wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox-leucine zipper protein HAT5 (HD-ZIP protein ATHB-1) (Homeodomain transcription factor ATHB-1) (Homeodomain-leucine zipper protein HAT5) (HD-ZIP protein 5) (Q02283)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription activator involved in leaf development. Binds to the DNA sequence 5'-CAAT[AT]ATTG-3'.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox-DDT domain protein RLT3
- RING-H2 finger protein ATL22
Sequence:
MESNSFFFDPSASHGNSMFFLGNLNPVVQGGGARSMMNMEETSKRRPFFSSPEDLYDDDFYDDQLPEKKRRLTTEQVHLLEKSFETENKLEPERKTQLAKKLGLQPRQVAVWFQNRRARWKTKQLERDYDLLKSTYDQLLSNYDSIVMDNDKLRSEVTSLTEKLQGKQETANEPPGQVPEPNQLDPVYINAAAIKTEDRLSSGSVGSAVLDDDAPQLLDSCDSYFPSIVPIQDNSNASDHDNDRSCFADVFVPTTSPSHDHHGESLAFWGWP
Protein: Catenin delta-2 (Neural plakophilin-related ARM-repeat protein) (NPRAP) (Neurojungin) (O35927)
Organism: Mus musculus (Mouse)
Function: Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses. Involved in the regulation of canonical Wnt signaling (By similarity). It probably acts on beta-catenin turnover, facilitating beta-catenin interaction with GSK3B, phosphorylation, ubiquitination and degradation. May be involved in neuronal cell adhesion and tissue morphogenesis and integrity by regulating adhesion molecules. Functions as a transcriptional activator when bound to ZBTB33.
Subcellular location: Nucleus {ECO:0000269|PubMed:15282317}. Cell junction, adherens junction {ECO:0000269|PubMed:10753311}. Cell projection, dendrite {ECO:0000250|UniProtKB:O35116}. Perikaryon {ECO:0000250|UniProtKB:O35116}.
Interaction partners:
- Transcription factor 7-like 1
- Transcription factor 7-like 2
- Lymphoid enhancer-binding factor 1
- Transcription factor 7
- Catenin beta-1
- Presenilin-1
- Catenin alpha-2
Sequence:
MFARKQSGAAPFGAMPVPDQPPSASEKNSSLSPGLNTSNGDGSETETTSAILASVKEQELQFERLTRELEAERQIVASQLERCKLGSETGSMSSISSAGEQFHWQTQDGQKDIEDELTTGLELVDSCIRSLQESGILDPQDYSTSERPSLLSQSALQLNSKPEGSFQYPASYHSNQTLALGDTAPSQLPARSTQARAAGQSFSQGTTGRAGHLAGSEPAPPPPPPREPFAPSLGSAFHLPDAPPAAAALYYSSSTLPAPPRGGSPLTTTQGGSPTKLQRGGSAPEGAAYAAPRGSSPKQSPSRLAKSYSTSSPINIVVSSAGLSPIRVTSPPTVQSTISSSPIHQLSSTIGTYATLSPTKRLVHASEQYSKHSQELYATATLQRPGSLAAGSRASYSSQHGHLAPELRALQSPEHHIDPIYEDRVYQKPPMRSLSQSQGDPLPPAHTGTFRTSTAPSSPGVDSVPLQRTGSQHGPQNAAAATFQRASYAAGPASNYADPYRQLQYCASVDSPYSKSGPALPPEGTLARSPSIDSIQKDPREFGWRDPELPEVIQMLQHQFPSVQSNAAAYLQHLCFGDNKIKAEIRRQGGIQLLVDLLDHRMTEVHRSACGALRNLVYGKANDDNKIALKNCGGIPALVRLLRKTTDLEIRELVTGVLWNLSSCDALKMPIIQDALAVLTNAVIIPHSGWENSPLQDDRKIQLHSSQVLRNATGCLRNVSSAGEEARRRMRECDGLTDALLYVIQSALGSSEIDSKTVENCVCILRNLSYRLAAETSQGQHMGTDELDGLLCGETNGKDTESSGCWGKKKKKKKSQDQWDGVGPLPDCAEPPKGIQMLWHPSIVKPYLTLLSECSNPDTLEGAAGALQNLAAGSWKGWAEDVAGMAYALRSLPEGAPCLPQWSVYIRAAVRKEKGLPILVELLRIDNDRVVCAVATALRNMALDVRNKELIGKYAMRDLVHRLPGGNNSNNSGSKAMSDDTVTAVCCTLHEVITKNMENAKALRDAGGIEKLVGISKSKGDKHSPKVVKAASQVLNSMWQYRDLRSLYKKDGWSQYHFVASSSTIERDRQRPYSSSRTPSISPVRVSPNNRSASAPASPREMISLKERKTDYESAGNNATYHGTKGEHTSRKDTMTAQNTGVSTLYRNSYGAPAEDIKQNQVSTQPVPQEPSRKDYETYQPFPNSTRNYDESFFEDQVHHRPPASEYTMHLGLKSTGNYVDFYSAARPYSELNYETSHYPASPDSWV
Protein: Protein pangolin, isoforms A/H/I/S (dTCF) (P91943)
Organism: Drosophila melanogaster (Fruit fly)
Function: Segment polarity protein. Functions together with arm to transduce the Wingless (Wg) signal in embryos and in developing adult tissues. Acts as a transcriptional activator, but in the absence of arm, it binds to gro and acts as a transcriptional repressor of wg-responsive genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:9783586}.
Interaction partners:
Sequence:
MPHTHSRHGSSGDDLCSTDEVKIFKDEGDREDEKISSENLLVEEKSSLIDLTESEEKGHKISRPDHSPVFNKLDTHAPSFNMGYLVSPYSYANGSPSGLPVTMANKIGLPPFFCHNADPLSTPPPAHCGIPPYQLDPKMGLTRPALYPFAGGQYPYPMLSSDMSQVASWHTPSVYSASSFRTPYPSSLPINTTLASDFPFRFSPSLLPSVHATSHHVINAHSAIVGVSSKQECGVQDPTTNNRYPRNLEAKHTSNAQSNESKETTNDKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHELSREEQSKYYEKARQERQLHMELYPGWSARDNYGYVSKKKKRKKDRSTTDSGGNNMKKCRARFGLDQQSQWCKPCRRKKKCIRYMEALNGNGPAEDGSCFDEHGSQLSDDDEDDYDDDKLGGSCGSADETNKIEDEDSESLNQSMPSPGCLSGLSSLQSPSTTMSLASPLNMNANSATNVIFPASSNALLIVGADQPTAQQRPTLVSTSGSSSGSTSSISTTPNTSSTVSPVTCMTGPCLGSSQERAMMLGNRFSHLGMGLSPPVVSTSTSKSEPFFKPHPTVCNNPIFALPSIGNCSLNISSMPNTSRNPIGANPRDINNPLSINQLTKRREYKNVELIEASESKTIVAHAATSIIQHVAVNGYHANHSLLNSNLGHLHHQLNNRTENPNRSEQTMLSVSNHSVNSSECHKESDSQAIVSSNPPNAGSSDNGVISVS
Protein: Adenylate cyclase, terminal-differentiation specific (ACR) (EC 4.6.1.1) (ACB) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q55F68)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Through the production of cAMP, activates cAMP-dependent protein kinases (PKAs), triggering terminal differential and the production of spores.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTNNRLKNRKKPNQIHTISEEEEEEEPLFNNEDLQTQHLNSPSSDSISTSSSSSLSSVGGSVVGNNNSNSNGIDNNNSNNNNNNNNNNNNNNNNNNSNNNNNYTGNSIGGNDFKNKASSSSSTPTTSTGIGSSKFPNIKRKNSFSNRYDSGGGGSGSSRSNSFGGSNSSGGASKEFFYFDNDDMIQDDDLIPMLMQDQEHQLQTQYQNQQQVQQQQNIINSFINHENLKFPFSIIYTNKLHIWLSYFLFTFVLIFCCLAVGPLLWIELPPNSGCMWCRIFKLEWVISFMSLISAMFHYTIRRDMFPLYLSIIGFYHVLTYSEPFLEPFRVNNFFSLILTVICIFIAFYPKNKLRRQQASNHHQQQQQQQQQQRQRQQNNNRQPEKSIIKRIIQNEWFHSLIQILIVLGIVVLLFFSIFILALFMKDDKTFSGDVIDGNINSNNNNNNNNNNNINNNNIDNNNNNIKNNNKGFIEEIEQGEEQLELYLENAYHIFKELVFKKFISSSVVYLILITLLFCISLVYHWEVRKPYTLMALASMIPQLTQALYKVELTLTGVMDKGTMSHNVTPLGGGIFYILNVISYTSFYCGLAIDVVVASGEKYKRLKKRGEKYHRRLSTQINEQNAFVNKIYASGTAQLLQKVEFMQKFVDKILFSTLEISNRLQRLESSDQDIPSSLVDQLNDIQYQTNRSLLLLNDTKLILAIESGVISREDVSVNLFDFLEDVLERTSKDIKFNNIELVYKIDKDVPLNIILDPTALTQICFQLLSNAIKYTEEGEIGILIKRILRNDYEYQQEQQQPQQDNELPPFGTISEEDEEYNSNNPPPPLNQQQQQRQQQQQQEPKQIYLEISIFDSGPGMDDDELDICNQFQPFPDIGDEDDIEIKKKGSGLGLLICNKVLKSIGGDLIVERYLETGGCIFKCCIPVLVDPQPKENFTFQIPLSQETNELLSDLSVLVIDDNPYARDSVGFIFSSVFNSAIVKSANSSVEGVRDLKYAIATDSNFKLLLVDYHMPGCDGIEAIQMIVDNPAFSDIKIILMILPSDSFAHMNEKTKNITTLIKPVTPTNLFNAISKTFKLKEFSSVVDLVDLNAPDTSTQIPLKRNRLKFKIDFPFRLPETGKPIMRVLIGESDKSTQSKIQKVIESFGYFSTFVTDGTALISLSKKNYYDLVIVDLELQSTDGFECAQIIRDTHGEIFSNTIFVPKPISTNSNDDNNNNNNNNNNNNNNDNNNNNNNNNNNNNNNNNNNNNNNNNNNNSILTSSVDTDGNHIVSSSTSTSSSFPTRRSSIGSFQTASPSMTEISHRRRVKLPIIGIWHHSDIIPDDIIKKIKRVGFDGYCSFDNLEFYLQEFLLEFDRKRKSNILSPIRLFPNGSPSTNIYDYSSIISNLNQASGNNNNSSPISGILNENVISSPISLDLDLNSVSSIQSQSSSSSSSFQHNNQQQQQQQHQHQLTPTQQSIGGGNNGINQLSFSSQQSTPIFNQSQIQHQIISNRSKHSSLSSSTSSNGSGGSGGKSRFSIPMLPSSTNRDSSPHSSSKMALKRVQDLESVISKFVPIEFQQLIAPSGMENVYLGDAICKSITIFFSDIRDFTSTTEKMLVDDVIDFLNTYLAFALPSITDSGGFIDKFIGDAIMAIFPNSDMKLQAINAVKAAIRMMRSLDFMSISGFRFSSVETGVGINTGKTIIGIVGTENRMEPTALGDAVNLASRTEQLCKEYQSRILITQFTMEAIGTSIDEFVIRLVDSVTVKGKSEAVNIYEVIDGEREDKRVLKMKILPWYQNGMDLYKRHCYEEALSYFQLCTEIMPNDKPTLIYIQRCIQNIKTLELQQIQLQQLQRQQLLQQQQQQLLLQQQLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQSQNIQQPQSQQSQYVQQPQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPQQQQQLQQQQQHQQQKQPSPQQQQQPQQPQQQQQQQIQNQYQHQLQYQRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHHHHHHQQQQFQQQSQQSQQQSQQQQQQQQQQSQQQSQQQSQQIQKKSQHPHSQQIQSQRHQSQPQNVDTNVKTKPQQ
Protein: T-box transcription factor TBX19 (T-box protein 19) (T-box factor, pituitary) (O60806)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator involved in developmental processes. Can activate POMC gene expression and repress the alpha glycoprotein subunit and thyroid-stimulating hormone beta promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
- Pituitary homeobox 1
- Pro-opiomelanocortin
- Pituitary-specific positive transcription factor 1
- Corticoliberin
Sequence:
MAMSELGTRKPSDGTVSHLLNVVESELQAGREKGDPTEKQLQIILEDAPLWQRFKEVTNEMIVTKNGRRMFPVLKISVTGLDPNAMYSLLLDFVPTDSHRWKYVNGEWVPAGKPEVSSHSCVYIHPDSPNFGAHWMKAPISFSKVKLTNKLNGGGQIMLNSLHKYEPQVHIVRVGSAHRMVTNCSFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERNHLRDVPEAISESQHVTYSHLGGWIFSNPDGVCTAGNSNYQYAAPLPLPAPHTHHGCEHYSGLRGHRQAPYPSAYMHRNHSPSVNLIESSSNNLQVFSGPDSWTSLSSTPHASILSVPHTNGPINPGPSPYPCLWTISNGAGGPSGPGPEVHASTPGAFLLGNPAVTSPPSVLSTQAPTSAGVEVLGEPSLTSIAVSTWTAVASHPFAGWGGPGAGGHHSPSSLDG
Protein: Chitobiosyldiphosphodolichol beta-mannosyltransferase (EC 2.4.1.142) (Asparagine-linked glycosylation protein 1) (Beta-1,4-mannosyltransferase) (GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase) (GDP-mannose-dolichol diphosphochitobiose mannosyltransferase) (O13933)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P16661}; Single-pass membrane protein {ECO:0000250|UniProtKB:P16661}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit alg13
- UDP-N-acetylglucosamine transferase subunit alg14
- Alpha-1,3/1,6-mannosyltransferase alg2
- Dolichol-phosphate mannosyltransferase
- GDP-Man:Man
- Mannose-1-phosphate guanyltransferase
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Protein argonaute
Sequence:
MLVLKIVLFLSLVIWFNLKKRTDKKRIIVLVLGDIARSPRMQYHAVSFAKLGWKVDLLGYQHPGSSVGLFESHENIRFYPIPSLPAYLQPKNRLQFLFLGPLKVLHQFLALNWALFVRKPASFLFIQNPPCIPVFFIAQCLHILRGTKFIIDWHNFGYSILALKLGKQHTFVKLLKIYEKYMARGAYAHLTVSKRMKDVLQTWGMNPCYVCYDRPPNHFTPIKNEQKKQMSIKKIPCEYNPSSTKLLITSTSWTPDEDIYILWEALNEYDKTLDTPKLLVLITGKGPMKEEFSQYIKKHPLHKVRFCMPWLSIEDYPQVMACADLGVCLHTSSSGLDLPMKVVDLFGCGVPVIALSYPTISELVHDGENGLIVNDSKALSKKMQYLLTHANELNSLKLGALKESEYRWDDEWNKVIPPIVQGSN
Protein: Uncharacterized protein, isoform A (EC 3.1.4.2) (Q9VVV5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVPMLLTPMEAQSPDDHMKNCAAFVDGASITYGTGNELESGSGSSAACKPTLREFNVRLEVPLAAEERLGLTGDVKALGEWQLSRSVALESLDELNWQATVALQSCRQLEYRYFVYVEDLSGYKQIRRWETHFKPRSLGPCTELQCSQLDVFGITSDNSDLKPQVHRGWLNHEAILQLKFNGEKMFQVHDIETFDPQHVQLKIVPVEKTAGLHVEYSKQEYGKSQLELQPTFGVPYTKGDIVIFHITLPLERMMEQHFRLECYSMSNELLGSATLVTSDLTGSEGVLHLPIKSAKNADETLARLRLPYVAVQPYRYSPLDFKNTYAHYWPKSWPNLDVGHRGNGKSYIADAPAERENTIASFLSAHEHHADMIELDVHLTADGVPVIYHDFGLRTAPPGKQISRPDQLEYVLIKDINYELLKRLRIFSVIAGQVREYPSHNAEPRMEHRIFPTLVEVLEKLPKSLGIDVEIKWPQRRQGGGSEAEQTIDKNFFADKVIHQVIQKGCGRPIIFSSFDADMCTMLRFKQNVFPVMFLTQGETKKWQPFLDLRTRTFIAAVNNAQAFELAGTAPHAEDFLGENASEMLRKAKDLGQIAVIWGDDCNSKERVQYFTRIGATATCYDRSDLFMPEGKREAFFKSPALMAEFAAQCRI
Protein: NADH-dependent flavin reductase StyB (EC 1.5.1.36) (Styrene monooxygenase small component) (O06835)
Organism: Pseudomonas fluorescens
Function: Reductase component of a two-component system that catalyzes the first step in the aerobic styrene degradation pathway by enantioselective epoxidation of the vinyl side chain. Utilizes NADH to reduce FAD, which is then transferred to the styrene monooxygenase StyA.
Interaction partners:
Sequence:
MTLKKDVAVDIDSTCFRQAVALFATGIAVLSAETEEGEVHGMTVNSFTSISLDPPTVMVSLKSGRMHELLTRGGRFGVSLLGESQKVFSAFFSKRVMDDTPSPAFTIQAGLPTLRDAMAWFECEVESTVQVHDHTLFIARVSACGTPEANAPQPLLFFASRYHGKPLPLN
Protein: Ionotropic receptor 52d (A1ZA17)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MVRIIIILLCLGYTKARILDATNTNHTDLEERLLSLLLRLQQEQFFNTLLIYGEDCAFSSLSRRLQVPTILVSSGSTSFEWNYSSLALILTCEFKAEREENYQTLKKLQMNRRLILLNGNIKPDSVCDFYSKKDQYNIAMVNNNFHQVGIIYACRLFQERNYEKVYLSEGNPIYVDQFRNMQGALLKSITFNLIPGSMAYRDPKTGQEKHIGYVANLLNNFVEKVNATLDMQVKLHKAGKKTSFYNITKWASEDLVDIGMSYAAYFEMTNFDTISYPYLMTSTCFMVPLPDMMPNSEIYMGIVDPPVLVVLIAIFCIFSVMLNYIKQRSWRSLSLVNVLLNDICLRGFLAQPFPFPRQSNRKLKLISMLVCFFSVITTTMYTSYLQSFMWGPPIDPKMCSFADLENSRYKLAIRRYDIEMLRPFNVSMDHVVVFDESSQLEYLRDSFDDNYMYPMSALSWSAFKEQQKLFAFPLFYYSEKLCLKPISFFSFPIRRHLPYRDLFEEHMLQQNEFGLSTYWIDRSFSDMVRLKLATMNDFSPPRLEDYIEVSDLSWVFGMYFTGLGISCCCFGLELLGLPSWTRRLRLTNWLRVRN
Protein: At5g26880 (tRNA (Cytidine(34)-2'-O)-methyltransferase) (Q6NPL4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AGAMOUS-like-56
- Agamous-like MADS-box protein AGL49
- AGAMOUS-like 102
- WAT1-related protein At1g68170
- AGAMOUS-like 58
- Agamous-like MADS-box protein AGL12
- AGAMOUS-like 83
- AGAMOUS-like-34
- Agamous-like MADS-box protein AGL104
- MADS-box protein AGL73
Sequence:
MESCCRSVIASRTFHLRSSGRLFPSLSLTHLKGKLSLSINSFSSKIQSHALRGVGIGESDKKNPLPRGAGEGVKEDARSKLLHVVLVSPQIPGNTGCIARTCAASAVGLHLVGPLGFQVDDARVKRAGLDYWPFVVVKAHSSWAEFQEYFRLQEGEKRMIAFTKRGTRIHSDFSYRSGDYLLFGSETSGLPPEALSDCNHEPYGGGTLRIPMVETYVRCLNLSVSVGIALYEASRQLNYEQIECAPQGCVNGEEPLLTEDIFA
Protein: LD02541p (Q95RX8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDSSKYSIYGTNVPPQQQQPGVGGDTAAVRPQSLYGINAPDLPPRIDRQSKPGDIPLNTSGSSSRNGTLGRSAQERLFGKAVVQDDVQAEYITRNALVGSGAAETLDRQQQQQQQTHASLERQARLNAQLKANGVGAGGGGASTYDSVSSYDSYNNTQMAMQNLGRLGPNAPDDLKSVPNANGRPLPPTGQSHEYGRTPHDHRSFGGPNDLNRQSSPGRPHYHDMNASRNIDPRNGTPQRPSNLGLESSPRKPLVETKTDYGKYSRNNSVTQADYTKLPKTAPHGVVPPPNVSNGQGQMNGSGTPSSNGSGPFKPVPPPKPKNYRPPVQSGGSSGSGGTTPWENGDSGSPRSPNGFYYPPTPSHHHYGQQATPGSPSNGHMQPPPPQQQQPTYGGSNGNYGQAPPPQSYPQANGYNGNGHHYNGGSGTGPYIAPHRGMPPPIGNLPPHTPERHALDLAGSREQRGSAFELYRKPQIGATAGHHHNMR
Protein: Coiled-coil domain-containing protein 181 (Q80ZU5)
Organism: Mus musculus (Mouse)
Function: Microtubule-binding protein that localizes to the microtubular manchette of elongating spermatids.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28283191}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:28283191}. Note=Localizes to the microtubular manchette of elongating spermatids (PubMed:28283191). Localizes to the sperm flagella and to the basal half of motile cilia (PubMed:28283191). {ECO:0000269|PubMed:28283191}.
Interaction partners:
- Large ribosomal subunit protein uL30m
- Stabilizer of axonemal microtubules 4
Sequence:
MDEDKDIDSKESGEYEDDFEKDLEWLINDKEKSNGSTIEMACKKEDDLDQVLKENETETELGQQLSDPDNSPKDEALPRRNDFISVPSIQPLDPISDSDSENSFQDSKPENQKDLEDEEDEEVRRYIMEKIIEANKLLQTQEPVNDKRERKLKFKDKLVDLEVPPLEDSDTCKALLENETNMSGKLSQLCISGDLEQESVLVSVTDGSCEENDRKILVERDGKFELMNLQDIESQGFLPPISSANSVEHESSQLPLRAPNPSVGGIKKEESEAKGHVLPISPAGEPLAQVPQLLPNPKNRPSSAANPDVTKKARRSNHRIQSAGVSPVTSTYCLSPRQKELQKQLERKREKLKREEEQRKLEEENEKKKENEMVFKAWLQKKREQVIEMRRVQRAKQIEDMSSRQVNRDPQQAFRLWLKKKHEEQMKERKTEELRKQEECLFFLRGTEGRERAFRQWLRRKQIEKIAEQQAVKERARQLRLEARRSKQLQSSLYSIPEAKAFRFTDHYN
Protein: Acid phosphatase, putative (Q38AR1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFLLPREVMRKYAIFSLAIILLLFTVVSSEPGERDAESGVKRGDEKQNLVLTKLIVLNRHGHRAPNAPYWSMCPNDRKNRRKYNVGAEDLTARGMKEEYELGEYLRNAYRDFIGPRFNRSRHFLRAVGEPRILQSAQAVAQGLFPDGYGPGGYLPRQPQFVPVFSDMDTHEYLLDDVPCFRRAERDMRRWLNTSLSDFIADPKVSEVLNYMKRMCGVSEKDMPPVYAFLKTVADGMTFNADFGLSVCHGKVTPEMLFKIRKVSLRLLMARLYHTDEQQTYTSVDLPYRILYMLNRSTSPGAKGVNDYSDTEQEAILYFMHREALYAVGEFFGFTFNVPGLPHGELPVASTIVWERLVPEKSVGEEIVPSRTYVRLILWTPKDGTATVAIPHCRTPQLCTLKELQDIYSARVKRTGSWLKLCNFTITELDHDTDIR
Protein: Melanoma-associated antigen F1 (MAGE-F1) (MAGE-F1 antigen) (Q9HAY2)
Organism: Homo sapiens (Human)
Function: Enhances ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin ligases. Proposed to act through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. MAGEF1-NSMCE1 ubiquitin ligase complex promotes proteasomal degradation of MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19 impairs the activity of several DNA repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters as cofactors. May negatively regulate genome integrity by inhibiting homologous recombination-mediated double-strand break DNA repair.
Interaction partners:
- Non-structural maintenance of chromosomes element 1 homolog
- Chondrosarcoma-associated gene 1 protein
- Neuronal PAS domain-containing protein 4
- Non-structural maintenance of chromosomes element 4 homolog A
Sequence:
MLQTPESRGLPVPQAEGEKDGGHDGETRAPTASQERPKEELGAGREEGAAEPALTRKGARALAAKALARRRAYRRLNRTVAELVQFLLVKDKKKSPITRSEMVKYVIGDLKILFPDIIARAAEHLRYVFGFELKQFDRKHHTYILINKLKPLEEEEEEDLGGDGPRLGLLMMILGLIYMRGNSAREAQVWEMLRRLGVQPSKYHFLFGYPKRLIMEDFVQQRYLSYRRVPHTNPPEYEFSWGPRSNLEISKMEVLGFVAKLHKKEPQHWPVQYREALADEADRARAKARAEASMRARASARAGIHLW
Protein: Phosphoribosyl pyrophosphate synthase-associated protein 2 (PRPP synthase-associated protein 2) (41 kDa phosphoribosypyrophosphate synthetase-associated protein) (PAP41) (O08618)
Organism: Rattus norvegicus (Rat)
Function: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 2
- Phosphoribosyl pyrophosphate synthase-associated protein 1
- Ribose-phosphate pyrophosphokinase 1
- ribose-phosphate diphosphokinase
- Ribose-phosphate pyrophosphokinase 1
Sequence:
MFCVAPPELETKMNITKGGLVLFSANSNSSCMELSKKIAERLGVEMGKVQVYQEPNRETRVQIQESVRGKDVFIIQTVSKDVNTTIMELLIMVYACKTSCAKSIIGVIPYFPYSKQCKMRKRGSIVSKLLASMMCKAGLTHLITMDLHQKEIQGFFNIPVDNLRASPFLLQYIQEEIPDYRNAVIVAKSPASAKRAQSFAERLRLGIAVIHGEAQDAESDLVDGRHSPPMVRSVAAIHPSLEIPMLIPKEKPPITVVGDVGGRIAIIVDDIIDDVDSFLAAAETLKERGAYKIFVMATHGLLSSDAPRLIEESAIDEVVVTNTIPHEIQKLQCPKIKTVDISMILSEAIRRIHNGESMSYLFRNIGLDD
Protein: Autophagy protein 5 (Q3MQ06)
Organism: Rattus norvegicus (Rat)
Function: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H1Y0}. Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. Also localizes to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. {ECO:0000250}.
Interaction partners:
- Autophagy-related protein 16-1
- Ubiquitin-like protein ATG12
- Ubiquitin-like-conjugating enzyme ATG3
- Ubiquitin-like modifier-activating enzyme ATG7
- Mitochondrial antiviral-signaling protein
- FAS-associated death domain protein
- Protein Atg16l2
- Ubiquitin-like-conjugating enzyme ATG10
- WD repeat domain phosphoinositide-interacting protein 2
- Gamma-aminobutyric acid receptor-associated protein
Sequence:
MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVMRQEDVSEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPCKDAVEAHFMSCVKEADALKHKSQVINEMQRKDHKQLWMGLQNDRFDQFWTINRKLMEYPPEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLREVCPSAVAPEDGEKKSQVMIHGIEPLLETPLQWLSEHLSYPDNFLHISIVPQPTD
Protein: Protein PTI1 (P39927)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation. PTI1 is required for 3'-end formation of snoRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819204}.
Interaction partners:
- Pre-mRNA polyadenylation factor FIP1
- Protein SYC1
- Endoribonuclease YSH1
- Cleavage factor two protein 2
- RNA end formation protein 2
- Protein CFT1
- Serine/threonine-protein phosphatase PP1-2
- mRNA 3'-end-processing protein YTH1
- Polyadenylation factor subunit 2
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Sequence:
MTDPRRRTGRHFLTPENLSSTLQITNLPPEWNQDIITSVVAGSGPVIDIKAKNDPRTGKLTGVLFDYLTSKDCKRAWEILNRIENFPVKIEQIIPPNYKDHLRETANKNSQKQVLQLNRDSYPFEAGLELPFEMVTEVPIPRRPPPPQAANNTNSVSNNTNIQFPDILSKASKHLPSFQDGSIIAPDKISQNLSKIPPLQLIEIISNLKILSNQENIQKSQLESFLDTNSDITISVTQALLEMGFIDYSVVTKVLKSQVGEAPSLLSSNNTSNSNTPVSVIRNNTPLHVPSNEVSNNPNNMPLNVAMPMPMSTPPFIPLPLQQQPFGFAPPGPFMPPAQGPSMGQPVLANQLGQVQQQNISSTEGPSNANKANDSGTINMAKLQLLPENQQDMIKQVLTLTPAQIQSLPSDQQLMVENFRKEYII
Protein: 5-cytosine rRNA methyltransferase NSUN4 (EC 2.1.1.-) (5-cytosine tRNA methyltransferase NSUN4) (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 4) (Sperm head and tail associated protein) (Q9CZ57)
Organism: Mus musculus (Mouse)
Function: Involved in mitochondrial ribosome assembly. 5-methylcytosine rRNA methyltransferase that probably is involved in mitochondrial ribosome small subunit (SSU) maturation by methylation of mitochondrial 12S rRNA at position 911; the function is independent of MTERFD2/MTERF4 and assembled mitochondrial ribosome large subunit (LSU). Targeted to LSU by MTERFD2/MTERF4 and probably is involved in a final step in ribosome biogenesis to ensure that SSU and LSU are assembled. In vitro can methylate 16S rRNA of the LSU; the methylation is enhanced by MTERFD/MTERF4.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21531335}.
Interaction partners:
- Transcription termination factor 4, mitochondrial
- Mitochondrial assembly of ribosomal large subunit protein 1
- Mitochondrial ribosome-associated GTPase 1
- 28S rRNA
- rRNA methyltransferase 2, mitochondrial
- Putative methyltransferase NSUN7
- Mitochondrial ribosome-associated GTPase 2
- Nucleolar complex protein 2 homolog
- tRNA
- Methionyl-tRNA formyltransferase, mitochondrial
Sequence:
MAAPVLRCVRKLLKLVDFTPVPRRYRYKKKWATTEPQFTASRLALQNFDMTYSVQFGDLWPSIRVSLLSEQKYGALVNNFAAWDSVSAKLEQLSAKDFVSEAISHQKLEPESGLSPTPSLDCSPNLRCFTFSRGDVSRFPPARLGSLGLMDYYLMDAASLLPVLALGLQHGDTVLDLCAAPGGKTLALLQTGCCRNLAANDLSTSRTGRLQKVLHSYVPQDIREGNQVRVTSWDGRKWGELEGDTYDRVLVDVPCTTDRHSLHEEENNIFQRSRKKERQMLPMLQVQLLAAGLLATKPGGHVVYSTCSLSHLQNEYVVQGAIELLANQYNIKVQVEDLSHFRKLFMDTFCFFPSCQVGELVIPNLMVNFGPMYFCKLHRLP
Protein: Gastrokine-1 (18 kDa antrum mucosa protein) (AMP-18) (Protein CA11 homolog) (Q9CR36)
Organism: Mus musculus (Mouse)
Function: Has mitogenic activity and may be involved in maintaining the integrity of the gastric mucosal epithelium.
Subcellular location: Secreted {ECO:0000269|PubMed:12851218}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9NS71}. Golgi apparatus {ECO:0000250|UniProtKB:Q9NS71}. Note=Shows abundant granular cytoplasmic staining, with perinuclear accentuation suggestive of the Golgi apparatus. {ECO:0000250|UniProtKB:Q9NS71}.
Interaction partners:
- Gastrokine-2
- Trefoil factor 1
Sequence:
MKLTMFVVGLLGLLAAPGFAYTVNINGNDGNVDGSGQQSVSINGVHNVANIDNNNGWDSWNSLWDYENSFAATRLFSKKSCIVHRMNKDAMPSLQDLDTMVKEQKGKGPGGAPPKDLMYSVNPTRVEDLNTFGPKIAGMCRGIPTYVAEEIPGPNQPLYSKKCYTADILWILRMSFCGTSVETY
Protein: High mobility group nucleosome binding domain 1 (A6NEL0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFEPNSPRRGGARYQWPEGAQVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD