wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear pore complex protein GP210 (Nuclear pore membrane glycoprotein 210) (Nucleoporin GP210) (Protein EMBRYO DEFECTIVE 3012) (F4KHD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP155
- Nuclear pore complex protein NUP35
- Protein SEH1
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP205
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP88
- Aladin
- AT4g11790/T5C23_220
- Nuclear pore complex protein NUP54
Sequence:
MVPVSFCFFFLLLLLSAGESSSQLVSGPHITDVNILLPPKMKNPVEYRLQGSDGCFKWSWDHHDILSVTPEFNSSSHCSTSARLRSISPYSGRKETAVYATDIQTGMVIRCKVFIDNFSRIQIFHNSIKLDLDGLSMLRVRAFDNEDNEFSSLVGLQFIWKLMPESGGSTHHLAHVPLKESPLTDCGGLCGYLDIQKKLEDSGVFADLFVVKGTKIGHEKVSVHLLEAPLTHIADEIVLTVAEAMSLEPRSPVYVLMGASFGYTLKVMRGNVPQAVDLPSPHHRWSVLNSSVAQVDSLIGLTKALSLGVTTVVVEDTRVAGHIQGSSINVVTPDTLILYISPWSMSGDLITESKPFPSSMHWYVVSGRQYLIQMKIFSGRPDAHEIYITETDDIKLYGKDSDYWKIVSLPDELSSEYGQRNSRILNAISPGLGELTSTLTYFSGHQESKEVLKVVQEIRVCEKVQFTLNSEDDTPKVLLPWTPAVYQEMELIVTGGCAKASSDYKWFTSDISILSVSAYGIIQAKRPGIATVKVVSTFDSQNFDEVIVEVSIPSSMVMLQNFPVETVVGSHLKAAVTMKALNGATFSRCDAFNSLIKWKTGSESFVIVNATSEMMMLDELRSMDSSPPCSRASIYTASTGRTVLQATLAKEFHYFDKSLSESIDLKATLTIGAYLPLSVRQDSDGNHHGGYWFDKAQEETDFGVSKLYLVPGTYVDVMLLGGPERWDDNVEFTETVKTLYEDEEDLTSRVNVHHEVDRRANMYRISCQKLGSYKLVFLRGNLLGIDHPVPAVAEALLSVHCSLPSSVVLIVDEPVNKLDVIRAASQADRAPGRLRVTPVTVANGQIIRVAAVGISEFGEAFSNSSTLSLRWELTSCNNLAYWDDDYNSKMTKSGWERFLALRNESGLCTVRATVSGIDYSFKSQYSTLLPQGSESTLTDAVRLQLVSTLRVTPEFNLVFFNPNAKVNLSMTGGSCLWEAVVNNSRVAEVIRPPSGLQCSQMMLSPKGLGTTIVTVYDIGVSPPLSALALIKVADVDWIKIASGDEISIMEGSTHSIDLLTGIDDGMTFDSSQYSLMDIMVHIEDDLVEHVTVDEDSLSVGEHVATSSFKIAARRLGITTLYVSARQQSGGKVLSQTIKVEVYSPPRLHPQGIFLVPGASYVLTIEGGPTMNVSVDYTTVDNEVAKIEKSGRLYATSPGNTTIYATIYGSEGAVICQAIGNAEVGLPATAMLVAQSDTVAVGHEMPVSPSFPEGDLLSFYELCSAYKWTIEDEKVLIFIASSINVEENAGFVNVVQGRSAGKTRVTIAFSCDFVSPGLYSESRTYEASMILSVVPDLPLSLGAPMTWVLPPFYTSSGLLPSSSEPQKHRDGQSHRGNIVYSILKDCSSRADFERDTISINGGSVKTTDSNNVACIQAKDRTSGRIEIAACVRVAEVAQIRMKSEGIPFHVIDLAVGGELELPINYYDTLGIPFLEAHGVTTYNVETNHRDVVFIKTVNDQPSAYIKGIKHGKALIRVSIGDNLRKSDYVLVSVGAHIFPQNPVIHTGNLLNFSITGADNEVTGQWFTSNRSVISVNVASGQAKAISQGSTHVTFKGHGLKLQTKVTVLFGNTIYVDSPGETLTNVHVPAEGYKFPVKFRENKFAVTEHGNKATFNCQVDPPFIGYTKPWMDLDTGNTYCLFFPYSPEHLVHSMSITKDMKPHVSFSVDASLKEARRVSGSASALLIGGFSVTGPDKLNINPDSNTTIISLVGNTDVQIHCRNKGRLSISLIKRDDFGIAGHAQYKVNVLRSEQFTDRIIITLPATGQIVEIDVCYDTGESLVASSKDGYSVLLKILWGVLVLVVSVIILMKVIDRQVPTGATGTATYSGNAAQGTPERRSGTVIYHEESPRTPSPFMEYVKRTVDETPYYRREGRRRFNPQNTM
Protein: FMRFamide-like neuropeptides 3 [Cleaved into: SPLGTMRF-amide; TPLGTMRF-amide; SAEPFGTMRF-amide; NPENDTPFGTMRF-amide; ASEDALFGTMRF-amide; EAEEPLGTMRF-amide; SADDSAPFGTMRF-amide; NPLGTMRF-amide] (Q23212)
Organism: Caenorhabditis elegans
Function: FMRFamides and FMRFamide-like peptides are neuropeptides. SAEPFGTMRF-amide inhibits the activity of dissected pharyngeal myogenic muscle system.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- FMRFamide-like neuropeptides 14
- Pre-mRNA-splicing factor ATP-dependent RNA helicase ddx-15
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 11
- FMRFamide-like neuropeptides 16
- FMRFamide-like neuropeptides 6
- FMRFamide-like neuropeptides 5
- FMRFamide-like neuropeptides 9
- FMRFamide-like neuropeptides 1
- FMRFamide-like neuropeptides 7
Sequence:
MISPNHLILLFCVNCAFLVASDATPKRSPLGTMRFGKRAIADEMTFEEDGYYPSNVMWKRSTVDSSEPVIRDQRTPLGTMRFGKRSAEPFGTMRFGKRNPENDTPFGTMRFGKRASEDALFGTMRFGKREDGNAPFGTMKFGKREAEEPLGTMRFGKRSADDSAPFGTMRFGKRNPLGTMRFGK
Protein: Sphingosine kinase 1 (SK 1) (SPK 1) (EC 2.7.1.91) (Acetyltransferase SPHK1) (EC 2.3.1.-) (Q91V26)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol (Probable). In contrast to proapoptotic SPHK2, has a negative effect on intracellular ceramide levels, enhances cell growth and inhibits apoptosis (By similarity). Involved in the regulation of inflammatory response and neuroinflammation. Via the product sphingosine 1-phosphate, stimulates TRAF2 E3 ubiquitin ligase activity, and promotes activation of NF-kappa-B in response to TNF signaling leading to IL17 secretion. In response to TNF and in parallel to NF-kappa-B activation, negatively regulates RANTES induction through p38 MAPK signaling pathway. Involved in endocytic membrane trafficking induced by sphingosine, recruited to dilate endosomes, also plays a role on later stages of endosomal maturation and membrane fusion independently of its kinase activity. In Purkinje cells, seems to be also involved in the regulation of autophagosome-lysosome fusion upon VEGFA (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16118219}. Nucleus {ECO:0000250|UniProtKB:Q9NYA1}. Cell membrane {ECO:0000250|UniProtKB:Q9NYA1}. Endosome membrane {ECO:0000250|UniProtKB:Q9NYA1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NYA1}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9NYA1}. Synapse {ECO:0000250|UniProtKB:Q8CI15}. Note=Translocated from the cytoplasm to the plasma membrane in a CIB1-dependent manner. Binds to membranes containing negatively charged lipids but not neutral lipids (By similarity). Recruited to endocytic membranes by sphingosine where promotes membrane fusion (By similarity). {ECO:0000250|UniProtKB:Q8CI15, ECO:0000250|UniProtKB:Q9NYA1}.
Interaction partners:
- Sphingosine-1-phosphate lyase 1
- Neutral ceramidase
- Acid ceramidase
- Alkaline ceramidase
- Alkaline ceramidase
- Alkaline ceramidase
- Sphingosine-1-phosphate phosphatase 1
- Sphingosine-1-phosphate phosphatase 2.
- Ceramide synthase 5
- Ceramide synthase 2
Sequence:
MQPADCPRGLLPRPCRVLVLLNPRGGKGKALKLFQSRVRPLLEEAEVSFKLMLTERQNHARELVCAEELGHWDALAVMSGDGLMHEVVNGLMERPDWESAIQKPLCSLPGGSGNALAASLNYYAGHEQVTNEDLLINCTLLLCCRQLSPMNLLSLHTASGRQLYSVLSLSWGFVADVDLESEKYRSLGEIRFTVGTFFRLASLRIYQGQLAYLPVGKAASKIPASSLAQKGPANTYLVPLEEPVPPHWTVVPEQDFVLVLVLLHTHLSTEMFAAPMGRCEAGVMHLFYIRAGVSRAMLVRLFLAMQKGKHMDLDCPYLVHVPVVAFRLEPRNQRGVFSVDGELMVCEAVQGQVHPNYLWMVSGSSDSPSGRDSQRRPPPEEPI
Protein: Polyserase-2 (EC 3.4.21.-) (Polyserine protease 2) (Serine protease 36) (Q5K4E3)
Organism: Homo sapiens (Human)
Function: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15536082}. Note=Not attached to membranes.
Interaction partners:
Sequence:
MARHLLLPLVMLVISPIPGAFQDSALSPTQEEPEDLDCGRPEPSARIVGGSNAQPGTWPWQVSLHHGGGHICGGSLIAPSWVLSAAHCFMTNGTLEPAAEWSVLLGVHSQDGPLDGAHTRAVAAIVVPANYSQVELGADLALLRLASPASLGPAVWPVCLPRASHRFVHGTACWATGWGDVQEADPLPLPWVLQEVELRLLGEATCQCLYSQPGPFNLTLQILPGMLCAGYPEGRRDTCQGDSGGPLVCEEGGRWFQAGITSFGFGCGRRNRPGVFTAVATYEAWIREQVMGSEPGPAFPTQPQKTQSDPQEPREENCTIALPECGKAPRPGAWPWEAQVMVPGSRPCHGALVSESWVLAPASCFLDPNSSDSPPRDLDAWRVLLPSRPRAERVARLVQHENASWDNASDLALLQLRTPVNLSAASRPVCLPHPEHYFLPGSRCRLARWGRGEPALGPGALLEAELLGGWWCHCLYGRQGAAVPLPGDPPHALCPAYQEKEEVGSCWNDSRWSLLCQEEGTWFLAGIRDFPSGCLRPRAFFPLQTHGPWISHVTRGAYLEDQLAWDWGPDGEETETQTCPPHTEHGACGLRLEAAPVGVLWPWLAEVHVAGDRVCTGILLAPGWVLAATHCVLRPGSTTVPYIEVYLGRAGASSLPQGHQVSRLVISIRLPQHLGLRPPLALLELSSRVEPSPSALPICLHPAGIPPGASCWVLGWKEPQDRVPVAAAVSILTQRICDCLYQGILPPGTLCVLYAEGQENRCEMTSAPPLLCQMTEGSWILVGMAVQGSRELFAAIGPEEAWISQTVGEANFLPPSGSPHWPTGGSNLCPPELAKASGSPHAVYFLLLLTLLIQS
Protein: Toll like protein (Q9XZF9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLTYLPVVWLFFALLVLRSATGQIIPLPTFCLGLSPQCTCAAEGNVVRFHCPDEYAMLLEVSEPGASLYMSYYASTELQWLPRFNISSLVKIEFDAYIFWPEKFLSDLLKTLGVQTVKTIIFRDRTLETVVTRDVLNSGNGYMETSQPENITTWHFGSVPGLKKFKFFSHVPELQESIFHGFDTLRDLHLSVNVTTLPGNMLSTVNGTLKTLTIESPGIVSFGNPLLRELQQLRNLSLALIHPFHERDKQLQPHFFGSMTNLEEVRLASATSSVNRSMFKGTNKLQLIKMNGNDDLMELPGEIFLDQVNLKTLDLSCNAIVTLHEDVFKGLGNLTLLDLSKNRLTNLSSTIFAPLTSLNVLRLNKNSLTAMSPSVFQDVVSLNYIEMVNTQFYGATLLMNYEAVVCTNDEACQYKSAEWQCDPRCICWVQRSVGSLIVDCRGTSLEELPDLPRTTLLSTVLKVGNNSLTSLPTVSEHSGYANVSGLFLSDNNLTSLGSGDQLPDNLTHLDVRGNQIQSLSEEFLLFLQEPNNTMTLSLSGNPITCGCESLSLLFFVRTNPQRVRDIADIVCTKQKKSFQQMEAFELCPSYVLLISCVVGGLVIVICLLTVFYLMFQQELKIWLYNNNLCLWWVSEEELDKDKTYDAFISYSHKDEELISKLLPKLESGPHPFRLCLHDRDWLVGDCIPEQIVRTVDDSKRVIIVLSQHFIDSVWARMEFRIAYQATLQDKRERIIIILYRELEHMNGIDSELRAYLKLNTYLKWGDPLFWSKLYYAMPHNRRVLKGQKKHAGPLI
Protein: UPF0641 membrane protein YHR140W (P38842)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11914276}; Multi-pass membrane protein {ECO:0000269|PubMed:11914276}.
Interaction partners:
Sequence:
MMSCLVPTRFTLTLNTACLLTSTWGFVRATSVVLPPSLSKAGHKQFLTIISIIATIINNAVNISNYYIQRNNKMNLETKKKSDFISRHVTLPVSLVLESIVATVYWPLRLFFVNLIMHGVESTAKTPFPMTVDMAIHLYPILYLLADHYLSGSGTKFKLSNKHAWLIVTSLAFSYFQYLAFLIDAGQGQAYPYPFLDVNEPYKSIIFVVVATITWAYYVFYQKFPPKYIKKSAKKGDKN
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q38G13)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQNQTATKVISHTAVAAGVPALLMLLSRCCQAQAVTEPSSDKVTNLCTEAKYTEYLANRIVAAAERQEREISDMQIYAEAWDLLAAVTNQTEKRAATYALAAYMSTAAATARRVHNGKYKAAVATAKFLHRRAALTRTLLAINIRGKTIVGVSKIQGYSVSIGECPGDETPILRGDGSCAHRTNDNSQPEGISVNLKTATHIKLLNSSKLRPLGITHLVEIKKTKGPESAEALVERCGHLLKGDHYVKFEASTTEKDSLITVEPIRIFEGSDSSTNCAVIQNESTKSEKDNDLLINKLCKYIKEPDPQIITISSLTPVTLANTTEVQLAFKSFFHETRGKSSAGSSVEAQLQKLYGGDKQNFTRDFVKVLWTKNVTYHIGSGFVTETLLDAVRNKNAQKALIYLEDQRPTEEAKQAQSDETEITKTGCSGKGKQDCSGECTWEGNEEKGRCESDERKDTKKQNETQMRKWPRALQWMMARQEGNCKAIQQEDCKEDCTWEDGVCDGAVGISALMSIPLFMAFLLLA
Protein: Ethylene-responsive family protein-like (Q6K7V4)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGEGHGWWSVNNLRPPFVEQLHNPASLFLPSSTTTSTTPSSSSSPLHSFSSLLLSNHYPLPSTATTSTAAAPWHDTGSRHGQHLQDSWNHILLGGLASGEEGYNKNWEGQVLFPTTPAAAAAEADHGSNSYNNIYSTTTTSHGSSTSDDASQLAVAARPSSSPWGGIHGHHPHHNALQQQASSPRSSCITSTTSLGSNGVLEFSNNTSPRECISTASGAAFKKARTQEPSPAQATVKVRKEKLGDRITALHQLVSPFGKTDTASVLLEAIGYIRFLHGQIEALSSPYLGNGGSSSNGGGGGGGGSNSKLQHQPEASRVQGERNSIFPEDPGQLLHDNAVKKRGQPDQDESCEEAKTMDLRSRGLCLVPVSCTVDVGVDAGPADYWAAPPAFGIGFGR
Protein: Very-long-chain enoyl-CoA reductase (EC 1.3.1.93) (Synaptic glycoprotein SC2) (Trans-2,3-enoyl-CoA reductase) (TER) (Q9NZ01)
Organism: Homo sapiens (Human)
Function: Involved in both the production of very long-chain fatty acids for sphingolipid synthesis and the degradation of the sphingosine moiety in sphingolipids through the sphingosine 1-phosphate metabolic pathway. Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Catalyzes the saturation step of the sphingosine 1-phosphate metabolic pathway, the conversion of trans-2-hexadecenoyl-CoA to palmitoyl-CoA.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:24220030}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Very-long-chain
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very long chain fatty acid elongase 6
- Very long chain fatty acid elongase 4
- Stearoyl-CoA desaturase
- Acyl-CoA
- Erythroid membrane-associated protein
Sequence:
MKHYEVEILDAKTREKLCFLDKVEPHATIAEIKNLFTKTHPQWYPARQSLRLDPKGKSLKDEDVLQKLPVGTTATLYFRDLGAQISWVTVFLTEYAGPLFIYLLFYFRVPFIYGHKYDFTSSRHTVVHLACICHSFHYIKRLLETLFVHRFSHGTMPLRNIFKNCTYYWGFAAWMAYYINHPLYTPPTYGAQQVKLALAIFVICQLGNFSIHMALRDLRPAGSKTRKIPYPTKNPFTWLFLLVSCPNYTYEVGSWIGFAIMTQCLPVALFSLVGFTQMTIWAKGKHRSYLKEFRDYPPLRMPIIPFLL
Protein: Zn(2)-C6 fungal-type trascription factor aoiH (Q2TXQ7)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
- 60S ribosomal protein L7
- Large ribosomal subunit protein uL23 N-terminal domain-containing protein
- Large ribosomal subunit protein uL18 C-terminal eukaryotes domain-containing protein
- Large ribosomal subunit protein uL2m
- KOW domain-containing protein
Sequence:
MSTGSTLNQRSGKPVKLRASCDFCALSKVKCDRGQPQCVRCIKSGIDCNYSESRRIGKAWHHCAPSAVRSTSATTQGTRRKQQTIAQHSPRRRIHRDTQALSAADDAMSPYDPSGYATPFSMFHTLPSPVPESTIRSQTHIESYPSLDGTMAPILCSPESADISLPDIPHVAQLRTNELEGESPSVLQYNPSWDRIMAEHSTAIGDAGDCITRAAAVLKSVRDPRTSCVRSRTPPRSHTQSLDATLDDGRTAMDTVKDILACPCAQEIRVALLLVLIIQQVLESYQALLTQQHDTPREESPLGINLSRYDTPMAIGRYLLDNELRSKIIVQVLSSELEKIGLILDILTRHAQSMAHQPDELILGTYIDSLQTTKKEVLESLEQGNDI
Protein: Anoctamin (A0A8I6GJA0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU280814}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU280814}.
Interaction partners:
Sequence:
MDPEHLPVINNYLDANEPASSEARLSRMHFHDNQRKVDYVLAYHYRKRGAHLGHGSPGHSLAVISNGETGKERHGGGPGDIELGPLDALEEERREQRDEFEHNLMAAGLELEKDLESKSQGSVFVRIHAPWQVLAREAEFLKIKVPTKKMYEIKAGGSIAKKFSAILQTLSSPLQPRVPEHSNNRMKNLSYPFSREKMYLYNIQEKDAFFDNATRSRIVHEILKRTACSRANNTMGINSLIANNIYEAAYPLHDGEYDSPGDDMNDRKLLYQEWARYGVFYKFQPIDLIRKYFGEKIGLYFAWLGLYTSFLIPSSVIGVIVFLYGCATIEEDIPSKEMCDHQNAFTMCPLCDKSCDYWNLSSACGTARASHLFDNPATVFFSIFMALWATMFLENWKRLQMRLGYFWDLTGIEEEEEHSRPEYETKVREKLLKESGKSAVQKLEANSPEDDEIALTFSIVFGVIVYRITTAAALSLNKATRSNVRVTVTATAVIINLVVILILDEIYGAVAKWLTKIEVPKTEQTFEERLILKAFLLKFVNAYSPIFYVAFFKGRFVGRPGSYVYVFDGYRMEECAPGGCLMELCIQLSIIMLGKQLIQNNIFEIGVPKLKKLFRKLKDETEPGESDPDHSKRPEQWDLDYSLEPYTGLTPEYMEMIIQFGFVTLFVASFPLAPVFALLNNVIEVRLDAKKFVTELRRPDAVRTKDIGIWFDILSGIGKFSVIINAFVIAVTSDFIPRLVYQYSYSHNGTLHGFVNHTLSFFNVSQLKEGTQPENSQFDQEVQFCRFKDYREPPWAPNPYEFSKQYWSVLSARLAFVIIFQNLVMFLSVLVDWMIPDIPTDISDQIKKEKSLLVDFFLKEEHEKVKLADEPAQRSQGGGNRSRRSRAASSAPSGRSQPGSIASSGSQHTNV
Protein: Tau-tubulin kinase 1 (EC 2.7.11.1) (Q6PCN3)
Organism: Mus musculus (Mouse)
Function: Serine/threonine kinase which is able to phosphorylate TAU on serine, threonine and tyrosine residues. Induces aggregation of TAU (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MQCLAAALKDETNMSGGGEQADILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDWEKAGTDALLSTSTSTPPQQNTRQTAAMFGVVNVTPVPGDLLRENTEDVLQGEHLSDQENAPPILPGRPPEGLGPGPHLVPHPGGPEAEVWEETDVNRNKLRINIGKTPCVEEEQSRGVGVPSSPVRAPPDSPTTPVRSLCYRRVNSPESERLSTAADGRVELQERRSRMDLPGSPSRQACSSQPAQMLSVDTGHADRQASGRMDVSASVEQEALSNAFRSVPLAEEEDFDSKEWVIIDKETELKDFPPGAEPSTSGTTDEEPEELRPLPEEGEERRRLGTEPTVRPRGRGMHTLTEEDPRQMLPQPAPPQLSQADGRSETSQPPTPGSPSHSPLHSGPRPRRRESDPTGPQRQVFSVAPPFEVNGLPRAVPLALPYQDFKRDLSDYRERARLLNRVRRVGFSHMLLTAPQVPLAPFQPQANGKEGEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEAGALGEVLGPRSGSSSEGSERSTERSQEGAPSTLLADDQKEARGRASMADGDLEPEEGSKTLVLVSPGDMKKSPVTAELAPDPDLGTLAALTPQHERPQPTGSQLDVSEPGTLSSILKSEPKPSGPGAGGGVGLVAPGAGVTAVTSPFTKVERTFVHIAEKSHLNVMSSGGQASRPEELSTGGELGLEVLSEGGIAEEGAPAPLENGMALAGLDGTEMESCALSGPPGETPSEVVTDSLPNGPALADGPAPASQQEPVTKKGTTISPSRHAMPGSRPRSRIPVLLSEEDTGSEPSGSLSAKERWSKRARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPTTALPRKAVRAATTRSRIPRPISVSMPVEGQQLPGRPHGAASATDLAITSRLQLQKPSGLAPAADLRPKQSASRGPGPGRAQVSKPAAPRSPGLPASTARHPSGSPRSQSLSRKESSSPSHQARPGVPPSRGVLQVRSQPEASPVAPKKGPKGKQLQTQRAATKGRAVVSEGRPGAR
Protein: S-adenosylmethionine synthase 1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1) (P10659)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Interaction partners:
- S-adenosylmethionine synthase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- Adenosylhomocysteinase
- S-adenosylmethionine decarboxylase proenzyme
- Aromatic/aminoadipate aminotransferase 1
- Free methionine-R-sulfoxide reductase
- Serine hydroxymethyltransferase, cytosolic
- Methylenetetrahydrofolate reductase 2
Sequence:
MAGTFLFTSESVGEGHPDKICDQVSDAILDACLAEDPHSKVACETAAKTGMIMVFGEITTKAQLDYQKIVRDTIKKIGYDDSAKGFDYKTCNVLVAIEQQSPDIAQGVHEEKDLEDIGAGDQGIMFGYATDETPEGLPLTILLAHKLNMAMADARRDGSLAWLRPDTKTQVTVEYKDDHGRWVPQRIDTVVVSAQHADEITTEDLRAQLKSEIIEKVIPRDMLDENTKYFIQPSGRFVIGGPQGDAGLTGRKIIVDAYGGASSVGGGAFSGKDYSKVDRSAAYAARWVAKSLVAAGLCKRVQVQFSYAIGIAEPLSLHVDTYGTATKSDEEIIDIISKNFDLRPGVLVKELDLARPIYLPTASYGHFTNQEYPWEKPKTLKF
Protein: Meiotically up-regulated gene 125 protein (O13859)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MILKDSLEAKSCFKSSQTSHLAARVAMENPQKGNVINAQSSRQPSSENEFRENLFFKEMRTNGKNEHETSCRSVVLYRNSKSAKRYPLSTKCARISYMQGNKDTKTALTKKYKSNEDVSRMRKKGNKYPQCKSKNLYDSLKLEECIESWSLNQKQNENFYEHTHLNSRDDSNPSSCDRETFFLSDEDSEISLMEGLSSIENGYPDEKETLAALDNVKLSDENAAHLGYLVKYFQNYTDKIILKETLMDWEDKEPSLQELTESTKYLENLADTDHRTSNKPFLFLR
Protein: BcDNA.GH11023 (Nuclear localized protein 1, isoform A) (Nuclear localized protein 1, isoform C) (Q9Y109)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ribosome quality control complex subunit NEMF homolog
- E3 ubiquitin-protein ligase listerin
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
Sequence:
MSARMLKKLQGDADKLAPPPDDEDCEELSDNDELEDSDMQRYRKSHLNPFDLLNQAGLSLSESEFKEDDNETEHPSAALPNATASAAKKKKKKRKKKAKSSGNHISSEDNERQDKYFEKVDPLLGKVYDAVPRQSAKQLVSAATGTTATKKLLAVELRHLNPQNEMRRTFGKRVVKVETKRGRQKPTLKSTYMVTAKDSWPALTKNTITMKLLPAPDSPSVSSKSITDNGADVQWFAFEHSQYYQGVQQMFLSALERIDSEFLITLIKRCPYHVDSLVQLSEVCKMTEDFSLASELLERALLLLESSLHINFSLTSGNCRLDYRRQENRSFYIVLFKHAQYLEERACSRTAFEISKLLLSLQPDTDPLAMILVIDYYALRSKQFEWLVEFYEKYNAARNLNQLPNMAYSYALALHTLYGACERSNQALQYALLMFPGVLRPLLDEMSVQTDKRVLASSYFFADVSGNQSPALHQLVCLYVCRARVVWRQNEVLPWLESNVNIVLDRIESKDPLVNEYKEKRSLRYSGTPPRPILRHVILSDYKEKVPLAVFVSKEKQAIMTYDPLPPPNSVNCYHRKSSSSSSPTTNTNNSVSMFFQSLLPSFNINNLAANAQLQEGAAPAAGAGAAAGDANIEVGIEQGAAGVAGEGEEAGLQQSLTLMMDAMRDFLQNFRIAEHLRSPETAAAQSTSSNDEEEGSSDYID
Protein: Uncharacterized protein (Q9XXU2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEQDENRDMPPVEQRSANPNVNIQSIQQEESGGGRRNHDSARNQEQLLDIENPTEMRSAEQVDVQQEPAPPLERPILNEIIRPVPIRPNNNSSYRQYVPTPPPSLSHMMRSPPINDEPLPHPIALSHQHGNIQFQREDLELNDQYARNRLLDQLVQLLLRPPEVQHVIHQHVFLQPPPPPPPAFFDHHYPHFPPYELNLQDLQEVEVVPEDPV
Protein: Fanconi anemia group D2 protein homolog (Q55F81)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Fanconi anemia group I protein homolog
- RING-type domain-containing protein
- Uncharacterized protein
- DNA excision repair protein ERCC-1
- Fanconi-associated nuclease 1 homolog
- DNA polymerase zeta catalytic subunit
- Large ribosomal subunit protein uL1
- DNA repair endonuclease XPF
- DNA repair protein Rad4 family protein
- Nuclear transport factor 2
Sequence:
MDRRFLEYEDMNDDDLKDDDDDESLNNNNNNNIIDQNSKKQRLYDTPCSFTSNIDDNDDDLSDFNTKDNQQQQQQRQRQQQQPINSKRKQEFQKLLDETMSKTKEFKVVLGKHMSIQDPIIVSDIVTFKRSLETYFNNQSSSNNALHSPRDNNSSESKLQSFKDGFALFIENESILELALSPVRSESSNDFIQKYGNNFSETCLIRLLLSTPIVQPLILDVLFDSMYTFAAEDTNGFCKKIFSQLRWLDTISDGPQLLAQIGTLLGLLDVNPELKKDIIRFLPDIVDNECHSEFIDILMGIYKENEEFVLPILDALANLNLNSAHLTNVRETVGESLRESDFNILPMRITFLLSTSSSKENSAITSKAIRERLDLKKPILINGSTTEILNDPNNKETDRDRKPTENLILEALKSGIRFKKDLCDAFIKEIEEARTHNILDFWLIVLIHSFGHKSTEKIFKKLVKSGLLSKKLLIESIYTHEFALQQYFTTMLTLCDFCIRSIETKVREFGESFYELLFKCYRDEGQQRELISMLLAHIISGNNSEVNCGLEVLYKLCSPLCSDMLIKFSHEIKRVLDYIDTLTESQIRTLFRIFGTLLYTDRISSNSYKLEPNGRIFTELDIFTRKQITSTKIKYKKIGIISMCSQISRISRVIINHNNELQLPRELFEEYEKLFQSLLLNCDKSRLARSYLFDELANVYMISPFHQSVTNSIGEYAQRYFQNDFIELVNQYDKSMIWGSMGNTFGDEGICIYPNLSEGTTTRDDNKLLCLSSAFRLIRILQPKDQSLEEIDVMLTHPFIMFNKEIVSINNSHNFKDDKEKELYCLSLYYSTNYIRELLNAFTTLLIPLRKNQQNQHQQHHTQSLLSNNEKLLNRLNILISMEDKFEMVLSHSNSFVIPHGTFESDQRKPFSIELKKNKKLPTSASTTATTTTLANSNSINQLIKYNIDLKDFVTPGESLIEIEKPYLKLIKPYYRSLDLSCFHLFKPQTNNTTTTTTSKSNQNNLEPNGMLYLLEEFYNKLDTVSTPDRTSHLHNEKIQLPFSYEQFILQTGVVFRYLLEHLKNLSNQFKQNRLKLLQLIKSTDVIVQQKNELQIELEEEYDASKDNEVKKLKKEIEKRCDQIQWSNNNQTITQHCIQLILQIFEKLFHTGGSISKTENDHKLFLDLLNSISTKANQLLGENIDQQQQQQPVGGGGDRNQQKLKIFNSIFTFFKSFIQIFVSSKSFKASFTLLQVLISLYSSRYIGNKNIEEMKFQIHNYSRILLAINWISSGKQKVSSQSLGVLLKAYFDHTSNEDESIKTSINYLKKYFGNESSKKNVLTTNSSSSQSSKNKRNNNNSSDSDEENDNDEKDDLINREAGGGGDDDDDDNKFINIVETGEGIEFKISSLNSTTLLPFLKSIYSALINNLKSSIEDKNLQTDQETACFFKRSSFFISMYASLVETAKERDKSLYLIETLKQAVSFVTVFIKLYIPVFKSLVKKKSLQIIGRVIKEIENLRLHNGILNNICSHGKETSDSSIIAMEPQVKKTLESLNMEVKGILAGVNASEAFGTKKVDKRKLNGDEFFSSDDDDGDDDSDQSSDYSDSDDNKKRKTKKKVNKKSTKKSTKKIKSNHSDEEEEEEEEEKKGVSSSKQKKQTKKVGSLSKGSKLRKMGSDDDDDDEKEVESESSPNVSDNEDYSRSVSRGRSRSRSISHRRRSTSRSLSISDRSRSRSVEEAEVGEPESNEELSSSEPDEGDSLGSQSDRSEDEEIESD
Protein: E3 ubiquitin-protein ligase MSL2 (EC 2.3.2.27) (Male-specific lethal 2-like 1) (MSL2-like 1) (Male-specific lethal-2 homolog) (MSL-2) (Male-specific lethal-2 homolog 1) (RING finger protein 184) (Q69ZF8)
Organism: Mus musculus (Mouse)
Function: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure (By similarity). Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histone H3 methylation at 'Lys-5' (H3K4me) and 'Lys-80' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:38030723}. Chromosome {ECO:0000269|PubMed:38030723}. Note=Associates with both promoters and enhancers of target genes, maintaining promoter-enhancer contacts. {ECO:0000269|PubMed:38030723}.
Interaction partners:
- MSL complex subunit 3
- Male-specific lethal 1 homolog
- MSL complex subunit 3B
- Histone acetyltransferase KAT8
- Histone acetyltransferase KAT5
- Enhancer of polycomb homolog 2
- Mortality factor 4-like protein 1
- Mortality factor 4-like protein 2
- KAT8 regulatory NSL complex subunit 3
- Enhancer of polycomb homolog 1
Sequence:
MNPVNATALYISASRLVLNYDPGDPKAFTEINRLLPYFRQSLSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYITQTTLARDIIEAVDCSSDILALLNDGSLFCEETEKPSDSSFTLCLTHSPLPSTSEPTADPQASLSPMSESTLSIAIGSSVINGLPTYNGLSIDRFGINIPSPEHPNTIDVCNTVDIKTEDLSDNLPPVCDTVATDLCSTGIDICSFSEDIKPGDSLLLSVEEVLRSLETVSNTEVCCPNLQPNLEATVSNGPFLQLSSQSLSHNVFMSTSPALHGLSCTAATPKVAKLNRKRSRSESDSEKVQPLPISTIIRGPTLGASAPVTVKRESKISLQPIATVPNGGTTPKISKTVLLSTKSMKKSHEHGSKKSHSKSKPGILKKDKAVKEKMPSHHFMPGSPTKTVYKKPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKKLEAFAVPEKALEQTRLTLGINVTSIAVRNASTSTSVINVTGSPVTTFLAASTHDDKSLDEAIDMRFDC