wanglab/gogpt-training-data huggingface dataset:
Protein: 5'-AMP-activated protein kinase subunit gamma (AMPK gamma) (AMPK subunit gamma) (Q10343)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (ssp2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta
- SNF1-like protein kinase ssp2
- Protein kinase domain-containing protein ppk9
- Protein sds23/moc1
- Multifunctional tryptophan biosynthesis protein
- ATP synthase subunit beta, mitochondrial
- Protein kinase kin1
- Serine/threonine-protein kinase ppk16
- Serine/threonine-protein kinase ppk25
- GMP synthase
Sequence:
MTDVQETQKGALKEIQAFIRSRTSYDVLPTSFRLIVFDVTLFVKTSLSLLTLNNIVSAPLWDSEANKFAGLLTMADFVNVIKYYYQSSSFPEAIAEIDKFRLLGLREVERKIGAIPPETIYVHPMHSLMDACLAMSKSRARRIPLIDVDGETGSEMIVSVLTQYRILKFISMNCKETAMLRVPLNQMTIGTWSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALLKRPANFDGVHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYIIYDKTTTPGVPEQTDNFESAV
Protein: Chaperonin 60 subunit beta 4, chloroplastic (CPN-60 beta 4) (Q9C667)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved specifically in the folding of NDHH, a subunit of the chloroplast NADH dehydrogenase-like complex (NDH).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:21483722}.
Interaction partners:
- 20 kDa chaperonin, chloroplastic
- 10 kDa chaperonin 2, chloroplastic
- Heat shock 70 kDa protein 9, mitochondrial
- Heat shock 70 kDa protein 10, mitochondrial
- 10 kDa chaperonin 1
- Protein CHLORORESPIRATORY REDUCTION 7
- NAD
- Heat shock 70 kDa protein 6, chloroplastic
- Protein CHLORORESPIRATORY REDUCTION 6
- Heat shock 70 kDa protein 7, chloroplastic
Sequence:
MAFSQAALSALPLSDRTFRKKPSSSSSSSPNFVLRVRAAAKEVHFNRDGSVTKKLQAGADMVAKLLGVTLGPKGRNVVLQNKYGPPRIVNDGETVLKEIELEDPLENVGVKLVRQAGAKTNDLAGDGSTTSIILAHGLITEGIKVISAGTNPIQVARGIEKTTKALVLELKSMSREIEDHELAHVAAVSAGNDYEVGNMISNAFQQVGRTGVVTIEKGKYLVNNLEIVEGMQFNRGYLSPYFVTDRRKREAEFHDCKLLLVDKKITNPKDMFKILDSAVKEEFPVLIVAEDIEQDALAPVIRNKLKGNLKVAAIKAPAFGERKSHCLDDLAIFTGATVIRDEMGLSLEKAGKEVLGTAKRVLVTKDSTLIVTNGFTQKAVDERVSQIKNLIENTEENFQKKILNERVARLSGGIAIIQVGALTQVELKDKQLKVEDALNATKSAIEEGIVVGGGCALLRLATKVDRIKETLDNTEQKIGAEIFKKALSYPIRLIAKNADTNGNIVIEKVLSNKNTMYGYNAAKNQYEDLMLAGIIDPTKVVRCCLEHASSVAQTFLTSDCVVVEIKEIKPRPIINPPLPTSSPATSSMFPDRKLPRFPQIMPRTRSHFPRK
Protein: Ras-related protein Rab-18 (EC 3.6.5.2) (Q5EB77)
Organism: Rattus norvegicus (Rat)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (By similarity). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). Required for the localization of ZFYVE1 to lipid droplets and for its function in mediating the formation of endoplasmic reticulum-lipid droplets (ER-LD) contacts (By similarity). Also required for maintaining endoplasmic reticulum structure (By similarity). Plays a role in apical endocytosis/recycling (By similarity). Plays a key role in eye and brain development and neurodegeneration (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP72}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q9NP72}. Lipid droplet {ECO:0000250|UniProtKB:Q9NP72}. Apical cell membrane {ECO:0000250|UniProtKB:P35293}.
Interaction partners:
- Rab3 GTPase-activating protein non-catalytic subunit
- Rab3 GTPase-activating protein catalytic subunit
- RAD50-interacting protein 1
- Centromere/kinetochore protein zw10 homolog
- Syntaxin-18
- TBC1 domain family, member 20.
- TIR domain-containing adapter molecule 1
Sequence:
MDEDVLTTLKILIIGESGVGKSSLLLRFTDDTFDPELAATIGVDFKVKTISVDGNKAKLAIWDTAGQERFRTLTPSYYRGAQGVILVYDVTRRDTFVKLDNWLNELETYCTRNDIVNMLVGNKIDKENREVDRNEGLKFARKHSMLFIEASAKTCDGVQCAFEELVEKIIQTPGLWESENQNKGVKLSPREESHGGGACGGYCSVL
Protein: Disks large-associated protein 2 (DAP-2) (PSD-95/SAP90-binding protein 2) (SAP90/PSD-95-associated protein 2) (SAPAP2) (Q8BJ42)
Organism: Mus musculus (Mouse)
Function: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000250}. Note=Postsynaptic density of neuronal cells. {ECO:0000250}.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 3
- SH3 and multiple ankyrin repeat domains protein 2
- Disks large homolog 4
- Disks large-associated protein 3
- Ras/Rap GTPase-activating protein SynGAP
- Disks large homolog 2
- SH3 and multiple ankyrin repeat domains protein 1
- Neuroligin-3
- Neurexin-1
- Disks large homolog 3
Sequence:
MGTAQVLPGILQKHCCILPDRNTESQCTLCGEPEEEEGGDLAQPGLSFPGPAEEDIDQQYSWSPTQHFNEERYSPAPRNMKGLTGSRNQPQLCAGHTCGLSPPDDCEHPHDHMHHGSDVRQPYLLSPAESCPMDHHRCSPRSSVHSECMMMPVMLGDHVSSSTFPRMHYSSHYDTRDDCAMSHTSTKVNRIPANLLDQFEKQLPLHRDGFHTLQYQRASAATEQRNESPGRIRHLVHSVQKLFTKSHSLEGSSKSNINGTKSDSRVDDHHQSHLSKHSKRSKSKERKPESKHKSGMSSWWSSDDNLDSDSTYRTPSVAHRHHMDHIPHCYPEALQSPFGDLSLKTSKSNNDVKCSACEGLALTPDTRYMKRSSWSTLTVSQAKEAYRKSSLNLDKPLVHPEIKPSLRPCHYLQVPQDDWGAYPTGGKEEEIPCRRMRSGSYIKAMGDEESGESDSSPKTSPTVAIRPEPLLKPIIQRPLGDHQTQSYLQAATEVPVGHSLNPSINYNSPKFRSRNQSYMRAVSTLSQASCVSQMSEAEVNGQFESVCESVFSEVESQAMDALDLPGCFRTRSHSYLRAIQAGYSQDDECIPVMTSSNMTSTIRSTAAVSYTNYKKTPPPVPPRTTSKPLISVTAQSSTESTQDAYQDSRAQRMSPWPQDSRGGLYNSMDSLDSNKAMNLALETAAAQRHAADTQSSSTRSIDKAVLASKAEELLKSRCSSIGVQDSEFPDHQPYPRSDVETATDSDTESRGLREYHSVGVQVEDEKRHGRFKRSNSVTAAVQADLELEGFPGHVSMEDKGLQFGSSFQRHSEPSTPTQYGALRTVRTQGLFSYREDYRTQVDTSTLPPPDPWLEPSLDTVETGRMSPCRRDGSWFLKLLHTETKRMEGWCKEMEREAEENDLLEDILGKIRSAVGSAQLLMSQKFQQFYWLCQQNMDPSAMPRPTSQDLAGYWDMLQLSVEDVSMKFDELHQLKLNDWKIIESPERKEERKIPPPIPKKPPKGKFPITREKSLDLPDRQRQEARRRLMAAKRAASFRQNSATERADSIEIYIPEAQTRL
Protein: Uncharacterized protein (Q583E0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- SET domain-containing protein
Sequence:
MGALPSRETQRRGLYSHRHGRNRRSEVILVPLTTEFFPSESCPLFERLFQARHHRTAKYYYRAVRSADTDRESDYYCQTTVHANNADLDSPGSLARDKRVETLFTDDISGLYQRLVRETECCMSETDEGLRERYKKQIQQQQRHQQRQQQYKSPHPQEYGAAFGDSYEEYFGFGPGAFANGYNDALAYIKGREQHTHCNEFGTHVTSPSAYYLRPVPCAIVSRSEAHKSAPDAGVEFLGSTVKVLGMFGLLPSTISITVHGEVVEQHMLKATMFVDKDVGDQILGNVVMLAVHMYVRQCIEAQIRAPYIPMIPMILRTPISNIPMLQFVREMRVRLRSLLNAGGKRRSFCSANSSGSSASSSPSTDSVHDAVEASSRCDADILYLFEEDVPGVVSQHRLFLDPSEAQSLKLRPAHNTNPDGTIPILLVSGVNVQATPLTHPSVTSMSHVRVPPWVLDGASDSAGGGPPNSCPQREAFRAASLLATRRNRFRMWVEDGRLCIWASAAYARRGCLMLAQQLTQTVDNSLLPIPRPWNYRGLLRGGMPMPEPELANDVFIVAEDMPSMGLYQGDVLRCSTPAEIGDRQRRGSPCKTPGSNSGTSLEMTFPHTKKSLNSTSTLLEPATPAEQKSPPVNYTSNHPSNVLLQDPGEAPSNAFWVCFPFDRDGPSVAPGERRQQQQQQDGVAYRATNVEEVLLSWIKIISLKTRDAAEEDDHWVRDPTTGAPLRVDRYIIRRVEHDGMRYFIGVTPRFVGQQRRLEKMLVDIKAQEDGGEDLDLERDKYYVAAMHYDAAFDREDDDSRDEDALGRVAMAKMLSAPSLILE
Protein: Protein Turandot M (Q9VMR8)
Organism: Drosophila melanogaster (Fruit fly)
Function: A humoral factor that may play a role in stress tolerance. Requires Mekk1 expression in the fat body to regulate response to septic injury and consequent immune response.
Subcellular location: Secreted {ECO:0000269|PubMed:11409894, ECO:0000305}.
Interaction partners:
- Protein Turandot C
- Protein Turandot A
- Protein Turandot X
- FI07211p
- Protein Diedel
Sequence:
MNPTIYLSCLMVFSVFLLGKVNAENEDEFVTEKQRLFSVYGDSSVDEATKYRNIDSLVTFYDKYFTRLQLKPDLNTRAHDLLRRYKEENARVVLVDGTPAQGGFWLPLVKLLIVQLGVEIASEGVKRAIES
Protein: Phosphatidylinositol 4-phosphate 5-kinase 5 (AtPIP5K5) (EC 2.7.1.68) (1-phosphatidylinositol 4-phosphate kinase 5) (Diphosphoinositide kinase 5) (PtdIns(4)P-5-kinase 5) (Q9SLG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phosphatidylinositol 4-kinase beta 1
- Phosphatidylinositol 4-kinase beta 2
- Phosphatidylinositol 4-kinase alpha 1
- Phosphoinositide phospholipase C 3
- Phosphatidylinositol 4-kinase gamma 1
- Phosphoinositide phospholipase C 1
- Phosphatidylinositol 4-kinase alpha 2
- Phosphoinositide phosphatase SAC7
- Phosphoinositide phosphatase SAC8
- Phosphoinositide phospholipase C 5
Sequence:
MSKDQSYVLKAWEVTVRKTQQAKKRANSVFGTVSVAPHTDNDTTTDDNDDETTTNRSSLEEFYHAERVLPNGDYYTGQWYDSFPHGHGKYLWTDGCMYIGDWYNGKTMGNGKFGWPSGATYEGEFKSGYMDGIGTYTGPSGDAYKGQWVMNLKHGHGVKSFANGDAYDGEWRRGLQEGQGKYQWSDGSYYIGEWKNGTICGKGSFVWTNGNRYDGFWDEGFPRGNGTFKWDNGSFYVGHWSKDPEEMNGTYYPSGNEGNLEWDPKDLFNNLSEYTICSGERVPTLPSQKKLSVWNSSKRIEKPRRTSVDGRVSVGVDRAFEKMNMWGNEIGEGGADMRKELDAELMRLDAEGLQSLKSSPVPMKLPKAGRKQGETISKGHRNYELMLNLQLGIRHSVGRQAPAASLDLKPSAFDPKDKIWRRFPREGTKYTPPHQSTEFKWKDYCPLVFRSLRKLFKVDPADYMLSICGNDALRELSSPGKSGSFFYLTNDDRYMIKTMKKSETKVLLGMLAAYYNHVRAFENSLVIRFFGLHCVKLNGPTQKKVRFVIMGNLFCSKYSVHRRFDLKGSSLGRTTDKPESEIDSNTILKDLDLNFIFRLQKAWYQEFIRQIDKDCEFLEQERIMDYSLLVGIHFREASVAGELIPSGARTPIGESEEESGPRLSRAEVDELLSDPSRWASIRLGTNMPARAERTMRKNDSELQLVGEPTGEFYEVVMIFGIIDILQDYDISKKLEHAYKSIQYDPSSISAVDPRQYSRRFRDFIFKVFTDDN
Protein: Unhealthy ribosome biogenesis protein 2 homolog (B0V0U5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Essential for hematopietic stem cell development through the regulation of p53/TP53 pathway.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14146}.
Interaction partners:
- Citrate synthase, mitochondrial
- Succinate--CoA ligase subunit alpha
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MAAIYSGIQLKLKNTRTPWPDKLKLARFAWISTQCLLPNKEQVLFDWTNHALTCFYNKKVEMPPEVVEGLWTYLDDILHSRKLHNVLSQGKTISLRLTVAQIINDRILDYTSGLRSVSFHTILSCCHGILTSPVLSVIYTAKYELLVQLLSRLCGLTSMQLRQQKYEEPLSLKAFEVLLVVLSNYLTVQKQQANSNRVFFQVTAHLLHPLLLLRHLLNTRVWTEKDDVKIRQNLSKEIRTKVDAVLQSALFLSDHLQSYKVEVSPSENEAGDRKSHIGKGLQGPLNTILTRICIHGASEEEEALFYAVKSNSLSLLFKFALDSFCRGGENKRVIFHLMAKLITALGFTDELDIDENFRASNWGICLLALENLLNSCLVGDIYNVAADRIQHGEVQFNFYRKVARLLFNNTQMGVPAWYRCLRALLALNHQILEPDLDELLSAVWVDAENMELRVRKAREALVSAVLQTYSKLRQLPKLIEELLDVVCRPAADELRPALLPEAIQKTLSQCLLDNPLRQNLEICGLILKRVQSCLLPHIQDETSDLALKVFSMSLLLHAVLFSFKTLDNSTPVPVVKQTLSLMTEMLKVVEDLLEQKLATKGPWMEKVQEVTLLLAHTWVEADALFQIHCTKYTSPSASQSSTLVDKALMLRNMDSPLGKLLQNLLALHKLKIHLLKSFSESSEMQKMAQFILNREELSVIHSLDQMWDFQFCNVNSSTYNAAHWFLVTSNLPLIAPYLDPNDRSVFAECMLKSLLQSLDASGSNLENTGISVCLISRQLLESPVLCELPEIFSALTKCIIKALFGLLDSSHMQLICPSFLTPPVENVEVKDEEMGMTPSMKRLKAIGLEMLYSVKMKSSVPLSKRQINGLLQLVKVTSVLNGYAMSYEDYLELFLTLLTLTSTIQCVEETNLSAFIELLKELFSVMASLLLAKNSQSILKVIHGSNLLEATMTTLFSRSSEGLFKSLDGPTWLSFLQSVQDFIQSLIRLIIDRKSSICLNLEKFTSFMVECNFTARVLTVDTGDLFSLQLHLVTLSALCREMMTTLGKNKQLDQALTHLLEKATAVMEPAIQAVLMGKGSCLLRQSFSVEVVTVMIRCELARASSSNDDGQEKISSMPFYRSFYQQILKELFPSPRPMDFLISSIHYLSAFHMAAEKTKVADLEDLHIEILQSIQALLSGTWMSLTDVKELEGPVKELLNQLMSNCSQEQFHLFLLMLREGLVAAKVEGGQCSEVLSAVTLIKLLACCLFPEHCSKAFWLITPQIISSLIFIIKESSKLPSLTRVLTVPGLEALTVLLRQGKAQISNPHQVIVVLGALQFVPLDSHCMEDYHSAFEAVHEALFAIIHCYPQVMLKASPTFLNCFYRLVSSVMHEGKQRSDTDRASEKDRESLLKCARLVERMYTHVASAAEDFTVLSSFMVAQYVSELQRVTLQPEIKAHLTEGIYCILDHCVEQDIKFLNTTLQMGVKEVFNELYSSYTHYHKSQRQGEEKYTV
Protein: Troponin C, slow skeletal and cardiac muscles (Q6IQ64)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Novel slow skeletal troponin T family protein
- Slow troponin T
- Troponin T2d, cardiac.
- Troponin T type 2a
- Troponin T type 2b
- Myosin, heavy polypeptide 2, fast muscle specific isoform X1
- Fast muscle troponin I, tandem duplicate 4)
- Troponin C, slow skeletal and cardiac muscles
- Troponin I type 1b
- Slow myosin heavy chain 1
Sequence:
MDDVYKAAVENLTEEQKNEFRAAFDIFVQDAEDGCISTKELGKVMRMLGQNPTQEELQEMVDEVDEDGSGTVDFDEFLVMMVRCMKEESKGKSEEELAEVFRMFDKNGDGYIDLDELKNMLESTGEAITEDDIEELMKDGDKNNDGKIDYDEFLDFMKGVE
Protein: Suppressor of cytokine signaling 2a (V9Q6E2)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MTCHSPESTETIENERTDTESRVVDSDETRIAQTMKDLKNTGWYWGSLTANEAKEILQDASEGTFLLRDSTQRDYLFTISAMTSAGPTNLRIEYKEGKFKLDSVVLIKPKLKQFDSVVHLVEHYVQMSRTTSKRPSSGASQSLAPPNGTVQLLLTKPVYTATPSLQHLSRIAINNATREVQELPLPNRLKNYLTDYSYNV
Protein: Glutamate dehydrogenase 2 (GDH 2) (EC 1.4.1.3) (Q38946)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022}.
Interaction partners:
- Ferredoxin-dependent glutamate synthase 1, chloroplastic/mitochondrial
- Ferredoxin-dependent glutamate synthase 2, chloroplastic
- Glutamate synthase 1, chloroplastic
- Glutamine synthetase, chloroplastic/mitochondrial
- Glutamine synthetase cytosolic isozyme 1-4
- Glutamine synthetase cytosolic isozyme 1-1
- Glutamine synthetase cytosolic isozyme 1-2
- Glutamine synthetase cytosolic isozyme 1-3
- Ferredoxin--nitrite reductase, chloroplastic
- Glutamine synthetase cytosolic isozyme 1-5
Sequence:
MNALAATNRNFRHASRILGLDSKIERSLMIPFREIKVECTIPKDDGTLVSYIGFRVQHDNARGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVADIPYGGAKGGIGCSPRDLSLSELERLTRVFTQKIHDLIGIHTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGREAATGRGVVFATEALLAEYGKSIQGLTFVIQGFGNVGTWAAKLIHEKGGKVVAVSDITGAIRNPEGIDINALIKHKDATGSLNDFNGGDAMNSDELLIHECDVLIPCALGGVLNKENAGDVKAKFIVEAANHPTDPDADEILSKKGVIILPDIYANAGGVTVSYFEWVQNIQGFMWEEEKVNLELQKYMTRAFHNIKTMCHTHSCNLRMGAFTLGVNRVARATQLRGWEA
Protein: Nuclear pore complex-interacting protein family member B7 (Nuclear pore complex-interacting protein-like 1) (O75200)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRLRFWLLIWLLLGFISHQPTPVINSLAVYRHRETDFGVGVRDHPGQHGKTPSPQKLDNLIIIIIGFLRRYTFNVLFCTSCLCVSFLKTIFWSRNGHDGSMDVQQRAWRSNRSRQKGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMAAAEHCHSSGLPYWLYLTAETLKNRMGRQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSVDDNIKECPLAPLPPSPLPPSVDDNLKECLFVPLPPSPLPPSVDDNLKECLFVPLPPSPLPPSVDDNLKTPPLATQEAEVEKPPKPKRWRVDEVEQSPKPKRQREAEAQQLPKPKRRRLSKLRTRHCTQAWAIRINP
Protein: PCNA-interacting partner (PARP-1 binding protein) (PARP1-binding protein) (A0A0C4DG30)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
ADSMLLALQLSMAENNKQHSGEFTVSLSDVLLTWKYLLHEKLNLPVENMDVTDHYEDVRKIYDDFLKNSNMLDLIDVYQKCRALTSNCENYNTVSPSQLLDFLSGKQYAVGDETDLSIPTSPTSKYNRDNEKVQLLARKIIFSYLNLLVNSKNDLAVAYILNIPDRGLGREAFTDLKHAAREKQMSIFLVATSFIRTIELGGKGYAPPPSDPLRTHVKGLSNFINFIDKLDEILGEIPNPRGCKSICWKINNWNEFWKCSSGQK
Protein: formate--tetrahydrofolate ligase (EC 6.3.4.3) (Q4Q735)
Organism: Leishmania major
Interaction partners:
- Putative C-1-tetrahydrofolate synthase,cytoplasmic
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Aminomethyltransferase
- Aminomethyltransferase
- Putative methylenetetrahydrofolate reductase
- Putative methionyl-tRNA formyltransferase
- Methionine synthase
- Isocitrate dehydrogenase
Sequence:
MATRKLHCVWPVPADIDIAQSVDAQPITSIAEAAGILLSELSPYGSTRAKVKLSVLKRLEGCPNGKYVVVAGMNPTPLGEGKSTTTIGLAQALGAHLHRRCFACIRQPSQGPTFGIKGGAAGGGYSQVIPMEDFNLHGTGDIHAITAANNLLAAALDTRIFHERTQDDAALYRRLTDELKTFTPIMQKRLDKLGIRKTDPKSLTEEERVCFARLDVDPGTISWRRVTDVNDRFLRDIEIGMGKAEKGISRRTGFDISVASEVMAILALVDDLADMRQRLGAIQVAKSKTGASVTAEDVGCAGAMAVLMKDAVEPTLMQTLEGTPVLVHAGPFGNIAHGNSSVVADRIALKLAGADGFVLTEAGFGADMGCEKFFNIKCRTSGLKPDAAVLVATVRALKYHGGVEPKDAAKENADALRAGLSNLVRHIQNIRKFGVPVVVALNRFSTDTEAELALVKELATQEGDAADVVVTDHWSKGGAGAVGLAQALIRVTETAPSNFQLLYPSNASLKEKIETVCREIYGAAGVEYLNDTEEKLADFEKMGYGDFPVCMAKTQYSFSHNPELRGAPTGFTVPIRDVRVNCGAKFVFPLLGDISTMPGLPTRPAYYNIDIDCETGRIVGLS
Protein: Small nuclear ribonucleoprotein G (snRNP-G) (Sm protein G) (Sm-G) (SmG) (O74966)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- U1 small nuclear ribonucleoprotein C
- Small nuclear ribonucleoprotein Sm D3
- Pre-mRNA-splicing factor spp42
- Small nuclear ribonucleoprotein F
- Pre-mRNA-splicing factor cwf14
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 17
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MSKAGAPDLKKYLDRQVFVQLNGSRKVYGVLRGYDIFLNIVLEDSIEEKVDGEKVKIGSVAIRGNSVIMIETLDKMT
Protein: Dihydropyrimidinase-like 3 (Q8IXW6)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSYQGKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHYQMPYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLIKDKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQTRMLEMGITGPEGHVLSRPEELEAEAVFRAITIASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRISVGSDSDLVIWDPDAVKIVSAKNHQSAAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSDYVYKRIKARRKMADLHAVPRGMYDGPVFDLTTTPKGGTPAGSARGSPTRPNPPVRNLHQSGFSLSGTQVDEGVRSASKRIVAPPGGRSNITSLS
Protein: Serine hydroxymethyltransferase (SHMT) (EC 2.1.2.1) (Glycine hydroxymethyltransferase) (Maternal effect lethal protein 32) (Serine methylase) (Q60V73)
Organism: Caenorhabditis briggsae
Function: Interconversion of serine and glycine.
Interaction partners:
- Glycine cleavage system P protein
- Trifunctional purine biosynthetic protein adenosine-3
- Aminomethyltransferase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Protein CBG12961
- Glycine cleavage system H protein
- Thymidylate synthase
- Glycine cleavage system H protein
- dihydrofolate reductase
- Phosphoserine phosphatase
Sequence:
MFARAVSRKTMTGLLAGSRVLLASQFTMADRQVHTPLEPVQRQKYANNENLLKDHVEKIDPEVFNIMKNEKSRQRRGLELIASENFTSKAVMDALGSAMCNKYSEGYPGARYYGGNEFIDQMEILCQKRALEVFGLDPAKWGVNVQSLSGSPANFAVYTALVGANGRIMGLDLPDGGHLTHGFFTPARKVSATSEFFQSMPYKVDAQSGLIDYDKLEENAMLFRPKVLIAGVSCYARHLDYERFRKIATKAGAYLMSDMAHISGLVAAGLIPSPFEYSDVVTTTTHKSLRGPRGAMIFYRKGVRSVNAKGVETLYDLEEKINSAVFPGLQGGPHNHTIAGIAVALKQCLSEDFVQYGEQILKNAKTLAERLKKHGYSLATGGTDNHLLLVDLRPIGVEGARAEHILDLAHIACNKNTCPGDVSALRPGGIRLGTPALTSRGFKEQDFEKVGDFIHEGVQIAKKYNAEAGKTLKDFKAFTATNEQFKQEVAELAKRVEEFSGKFEIPGNDLF
Protein: Profilin-3 (Profilin III) (Q8T8M2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Protein VASP homolog
- Cofilin-1A
- HP domain-containing protein
- Actin domain-containing protein
- Adenylyl cyclase-associated protein
- Exportin-6
- Severin
Sequence:
MTWQAYIDTNLIGSGFISAQILSSADGSSWANSNGFSVSATEAQHILSCFKDSNKASAMGITINNVKNFVLKADDKSIYAKKDAGGVVLVKTNQTILVAVYNSNLQPGAAANACEALGDYLREQGF
Protein: Angiopoietin-related protein 4 (Angiopoietin-like protein 4) (Hepatic fibrinogen/angiopoietin-related protein) (HFARP) [Cleaved into: ANGPTL4 N-terminal chain; ANGPTL4 C-terminal chain] (Q9BY76)
Organism: Homo sapiens (Human)
Function: Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. May also play a role in regulating glucose homeostasis and insulin sensitivity (Probable). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro). Depending on context, may modulate tumor-related angiogenesis (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10698685, ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:19270337, ECO:0000269|PubMed:21398697, ECO:0000269|PubMed:29899519}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:21398697}. Note=The unprocessed form interacts with the extracellular matrix (PubMed:17068295, PubMed:21398697). This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (Probable). {ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:21398697, ECO:0000305|PubMed:17068295}.
Interaction partners:
- Lipoprotein lipase
- Angiopoietin-like protein 8
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
- Angiopoietin-related protein 3
- Claudin-5
- Peroxisome proliferator-activated receptor gamma
- Cadherin-5
- Integrin beta-1
- Fascin
- Peroxisome proliferator-activated receptor alpha
Sequence:
MSGAPTAGAALMLCAATAVLLSAQGGPVQSKSPRFASWDEMNVLAHGLLQLGQGLREHAERTRSQLSALERRLSACGSACQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKVAQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAEAAS
Protein: 25S rRNA (cytosine-C(5))-methyltransferase rcm1 (EC 2.1.1.-) (rRNA m(5)C methyltransferase 1) (O14039)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of a cytosine in 25S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA N
- 60S ribosome subunit biogenesis protein nip7
- Ribosome biogenesis protein nsa1
Sequence:
MDFYNHAANILSDLSKKKGSIKQLAFNSKKHDPKRTYALVCETLKYKPVLDEIIARSELLVLEKKLKENLARVLVHDLLMSKRGLSISNGPIKECILRHKTRLNAEFVKLKVKKGVKSHEELALKNPVSLPRWLRINTIKSTKDEVLQGLGLDKVSSIEELGPDKFYIDDCVENLIAIDPSFPIVENSLYKEGKVIIQDKASCFPAAVLAGLTGHVGDIIDGCAAPGNKTTHLAACFPKSHIFAFERDAKRVQTLRKMVGISGANNVTIEHQDFTLTDPKSDLYRNVTHILLDPSCSGSGIVSRQDYLLGNEQDVTEDTERLENLCSFQSTILKHALQFPNCRHVTYSTCSVHRLENEQVVCEVLSQEPDWKCNSLTKTLPNWKTRGIPEYCAQPSMAEGMIRCKPGAGGTIGFFVANLYHPQREQETFKMYKNDDDTKKRKRKKKKKEVKKKARIQGEE
Protein: DUF5655 domain-containing protein (E7DNC4)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MSKIKFENLKKGDVVLRAKSQTKFKIVSILADEKKADLESLEDGGELHLSASTLERWYTMEDETEPKKEEAAKPAKKAAPAVARPARKGRVVPKPKKEVLEEEIPEVKEQPEEVGSVSEKSTVRKPAPKKESVMAITKALESRIVEAFPASTRIVTQSYIAYRSKKNFVTIEETRKGVSIGVRAKGLTEDQKKLLASIAPASYEWAIDGIFKLVKEEDIDTAMELIEASHLSSL