wanglab/gogpt-training-data huggingface dataset:
Protein: 4-coumarate--CoA ligase-like 6 (EC 6.2.1.-) (4-coumarate--CoA ligase) (EC 6.2.1.12) (4-coumarate--CoA ligase isoform 7) (At4CL7) (4-hydroxybenzoate--CoA ligase) (EC 6.2.1.27) (Q84P24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors. Acts as a carboxylate--CoA ligase that can use preferentially p-coumarate, ferulate and caffeate as substrates and, with a lower efficiency, (E)-cinnamate and 4-hydroxybenzoate as substrates. Involved in the biosynthesis of ubiquinone from phenylalanine by activating the propyl side chain of 4-coumarate, and possibly trans-cinnamate and 4-hydroxybenzoate, for subsequent beta-oxidative shortening and the formation of the benzenoid moiety of ubiquinone. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:24838974}.
Interaction partners:
- Trans-cinnamate 4-monooxygenase
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Cytochrome P450 84A1
- F5F19.5 protein
- Flavone 3'-O-methyltransferase 1
- Phenylalanine ammonia-lyase 1
- Phenylalanine ammonia-lyase 3
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 4
Sequence:
MAATHLHIPPNPKTQTSHQNPPFWFSSKTGIYTSKFPSLHLPVDPNLDAVSALFSHKHHGDTALIDSLTGFSISHTELQIMVQSMAAGIYHVLGVRQGDVVSLVLPNSVYFPMIFLSLISLGAIVTTMNPSSSLGEIKKQVSECSVGLAFTSTENVEKLSSLGVSVISVSESYDFDSIRIENPKFYSIMKESFGFVPKPLIKQDDVAAIMYSSGTTGASKGVLLTHRNLIASMELFVRFEASQYEYPGSSNVYLAALPLCHIYGLSLFVMGLLSLGSTIVVMKRFDASDVVNVIERFKITHFPVVPPMLMALTKKAKGVCGEVFKSLKQVSSGAAPLSRKFIEDFLQTLPHVDLIQGYGMTESTAVGTRGFNSEKLSRYSSVGLLAPNMQAKVVDWSSGSFLPPGNRGELWIQGPGVMKGYLNNPKATQMSIVEDSWLRTGDIAYFDEDGYLFIVDRIKEIIKYKGFQIAPADLEAVLVSHPLIIDAAVTAAPNEECGEIPVAFVVRRQETTLSEEDVISYVASQVAPYRKVRKVVMVNSIPKSPTGKILRKELKRILTNSVSSRL
Protein: Oxidoreductase (Q7S4Y9)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Interaction partners:
- Nitrate reductase
Sequence:
MGSIAVDDATLSRPPFKVLVVGGSYGGLSAALNLQDICSGRAARCGPDAKKAALDGTSAAHDGPQFAVDITVVDERDGFYHLIGTPLAFADESYAEKCWVKYEDVPALQQSPNNIRILRGSVQSIDQERKIAKVLGSENGPGPIELKYDYLIAAAGLRRVFPVVPQSLLRKQFLFEAGDHIQAATANRHGVAVVGGGAVGIEMAAELKLVCPDLKVTLIHSRDKLLSAEPLPEEVKDRSLELVHEAGVEVLMSHRVDRTEEFVDNGHKAYKVYFTNGHTLIADSVIMAISRSVPSTTFLPRDVLNEEGYVKIQPSLHFPSESPNSDDHLAIGDLVKWSGIKRCGGAMHMGYLAANNIHMRMKQAVSGTEPTYLELDEIPPMIGLAVGKKAVAYWPTNGVSSGEDVNKLFFGDDLGFDICWNHLRLGGYDVVKA
Protein: Doa1p (A0A1D8PEM3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- AAA family ATPase
- Nuclear protein localization protein 4
- Ubiquitin fusion degradation protein 1
- Ubiquitin thioesterase OTU
- Protein phosphatase regulator
- UBX domain-containing protein
- Polyubiquitin
- Ubiquitin-ribosomal protein eS31 fusion protein
- AAA family ATPase
- Altered inheritance of mitochondria protein 21
Sequence:
MSYKLSSTLLGHEQDVKDVATTEYGGLVSVSRDGTTRIWSDIYTTHSEATIVFHSPTNSFINSVACINGLIASGGQDTMIYLSDEHGEDKYQLIGHEGNVCSMSYSHGQLISSSWDCTAIVWNLKEFVPKYILSGHESSVWDCQVLGEDHYLTCSADKTIRFWHGKSEVKQFVGHSDVIRKLLILEGGEQFLSCSNDGTIKLWDLQTGKNLQTFYGHESFVYDLALIANGKFVSTGEDRTVRIWDLATGNVLQVITLPCISVWCVTALPNGDFAVGGSDNLVRVFTAHPEKVAPEEELLKFKEAVQSSSIAEQSLDDLKKTDIPGYEALSQPGKQEGSTIMVKNPDNGTIEAHQWSGGEWHKIGDVVGSSSSGKKQTYQGKEYDFVFDVDIKDGEPPLKLPYNVNDNPYTVAEKFLSDNDLPASYTDEVVRFLQKNTEGVSLQESTNDSNNPSAGRVIDPYSDAYNKQQKQQGNLALKVIPSKSYIYFTDYKRESLVNGLKKLNSSQDSELQLSDQDFLAVESSLSELNSKQALELITKYCSHIIRKWTASAKLIGFDLLRVSIPKVTTVDILTSTDAAEIILDVVNLGLENINVENPALLMMILKVLNNLVGTTLFVQLYIDPCGTDNKLYEYNTFFQNLLKKLQNSTAKLTQSAKLYTSTMTALTTLVYNLSAYQLQTSALKNNMGSAKPVIEFMDNLGNQIVASSSEAAYRLAVAYGNFKYGKLYTNETPSWLAEAGTLYAINGEQRFLDIAEDLKNI
Protein: Transcription factor TCP13 (Plastid transcription factor 1) (TFPD) (Q9S7W5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a pivotal role in the control of morphogenesis of shoot organs by negatively regulating the expression of boundary-specific genes such as CUC genes, probably through the induction of miRNA (e.g. miR164). Binds to the 3'-ACC-5' repeats in the light-responsive promoter (LRP) of psbD, and activates its transcription. Participates in ovule develpment.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701, ECO:0000269|PubMed:11161017}. Plastid, chloroplast {ECO:0000269|PubMed:11161017}.
Interaction partners:
- Transcription factor TCP14
- Transcription factor TCP15
- Transcription factor TCP19
- Transcription factor TCP21
- Transcription factor TCP8
- Transcription factor TCP7
- Transcription factor TCP20
- Transcription factor TCP23
- Zinc finger AN1 and C2H2 domain-containing stress-associated protein 11
- Transcription factor TCP22
Sequence:
MNIVSWKDANDEVAGGATTRREREVKEDQEETEVRATSGKTVIKKQPTSISSSSSSWMKSKDPRIVRVSRAFGGKDRHSKVCTLRGLRDRRVRLSVPTAIQLYDLQERLGVDQPSKAVDWLLDAAKEEIDELPPLPISPENFSIFNHHQSFLNLGQRPGQDPTQLGFKINGCVQKSTTTSREENDREKGENDVVYTNNHHVGSYGTYHNLEHHHHHHQHLSLQADYHSHQLHSLVPFPSQILVCPMTTSPTTTTIQSLFPSSSSAGSGTMETLDPRQMVSHFQMPLMGNSSSSSSQNISTLYSLLHGSSSNNGGRDIDNRMSSVQFNRTNSTTTANMSRHLGSERCTSRGSDHHM
Protein: Fgr18p (A0A1D8PIC3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Predicted GPI-anchored protein 44
Sequence:
MNKQTNLNDNKEVKGVEGEIPNKWRIFTHCSKLFQFQIVLKNRGSVARDHMANERTFLSWIRTALVFLTFSIGFLQFYRLEIKANTNTLGDSNLSQMIQTLGKPLGAMGTILSGLTVTFGTIRYFQVQELLLDDYYPVTRFTIIILILINLSILVVSFILNIDISLFVMS
Protein: Chaperone protein DNAJ, putative (Q385P6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQLHLSSISMMCLLLVTLQLSFTPKVTNASIFGQPNDRDLYGLLGVSRGSTKAEIKRAFRTITREHHPDMQEGAEAKEKAKEYMAKVLVAYNILSDDIKRSDYDQFGRIAGERLNAADFTSDELFERFNQHPPILSKSLQLENLIVLRRILNFRGNRLFLLQVYDDTCKSCQLFSSVWENLVHSTLVESGAVVLLRIDAYSDEGPELLKELHASYDKEVKVYGIADGVVWNMPQMAVAVKSNSQRQLDYALMEFVGNFFYDRRAEVNSMGNVEDVQVLLQWLRERRSEGDSVRVLLPPLATNDMGVALSALYEGSALVRSVPRAVLLSLVEEYCAQSVDVLGGGGEPVPLPEFVVASVEQLPNISSDESAGNKSQMRSCRGIVVGAAAALTYRKAVNFLKESFPQRHLGMSGLTHVTSVSFFDICKKHCLLWLRDNCEGEPTGTWLEALRGDYKPFKVGYICLSSEPSLRDAVPLPLGTTGNLLLALVDGDDSKLHVMPDIPDKVNIAQSLSSILAEVGSTTPLQLDAPLSRILSSVPFRMSRNQYLYMCFLWIFGLVYPFFSTCYPFFMMFVTHKLLQRYNLLGNNRNDNNSQTNEQPSGASNTCSRCSGTAPSGSCKSTASVTRGSACDNGTSSKEVISCPIEVYTSADLREAKDGRGFLILIFAENGKTIEPPQCFAKDSRFVFRAVPEDDTLWRQWLSQHVTSTHTGGAEENGLNKGGALHVVAIRRGKMLAAIKSLCASVEAWLFDMADGTIVADLPLPEL
Protein: glucose-6-phosphate 1-epimerase (EC 5.1.3.15) (Q581U5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Glucose-6-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- Fructose-bisphosphate aldolase
- Transketolase
- Glucose-6-phosphate 1-dehydrogenase
- Transaldolase
- deoxyribose-phosphate aldolase
- Fatty acyl-CoA reductase
- Phosphoacetylglucosamine mutase
Sequence:
MAKSPIVARNDDGSSILVHLQGAHLTNWRNKEGTELLYTSSKAVYEKGIPIRGGVPIVFPQFGNMGPLPPHGFARVRMWAVKEVTNGSASFTLNVPLRDLLGHDSGMIAEAPIAEAPSAETETVALLYTITFSNSHLDLQMEILNQHPTSVAEFTFAFHTYFAVGNVEKTVVEGVNMTSYVNNMAPHQGVLPPRRLWIIKKETDRTYFNQACAVLLVDAMKGHTVHVSGENLPDVVVWNPHVEKSKKLKDLPADGYKEFVCIEHGVIAKRVKLQPQFEWKGRQRILVLPSSKM
Protein: Alpha-crystallin A chain (E7EWH7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSACPRLAKLLASLLRCPAKAKRTGNGRPPPHPTTGLLSEPRVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS
Protein: Signal transducer and activator of transcription (B0S789)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
- Interferon regulatory factor 9.
- Tyrosine-protein kinase JAK1
- Tyrosine-protein kinase.
- Tyrosine-protein kinase
- Tyrosine-protein kinase.
- Signal transducer and activator of transcription.
- Inhibitor of nuclear factor kappa B kinase subunit epsilon
- Cytokine receptor family member b2
- Signal transducer and activator of transcription.
- Tyrosine-protein kinase
Sequence:
MTLWNQLQLLDSMYLEQVDQLYDEAFPMEIRQYLCHWIESHDWESIASNESLAIVRFHELLNQLDEHYSRLNLGNNFLLQHNIRKIKRNLQEHFQENPVYMAMIISSTLNEERKILQVALSSQGKGDSMQGNIMMEHQNELVNKVNNLKMSVQEMEKHVQALEDMQDDYDFNMKSLQSRIEAEGVQMNDPMPKEIQQEEMAIKRMFTVQGIKREVVMKEISNVLTLAEQIQFTLITEELPEWKKRQQMACIGGPPNACLDQLQNWFTVVAECLQQIRQQLKKVQELVQKFTYSNDPLNLGRGQLDEQAISLFKSLILNSLVVERQPCMPTHPQRPLVIKTGVQFTVKIRSLVKLPELNCQLKVKVFIDKNLTERDTIKGGRKFNILGTNTKVMNLEESSGCLAAEFRHLQLKEMKTSRTNETPLIVTEEMHLLSFETQLIQPELSVDLSIISLPIVVISHVNQLPSAWGSILWYNMLSGEPHNLTFFLNPPPVKWVQLSKVISWQFSSVSKRALTSDQLRTIADKLLGHKAQGDPEGLIQWSAFCKTSPNERGIPFWLWIDGILDLIKRHLLNIWNDGYIVGFLSRKQEKAMLRDKAPGTFLLRFSESCRDGGITFTWVEESQDGEPKIHSVKPYTKADLATISMPNIIRDYTLAAPMKVPVYPLIYLYPNIPKDEAFGRYYTSESEDSEDMETDKPINSDANPYLRRHLMHVSDKPVARPVARF
Protein: Leukocyte cell-derived chemotaxin-2 (LECT-2) (hLECT2) (O14960)
Organism: Homo sapiens (Human)
Function: Has a neutrophil chemotactic activity. Also a positive regulator of chondrocyte proliferation. Does not show metalloendopeptidase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8877413}. Secreted {ECO:0000269|PubMed:8877413}.
Interaction partners:
- Leukocyte cell-derived chemotaxin 1
- Tyrosine-protein kinase receptor Tie-1
- Plasminogen
- Apolipoprotein
Sequence:
MFSTKALLLAGLISTALAGPWANICAGKSSNEIRTCDRHGCGQYSAQRSQRPHQGVDILCSAGSTVYAPFTGMIVGQEKPYQNKNAINNGVRISGRGFCVKMFYIKPIKYKGPIKKGEKLGTLLPLQKVYPGIQSHVHIENCDSSDPTAYL
Protein: Uracil phosphoribosyltransferase homolog (Q9U3L5)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable uridine-cytidine kinase
- Uridine kinase
- Uridine and thymidine phosphorylase
- Uridine 5'-monophosphate synthase
- Serine hydroxymethyltransferase
- Purine nucleoside phosphorylase
- Thymidylate kinase
- Dihydropyrimidine dehydrogenase [NADP
- UMP-CMP kinase 2
- UMP-CMP kinase 1
Sequence:
MAGHVNGTCAPVIPKVGDEEDGVGQLVANLKEKGTNFVLLKKTPQILELQTILKDRSTNHSDFVFNADRLMRLVIEECLNHLPFTEHTVTTPTGFKYEGIQFNRGNCGVSLCRSGEAMEVSLRQCCRCIRIGKILIGDEQKVLYARLLPDITSRRVLLLYPTIGSGTTVCKAIEVLKEARVPDENIYLVSLFISPTGLKNITRKYPYITVVASDITSLYPNHFSTSYFGAV
Protein: yemanuclein (Yemanuclein-alpha) (P25992)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a key role in egg organization. May be a transcriptional regulator having a role in chromatin remodeling in concert with Hira, a histone chaperone. Involved in chromosome segregation by affecting kinetochores function in the first meiotic division.
Subcellular location: Nucleus, nucleoplasm. Chromosome. Chromosome, centromere, kinetochore. Note=Abundant in the nucleoplasm. Only a fraction of the protein is associated with the chromosomes. Localizes to the chromosome arms and coexpresses with cid at the centromere.
Interaction partners:
- Protein HIRA homolog
- Histone chaperone asf1
- Germ cell nuclear acidic peptidase, isoform B
Sequence:
MSKGGEHKRVTLTSIIQGDAGFSRFGSNILEPDAASAAPDNSSKPTTKTAKCIRIKLDLFETDSNKYPEFNYSRLLYLEKKKTKKLKQVSTTNGSASTDPFADNDDDVARIVKELEAKYGNSYATGRGKSKKDDYRDIGMGYDESDSFIDNTEAYDEIIPEEAETLEGGFYINCGALEFKNLTKKSYTTRTDAIIKMPERSRKRMVSSSSESSSSSSGDDDENDDGNNEEDDESDSEDDSEENDESDSEDDSESESLEDEDSAATAKSSSKYKDNHQAKRAKVIVTGKSKPSSSSLTSGKKPPTKPITTSSSSNSPRPSTVEISDTEDGQDPIQTQPSSQLQSLPQSQAQAQALKKVVKTTTVKDMLKAKRDSFLKSQSGTAAVKGVGNGELKCVSTDVSSSDSSDMESEHGRADRQAGQHGKDGQENLRTADTLLPTTLDADIVTAVNSFKEAVKSRDMCGKKFNLDVKLSPLLLRVYEAVLCTDRNERNMVFSHIEYQLQLPKYYMLRKGKQVRAKEEKRKSTIMLEKLRRAVAVVMPKAVANYETELRTFAEQAAADVNSELPPKMPRKKFQWTSELRHLLYDVYQARWTSYAFLAKRKESLEEFINWYLKEKVVELWPPGWMRLDELQREITRYKNAKLKAKEKPKAPPASASPKPVGVVSAPEQMPPASSYLKAVEDPRSRGNSDTDSATSASSNSLKRKLKEMPKQTSKPPKKKVAKQVPLQPQLTPHPQFQLAPAATAAVSIPAISNNNNHLPHLDTLLSMPSTSAQAAALNAAAVAAASTVLDLASPSRKIDLNTSNNFYNLITAASLAASGNPSPHSGDGQAKVIVGARPSPHVINLDDYQCTSDILQTSKQLAATTTVITAISKAAQTTSVARESSSESDGVEIVGVFPASKPQKKVQSKPKNKTQNRGRSSLGAVGQVNGSLGYSANNMYIYNSPRTLGPVYDLTDPHIMKTMSNLKEMEKQFIQAAFSPNSVKGASGGMGSSAPSTPTRQ
Protein: Ciliary neurotrophic factor receptor subunit alpha (CNTF receptor subunit alpha) (CNTFR-alpha) (O88507)
Organism: Mus musculus (Mouse)
Function: Binds to CNTF. The alpha subunit provides the receptor specificity (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Leukemia inhibitory factor receptor
- Ciliary neurotrophic factor
- Interleukin-27 receptor subunit alpha
- Cardiotrophin-like cytokine factor 1
- Cardiotrophin-1
- Interleukin-6
- Leukemia inhibitory factor
- Cardiotrophin-2
- Interleukin-6 receptor subunit beta
- Interleukin-11
Sequence:
MAASVPWACCAVLAAAAAAVYTQKHSPQEAPHVQYERLGADVTLPCGTASWDAAVTWRVNGTDLAPDLLNGSQLILRSLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNTTAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAPETTTSTTSSLAPPPTTKICDPGELGSGGGPSILFLTSVPVTLVLAAAAATANNLLI
Protein: protein disulfide-isomerase (EC 5.3.4.1) (A0A1D8PR99)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- ER oxidoreductin
- Endoplasmic reticulum chaperone BIP
- Calnexin
- Hsp70 family chaperone
- Tubulin beta chain
- Protein transport protein SEC61 subunit alpha
- Repressor of filamentous growth 1
- V-type proton ATPase subunit B
- Dihydrolipoyl dehydrogenase
- Protein transport protein SEC23
Sequence:
MKFWTYSTKVLATLLAVVSITHASGPTDGDAVADPNSAVVKLTSENFASFIEENPLILAEFFAPWCGYCKMLGPEYSKAADSLNESHPKIKLAQIDCTEDEALCMEHGIRGYPTLKIIRDGDSKTAEDYQGPREAAGIADYMIKQSLPAVQFPETFEELDTLIDAQTKPFVLQINPTEDGNATFNKVANQKRKDYVFINVEDKQIIKDLNKKFKNVDITGKKPSYLVVQPKQFDEVAKFDGKKIDAESLTEFIGVEAVPYFGEINQDTYMTYMTSPLPIAYYFYNNAEQREAIADDLTKLGKKYRGKLNIVGLDASLFGRHAEVINMDPEVVPLFAIHHISDNKKFGVNQTDYPEGPSFKVIEKFVADYFADKLTPIIKSEPLPTEEEKSANPVVKLVAHNYKDVLEQTDKDVFVKYYAPWCGHCKKLAPTWEELAEIFGSNKDDAKVVVADIDHTNNDVDVPYNIEGYPTLLMFPANGKVDEKTGIREPIVFEGPRELDTLIEFIKEKGALNVDGAELKAKLDEQKATKEDEEVEEEKEEEEEEAPVEDKENVEHDEL
Protein: Ribonuclease P protein component 4 (RNase P component 4) (EC 3.1.26.5) (Rpp21) (P62378)
Organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757, ECO:0000269|PubMed:20675586}.
Interaction partners:
- Ribonuclease P protein component 2
- Large ribosomal subunit protein eL8
- Ribonuclease P protein component 3
- Ribonuclease P protein component 1
- Endoribonuclease Nob1
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS11
- uroporphyrinogen-III C-methyltransferase
- Small ribosomal subunit protein uS2
Sequence:
MKLKKKFLEKSKKVAEERINILMNLAEKESNSGKTERSKNYVLLGKKIAMRMRMPYPKEWKRRICKNCGSFLIYGKNARVRTKAKNYPHVVITCLECNSITRIPIKTAKK
Protein: T. brucei spp.-specific protein (Q38BQ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNLNCEGRDVGRNLLMEGKGKKKKIAHLFIYIYLYICATNRWGEMKISLILFVVFVHLHSFFFLIYGLINSFVSVTCFFFSVVVEEPALFWCIQLDMTILPFYAINFFIIVIVLVPFENVARTLLSLQIIARLNTFFFFFFLLSFFLKKNIYIYL
Protein: General transcription and DNA repair factor IIH subunit tfb5 (TFIIH subunit tfb5) (RNA polymerase II transcription factor B subunit 5) (Q9HDW3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- General transcription and DNA repair factor IIH subunit tfb2
- Transcription initiation factor IIE subunit beta
- Transcription initiation factor IIE subunit alpha
- General transcription and DNA repair factor IIH subunit tfb4
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription and DNA repair factor IIH subunit ssl1
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription and DNA repair factor IIH subunit tfb1
- RNA polymerase II transcription factor B subunit 3
- TATA-box-binding protein
Sequence:
MPRAQKGLLLVECDPTVKQLILNMDEQSPGIVIEEIDEERLLVNESRLEQVKAELERRLEENTYQVEE
Protein: TSC22 domain family protein 2 (E9Q7M2)
Organism: Mus musculus (Mouse)
Interaction partners:
- Nuclear receptor-binding protein
Sequence:
MSKMPAKKKSCFQITSVTTAQVATSITEDTESLDDPDESRTEDVSSEIFDVSRATDYGPEEVCERSSSEETLNNVGDAETPGTVSPNLILDGQLAAASAAPANGGGGGVSARSVAGALAQTLAAAAASVSTPGPSSATPSQPPATCSSRFRVIKLDHGSGEPYRRGRWTCMEYYERDSDSSVLTRSGDCIRHSNTLEQTAERDSGLGATGGSVVVVVASMQGAHGLDSGTDSSLTAVSQLPPSEKMSQPTLAQPQSFSVGQPQPPPPVGGAVAPSSASLPPFPGAATGPQPMTAAVQPTQLQGAVAGGALPGPVGQGLPPPPNVNLAQPVALAAQPGPAGGSSLSQQFAYPQPQIPPGHLLPMQPSGQSEYLPPHVALQPPSPAQPLSTSASATSASAASFPLGSGQSVSSLGAQMMGASAQPSEAVAPGPVPVGQAAPCQPAGVAPAALGGVVQPGSGLTGVGQPQPVQPPQQMGGSGQLPAVPGGPHTVVPGVPNVPAAVPVPSVPSVPTTSVTMPNVPAPLGQSQQLSSHTPVSRSSSVIQQVGSPLAQGTHSAPTSLPQSDLSQFQTQTQPLVGQVDDTRRKSEPLPQAPLSLIAESKPVVKPPVADALTNPLQLTPMNSLATSVFSIAIPVDGDEDRNPSTAFYQAFHLNTCQESKSLWDSASGGGVVAIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELVERNSLLERENALLKSLSNNDQLSQLPAQQANPGSTSQQQAMIAQPPQPTQPPQQPNVSSA
Protein: Protein gar2 (P41891)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Helps the assembly of pre-ribosomal particles containing 18S rRNA.
Subcellular location: Nucleus, nucleolus.
Interaction partners:
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit gar1
- H/ACA ribonucleoprotein complex subunit cbf5
- Protein pxr1
- Pre-rRNA-processing protein esf2
- Nucleolar protein 58
- ATP-dependent RNA helicase dbp2
- Ribosome production factor 2 homolog
- GTPase grn1
Sequence:
MAKKDKTSVKKSVKETASKKGAIEKPSKSKKITKEAAKEIAKQSSKTDVSPKKSKKEAKRASSPEPSKKSVKKQKKSKKKEESSSESESESSSSESESSSSESESSSSESESSSSESSSSESEEEVIVKTEEKKESSSESSSSSESEEEEEAVVKIEEKKESSSDSSSESSSSESESESSSSESEEEEEVVEKTEEKKEGSSESSSDSESSSDSSSESGDSDSSSDSESESSSEDEKKRKAEPASEERPAKITKPSQDSNETCTVFVGRLSWNVDDQWLGQEFEEYGTIVGARVIMDGQSGRSKGYGYVDFETPEAAKAAVAANGTKEIDGRMVNLDLSNPRPANPQPYAQQRAGNFGDQLSEPSDTVFVGNLSFNATEDDLSTAFGGCGDIQSIRLPTDPQSGRLKGFGYVTFSDIDSAKKCVEMNGHFIAGRPCRLDFSTPRTGGGSRGGRGGFGGRGGFGGRGGFGGGRGRGRGGARSGNPNRGSVAPFSGNKVTFD
Protein: Orfb protein (Q38011)
Organism: Streptococcus phage Cp-1 (Bacteriophage Cp-1)
Interaction partners:
Sequence:
MIAQFQIILEGVTPLKIQCIDKFPDDKLETEKEVYRNRGYKEVHENYFKNERLNTLIIFEEVKNLKYSKYSHYCLKSAFERYVQGRDGY
Protein: Triokinase/FMN cyclase (Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)) [Includes: ATP-dependent dihydroxyacetone kinase (DHA kinase) (EC 2.7.1.28) (EC 2.7.1.29) (Glycerone kinase) (Triokinase) (Triose kinase); FAD-AMP lyase (cyclizing) (EC 4.6.1.15) (FAD-AMP lyase (cyclic FMN forming)) (FMN cyclase)] (Q4KLZ6)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response (By similarity).
Interaction partners:
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Triosephosphate isomerase.
- Triosephosphate isomerase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase B
- Interferon-induced helicase C domain-containing protein 1
- Fructose-bisphosphate aldolase A
- Fructose-bisphosphate aldolase C
- Fructose-bisphosphate aldolase
- Sorbitol dehydrogenase
Sequence:
MSSKKMVNSVEGCAGDALAGFVACNPDLQLLQGYRVALRSDLDSLKGRVALLSGGGSGHEPAHAGFIGKGMLTGVIAGAVFASPAVGSILAAIRAVAQAGTAGTLLIVKNYTGDRLNFGLAMEQAKAEGISVEMVVIEDDSAFTVLKKAGRRGLCGTILIHKVAGALAEEGMGLEEITKKVSVIAKAIGTLGVSLSPCSVPGTKPTFELAADEMELGLGIHGEAGVRRIKLVPVDQIVTLMLDHMTDTSNISHVPVKSGSSVVLMVNNLGGLSFLELGIIADAAIRLLEGRGVKVARALVGTFMSALEMRGVSLTLMLVDEPLLKLIDAETNAKAWPHMSKVSVTGRNRIRAAPTEPAEAPEATAAGGVASKQMTLVLDRISTTLIGLEEHLNALDRAAGDGDCGSTHSRAAKAIQGWLKEGPTPASPAQVLSKLSVLLLEKMGGSSGALYGLFLTAAAQPLKANTDLPAWSAAMDAGLKAMQKYGKAAPGDRTMLDSLWAAAQELQAWKSPGASLLPVLTKAVKSAEAAAEATKNMEAGAGRASYISSAQLDQPDPGAVAAAAIFRAILEVLQTKAA
Protein: Tachykinin-related peptide 3 (TKRP-3) (P86577)
Organism: Nezara viridula (Southern green stink bug) (Cimex viridulus)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
GPSSGFFGMR
Protein: Hyaluronidase PH-20 (Hyal-PH20) (EC 3.2.1.35) (Hyaluronoglucosaminidase PH-20) (Sperm adhesion molecule 1) (Sperm surface protein PH-20) (P48794)
Organism: Mus musculus (Mouse)
Function: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Alpha-L-iduronidase
- Beta-glucuronidase
- Arylsulfatase B
- Heat shock-related 70 kDa protein 2
- Zona pellucida sperm-binding protein 3 receptor
- Disintegrin and metalloproteinase domain-containing protein 2
- Zonadhesin
Sequence:
MGELRFKHLFWGSFVESGGTFQTVLIFLLIPCSLTVDYRAAPILSNTTFLWIWNVPTERCVGNVNDPIDLSFFSLIGSPRKTATGQPVTLFYVDRLGLYPHIDANQAEHYGGIPQRGDYQAHLRKAKTDIEHYIPDDKLGLAIIDWEEWRPTWLRNWKPKDNYRNKSIELVQSTNPGLSITEATQKAIQQFEEAGRKFMEGTLHLGKFLRPNQLWGYYLFPDCYNNKFQDPKYDGQCPAVEKKRNDNLKWLWKASTGLYPSVYLKKDLKSNRQATLYVRYRVVEAIRVSKVGNASDPVPIFVYIRLVFTDRTSEYLLEDDLVNTIGEIVALGTSGIIIWDAMSLAQRAAGCPILHKYMQTTLNPYIVNVTLAAKMCSQTLCNEKGMCSRRKESSDVYLHLNPSHFDIMLTETGKYEVLGNPRVGDLEYFSEHFKCSCFSRMTCKETSDVKNVQDVNVCVGDNVCIKAKVEPNPAFYLLPGKSLLFMTTLGHVLYHLPQDIFVFPRKTLVSTP
Protein: Malic enzyme (Q9NIW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYSILRRCSGIRKTFGPTPVYPTANNSQSPSSYSRGKERELGCYTKRNSNSNNNNSHERESQSCCSSRVCKNHTTTTTTTLEYELSNFAKLTTRITTQSAAEVDTSPHTDTETHRDRDSNPGNIALATDLELPKGLPLSLSSRHHWNQLQSSLHALHHQQQQQQQQLRSYSSTSETNLEDKMSKPDSKLDKYAQRDRLGLWGTGDNEVVGSLSGFTRLLDKRYSKGLAFTHEERQQLGIHGMLPYVVREPSEQVEHCRALLARLDQDLDKYMYLISLSERNERLFYNVLSSDIGYMMPLVYTPTVGLACQRYSLIHQNAKGMFISIKDKGHIYDVLKNWPETDVRAIVVTDGERILGLGDLGANGMGIPVGKLSLYTALAGIKPSQCLPITLDVGTNTESILEDPLYIGLRERRATGDLYDEFIDEFMHACVRRFGQNCLIQFEDFANANAFRLLSKYRDSFCTFNDDIQGTASVAVAGLLASLKIKKTQLKDNTLLFLGAGEAALGIANLCLMAMKVEGLTEEEAKARIWMVDSRGVITRDRPKGGLTEHKLHFAQLHEPIDTLAEAVRKVRPNVLIGAAAQGGAFNQEILELMADINETPIIFALSNPTSKAECTAEEAYTYTKGRCIFASGSPFAPVTYNNKKFYPGQGNNSYIFPGVALGVLCAGMLNIPEQVFLVAAERLAELVSKDDLAKGSLYPPLSSIVSCSMAIAERIVEYAYKNGLATVRPEPVNKLAFIKAQMYDLDYPRSVPATYKM