf senescence (developmental, light-induced and ABA-induced senescence) and regulates fruit yield and sugar content, probably by establishing abscisic acid (ABA) homeostasis. Activates the expression of senescence and ABA associated genes including NCED1, ABCG40, CYP707A2, SAG113, SGR1 and PAO, by directly binding to their promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353}.
Interaction partners:
- Protein STAY-GREEN 1, chloroplastic
- Homeobox domain-containing protein
Sequence:
MVGKNNSNHLPPGFRFHPTDEELIMYYLRNQATSKPCPSSIIPEVDVYKFDPWELPEKTEFGEKEWYFFTPRDRKYPNGVRPNRAAVSGYWKATGTDKGIYSGTKYVGIKKALVFYKGKPPKGIKTDWIMHEYRLSESRTQPTRPNGSMRLDDWVLCRIYKKKNLERAIEMMKVEEDTQEPQIMSVTNPIHEVVASNGQQTLKLPRTCSLSHLLEMDYFGSISQLFDDNNSYNTISQNNTLMTNVNGYVMPHQAMEKFQLGEVSQISMNPSYQFQ
Protein: P-type Cu(+) transporter (EC 7.2.2.8) (A0A669KA36)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
Sequence:
VEGMTCQSCVSSIEGKVRKLQGVVRVKVSLSNQEAVITYQPYLIQPEDLRDHVNDMGFEAAIKSKVAPLSLGPIDIERLQSTNPKRPLSSANQNFNNSETLGHQGSHVVTLQLRIDGMHCKSCVLNIEENIGQLLGVQSIQVSLENKTAQVKYDPSCTSPVALQRAIEALPPGNFKVSLPDGAEGSGTDHRSSSSHSPGSPPRNQVQGTCSTTLIAIAGMTCASCVHSIEGMISQLEGVQQISVSLAEGTATVLYNPSVISPEELRAAIEDMGFEASVVSESCSTNPLGNHSAGNSMVQTTDGTPTSVQEVAPHTGRLPANHAPDILAKSPQSTRAVAPQKCFLQIKGMTCASCVSNIERNLQKEAGVLSVLVALMAGKAEIKYDPEVIQPLEIAQFIQDLGFEAAVMEDYAGSDGNIELTITGMTCASCVHNIESKLTRTNGITYASVALATSKALVKFDPEIIGPRDIIKIIESKTSEALAKLMSLQATEATVVTLGEDNLIIREEQVPMELVQRGDIVKVVPGGKFPVDGKVLEGNTMADESLITGEAMPVTKKPGSTVIAGSINAHGSVLIKATHVGNDTTLAQIVKLVEEAQMSKNPNKHISQTEVIIRFAFQTSITVLCIACPCSLGLATPTAVMVGTGVAAQNGILIKGGKPLEMAHKIKTVMFDKTGTITHGVPRVMRVLLLGDVATLPLRKVLAVVGTAEASSEHPLGVAVTKYCKEELGTETLGYCTDFQAVPGCGIGCKVSNVEGILAHSERPLSAPASHLNEAGSLPAEKDAVPQTFSVLIGNREWLRRNGLTISSDVSDAMTDHEMKGQTAILVAIDGVLCGMIAIADAVKQEAALAVHTLQSMGVDVVLITGDNRKTARAIATQVGINKVFAEVLPSHKVAKVQELQNKGKKVAMVGDGVNDSPALAQADMGVAIGTGTDVAIEAADVVLIRNDLLDVVASIHLSKRTVRRIRINLVLALIYNLVGIPIAAGVFMPIGIVLQPWMGSAAMAASSVSVVLSSLQLKCYKKPDLERYEAQAHGHMKPLTASQVSVHIGMDDRWRDSPRATPWDQVSYVSQVSLSSLTSDKPSRHSAAADDDGDKWSLLLNGRDEEQYI
Protein: MORN repeat-containing protein (Q38AY3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein transport protein Sec61 gamma subunit, putative
Sequence:
MLTVTEDKISIPLIPDAELCDVRIGVTDPALFFSIKLEKPSQVLIEFQEFNTASRCVLLLSPTDPHPSKHTAVWKHLSPDPNKMLTILPADPSYSLGTLYLAVRYVEDNGNSFIRLKLTLRDSYEAEWYSLINKSLYCGSWLGFYYHGFGRVIYGLDARNVEEGAVRWSAHSLRKQNSRSYRREEATPVARASLLGVSRREVSWSIIALPLLTAEVYEGEWVNGKKEGLGVYQWSDRSYWGMWKEGMREGFGVFCTSNGLHYEGEWHLDNKHGLGKAFYPDGSRYQGHWEDDVRSGEGLFVYSSGVAVTGKWENDELCPEVRANYPDGSFYVGEWTKGCRHGNGTHTDAPGNVFVGKWEDDKRTGEGKLTFANGVVCVADWENGQRQGGVFTFPNGEVYVGGWNDESLCREGIGCCTYPNGDKYEGSWKDDKRHGFGKFVETGLNRSYAGEWFKGVRCGLGVQRAVDGTYHGEFEDDVRCGEGYYQGCNGSMYRGSWKGDRQVGHGIALEGETGTQYEGLFLLGKLESYGTSRSAEDIYEGTWLDGKRQGVGVASFPDGTVLRCLWHQGASQDGFVHYRYNNGDVYEGDWSNGGRCGSGTLRYADGSVYVGEWRNDKPHGCGCFTDACGETHVGEWCSGTQKDVRGKIQFIDGSMYEGDVCNRRPHGKGRLCYPDGTVFDGTFKNGIYAA
Protein: Carbon catabolite-derepressing protein kinase (EC 2.7.11.1) (Q00372)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8 (By similarity).
Subcellular location: Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma
- Candida glabrata strain CBS138 chromosome F complete sequence
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase ATG1
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
Sequence:
MENKEHHHHHHHHHHHHSNGSYVSNKVSSLADGSRVGNYQIVKTLGEGSFGKVKLAYHVTTGQKVALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRNKMSEQEARRFFQQIISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGASDLIKRMLIVNPLNRISIHEIMQDEWFKVDLAEYLVPQDLKQQEQFNKKSGNEENVEEIDDEMVVTLSKTMGYDKDEIYEALESSEDTPAYNEIRNAYILIKDNKSLIKDMKQDNNVTQELDTFLSQSPPTFQQNGDGMKASEDQKKKHSGRRLASSVTQQRTFHQPPFMDQSKEEDSTISILPTSLPQIHRANMLAQGLPAASKISPLVTKKSKTRWHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIRVRWKYDSDESRLIEDGVKKIPNLMKIVIQLFQIETNNYLVDFKFDGWESTYGDSTISTNMSEDEMSTFSAYPFLHLTTKLIMELAVNSQGN