wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase II subunit B3-1 (Nuclear factor Y, subunit C10) (AtNF-YC10) (Q9LN09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor which promotes the expression of heat stress-inducible genes by contributing to the formation of a heat stress-specific transcriptional complex with NF-Y subunits (e.g. NF-YA2 and NF-YB3) and DREB2A at the promoter of target genes, thus promoting heat tolerance. Together with the glyceraldehyde-3-phosphate dehydrogenase (GAPC), enhances heat tolerance.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:25490919}.
Interaction partners:
- DNA polymerase II subunit B4
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit A-2
- At3g12480/MQC3.32
- AT4g11790/T5C23_220
- Nuclear transcription factor Y subunit A-1
- Nuclear factor Y, subunit C13
- Nuclear transcription factor Y subunit C-8
- DNA ligase
- Dehydration-responsive element-binding protein 2A
Sequence:
MVSSKKPKEKKARSDVVVNKASGRSKRSSGSRTKKTSNKVNIVKKKPEIYEISESSSSDSVEEAIRGDEAKKSNGVVSKRGNGKSVGIPTKTSKNREEDDGGAEDAKIKFPMNRIRRIMRSDNSAPQIMQDAVFLVNKATEMFIERFSEEAYDSSVKDKKKFIHYKHLSSVVSNDQRYEFLADSVPEKLKAEAALEEWERGMTDAG
Protein: Probable GTPase-activating protein GYL1 (GYP5-like protein 1) (Q04322)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable GTPase-activating protein which stimulates the GTP hydrolysis rate by GYP5 of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15331637}. Bud {ECO:0000269|PubMed:15331637}. Bud neck {ECO:0000269|PubMed:15331637}.
Interaction partners:
- GTPase-activating protein GYP5
- Reduced viability upon starvation protein 167
- Reduced viability upon starvation protein 161
- Protein YSC84
Sequence:
MNSNEDIHEERIEVPRTPHQTQPEKDSDRIALRDEISVPEGDEKAYSDEKVEMATTNASSNFGSNESAKDGESIGAFSNPHEALMQSKLREESQSKTILPSDDLSQQLETEESKVEEALKRITSPPLPPRADCIEESASALKSSLPPVLAGNKNDQAPLDRPQLPPRQVVNAETLHLKAPHGNATPSKSPTSAVGNSSSSTPPTLPPRRIEDPLDLAAQKHFLASTFKRNMLFYKSEDNSIKCDLDKNILNLKEDSKKINNNEIPEEVSSFWLKVIGDYQNILINDIETLHFQLSRGIPAAYRLVVWQLVSYAKSKSFDPIYETYLTEMAPFDVQEFENQLKMMDEVPSEYVKRISNVLKAYLLFDPECEFSTDIAYIINMILDVCEEEANAFGLLVRLMKVYGLRLLFLPSASEIDILCYKFDRLVEEFYPEIHNHMVEKGVRSSMFLPGFFTTLFQKKLPTEIQPRIGDMVFLEGIDSIMRILATLLSNSRDHLLKMGFDDMLELLKSGLLDAYIKQNDGTRGDTLLSNECMDKLLQDSMMKVAITPKTMKKYSSEYEEIHRLDNEKEVQYKSITEKNLHLQKHVRKLENDYTSLNREHVTIANELVKNRLNIESVLNENNGYKLQILDLKKKLDSEKKKQVLGVYVPNDLKKDLEETMKKNTQVMDENLKLQDRISELERLIEEIKTANKNGTLFEYSNSKNNPLGAGWSGFKKVFK
Protein: BBSome complex member BBS2 (Bardet-Biedl syndrome 2 protein homolog) (Q98SP7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for ciliogenesis.
Subcellular location: Cell projection, cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}.
Interaction partners:
- Bardet-Biedl syndrome 7 protein homolog
- BBSome complex member BBS5
- Bardet-Biedl syndrome 9.
- Bardet-Biedl syndrome 1.
- Tetratricopeptide repeat domain 8.
- BBSome-interacting protein 1
- BBSome complex member BBS4
- Leucine zipper transcription factor-like 1.
- Bardet-Biedl syndrome 10.
- Bardet-Biedl syndrome 12
Sequence:
MLVPIFTLKLNHKINPRMVAIGKYDGIHPCLTAATQAGKVFIHNPHTRAQRPTAHRLSQSTQDSDISLLNINQSVSCLTAGTLGPKSTGDTLLVGSQTNLLAYDVHDNTDVFYKEVTDGANAIVLGKLGDIQSPLAIIGGNCALQGFDYEGNDLFWTVTGDNVRSLVLCDFTADGKNELLVGSEDFDIRVFKEDELVTEMAENETVTSLCHMHGSRFGYALANGTVGVYDRTARYWRIKSKNHAMSIHAFDLNADGVVELITGWSNGKIDARSDRTGEVIFKDNFSSSVAGVVEGDYRMDGQIQLICTSVEGEVRGYLPASKEMKGNLMDSSIEQDLIRELSQRKQNLMLELRNYEENAKALPGLSEGESKMGVIPANTQLQTALSVRRASESQKAHIELNISTPNETIIRAVLIFAEGIFEGESHVVHPSAQNLSGCVRVPIIPPKDIPVDLHIKAFVGGKTSTQFHVFEITRQLPRFSMYDLNVDPSAPEPTGKVTFCINDRPQRVVMWLNQNFLLPEGIDSPDVTFSALRGGGLLRISLQTSGEITLRTDDIDLAGDLVQSLASFLAIEDLQAESDFPVYFKELRATLTEVDEFHSVHQKLTAAMADHSNYIRNMLVQAEDARLMGDWRNMKKRYIELYDLNRDLVNEYKIRSNNHNALLARLKSVNQAIQRAGRLRVGKPKSQVITACRDAIKNNNINALFKIMRAGTTSS
Protein: Ribosome biogenesis protein Nop10 (Q8U1R4)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Involved in ribosome biogenesis; more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA.
Interaction partners:
- Small nucleolar rnp gar1-like protein
- Probable tRNA pseudouridine synthase B
- Large ribosomal subunit protein eL8
- DNA-directed RNA polymerase subunit Rpo11
- Translation initiation factor 2 subunit alpha
- tRNA pseudouridine synthase A
- Probable tRNA pseudouridine synthase D
- tRNA pseudouridine synthase Pus10
Sequence:
MRFRIRKCPKCGRYTLKEVCPVCGEKTKVAHPPRFSPEDPYGEYRRRWKREVLGIGRKEK
Protein: transaldolase (EC 2.2.1.2) (F4IC59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Fructose-1,6-bisphosphatase, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Fructose-1,6-bisphosphatase 1, chloroplastic
Sequence:
MPLSLQSPPCATLSASIRKGRWKTLAAGFSVTPLPAVNFSLRRSIPRILASASSSSSPASSSLEAGENNELNAVSAFSEIVPDTVVFDDFESFSLDRGYKKEISLRCKNSLPHKFPPTAATVSSALLLGICGLPDTIFRNAVDMALADSSCAGLETTESRLSCFFNKAIVNVGGDLVKLVPGRVSTEVDARLAYDTNGIIRKVHDLLRLYNEIDVPHDRLLFKIPATWQGIEAARLLESEGIQTHMTFVYSFAQAAAASQAGASVIQIFVGRLRDWARNHSGDTEIESAIKSGEDPGLALVKRSYNYIHKYGYKSKLMAAAVRNKQDLFSLLGVDYVIAPLKVLQSLKDSPAIPDDEKYSFVRKLTPETATHYHFTNKELVKWDQLSLASSMGPASVELLSAGVEGYANQAKRVEELFGKIWPPPNV
Protein: Metallophosphoesterase MPPED2 (EC 3.1.-.-) (239FB) (Fetal brain protein 239 homolog) (Metallophosphoesterase domain-containing protein 2) (B1WBP0)
Organism: Rattus norvegicus (Rat)
Function: Displays low metallophosphoesterase activity (in vitro). May play a role in the development of the nervous system (Probable).
Interaction partners:
Sequence:
MAHGIPSQGKVTITVDEYSSNPTQAFTHYNINQSRFQPPHVHMVDPIPYDTPKPAGHTRFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDKEFMADLVKQDYYRFPSVSKLKPEDFDNVQSLLTNSIYLQDSEVTVKGFRIYGAPWTPWFNGWGFNLPRGQSLLDKWNLIPEGTDILMTHGPPLGFRDWVPKELQRVGCVELLNTVQRRVRPKLHVFGGIHEGYGTMTDGYTTYINASTCTVSFQPTNPPIIFDLPNPQGS
Protein: Nuclear receptor-binding factor 2 (NRBF-2) (Q9QYK3)
Organism: Rattus norvegicus (Rat)
Function: May modulate transcriptional activation by target nuclear receptors. Can act as transcriptional activator (in vitro).
Subcellular location: Nucleus {ECO:0000269|PubMed:10786636}. Cytoplasm {ECO:0000269|PubMed:10786636}. Cytoplasmic vesicle, autophagosome {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Beclin 1-associated autophagy-related key regulator
- Phosphoinositide 3-kinase regulatory subunit 4
- Beclin-1
- RB1-inducible coiled-coil protein 1
- Activating molecule in BECN1-regulated autophagy protein 1
- UV radiation resistance associated
- Beclin 2
- non-specific serine/threonine protein kinase
- Autophagy-related protein 101
Sequence:
MEVMEGPLNLAHQQSRRADRLLAAGKYEEAISCHKKATAYLSEAMKLTQSEQAHLSLELQRDSHMKQLLLIQERWKRAKREERLKAQQSTDRDGVPHLQASHRPSEDSEGQSPLLSQTYIPSTEKRLPEEQGVFDRDPDTLLFLLQQKNEPSEPCIGSKAPKDDKTIIEEQATKIAELKRHVEFLVAENERLRKENKQLKAEKARLLKGPAEKELDVDADFVEKSELWGLPPHSDTATASSTWQKFAANTGKAKDIPIPNLPPLDFPSPELPLMELSEDILKGFMND
Protein: Ribosomal oxygenase 1 (60S ribosomal protein L8 histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66) (EC 1.14.11.27, EC 1.14.11.79) (Myc-associated protein with JmjC domain) (Nucleolar protein 66) (hsNO66) (Ribosomal oxygenase NO66) (ROX) (Q9H6W3)
Organism: Homo sapiens (Human)
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2) (By similarity). Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). Also catalyzes demethylation of non-histone proteins, such as CGAS: demethylation of monomethylated CGAS promotes interaction between CGAS and PARP1, followed by PARP1 inactivation (By similarity). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216', thereby playing a role in ribosome biogenesis. Participates in MYC-induced transcriptional activation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14742713, ECO:0000269|PubMed:17308053}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17308053}. Note=Granular part of nucleoli (PubMed:14742713). Nucleoplasm, nucleoplasmic foci, some of them associated with nucleoli (PubMed:14742713). {ECO:0000269|PubMed:14742713}.
Interaction partners:
- Large ribosomal subunit protein uL2
- PHD finger protein 19
- Transcription factor Sp7
- Serine/threonine-protein kinase RIO1
- Ras-GEF domain-containing family member 1A
- Protein strawberry notch homolog 1
- Transforming growth factor-beta receptor-associated protein 1
- 2-oxoglutarate and iron-dependent oxygenase JMJD4
- tRNA wybutosine-synthesizing protein 5
Sequence:
MDGLQASAGPLRRGRPKRRRKPQPHSGSVLALPLRSRKIRKQLRSVVSRMAALRTQTLPSENSEESRVESTADDLGDALPGGAAVAAVPDAARREPYGHLGPAELLEASPAARSLQTPSARLVPASAPPARLVEVPAAPVRVVETSALLCTAQHLAAVQSSGAPATASGPQVDNTGGEPAWDSPLRRVLAELNRIPSSRRRAARLFEWLIAPMPPDHFYRRLWEREAVLVRRQDHTYYQGLFSTADLDSMLRNEEVQFGQHLDAARYINGRRETLNPPGRALPAAAWSLYQAGCSLRLLCPQAFSTTVWQFLAVLQEQFGSMAGSNVYLTPPNSQGFAPHYDDIEAFVLQLEGRKLWRVYRPRVPTEELALTSSPNFSQDDLGEPVLQTVLEPGDLLYFPRGFIHQAECQDGVHSLHLTLSTYQRNTWGDFLEAILPLAVQAAMEENVEFRRGLPRDFMDYMGAQHSDSKDPRRTAFMEKVRVLVARLGHFAPVDAVADQRAKDFIHDSLPPVLTDRERALSVYGLPIRWEAGEPVNVGAQLTTETEVHMLQDGIARLVGEGGHLFLYYTVENSRVYHLEEPKCLEIYPQQADAMELLLGSYPEFVRVGDLPCDSVEDQLSLATTLYDKGLLLTKMPLALN
Protein: Pentatricopeptide repeat-containing protein At2g46050, mitochondrial (O82363)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MRFTFLRSTRIFLANHQNHLSSLQNIRTIPSSSSSPVAISSVSKLSASLDHLSDVKQEHGFMVKQGIYNSLFLQNKLLQAYTKIREFDDADKLFDEMPLRNIVTWNILIHGVIQRDGDTNHRAHLGFCYLSRILFTDVSLDHVSFMGLIRLCTDSTNMKAGIQLHCLMVKQGLESSCFPSTSLVHFYGKCGLIVEARRVFEAVLDRDLVLWNALVSSYVLNGMIDEAFGLLKLMGSDKNRFRGDYFTFSSLLSACRIEQGKQIHAILFKVSYQFDIPVATALLNMYAKSNHLSDARECFESMVVRNVVSWNAMIVGFAQNGEGREAMRLFGQMLLENLQPDELTFASVLSSCAKFSAIWEIKQVQAMVTKKGSADFLSVANSLISSYSRNGNLSEALLCFHSIREPDLVSWTSVIGALASHGFAEESLQMFESMLQKLQPDKITFLEVLSACSHGGLVQEGLRCFKRMTEFYKIEAEDEHYTCLIDLLGRAGFIDEASDVLNSMPTEPSTHALAAFTGGCNIHEKRESMKWGAKKLLEIEPTKPVNYSILSNAYVSEGHWNQAALLRKRERRNCYNPKTPGCSWLGDYSI
Protein: KN motif and ankyrin repeat domain-containing protein 2 (Ankyrin repeat domain-containing protein 25) (Matrix-remodeling-associated protein 3) (SRC-1-interacting protein) (SIP) (SRC-interacting protein) (SRC1-interacting protein) (Q63ZY3)
Organism: Homo sapiens (Human)
Function: Involved in transcription regulation by sequestering in the cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3. Involved in regulation of caspase-independent apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria. Pro-apoptotic stimuli can induce its proteasomal degradation allowing the translocation of AIFM1 to the nucleus to induce apoptosis. Involved in the negative control of vitamin D receptor signaling pathway. Involved in actin stress fibers formation through its interaction with ARHGDIA and the regulation of the Rho signaling pathway. May thereby play a role in cell adhesion and migration, regulating for instance podocytes migration during development of the kidney. Through the Rho signaling pathway may also regulate cell proliferation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17476305, ECO:0000269|PubMed:17996375, ECO:0000269|PubMed:22371500, ECO:0000269|PubMed:25961457}. Mitochondrion {ECO:0000269|PubMed:22371500}.
Interaction partners:
- Kinesin-like protein KIF21A
- Rho GDP-dissociation inhibitor 1
- Liprin-beta-1
Sequence:
MAQVLHVPAPFPGTPGPASPPAFPAKDPDPPYSVETPYGYRLDLDFLKYVDDIEKGHTLRRVAVQRRPRLSSLPRGPGSWWTSTESLCSNASGDSRHSAYSYCGRGFYPQYGALETRGGFNPRVERTLLDARRRLEDQAATPTGLGSLTPSAAGSTASLVGVGLPPPTPRSSGLSTPVPPSAGHLAHVREQMAGALRKLRQLEEQVKLIPVLQVKLSVLQEEKRQLTVQLKSQKFLGHPTAGRGRSELCLDLPDPPEDPVALETRSVGTWVRERDLGMPDGEAALAAKVAVLETQLKKALQELQAAQARQADPQPQAWPPPDSPVRVDTVRVVEGPREVEVVASTAAGAPAQRAQSLEPYGTGLRALAMPGRPESPPVFRSQEVVETMCPVPAAATSNVHMVKKISITERSCDGAAGLPEVPAESSSSPPGSEVASLTQPEKSTGRVPTQEPTHREPTRQAASQESEEAGGTGGPPAGVRSIMKRKEEVADPTAHRRSLQFVGVNGGYESSSEDSSTAENISDNDSTENEAPEPRERVPSVAEAPQLRPAGTAAAKTSRQECQLSRESQHIPTAEGASGSNTEEEIRMELSPDLISACLALEKYLDNPNALTERELKVAYTTVLQEWLRLACRSDAHPELVRRHLVTFRAMSARLLDYVVNIADSNGNTALHYSVSHANFPVVQQLLDSGVCKVDKQNRAGYSPIMLTALATLKTQDDIETVLQLFRLGNINAKASQAGQTALMLAVSHGRVDVVKALLACEADVNVQDDDGSTALMCACEHGHKEIAGLLLAVPSCDISLTDRDGSTALMVALDAGQSEIASMLYSRMNIKCSFAPMSDDESPTSSSAEE
Protein: Zinc fingers and homeoboxes protein 1 (P70121)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional repressor. Increases DNMT3B-mediated repressive transcriptional activity when DNMT3B is tethered to DNA. May link molecule between DNMT3B and other co-repressor proteins (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:17056598}. Note=Colocalized in the nucleus with DNMT3B. {ECO:0000250}.
Interaction partners:
- TBC1 domain family member 31
Sequence:
MASRRKSTTPCMVLASEQDPDLELISDLDEGPPILTPVENAKAESVSSDEEVHGSVDSDNQQNKKVEGGYECKYCTFQTPDLNMFTFHVDSEHPNVVLNSSYVCVECNFLTKRYDALSEHNLKYHPGEENFKLTMVKRNNQTIFEQTINDLTFDGSFVKEENTEQGESIDVSSSGISISKTPIMKMMKNKVENKRITVHHNSAEGTSEEKENGVKASQEENAESVSSSALESNTSTSTINRVHPSPASTVVTPTAVLPGLAQVITAVSAQQNSNLLPKVLIPVNSIPTYNAALDNNPLLLNTYNKFPYPTMSEITVLSAQAKYTEEQIKIWFSAQRLKHGVSWTPEEVEEARRKQFNGTVHTVPQTITVIPTHISTGSNGLPSILQTCQIVGQPGLVLTQVAGTNTLPVTAPIALTVAGVPNQTNVQKSQVPAAQPATDTKPATAAVPSSPSVRPEAALVNPDSFGIRAKKTKEQLAELKVSYLKNQFPHDSEIIRLMKITGLTKGEIKKWFSDTRYNQRNSKSNQCLHLNNDSSATIIIDSSDETPEPPAAAASQQKQSWNPFPDFAPQKFKEKTAEQLRALQASFLNSSVLTDEEVNRLRAQTKLTRREIDAWFTEKNKTKALKDEKIEVDESNVGSSKEEPGESSPGDETVAPKSGGTGKICKKTPEQLHMLKSAFVRTQWPSAEEYDKLAEESGLARTDIVSWFGDTRYAWKNGNLKWYYYYQSSNSSSLNGLSSLRRRGRGRPKGRGRGRPRGRPRGGKRMNTWDRVPSLIKFKTGTAILKDYYLKHKFLNEQDLDELVNRSHMGYEQVREWFAERQRRSELGIELFEENEEEDEVVDDQEEDEEETDDSDTWEPPRHVKRKLSKSDD
Protein: 60S ribosome subunit biogenesis protein NIP7 homolog (KD93) (Nucleolar pre-rRNA processing protein NIP7) (Q9Y221)
Organism: Homo sapiens (Human)
Function: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22195017}.
Interaction partners:
- Ribosome biogenesis protein BRX1 homolog
- Ribosome biogenesis protein WDR12
- Probable rRNA-processing protein EBP2
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- mRNA turnover protein 4 homolog
- Probable ribosome biogenesis protein RLP24
- Ribosome production factor 1
- 28S rRNA
- Ribosome biogenesis protein NSA2 homolog
- GTP-binding protein 4
Sequence:
MRPLTEEETRVMFEKIAKYIGENLQLLVDRPDGTYCFRLHNDRVYYVSEKIMKLAANISGDKLVSLGTCFGKFTKTHKFRLHVTALDYLAPYAKYKVWIKPGAEQSFLYGNHVLKSGLGRITENTSQYQGVVVYSMADIPLGFGVAAKSTQDCRKVDPMAIVVFHQADIGEYVRHEETLT
Protein: Cyclin-dependent kinase inhibitor FAR1 (CKI FAR1) (Factor arrest protein) (P21268)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Inhibitor of the cyclin-dependent kinase CDC28. Necessary for cell cycle arrest. Involved in pheromone response. Contributes to mating efficiency. Required for oriented polarization of yeast cells in response to mating pheromones.
Interaction partners:
- Cell division control protein 24
- Mitogen-activated protein kinase FUS3
- G1/S-specific cyclin CLN2
- Cyclin-dependent kinase 1
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein subunit gamma
- G1/S-specific cyclin CLN1
- Mitogen-activated protein kinase KSS1
- Cell division control protein 4
- G1/S-specific cyclin CLN3
Sequence:
MKTPTRVSFEKKIHTPPSGDRDAERSPPKKFLRGLSGKVFRKTPEFKKQQMPTFGYIEESQFTPNLGLMMSKRGNIPKPLNLSKPISPPPSLKKTAGSVASGFSKTGQLSALQSPVNITSSNKYNIKATNLTTSLLRESISDSTTMCDTLSDINLTVMDEDYRIDGDSYYEEDSPTFMISLERNIKKCNSQFSPKRYIGEKCLICEESISSTFTGEKVVESTCSHTSHYNCYLMLFETLYFQGKFPECKICGEVSKPKDKDIVPEMVSKLLTGAGAHDDGPSSNMQQQWIDLKTARSFTGEFPQFTPQEQLIRTADISCDGFRTPRLSNSNQFEAVSYLDSPFLNSPFVNKMATTDPFDLSDDEKLDCDDEIDESAAEVWFSKTGGEHVMVSVKFQEMRTSDDLGVLQDVNHVDHEELEEREKEWKKKIDQYIETNVDKDSEFGSLILFDKLMYSDDGEQWVDNNLVILFSKFLVLFDFEEMKILGKIPRDQFYQVIKFNEDVLLCSLKSTNIPEIYLRFNENCEKWLLPKWKYCLENSSLETLPLSEIVSTVKELSHVNIIGALGAPPDVISAQSHDSRLPWKRLHSDTPLKLIVCLNLSHADGELYRKRVLKSVHQILDGLNTDDLLGIVVVGRDGSGVVGPFGTFIGMINKNWDGWTTFLDNLEVVNPNVFRDEKQQYKVTLQTCERLASTSAYVDTDDHIATGYAKQILVLNGSDVVDIEHDQKLKKAFDQLSYHWRYEISQRRMTPLNASIKQFLEELHTKRYLDVTLRLPQATFEQVYLGDMAAGEQKTRLIMDEHPHSSLIEIEYFDLVKQQRIHQTLEVPNL
Protein: Possible transcriptional regulatory protein (O33179)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator Rv0377
- Cytochrome P450 144
- Possible transcriptional regulatory protein
- Probable transcriptional regulatory protein
- Uncharacterized HTH-type transcriptional regulator Rv2282c
- HTH-type transcriptional regulator LysG
- Transcriptional regulatory protein
- Putative mycofactocin biosynthesis transcriptional regulator MftR
- Uncharacterized protein Rv1359
- Transcriptional regulatory protein TcrA
Sequence:
MPGNDWIVGGNRRTIAAERIYAAATDLITRYGLNALDIDKLAREVHCSRATIYRRAGGKAQIRDVVLTRAAARIADGVRSDVETLRGRERVVAAILLSLQRIRSDPLGKLMFGSIHGGAGELAWLTESPLLADFATELTGIAGGDPQGAKWVVRVVLSLMYWPAENDEAERRLVEKYVAPAFAEQS
Protein: Reticulocyte-binding protein 1 (Q00798)
Organism: Plasmodium vivax (strain Belem)
Function: Involved in reticulocyte adhesion. Specifically binds to human reticulocyte cells.
Subcellular location: Membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MKRGICLAALLCLFNYLGAGHGENAEEDIRNSEGKVNFFSLDSNLKKNKKSKHNRVKRRNAKISNFLSQKAYVKETDNASGKDAEGSRPSHDSSFVNLNGHVDGKSLSYSVHVKESTPHSTTRESTEKGKENEKIQGVLSSFVQSQEGGESDDLEGMYNSIVDMSEKLKENDKYNLVFDMEIDFVDLQFFNLILELIPKDSQYHTYYEETLKQQVTEYTNSLKTLMDSCISEKDQMIILEYEINYAKRKSIETETLGDKETKLSAVSQAYAKHLESYKGVLKPKLNDIKNNAFSVLKDSYCKDNCGEYVQKYNTMRKNFISSSDQYKMEAYVYIPKSINDYTVLDKILSESNELGIDIQETVNSLKLLGEEISEVSHLYVINSTLIDDAAKKLESINEEDESAEIDLQKFEDNSKALANNYCIFQYIKTLNEPIKKAYESKVIKSNELLSTIIDTLGKSATALQESTFDQEECNKIKTEAEKVKDDAEDICEKNEQIYYEIPESEDETIDDKINDLQDLIDQMKEYKDEIVNNSEFISNRYKNIYENLKETYETELNDIGKLENDTSKVNFYLMQIRKINTEKTKIDESLQTVEKFYKEILDSKEKIYELKIEFEKSVTEINRLQDGESARDLHEEQIKEILDKMAKKVHYLKELLSLKGKSSVYFTEMNELLNTASYDNMEGFSAKKEKADNDINALYNSVYREDINALIEEVEKFVTENKESTLEMLKDEEMEEKLQDAKETFAKLNFVSDDKLTDVYTKMSAEVTNAEGIKKEIAQKQFENVHKKMKEFSDAFSTKFEALQNSMQQYNQEGDAIEKHKQNRSEKEEEYFKNESVEEDLSREETEEQEYTKHKNNFSRRKGEISAEITNMREVINKIESQLNYYGVIEKYFSLIGDQNEVSTAKALKEKIVSDSLRDKIDQYETEFKEKTSAVENTVSTIQSLSKAIDSLKRLNGSINNCKKYNTDIDLLRSKIKTLREEVQKEIAETEGDKVVGENTTALLLKSLRDKMGKINEKLNDGRLNSLDTKKEDLLKFYSESKSKIHLSKDQKGPQDPLNRIDEWEDIKREVDELNVNYQVISENKVTLFKNNSVTYIEAMHSHINTVAHGITSNKNEILKSVKEVEDKLNLVEQNEDYKKVKNPENEKQLEAIRGSMSKLKEVINKHVSEMTQLESTANTLKSNAKGKENEHDLEELNKTKGQMRDIYEKLKKIAEELKEGTVNELKDANEKANKVELEFERNIIGHVLERITVEKDKAGKVVEEMNSLKTKIEKLIQETSDDSQNELVTTSITKHLENAKGYEDVIKRNEEDSIQLREKAKSLETLDEMKKLVQQVNMNLQSAIQGNAGISKELNELKGVIELLISTNYSSILEYVKKNSSESVRFSQLANGEFTKAEGEEKNASARLAEAEKLKEQIVKDLDYSDIDDKVKKIEGIKREILKMKESALTFWEESEKFKQMCSSHMENAKEGKKKIEYLKNNGDGGKANITDSQMEEVGNYVSKAEHAFHTVEAQVDKTKAFYESIVAYVTKMDNLFNESLMKEVKVKCEKKNDEAEQIFGQIKTVDGRIKARVSENERKISELKEKAKVEKKESSQLNDVSTKSLLQIDNCRQQLDSVLSNIGRVKQNALQYFDSADKSMKSVLPISELGAEKSLDKVKAAKESYEKNLETVQNEMSRINVEEGSLTDIDKKITDIENDLLKMKKQYEEGLLQKIKENADKRKSNFELVGSEINALLDPSTSIFIKLKLKEYDMTGDLKNYAVKMNEIHGEFTKSYNLIETHLSNATDYSVTFEKAQSLRELAEKEEEHLRRREEEAIKLLNDIKKVESLKLLKEMMKKVSAEYEGMKRDHTSVSQLVQDMKTIVDELKTLNDISECSSVLNNVVSIVKKVKESKHADYKRDANSMYESMVTLANYFLSDEAKISSGMEFNAEMKSNFKTDLELEIFSVISNSNELLKKIEQDSNDVIQKERESEQLAKDATDIYNVIKLKNEFNEKLEEAKNKEEVVSEKVREALKRLSQVEGIRCHFENFHRLLDNTEELENLKKMVTIYRDKKSEAPKESGLQEMENEMNTYSNSITQLEGIVVSAGESKEDIEKLERSNEEMRNISEKISTIDSKVIEMNSTIDELYKLGKNCQAHWISLISYTANMKTSKKLIMINKEKENTEKCVDYIKDNSSSTDGYVETLKGFYGSKLTFSSASEIVQNADTYSVNFAKHEKESLNAIRDIKKELYLFHQNSDISIVEGGVQNMLALYDKLNEEKREMDELYRNISETKLKQMEHSTDVFKPMIELHKGMNETNNKSLLEKEKKLKSVNDHMHSMEAEMIKNGLKYTPESVQNINNIYSVIEAEVKTLEEIDRDYGDNYQIVEEHKKQFSILIDRTNALMDDIEIFKKENNYNLMEVNTETIHRVNDYIEKITNKLVQAKTEYEQILENIKQNDDMLQNIFLKKVSIIEYFENVKKKKESILNDLYEQERLLKIGEHLDEIKRNVTETLSSYEIDQKMEMMSKNLLEKKSKMMNYTSIYELEREANEINRDAKQIKDDDTILNSVLEAAIQKRGDMDAIFSQMSADRNPNEYKSAEKYMNEANEIIRQLEVKLREIGQLVQDSESILSEMNSKKSAIEKEKTARALRTSENNRREEEERARVQEMSMNNDPTQSETTHSEGSIGEGKESDSDETGLTHDAGADEDSTSSAKGAHELEEEETTAPMEETEMNDNTLLGYDTTRSDEPDMHTENTQDGTYQDTSNSSDEADILNGKFNFNNVKYAGAFVLLCTSAVIGAIIAHKKDDQEELNNGVEDDKVFEVKKSMHPENKEEIIDDSFVDIEY
Protein: Mitochondrial dicarboxylate carrier (DIC) (Solute carrier family 25 member 10) (Q9UBX3)
Organism: Homo sapiens (Human)
Function: Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane. Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, particularly in liver, by supplying the substrates for the different metabolic processes. Regulates fatty acid release from adipocytes, and contributes to systemic insulin sensitivity (By similarity).
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Mitochondrial carrier homolog 1
- Mitochondrial carrier homolog 2
Sequence:
MAAEARVSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALRVVRTDGILALYSGLSASLCRQMTYSLTRFAIYETVRDRVAKGSQGPLPFHEKVLLGSVSGLAGGFVGTPADLVNVRMQNDVKLPQGQRRNYAHALDGLYRVAREEGLRRLFSGATMASSRGALVTVGQLSCYDQAKQLVLSTGYLSDNIFTHFVASFIAGGCATFLCQPLDVLKTRLMNSKGEYQGVFHCAVETAKLGPLAFYKGLVPAGIRLIPHTVLTFVFLEQLRKNFGIKVPS
Protein: Inositol oxygenase 2 (EC 1.13.99.1) (Myo-inositol oxygenase 2) (AtMIOX2) (MI oxygenase 2) (O82200)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. May be also involved in plant ascorbate biosynthesis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable glucuronokinase 2
- Inositol-phosphate phosphatase
- Glucuronokinase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phosphatase IMPL1, chloroplastic
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Bifunctional phosphatase IMPL2, chloroplastic
- Inositol 3-kinase
- Aldo-keto reductase family 4 member C10
Sequence:
MTILVEHFVPDSRVDEKKVIEERDNELVLDGGFVVPKSKETDAFDAPDMNFLGHSFRDYENGESERQQGVEEFYRMQHIHQTYDFVKKMRKEYGKLNKMEMSIWECCELLNNVVDESDPDLDEPQIQHLLQTAEAIRRDYPDEDWLHLTALIHDLGKVLLLPEFGGLPQWAVVGDTFPVGCTFDSANIHHKYFKGNHDINNPKYNTKNGVYTEGCGLDNVLMSWGHDDYMYLVAKKNGTTLPHAGLFIIRYHSFYPLHKAGAYTHLMNDEDRDDLKWLHVFNKYDLYSKSKVLVDVEQVKPYYISLINKYFPAKLKW
Protein: Proline-rich protein 7 (O35327)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
NSSEGDEEEEEVEAADEDDEEEDEEGVLGRGPGHDRSRDRHSPPSCHLFPPPPPPLPPPPPPDKDDIRLLPSALGVKKRKRGPKKQKENKPGKPRKRKKLDSEEEFGSERDEYREKSESGGSEYGTGPGRKRRRKHREKKKKKKAWALF
Protein: Uncharacterized protein YiiR (P0AF34)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YcgY
- Uncharacterized protein YncH
- Sel1-repeat-containing protein YbeT
- UPF0381 protein YiiS
- Uncharacterized protein YebY
- Inner membrane ABC transporter permease protein YcjO
- Probable endopeptidase YafL
- Uncharacterized protein YbaE
Sequence:
MTIQQWLFSFKGRIGRRDFWIWIGLWFAGMLVLFSLAGKNLLDIQTAAFCLVCLLWPTAAVTVKRLHDRGRSGAWAFLMIVAWMLLAGNWAILPGVWQWAVGRFVPTLILVMMLIDLGAFVGTQGENKYGKDTQDVKYKADNKSSN