wanglab/gogpt-training-data huggingface dataset:
Protein: Polyhomeotic-like protein 3 (Q8CHP6)
Organism: Mus musculus (Mouse)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Chromobox protein homolog 8
- Chromobox protein homolog 2
- Polycomb group RING finger protein 2
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- E3 SUMO-protein ligase CBX4
- Polycomb complex protein BMI-1
- Chromobox protein homolog 7
- Polycomb group RING finger protein 6
- Chromobox protein homolog 6
Sequence:
MDSEPSSGTSVSTTASSTTTTTITTSSSRMQQPQISVYSGSDRHAVQVIQQALHRPPSSAAQYLQQMYAAQQQHLMLHTAALQQQHLSSSQLQSLAAVQASLSSGRPSTSPTGSVTQQSSMSQTSILSASPAPAQLMNRSQTSSSTSGSITQQTMLLGSTSPTLTASQAQMYLRAQMLIFTPATTVAAVQSDIPVVSSSPSPSCQSAAAQVQNLTLRSQKLGVLSSSQNGSPKSAGQTQSLTICHNKTTVTSSKISQRDPSPESKKGGSPGLESRSTAVTRTSSIHQLIAPASYSPIQPHSLIKHQQIPLHSPPPKVSHHQLLLQQQQQQIQPITLQSPSQDPPPSQHCIPLPNHGLSPAPSNAQPQHCSPVQSHPPPLTVSPNQAQSAQQSVVVSPPPPHSPSQSPTIIIHPQALIQPHPLVSSALQTGPNLQQAAADQVQSTAQLNLPSHLPLPASPVVHIGPVQQSALVSPGQQMVSPTSHQQYSALQSSPIPIATPPQMSASPPAQLPPLPLQSMQSLQVQPEILSQGQVLVQNALVSEEELPAAEALVQLPFQTLPPPQTVAVNLQVQPPAPVDPPVVYQVEDVCEEEMPEESDECARMDRTPPPPTLSPAAVTVGRGEDLTSEHPLLEQVELPAVASVSASVIKSPSDPTHASAPAPPLLIPAASTRSSSTSLASSTPSLENKPPQAIVKPQILTHVIEGFVIQEGLEPFPVSRSSLLIEQPVKKRPLLDNQVVNSVCVQPELQNNTKHADNSSDTEIEDMMAEETLEEMDSELLKCEFCGKMGYPNEFLRSKRFCTMSCAKRYNVSCSKKFALSRWNRKPDNQSLGHRGRRPSGPEGAAREHILRQLPITYPSAEEDVASHEDPVPSAMTTRLRRQSERERERELRDVRIRKMPENSDLLPVAQTEPSIWTVDDVWAFIHSLPGCQDVADEFRAQEIDGQALLLLKEDHLMSAMNMKLGPALKICARINSLKDS
Protein: Type IV secretion system protein virB4 (Q2NKG6)
Organism: Escherichia coli
Interaction partners:
Sequence:
MGAIESRKLLASETPVGQFIPYSHHVTDTIISTKNAEYLSVWKIDGRSHQSASEADVFQWIRELNNTLRGISSANLSLWTHIVRRRVYEYPDAEFDNVFCRQLDEKYRESFTGYNLMVNDLYLTVVYRPVSDKVLSFFAKRERETPDQKKHRQESCIKALEDINRTLGQSFKRYGAELLSVYEKGGHAFSAPLEFLARLVNGEHIPMPICRDRFSDYMAVNRPMFSKWGEVGELRSLTGLRRFGMLEIREYDDATEPGQLNVLLESDYEFVLTHSFSVLSRPAAKEYLQRHQKNLIDARDVATDQIEEIDEALNQLISGHFVMGEHHCTLTVYGETVQQVRDNLAHASAAMLDVAVLPKPVDLALEAGYWAQLPANWQWRPRPAPITSLNFLSFSPFHNFMSGKPTGNPWGPAVTILKTVSGTPLYFNFHASKEEEDATDKRLLGNTMLIGQSSSGKTVLLGFLLAQAQKFKPTIVAFDKDRGMEISIRAMGGRYLPLKTGEPSGFNPFHAPADARKPDFPQTVREEARGCRWRGHAPGRGRNRPGHYAMMSDSIDKSLRRLSLLLQFLPNPRSDDMDARPTVHARLVKWCEGGDYGWLFDNPTDALDLSTHQIYGFDITEFLDNPEARTPVMMYLLYRTESMIDGRRFMYVFDEFWKPLQDEYFEDLAKNKQKTIRKQNGIFVFATQEPSDALESNIAKTLIQQCATYIFLANPKADYEDYTQGFKLTDSEFELVRGLGEFSRRFLIKQGDQSALAEMNLGKFRTIVDGETVERDFDDELLVLSGTPDNAEIAESIIAEVGDSPAVWLPIFLDRVKAERSDV
Protein: Evasin P1086 (A0A0K8RK34)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL10, CXCL12 and CXCL13.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAFNVITFLQLAVFVVILFNINLHSASAGSKGQRASQVSETSITAEFCDTSCTQGTDKTWSGCSGDCFCVHVGNDTEGRCMRWDGDYPSAEEEE
Protein: Heat shock protein SSA2 (SSA subfamily protein 2) (P46587)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16720580, ECO:0000269|PubMed:8757872}. Secreted, cell wall {ECO:0000269|PubMed:12782322, ECO:0000269|PubMed:16720580, ECO:0000269|PubMed:17999963, ECO:0000269|PubMed:8757872}.
Interaction partners:
- Hsp90 cochaperone
- Type I HSP40 co-chaperone
- Chaperone ATPase
- Hsp70 chaperone Ssb
- Heat shock protein HSP70
- Fgr32p
- Heat shock protein 90 homolog
- Type II HSP40 co-chaperone
- Zuotin
- Heat shock protein 60, mitochondrial
Sequence:
MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRKFDDHEVQGDIKHFPFKVVDKASKPMIQVEYKGETKTFSPEEISSMILGKMKETAEGFLGTTVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKKSEAEKNVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNFFIQEFKRKNKKDISTNQRALRRLRTACERAKRTLSSSAQTSIEIDSLYEGIDFYTSITRARFEELCADLFRSTLEPVDKVLSDAKIDKSKVDEIVLVGGSTRIPKVQKLVSDYFNGKEPNRSINPDEAVAYGAAVQAAILSGDTSSKTQDLLLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSETFSTYADNQPGVLIQVFEGERAQTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIEKMVSEAEKFKEEDEKEASRVQAKNQLESYAYSLKNTLGEEQFKSKLDASEIEEVTKAADETISWLDANQTATQEEFADQQKELESKANPIMTKAYQAGATPSGAAGAAPGGFPGGAAPEPSNDGPTVEEVD
Protein: RING finger protein 207 (Q6ZRF8)
Organism: Homo sapiens (Human)
Function: Plays a role in cardiac repolarization possibly by stabilizing membrane expression of the potassium channel KCNH2/HERG, or by assisting its synthesis, folding or export from the endoplasmic reticulum, in a heat shock protein-dependent manner.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25281747}. Note=Probably located in the endoplasmic reticulum and/or possibly the cis-Golgi apparatus. {ECO:0000269|PubMed:25281747}.
Interaction partners:
- Voltage-gated inwardly rectifying potassium channel KCNH2
Sequence:
MSGAIFGPLEGPSSLDAPSIHPLVCPLCHVQYERPCLLDCFHDFCAGCLRGRATDGRLTCPLCQHQTVLKGPSGLPPVDRLLQFLVDSSGDGVEAVRCANCDLECSEQDVETTYFCNTCGQPLCARCRDETHRARMFARHDIVALGQRSRDVPQKCTLHAEPYLLFSTDKKLLLCIRCFRDMQKESRAHCVDLESAYVQGCERLEQAVLAVKALQTATREAIALLQAMVEEVRHSAAEEEDAIHALFGSMQDRLAERKALLLQAVQSQYEEKDKAFKEQLSHLATLLPTLQVHLVICSSFLSLANKAEFLDLGYELMERLQGIVTRPHHLRPIQSSKIASDHRAEFARCLEPLLLLGPRRVAAAASGANTLAGGLGPKALTGPHCPSPVGKMSGSPVQKPTLHRSISTKVLLAEGENTPFAEHCRHYEDSYRHLQAEMQSLKDQVQELHRDLTKHHSLIKAEIMGDVLHKSLQLDVQIASEHASLEGMRVVFQEIWEEAYQRVANEQEIYEAQLHDLLQLRQENAYLTTITKQITPYVRSIAKVKERLEPRFQAPVDEQSESLQNTHDDSRNNAASARNNPGSVPEKREKTSEPKGNSWAPNGLSEEPLLKNMDHHRSKQKNGGDVPTWREHPT
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B) (Q9VL46)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLPTWLTAAYLQPRLRAYCQDDRLQVLRIWAKPATGKGENFVGVMTRIYVDYQLGDGSVVNKTYIVKQALSAEVPQAEVFFEYELYTREMDMYEFILPKLKELLQEAGLDQKLTADAITVDREYNTMILEDLAPYKFVNADRVKQLDMAHTELTLEMLAKFHAASIVLQERHPNLLTKCFYTHFFSRDKKAYSVVFAGLFKAFLRFIDGQPNLKEAYGDKLHKLRTHIMEYGARAYDVGESDLKTLNHGDCWTTNIMFQYDDAGEPRSVVAIDFQFSNCTSPTIDLHYFFTTSLREEVGDKESELVEHHYKALKANLEKFSYKGSLPTLQEYRLQFERRRFMSLLAHMFKPCMIYNGSEETSDFSSLYAESPEGLRYQKSVYASEAVIRSATKLLAILDAKGLLELQ
Protein: Tropomyosin 3 (Tropomyosin alpha-3 chain isoform X3) (A0A2R8Q650)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEAVKKKMMMLKLDKENALDQAEQAETDRKAAEERSKQHEDELIQMQKKLKGTEDELDKYSEALKDAQEKLEISEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELNSF
Protein: Disks large-associated protein 1 (DAP-1) (Guanylate kinase-associated protein) (PSD-95/SAP90-binding protein 1) (SAP90/PSD-95-associated protein 1) (SAPAP1) (Q9D415)
Organism: Mus musculus (Mouse)
Function: Part of the postsynaptic scaffold in neuronal cells.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000269|PubMed:24153177}.
Interaction partners:
- Disks large homolog 4
- SH3 and multiple ankyrin repeat domains protein 3
- SH3 and multiple ankyrin repeat domains protein 1
- Disks large homolog 2
- SH3 and multiple ankyrin repeat domains protein 2
- Disks large homolog 3
- Glutamate receptor ionotropic, NMDA 2B
- Ras/Rap GTPase-activating protein SynGAP
- Glutamate receptor ionotropic, NMDA 1
- Neuroligin-1
Sequence:
MKGLSGSRSHHHGITCEAACDSLSHHSDHKPYLLSPVDHHPADHPYYTQRNSFQAECVGPFSDPLASSTFPRRHYTSQQELKDESALVPRTLATKANRLPTNLLDQFERQLPLSRDGYHTLQYKRTAVEHRSDSPGRIRHLVHSVQKLFTKSHSLEGPSKGSVNGGKASPDESQTLRYGKRSKSKERRSESKARSNASNASPTSPSWWSSDDNLDGDMCLYHTPSGVMTMGRCPDRSASQYFMEAYNTISEQAVKASRSNNDIKCSTCANLPVTLDAPLLKKSAWSSTLTVSRAREVYQKASVNMDQAMVKSEACQQERSCQYLQVPQDEWSGYTPRGKDDEIPCRRMRSGSYIKAMGDEDSGDSDTSPKPSPKVAARRESYLKATQPSLTELTTLKISNEHSPKLQIRSHSYLRAVSEVSINRSLDSLDPAGLLTSPKFRSRNESYMRAMSTISQVSEMEVNGQFESVCESVFSELESQAVEALDLPLPGCFRMRSHSYVRAIEKGCSQDDECVSLRSSSPPRTTTTVRTIQSSTGVIKLSSAVEVSSCITTYKKTPPPVPPRTTTKPFISITAQSSTESAQDAYMDGQGQRGDMISQSGLSNSTESLDSMKALTAAIEAANAQIHGPASQHMGSNAAAVTTTTTIATVTTEDRKKDFKKNRCLSIGIQVDDAEEPEKMAESKTSNKFQSVGVQVEEEKCFRRFTRSNSVTTAVQADLDFHDNLENSLESIEDNSCPGPMARQFSRDASTSTVSIQGSGNHYHACAADDDFDTDFDPSILPPPDPWIDSITEDPLEAVQRSVCHRDGHWFLKLLQAERDRMEGWCKLMEREERENNLPEDILGKIRTAVGSAQLLMAQKFYQFRELCEENLNPNAHPRPTSQDLAGFWDMLQLSIENISMKFDELHQLKANNWKQMDPLDKKERRAPPPVPKKPAKGPAPLIRERSLESSQRQEARKRLMAAKRAASVRQNSATESAESIEIYIPEAQTRL
Protein: Phosphatidylcholine:ceramide cholinephosphotransferase 4 (EC 2.7.8.27) (Ethanolamine-phosphorylceramide synthase) (EPC synthase) (Sphingolipid synthase) (Sphingomyelin synthase) (SM synthase) (Q38E56)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:B3A0M2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:B3A0M2}.
Interaction partners:
- sphingolipid 4-desaturase
- Phosphatidic acid phosphatase, putative
- Phosphatidylinositol:ceramide inositolphosphotransferase
- Phosphatidylcholine:ceramide cholinephosphotransferase 3
- Phosphatidic acid phosphatase alpha, putative
- serine C-palmitoyltransferase
- Serine-palmitoyl-CoA transferase, putative
Sequence:
MISYPFFSLSPPGLVPPPMAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFELLTKVPGMYVLADCCIGFLNILSVFTAFKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNVHTIAWIRFITSYALLLLFRSVVIVMTSLPAPDDLCQDPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFGYYCIVASRFHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWLPCCGANSREMTEDSQPVMVAFKSEELDEMNGVLEGRQKKHGGVGDGEALMFKCGAYV
Protein: F-box/WD repeat-containing protein 7 (B7ZDC8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- S-phase kinase-associated protein 1
- S-phase kinase-associated protein 2
- F-box and WD repeat domain-containing 11-B
- E3 ubiquitin-protein ligase RBX1
- F-box only protein 2
- F-box protein 4.
- Cullin 1b
- Cullin-1
- E3 ubiquitin-protein ligase SHPRH isoform X1
- Cullin 3
Sequence:
MGFYGTLKMIFYKMKRKLDHGPEVRSFTTGKKPCPSPTGQQYPATFGDLRAVNGQVPQRRRITSIQPPTGLQEWLRTFQSWSGPEKLLALDELIDSCEPTQVKHMMQVIEPQFQRDFISLLPRELALHVLSFLEPKDLLQAAQTCRYWRILAEDNLLWKEKCKEEGIDEPLHIKRRKVIKPGFTHSPWKSAYIRQHRIDTNWRRGDLKSPKVLKGHDDHVITCLQFCGNRIVSGSDDNTLKVWSAVTGKCLRTLVGHTGGVWSSQMRDNIIISGSTDRTLKVWNAETGECIHTLYGHTSTVRCMHLHEKRVVSGSRDATLRVWDIETGQCLHVLMGHVAAVRCVQYDGRRVVSGAYDFMVKVWDPETETCLHTLQGHTNRVYSLQFDGIHVVSGSLDTSIRVWDVETGNCIHTLTGHQSLTSGMELKDNILVSGNADSTVKIWDIKTGQCLQTLQGPHKHQSAVTCLQFNKNFVITSSDDGTVKLWDLRTGEFIRNLVTLESGGSGGVVWRIRASNTKLVCAVGSRNGTEETKLLVLDFDVDMK
Protein: FAD-dependent urate hydroxylase (EC 1.14.13.113) (FAD-dependent urate oxidase) (A6T923)
Organism: Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Function: Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU).
Interaction partners:
- Acetyl-coenzyme A synthetase
- 5-hydroxyisourate hydrolase
- 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
Sequence:
MKAIVIGAGIGGLSAAVALKQSGIDCDVYEAVKEIKPVGAAISVWPNGVKCMAHLGMGDIMETFGGPLRRMAYRDFRSGENMTQFSLAPLIERTGSRPCPVSRAELQREMLDYWGRDSVQFGKRVTRCEEDADGVTVWFTDGSSASGDLLIAADGSHSALRPWVLGFTPQRRYAGYVNWNGLVEIDEALAPGDQWTTFVGEGKRVSLMPVSAGRFYFFFDVPLPAGLAEDRDTLRADLSRYFAGWAPPVQKLIAALDPQTTNRIEIHDIEPFSRLVRGRVALLGDAGHSTTPDIGQGGCAAMEDAVVLGAVFRQTRDIAAALREYEAQRCDRVRDLVLKARKRCDITHGKDMQLTEAWYQELREETGERIINGMCDTILSGPLG
Protein: BHLH domain-containing protein (Q8BWA4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVPTQKVPSLQHFRKTEKEVIGGLCSLANIPLTPETQRDQERRIRREIANSNERRRMQSINAGFQSLKTLIPHTDGEKLSKAAILQQTAEYIFSLEQEKTRLLQQNTQLKRFIQELSGSSPKRRRAEDKDEGIGSPDIWEDEKAEDLRREMIELRQQLDKERSVRMMLEEQVRSLEAHMYPEKLKVIAQQVQLQQQQEQVRLLHQEKLEREQQHLRTQLLPPPAPTHHPTVIVPAPAPPSSHHINVVTMGPSSVINSVSTSRQNLDTIVQAIQHIEGTQDKQELEEEQRRAVIVKSVRSCPDAHTSDTASDSEASDSDAMDQSREEPLGDGELP
Protein: WAS protein family homolog DDB_G0292878 (Q54CK9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts as a nucleation-promoting factor by activating the Arp2/3 complex to induce actin polymerization.
Interaction partners:
- WASH complex subunit 5
- WASH complex subunit 3
- WASH complex subunit 2
- WASH complex subunit 4
- Uncharacterized protein
- Apoptosis inhibitor 5 homolog
- Maestro heat-like repeat-containing protein family member 1
Sequence:
MTTQIYQVPVVSNGLRETESILQIVDSLEKLEKVFNDMYSTISARVSHEKSRIDNVANRLNNAQHKVNQIVGSKQAITVFSSAKYPADKKWGDYVPIYSGKHKLPFKPSHYHGLNSEDSPIKKRPEDSYLDVNDLVFIEKSIDTTSKEVEVKEGLGRIPAQIPSVSNLLLFNTQENPYKKYSNTLDNLSGGDGGEDDYTIFGDQLSKKKRLGDAPVTVKDGDSRIDAENVKIGYEPGTFEIPVYNFPSILPLPNVAENITWAAESQSIAPSQKATLNLLPTYDNSNSGSAPVNQSSGGDNNVNNNNNNNNSNNSTGIMQPPQPTNAPPPPPPPPQSANAPPPPPPPPVSAPPPFNPPSVNSNNDDDDDDDDDNGGGGGPGGAIGDLLADIRRGHKNRLKKADVGGDNGDGEDNKPPPVSDGGGGLMGDLFKKLALRRQSIATTKSTKKQSKSKKEDTDDQDGESDTDSSEWE
Protein: Forkhead box protein N1 (Winged helix nude b protein) (Q7ZTC0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MSSEPQGLSFLSISSSSSSPSPSPGQLQSFDPLESPCFQMPESQCHQSNGGEEFVPYSQRESDPYSQKSAERFRRHSVDGSPVGRDCDLTENSHYHPYRRQCSEGAISEGQPFSCVRRAGLAREIASADGLEEQSSWTTLGTDVETTSIMGTRRPYSEPQESSEEPPGYTTVNHQSYSAISPLQHQYYPSRGIDTVSHYYNQSLSTQTSQDSSPQPLYPKPVYSYSILIFLALRNSKTGSLPVSEIYSFMTEHFPYFKTAPDGWKNSVRHNLSLNKCFEKVENKNGNSSRKGCLWALNPAKVEKMQEELHKWRRKDPLTVRRSMARPEELERLLGERPEKLKSHFSLPSSHTHSQPFRVNMHPAYGHQPVHENRILNQKALYNPLTSQNAVLPPPYISPDPLAFQYYSPATHQPSVGHPSSPRTGSLDSPLPAHTPPSYSTALQAGHSGTASMQELLLDGEINNDVDALNPSLTDLQLHGSLWEELRNDSLAPDSLIVMDSASSLAQLSPPPARDSAGVCAETEDGVQGSISELYLSSFYTTAFTSAENMPGLISSQANTAIPLL
Protein: C3H1-type domain-containing protein (O02289)
Organism: Caenorhabditis elegans
Interaction partners:
- Mitogen-activated protein kinase mpk-1
- CCCH-type zinc finger protein oma-2
- Cytoplasmic polyadenylation element-binding protein 3
- Inositol polyphosphate-4-phosphatase
Sequence:
MLYQPSLLKSRLTPAPPGFSFQPQPLLNSDMDPVRNLESLGNYTVYQDSSQCFWQHQNFTSNREHNPALRKTKICDHWRRSGSCSYGDACWYAHGEDDLRKVVRIDRSNEEENERPATAEIQKSPTKRASTNVKGLTVNIPSNTAFKEQNSSMPLSPAQERWISMSIGAVPPPTSSAAEKDAISSLSKNGVEQEQEKKHEICSRDDDIDDYGFLSPNPFPYPQQSMFSAGFPSHGHHQRSSNRATQGVPSQQFGGPVNIPGQDPNRLGSGAYHIPPQHQRSRSNVRTSREVGGPPPQFQQAIWNVAGEIYQRQKDIEIGGQRVGPNDRQPTQQKNSEMDRLLSKLKMKDLNYLRFMIERGYINERDVSRQTSSDQMSNGHHFNAPMTPPYHPRLAGNEPNTSDCHYHGTGNRLSNFMPGRHRPPHQHPIHHHHQSQHQLHQHQQYLHHAAQQYRYSHQQGPQHPFAALLSPPEISESLLPPDDSFSIWLEPKPKKQSGAMTRTRGAATINESSSAASLLTKMDALRSDKYPITDEEMMMANDFVRQGDRDDKLSSSESSSPVVMSLMELLSNENLLDQVATEKPKCSMFDFDTLKIAETLKEPLQSSECSTTTSSKMTCSPMFFFVDEKTPNYDGSGSKSLFTPSSSAGQTPSFLEPCDFFAATGSCPFGDACHQSHSI
Protein: Integrin alpha 3 variant B (Integrin subunit alpha 3) (I4DUB5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MGPGPRRVPRDPGWMLRALALMVAASGRVAFAFNLDTKFLVVKEAVNPGSLFGYSVALHRQTERQQRYLLLAGAPRDLAVDDDYTNRTGAVYLCPLTALKNDCERMDISEKSDPDHHIIEDMWLGVTVASQGPAGRVLVCAHRYTKVLWSGLEDQRRMVGKCYVRGNDLQLDPGDDWQTYHNEMCNSNTDYLQTGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKDWDLSEYSYRGSEDQGNLYIGYTMQVGSAILHPSEITLVTGAPRHQHMGAVFLLKQESGGDLQRRQVLKGTQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAVYVFMNQAGTSFPDQPSLLLHGPSRSAFGISVASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSGGLLKQPQQIIHGETLGLPGLATFGYSLSGKMDVDENLYPDLLVGSLSDHIVLLRARPVINILHRTLVARPAVLDPSLCTVTSCVQVELCFAYNQSAGNPNYRRNITLAYTVEADRDRRPPRLRFARSQSSVFHGFFSMPETHCQTLELLLMDNVRDKLRPIVITMNYSLPLRMPDRLKLGLRSLDAYPVLNQAQAMENHTEVHFQKECGPDNKCDSNLQMRAAFVSEQLQPLSRLQYSRDTKKLFLSINVTNSPSRQRAGEDAHEALLTLEVSSALLLSSVRPAGTCQANETNTVCELGNPFKRNQRMELLIAFEVTGVTLHTRDLRAHLQLSTSSHQDNLQPMFLTLQVDYTLQASLSLMNHRLQSFFSGTVMGEAAMKTVKDVGSPLKYEFQVSPVGDGLAALGTLVLGLEWPYEVTNGKWLLYPTEITIHSNGSWPCQPHGNLVNPLNLTLSDPGVKPLSPQRRRRQLDPGGDQGPPPVTLAAAKKAKSETVLTCSNGRARCVWLECPLPDASNITNVTVKARVWNSTFIEDYKDFDRVRVDGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVGAGLLLLGLIIILLWKCDFFKPTRYYRIMPKYHAVRIREEDRYPPPGSTLPTKKHWVTSWQIRDRYY
Protein: Transmembrane anterior posterior transformation protein 1 (Q4VBD2)
Organism: Mus musculus (Mouse)
Function: Plays a role in primary cilia formation (By similarity). May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). May be involved in cartilage and bone development (By similarity). May play a role in the differentiation of cranial neural crest cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6NXT6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6NXT6}. Membrane {ECO:0000250|UniProtKB:Q6NXT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6NXT6}.
Interaction partners:
- Cleavage stimulation factor subunit 1
Sequence:
MAGVCDAAAPGEGGGGGADGPERTGRGEAEQPGGGGHGPAPQHTETLGFYESDRRREKRRGRAELSLLRFLSAELTRGYFLEHNEAKYTERRERVYTCMRIPRELEKLMFFGIFLCLDAFLYVFTLLPLRVFLALFRLLTLPCYGLRDRRLLQPAQVCDILKGVILVICYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYVLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDIVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVARRMGFIPLPLAVLLIRVVTSSIKVQGILSYACVILFYFGLISLKILNSIVLLGKSCQYVKEAKMEEKLFNPPPASTPGKPSSKSQSKGKPSQGLSTEENLSASVTSQPGHQKENVIPLLVTSNSDQFLTTPDGDEKDITQENSELKHRSSKKDLLEIDRFTICGNRID
Protein: At1g70990 (Proline-rich family protein) (A0JQ68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MHPLTKPPHQIFNSFYVQPKNLPKPLFIRFSRHITTLTMPEKTRRTKALAATLLTTVVFLTFPMIINASDSSTNRKLEEDPIKCTPCLQNIPPPSPPPPSPPPPSQACPPPPLPPSPPKKSYCPPPPSTYIYMTGPPGELYPIDQQFGAAVTKSFTVVKISGLIAFGVMSFLMIMN
Protein: Aldose 1-epimerase (A0A0H2UNW4)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MSYEQEFMKEFEAWVNTQIMINDMAHKESQKVYEEDQDERAKDAMIRYESRLDAYQFLLGKFENFKVGKGFHDLPEGLFGERNY
Protein: Histone deacetylase 15 (EC 3.5.1.98) (Q8GXJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (Probable). Represses chlorophyll biosynthesis and photosynthesis in the dark. Is recruited by PIF3 to the promoters of chlorophyll biosynthetic and photosynthetic genes, and represses their transcription by histone deacetylation. Involved in the repression of hypocotyl cell elongation to promote photomorphogenesis. Is recruited by HY5 to the promoters of a subset of cell wall organization and auxin signaling-related genes, and represses gene expression by decreasing the levels of histone H4 acetylation in a light-dependent manner. Promotes abscisic acid (ABA) signaling. Is recruited by MYB96 to the promoters of a subset of Rho GTPase (ROP) genes, which repress ABA signaling at the early stages of signal transduction. Represses ROP expression by removing acetyl groups of histone H3 and H4 from the cognate regions, particularly in the presence of ABA. Represses the plant response to elevated ambient temperature by directly repressing warm temperature-responsive genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:22363501, ECO:0000269|PubMed:23548744, ECO:0000269|PubMed:31061103}. Cytoplasm {ECO:0000269|PubMed:22363501}. Note=Shuttles in and out of the nucleus upon light exposure. In the absence of light, is exported out of the nucleus, and upon further exposition to light is imported to the nucleus. {ECO:0000269|PubMed:22363501}.
Interaction partners:
- Transcription factor PIF3
- Histone deacetylase 17
- Putative histone deacetylase 10
- NAD-dependent protein deacylase SRT2
- NAD-dependent protein deacetylase SRT1
- Transcription factor HY5
- Transcription factor MYB96
- High mobility group B protein 15
- High mobility group B protein 10
- High mobility group B protein 9
Sequence:
MVVETIERSCEGSKRRHVNGGDIAVPCSGEECSNGDINVAPGVSAKRARVSREMTFEDIYGADALLNDDDDEDDDCDWEPVQAPMEFVKWCCVNCTMSNPGDMVHCCICGEHKESGILRHGYLASPFFKDTGLIEVEEKYGGSSSATSSTAVGFDERMLLHSEFEVKAQPHPERPDRLRAIAASLATAGVFPGRCLPINAREITKQELQMVHTSEHVDAVDTTSQLLYSYFTSDTYANEYSARAARLAAGLCADLATDIFTGRVKNGFALVRPPGHHAGVRHAMGFCLHNNAAVAALVAQAAGAKKVLIVDWDVHHGNGTQEIFEQNKSVLYISLHRHEGGNFYPGTGAADEVGSNGGEGYCVNVPWSCGGVGDKDYIFAFQHVVLPIASAFSPDFVIISAGFDAARGDPLGCCDVTPAGYSRMTQMLGDLCGGKMLVILEGGYNLRSISASATAVIKVLLGENPENELPIATTPSVAGLQTVLDVLNIQLEFWPSLAISYSKLLSELEARLIENKKNQMKRKVVRVPTWWKWGRKKLLYNFLSARMISRSK
Protein: NAD kinase 2, mitochondrial (EC 2.7.1.23) (Mitochondrial NAD kinase) (NAD kinase domain-containing protein 1, mitochondrial) (Q8C5H8)
Organism: Mus musculus (Mouse)
Function: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor (By similarity).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- NAD kinase
- Glutamine-dependent NAD
- NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD-capped RNA hydrolase NUDT12
- NAD-dependent protein deacetylase sirtuin-3
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
Sequence:
MTCYRGFLLGSCRRVAGGRAALRGSGSGADGRRHLGHGQPRELAGGGSPADGGFRPSRVVVVAKTTRYEFEQQRYRYAELSEEDLKQLLALKGSSYSGLLERHHIHTKNVEHIIDSLRDEGIEVRLVKRREYDEETVRWADAVIAAGGDGTMLLAASKVLDRLKPVIGVNTDPERSEGHLCLPVRYTHSFPEALRRFSRGEFRWLWRQRIRLYLEGTGINPTPVDLHEQQLSLNQHSRAFNIERAHDERSEASGPQLLPVRALNEVFIGESLSSRMPYCWAVAVDNLRRDIPNLKGLASYYEISVDDGPWEKQKSSGLNLCTGTGSKAWSFNINRVAAQAVEDVLHIARRQGNLTLPLNKDLVEKVTNEYNESLLYSPEEPKILFSIREPIANRVFSSSRQRCFSSKVCVRSRCWDACMVVDGGTSFEFNDGAIASMMINKEDELRTVILEQ
Protein: Armadillo repeat-containing protein 1 (Q38A48)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSLNTELALAKRFHMLSKNYSNRPVIARRNTLPTLVRFIRSNDRETRHYSLSALLLLAQHEENVELLCLERGLVPGVYAVYKDADYDDPQLREIADQILNCLEPVLQGRDPRKASQTSVTPVGSSSDAVDSDPLNDSFSPSRRARAGRVLRGVGSDAIHTVLLDIPALDPNGGDNIEAIEDIFQTTRGVLSYSIFVENRQARLFVTCATQVVQQVLSDSGFESVVVRDDVVNQEMFGGGADGSAGLNSGGNRSNTSYYDGGSPQHRPSYLQSVANSIYQSALVLGGGSRNNDTLSARVNEQRTREQEGESTFGYISKTLSKWW