wanglab/gogpt-training-data huggingface dataset:
Protein: Sterol regulatory element-binding protein 2 (SREBP-2) (Sterol regulatory element-binding transcription factor 2) [Cleaved into: Processed sterol regulatory element-binding protein 2 (Transcription factor SREBF2)] (Q60429)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 2), which is embedded in the endoplasmic reticulum membrane. Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis.
Subcellular location: [Sterol regulatory element-binding protein 2]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q12772}; Multi-pass membrane protein {ECO:0000255}. Note=At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum. Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed. {ECO:0000250|UniProtKB:Q12772}.; SUBCELLULAR LOCATION: [Processed sterol regulatory element-binding protein 2]: Nucleus {ECO:0000250|UniProtKB:Q12772}. Note=Transported into the nucleus with the help of importin-beta. Dimerization of the bHLH domain is a prerequisite for importin beta-dependent nuclear import. {ECO:0000250|UniProtKB:Q3U1N2}.
Interaction partners:
Sequence:
MDESSELGGLETMDTLTELGDELTLGDIDEMLQFVSNQVGEFPDLFSEQLCSSFPGGGSSGSSSSSNSSSSSGSNSRGNGGAATDPGVQRSFSQVPLPTFSPSTASPQALALQVKVSPTPPRATPVLQPRPQPQPQPQPSAQLQQQTVMITPTFSTAPQTRIIQQPLIYQNAATSFQVLQAQVQSLVTSSQVQPVTIQQQVQTVQAQRVLTQTANGTLQTLAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGSPVMAAVQNPALTALTTPLQTGALQVPTLVGSNGTILTTMPVMMGQEKVPIKQVPGGVKQLEPPKEGERRTTHNIIEKRYRSSINDKIIELKDLVMGTDAKMHKSGVLRKAIDYIKYLQQVNHKLRQENMVLKLANQKNKLLKGIDLGSLVDSDVDLKIEDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILLCVLTFLGLSFSPLTSLLQWGGAHDTDQHPYSGSGRSVLSLESGSGGWFDWMMPTLLLWLVNGVIVLSVFVKLLVHGEPVIRPHTRSSVTFWRHRKQADLDLARGDFAAAAANLQTCLSVLGRALPTSRLDLACSLSWNVIRYSLQKLRLVRWILKKVFQRWRATPATAAGFEDEAKSSARDAALAYHRLHQLHITGKLPAGSTCSDVHMALCAVNLAECAEEKIPPSTLIEIHLTAAMGLKTGCGGKLGFLASYFLNRAQSLCGPEHSTVPDSLRWLCHPLGQKFFMERSWSIKSAAKESLYCAQRNPADPIAQVHQAFCKNLLERAVESLVKPQSKKKSGDQEDESCEFSSALEYLRLLHSFVDSVGFVTPPFSSSSVLKSALGPDIICRWWTSAVTMAISWLQGDDAAVRSHFTEVERIPKALEVTESPLVKAVFYACRAMHASLSGKGDGQQNSFCHCERASGHLWNSLNVSGATSDPSLNHVVQLLTCDLLLSLRTALWQKQAGASQGLGETYHASGTELAGFQRDLGSLRRLAHSFRPAYRKVFLHEPTVRLMAGANPTRTHQLLEHSLRRRTSQNTKHGEIDTWPGQRERATAILLACRHLPLSFLSSPGQRAVLLAEAARTLEKVGDRRSCNDCQQMIVKLGGGTAIAAS
Protein: Vacuolar protein-sorting-associated protein 46 (Charged multivesicular body protein 1) (DOA4-independent degradation protein 2) (Fifty two inhibitor 1) (P69771)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripherally associated component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1.
Subcellular location: Endosome membrane; Peripheral membrane protein. Endomembrane system; Peripheral membrane protein. Note=Endosomal and other punctate structures.
Interaction partners:
- Vacuolar protein-sorting-associated protein 24
- DOA4-independent degradation protein 4
- Vacuolar protein-sorting-associated protein 60
- Vacuolar protein sorting-associated protein VTA1
- Vacuolar-sorting protein SNF7
- Vacuolar protein sorting-associated protein IST1
- Vacuolar protein sorting-associated protein 4
- Vacuolar protein sorting-associated protein 20
- Uncharacterized protein YJL049W
- Vacuolar protein-sorting-associated protein 25
Sequence:
MSRNSAAGLENTLFQLKFTSKQLQKQANKASKEEKQETNKLKRALNENEDISRIYASNAIRKKNERLQLLKLASRVDSVASRVQTAVTMRQVSASMGQVCKGMDKALQNMNLQQITMIMDKFEQQFEDLDTSVNVYEDMGVNSDAMLVDNDKVDELMSKVADENGMELKQSAKLDNVPEIKAKEVNVDDEKEDKLAQRLRALRG
Protein: Zinc finger protein 350 (KRAB zinc finger protein ZFQR) (Zinc finger and BRCA1-interacting protein with a KRAB domain 1) (Zinc finger protein ZBRK1) (Q9GZX5)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Binds to a specific sequence, 5'-GGGxxxCAGxxxTTT-3', within GADD45 intron 3.
Subcellular location: Nucleus. Nucleus matrix. Note=Associated with the nuclear matrix.
Interaction partners:
- Breast cancer type 1 susceptibility protein
- DNA endonuclease RBBP8
- Transcription intermediary factor 1-beta
Sequence:
MIQAQESITLEDVAVDFTWEEWQLLGAAQKDLYRDVMLENYSNLVAVGYQASKPDALFKLEQGEQLWTIEDGIHSGACSDIWKVDHVLERLQSESLVNRRKPCHEHDAFENIVHCSKSQFLLGQNHDIFDLRGKSLKSNLTLVNQSKGYEIKNSVEFTGNGDSFLHANHERLHTAIKFPASQKLISTKSQFISPKHQKTRKLEKHHVCSECGKAFIKKSWLTDHQVMHTGEKPHRCSLCEKAFSRKFMLTEHQRTHTGEKPYECPECGKAFLKKSRLNIHQKTHTGEKPYICSECGKGFIQKGNLIVHQRIHTGEKPYICNECGKGFIQKTCLIAHQRFHTGKTPFVCSECGKSCSQKSGLIKHQRIHTGEKPFECSECGKAFSTKQKLIVHQRTHTGERPYGCNECGKAFAYMSCLVKHKRIHTREKQEAAKVENPPAERHSSLHTSDVMQEKNSANGATTQVPSVAPQTSLNISGLLANRNVVLVGQPVVRCAASGDNRGFAQDRNLVNAVNVVVPSVINYVLFYVTENP
Protein: Keratin-associated protein (Q9D6S9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTYSCRSGSFSSRSYGGQLCYPSSCGSSFPRQLTHRTNFCSPRNRHLGSSFRHGYHQNCFQPIRCQTSHVVHSSCQRPCYRPSVSSFCSPCRATYAGFLGFRSSSCHSQVYGSRRVYTSGCGSSCFRPVSYRVCGYPSFGYGSRFCHPTYVTSRNFQSSCHRPTCGSTKWRSSC
Protein: Carboxypeptidase (EC 3.4.16.-) (Q2TZ11)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MRGYEFLSVLPLVAASWALPGSTPASVGRRQLPKNPTGVKTLTTANNVTIRYKEPGAEGVCETTPGVKSYSGYVDTSPESHTFFWFFEARHNPETAPITLWLNGGPGSDSLIGLFEELGPCHVNSTFDDYINPHSWNEVSNLLFLSQPLGVGFSYSDTVDGSINPVTGVVENSSFAGVQGRYPTIDATLIDTTNLAAEAAWEILQGFLSGLPSLDSRVQSKDFSLWTESYGGHYGPAFFNHFYEQNERIANGSVNGVQLNFNSLGIINGIIDEAIQAPYYPEFAVNNTYGIKAVNETVYNYMKFANQMPNGCQDLISTCKQTNRTALADYALCAEATNMCRDNVEGPYYAFAGRGVYDIRHPYDDPTPPSYYNKFLAKDSVMDAIGVNINYTQSNNDVYYAFQQTGDFVWPNFIEDLEEILALPVRVSLIYGDADYICNWFGGQAVSLAANYSQAAQFRSAGYTPLKVNGVEYGETREYGNFSFTRVYEAGHEVPYYQPIASLQLFNRTIFGWDIAEGQKKIWPSYKTNGTATATHTQSSVPLPTATSMSSVGMA
Protein: Sm domain-containing protein (Q23543)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm6
- Probable U6 snRNA-associated Sm-like protein LSm4
- Small nuclear ribonucleoprotein Sm D3
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm3
- Probable small nuclear ribonucleoprotein Sm D2
- ATP-dependent RNA helicase cgh-1
Sequence:
MSKDEGKRKKESVVDLTRFLDKEIRVKFQGGREASGVLRGFDQLLNMVLDDCREYLRDPQNPSVVGDETRQLGLIVARGTAITVVSPADGLEQIANPFATQEEE
Protein: Phosphatidylethanolamine:ceramide ethanolaminephosphotransferase (EC 2.7.8.-) (Ethanolamine-phosphorylceramide synthase) (EPC synthase) (Sphingolipid synthase) (Q38E54)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Bidirectional lipid ethanolaminephosphotransferase capable of converting phosphatidylethanolamine (PE) and ceramide to ethanolamine-phosphorylceramide (EPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoethanolamine acceptors. 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: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- serine C-palmitoyltransferase
- Serine-palmitoyl-CoA transferase, putative
Sequence:
MAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILAVALQITHERMPDPKVTKPLPDLGFEVLHKYPFLFSVADCCIGFLNILSVFTAFKLYLLHRHCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNVHTIAWIRFITSYALLLLSRSVIMVVTSLPNPDDLCQDPPKIENRVKDVILTVLTAGAGSIHCGDLMYSGHTVILTLHLMFHWIYGAMVHWSFRPVVTVVAIFGYYCIVASRFHYTDDVLVAIYLTIATFIAVGHNADGAPWQLQLFIRWLPCCGANSREVTEDGVPVAIVIKNEEMMNFEGKS
Protein: Negative elongation factor B (A0A5H1ZRP4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LAELEGAGERGSGGPRGPAERASGVSAAAPGERAGDGAPSRAVAGASAMFAGLQDLGVANGEDLKETLTNCTEPLKAIEQFQTENGVLLPSLQSALPFLDLHGTPRLEFHQSVFDELRDKLLERVSAIASEGKAEERYKKLEDLLEKSFSLVKMPSLQPVVMCVMKHLPKVPEKKLKLVMADKELYRACAVEVKRQIWQDNQALFGDEVSPLLKQYILEKESALFSTELSVLHNFFSPSPKTRRQGEVVQRLTRMVGKNVKLYDMVLQFLRTLFLRTRNVHYCTLRAELLMSLHDLDVGEICTVDPCHKFTWCLDACIRERFVDSKRARELQGFLDGVKKGQEQVLGDLSMILCDPFAINTLALSTVRHLQELVGQETLPRDSPDLLLLLRLLALGQGAWDMIDSQVFKEPKMEVELITRFLPMLMSFLVDDYTFNVDQKLPAEEKAPVSYPNTLPESFTKFLQEQRMACEVGLYYVLHITKQRNKNALLRLLPGLVETFGDLAFGDIFLHLLTGNLALLADEFALEDFCSSLFDGFFLTASPRKENVHRHALRLLIHLHPRVAPSKLEALQKALEPTGQSGEAVKELYSQLGEKLEQLDHRKPSPAQAAETPALELPLPSVPAPAPL
Protein: Stromal interaction molecule homolog (P83094)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in mediating Ca(2+) influx following depletion of intracellular Ca(2+) stores.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Calcium release-activated calcium channel protein 1
- Inositol 1,4,5-trisphosphate receptor
- Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type
- Nuclear factor of activated T-cells 5
- Calmodulin
- EF-hand domain-containing protein
- Transient receptor potential cation channel trpm
- Calmodulin-related protein 97A
- AT10229p
- Calcium-binding protein E63-1
Sequence:
MRKNTIWNYSLIFFCCVLKSISTLDHGPHTVSVDSNRHNTQHQYKQNPNVASQRHSSHESGQSLHNSQSEHVTHIAASHAGSGGEHSTHLAQNLHRSSYNLLSEAMSQAVSNEFSSMGSGSADGACAADDFDCYSGSVQDRFGMEAIASLHRQLDDDDNGNIDLSESDDFLREELKYDSGYEKRQKAFHFNDDMHISVKELWEAWLRSEVHNWTIEQTTDWLAQSVQLPQYVDLFKLHKVTGAALPRLAVNNLQYVGNVLGIKDPIHKQKISLKAMDVVLFGPPRETGTRWKDYILVTLLLSAIIGCWYAYQQNKNAKRHLRRMAQDMEGLQRAEQSLQEMQKELERARMEQENVATEKLDLERRLKEAPTLSSSNSDLEVQQLKKEIEMLRNELSRAEFELVDNCWSPPPQLQSWLQYTYELESKNHQKKRTSAEKQLQSAREACEKLRKKRSSLVGAFVSTHGKSIDDVDRSIVEARNALGDVTNELQERLHRWKQIETCLGLNIVNNNGLPYLENVLYGRNGGLQSSMGMSSTKGSRARITNSTEDLDDESIQGKLNFENFSLLATE
Protein: Schnurri, isoform F (A0A0B4KFC0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein decapentaplegic
- Brinker
- Protein mothers against dpp
- receptor protein serine/threonine kinase
- Mothers against decapentaplegic homolog
- Serine/threonine-protein kinase receptor
- Suppressor of hairless protein
- Protein hairless
Sequence:
MARRKGSGRGKSTVNSRKSALETAREKTKDEPTANTSQDNKFDNNMENATTTTAKHYKTAGKQYKTNKVNNTRRATAAAAAAAAAAATTTVTTAATPTKKRTYRETATATIVTQRSTNKANIAAAIALAAATEATASASASATATATDATLTASKAAATAAATTDAASGNSNSSSKPSTSTRDKLGEVPLPTVDSNHIISNNNNNNNNNNTSNNNNNNHHSDNSISENNYEFKSRDKASLSDSKMTLQQMAAVSSNQEPVAPNVANTMSNSSIINSQQTTVNATPATDEAPLGDRSNISRYLHKKFKRLASTTEVDSWSATNGGGALQASGDAVRTTSLSSNSSLSPPPTTPLANGHHLMTQQQSHQQVQQQQQQQQTPPPSVAIHEFSANFVNSNHVNAIGHEESIISNSGYKAAGRTRTPLANSNSNTNSTSNSNSNHAANATLSPASFAQHQQLTQPTTVSPGIPGGAAAPNPACEKSGRYVCQYCNLICAKPSVLEKHIRAHTNERPYPCDTCGIAFKTKSNLYKHCRSRSHAARARGLEVPADADDGLSDQDAELSNSSSELPSRAGSPYEEPINSPTPSPSTLSAAKSAYIQQPPLPTYMQQLPLGSPAAGTLPPTTADNHHSATAQHRQSIDYKPYKPKFHNASLYSCSSKELQQQQQQLQIQQQQQQHQLAQQKLSIQLPLVQQPSLAHPTLSPSTQMKMKHHINSHQIQLQLQQQQSLLAQQSLLAAMPPGGVYYLGQPSYYNQDTAAAIHQHALAIQQFQIHLAQQQQQQQQQHPPLVKATPPMQQPPSLPPQQLVRANSQISSVATAPATPTPAANLSTFASSSGGKQVNVAKVQEHISKLISQNEAIVENKEILLQKKYPKQLSRSRSFNNANSNNASQHGSNASALHANNSQNNTNAQMPERETKVNLAQAIFQKQQHQLQQQQQQQITQQQQQQLEQQNYYTYIQQQQECQQQQLEPPNGVVKRNAYKPGVVMTTPVKQQQQLPPPPSPLPMQTMQYRQDPATPVTKIEQPTTAVPVMPLNLSAKPKPTLVTVPVSSLSTSSLAPTPTTSTNPTSSSKTAPPPAQVNNSIIKNLLLNARGLAVPIGEGDDAVYSCPICASEFRSADDLKLHNSTYCQDASSSAPMSPASSPFRSNSISLSLPELKSHMANSKNPLSLAKLAWSQLKTKRSSLVLSRLSAAQTPARTSTVTAPTVTASAPAPAVATVTAPSSAPAPQIEALRFVDAPLPSPGPLLGKTPLVDYAQQSTPRKAQDSVVITKMHEDRQFVIEAQPAKRIKTSDLVVASSSQQPTSFNFSFNNQNSSNSVPELQSSKEERLRRFTSSGGSMIPISECPDLDNSPKMIRTPLLSGGSFQDVSVKVNNETGSSSKERKLMALVSGSGLLGVSSGPQHFQFPPINSITAFNPLTLPPMSGGDKTTPVTPIPHVPGMPGPGSLTPQMPLLPPPPQQLQLPIPSSRGRSPNRKQPSPLLLGGGSGELKALSPFGGVQNVPSEFSRQPPTPAQRQALQWNSKEAPKKAPFNFLRMADNVKTTEPEVRHFNLENVISGKQQELPLTPLHVDTPNGNAPEETSPVASASASAKSKFLRPTSLPLKPGTFTPKRHHGITPTANTLPLISPETPRPSKSCVQLYLNGHAYTYLGLKCSTKMFYCTVNCPQPSYVAGMHKLSMYSVWQVCEENQPHPLGFKLKQVMALYDSRQRMLGNGSSTAMAGSGKLSYNLVASQQIVSSPSTSSTSSAFYQGPLKTPPTVTIAALSEANVAAKANEEAQAKKLETSPSGQPLVGGYESHEDYTYIRGRGRGRYVCSECGIRCKKPSMLKKHIRTHTDVRPFTCSHCNFSFKTKGNLTKHMQSKTHFKKCIELGINPGPMPPDSEFLDVDMDFDQQSSTSAGGRTSSMAGESDSDDYSDNESESSDTDESKSRQKEHEAARGLLSLSMTPPIPQSVSPYPQLQDTPLPAASPANSIGSSGSQPKRLVCSFTSPKPPFDYQKQEQYYSNPEESKPKRSVANEESAPMDLTKPRGSILLISPSPVSVPAHDLPKSQAQQMHDVIFGTSGNESGFMKTLISVSDKVRISAEMEEQAKHEAEGEDVQLQTYIKEHALHQAKIKQSQFSRSYLINTLYTAASPVMSSSSTLFTANSRPVMSVNEVPSIEVHEVKTPEAIESPRSAPEQAPVILAQIAQEENEEPNIAEPHNANLPAAVQQPDVNEFTGVLGNPTAPPTSSVTATSVSTTTAAPVAPSSTANSTQPAQRTVIVGEDGFKSSTPTSKSGDLQHVSYGRGVPPAPIAGDARPTCTMCSKTFQRQHQLTLHMNIHYMERKFKCEPCSISFRTQGHLQKHERSEAHKNKVMMTSTFGVPTTSNPRPFECTDCKIAFRIHGHLAKHLRSKTHVQKLECLQKLPFGTYAEIERAGISLTEIDTSDCENSLISLKLLAQKLQEKDPGKLSSYTTPSGMMQLAQDAAGPVSQDSASEDGFSAAIASAIASLDNDSAGNTPKRASSMSEDETVANGLNHSLKRRLPGSFSSTGEESDNPPESSGEKRARSGQELPVPVAVPVAASAAASNXQYMYMLQPS
Protein: Autophagy-related protein 101 (F4K265)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory protein involved in autophagy. Acts as scaffold protein of the ATG1-ATG13 complex for faithful delivery of autophagic vesicles to the vacuole. Required for selective mitophagy.
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24563201}.
Interaction partners:
- Autophagy-related protein 11
- Autophagy-related protein 13a
- Autophagy-related protein 13b
- Phosphatidylinositol 3-kinase VPS34
- Serine/threonine-protein kinase ATG1b
- Serine/threonine-protein kinase ATG1c
- Serine/threonine-protein kinase VPS15
- Beclin-1-like protein
- Serine/threonine-protein kinase ATG1a
- Regulatory-associated protein of TOR 1
Sequence:
MNCEVCQLKELEVESFEIREVLRCILHTIVFHRALGLIRPKDIDLELFEITYVQCGEIEVEKKIDEKIEQFINWIEKHPNKKSQICLSFYEVKSKQPSWFTKIERLYWEQWYINLNVLQPTKPPVGKSHHSKLVMDPGEASEERSSRRTLLEQSLQEVLFQIIKFVNEKKDHVPPINDGVIYYPFEITIPSSSDSAFGMDMFKRILHSGHPSMLG
Protein: tRNA pseudouridine synthase Pus10 (EC 5.4.99.25) (tRNA pseudouridine 54/55 synthase) (Psi54/55 synthase) (Q8U1R6)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
Interaction partners:
- Probable tRNA pseudouridine synthase D
- tRNA pseudouridine synthase A
- Probable tRNA pseudouridine synthase B
- tRNA
- Ribosome biogenesis protein Nop10
- Anhydromevalonate phosphate decarboxylase
- tRNA
Sequence:
MILEKAREILEEHQLCNHCLGRLFGKLGKGTNEERGRAIRLLLSMETGKEYKEPEKCELCGGVFNNLDKFAELCIKAAEGIEFETFWVGSRFPEEIEKKEEEIWRKFRVVSGEKITKEFNRELGKVIAVRYGKTPVKERPDVVFIVEPFSEKVELQVNPIYVAGRYRKLIRGIPQTPAPGFKESIATIICRAFKKHFHGKCIFKGAGREDVDVRMLGNGRPFVVEIKRPRKRKVNLKDIEEEINQSGKVEVLNLRFITPEEAERILTTRHRKVYEAIVYVKDGITKEEVEKVVKSLKNAEIKQRTPRRVLNSRADLVRVRKVYDVKGELIDDKHFKLRLVTDGGLYIKELISGDRGRTTPSVSEILGKEAWCEILDVLEVLDDVEGDN
Protein: LD45234p (Q8MSU5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MDSEKVAKPAMEPPQPPPNASPNPPMRAQAPPEIKPRSGKIGSPVKSPPLPPIPAVKPKNVSPVKFNPDRLRQSPTKTADNSPPPPPAKSAAVLQRSLMQEQQELLRNSCDQGVAPIPPEKPRKKSVDLIEDTLPLTNCSTPSSCASPTSSYLMQPAKRGSLDGGSGNGQYPGNGLSGSTNSATSGSPVASASSGPSSPVHTEDEKQENESTEKSEMEYYHGGNYNSVPRRRRSENEGRKSVDESSPSANNSQQQQQHSIPGSAAGSPQRVANKRSSITVNMPAAGLGQRPPSIISTTSQDEGGFNESAPELKAKLQPAYDQTEEQPHSLNYVDVGYRLNPDGSESREVYGSEAELYDTAKVTDMQRKFHGANGFGQESSTVYAIIKPDVQESQPVAPSRSVLIQSPNSSSVEGSPLHRGSYSSPPVGVVSPIRRRNSSNQDQSVGGGGSAKTTPQCSPARSALVKGIAPIASIDAHEEEELDLVEEDEHLAVEYVEVLELQQDEEEEEAPVLPERRAPAQGSLELQDLEYADTSAGEDEEDIINHLKDGDVLDVELIDDVVDEVIKVHVNHSVATAPSIQAATPAAAIPREDSLPDDMTAAEAERLLSSRQQSLLSDEQAKEVEQILNAAPSVGVAVATVVATATSPTSIKNLIEDLPGQSAVAASAANGEQDIQIAAVPAIVEEDEDEEEDFPEDDEEDHARADFDANGGDADGDSDDVEAVDIVGYGHASTALNATFVKADSTETETTTTTPSTATTATTRHDDDEPEWLRDVLEAPKRSLENLLITSATSSRAPGQREELENGYDLHEKHSDLNQTYITGGESLHESIVSVESTQSDATLNQTTTIDDSIISSKHNSTYSLADAEQATSSTVLSTGVTELDDSQYYIPEYPPVRSKEVLVEAGVHYFEDGNFWMEVPGLLDFDDDDCSYPPITVRKNPKVRFSSGPIHVYSTFSVNDYDRRNEDVDPVAASAEYELEKRVEKMHVFPVELMKGPEGLGLSIIGMGVGADAGLEKLGIFVKTITDNGAAARDGRIQVNDQIIEVDGKSLVGVTQAYAASVLRNTSGLVKFQIGRERDPENSEVAQLIRLSLQADREKEERLKRQQEEYLRRTLDYSEDSTQPVSANSSVCEGPSSPVQVEHPMEVEATHSQEVESLKRLLQESEMGCLVKEEIIQNLKRKLVKLETTGNENELLSERLRQSERELGNIRKEAANLQNMLQQSQGQYMALDKKYNKAKRLVREYQQRELDMCHREEFYQQLLQEKDTEYNALVKKLKDRVINLEHELQETQRKAGFPVGLPYDSATLKLTPQMMRKTPPKPLFHKLETELSDTEISDLSPDGDGVKTATVERKVPVKDELDAAVPQHELLDNSINKTKIDLANRQLPSANGNSSTSNGAAVDLGQLSNGNLLKRSRSNSRSSDCTLDDTDEEEEREGSALNLAGAPVAHETISLSNGNSHLLANVNNLLQHHPPAMATVIATPSNGHLGTTTPILLNSTSSASSSSSNQSTAREAQINQLYAQVHKDPSKQQHQQQQQQQQQAQAVTTSIPSIFKNALGSPADNGLNDFHRGSMTTFGTGPATSSNRDLNSSYDSILGSNDKLAENDPAESWMYPSRRRVAPNGSKVPLPGSSFTDQLNQALSDRERRLGDGSSRHSSDDYTEINKSQSAAAINCKTLINEIRQAVNEAQPKVPWQQQHHQQIQQQPSAHTTGPPSPTSMSSGCSSPGYSPSRTLDLSGSSSSFSDRKAMAAGYTYKGGPVHEWTKDQVGHWLMGIELERYIPVFKENNVEGGALLTLDSKDFKTLGICGDDKHRLKKRLKDLKANIEKERKDMERERREREKAIRKAEKKAAKKK
Protein: Uncharacterized protein C212.02 (Q9HGQ0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MTALMNHIYIDNPLISNSTNNVTHELLIDLHELYNDGEISRIVLLRTLVTQSADDATWIINLTDDVLNGLPLLKKRDRYTTQCHSTNMASTYDCDTGANAVGARGGATLAADYRGDWGGGVMLYKPLVVKACLTEI
Protein: E3 ubiquitin-protein ligase Midline-1 (EC 2.3.2.27) (Midin) (RING finger protein Midline-1) (RING-type E3 ubiquitin transferase Midline-1) (Tripartite motif-containing protein 18) (O70583)
Organism: Mus musculus (Mouse)
Function: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15344}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15344}. Note=Microtubule-associated. {ECO:0000250|UniProtKB:O15344}.
Interaction partners:
- Mid1-interacting protein 1
Sequence:
METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMSSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVIRLRKLAQQIANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPAIREELCTASYDTITVHWTSEDEFSVVSYELQYTIFTGQANVVNVACDGTCLLGSAGLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFTVKAINQAGSRSSEPGKLKTNSQPFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVWNKCLTIVTGLPIPDHLDCTEQRP
Protein: UDP-N-acetylhexosamine pyrophosphorylase (Antigen X) (AGX) (Protein-pyrophosphorylation enzyme) (EC 2.7.4.-) (Sperm-associated antigen 2) (UDP-N-acetylgalactosamine pyrophosphorylase) (EC 2.7.7.83) (UDP-N-acetylglucosamine pyrophosphorylase) (EC 2.7.7.23) (Q16222)
Organism: Homo sapiens (Human)
Function: Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8025165}. Note=In spermatozoa, localized to the principal piece of the tail, the neck region of the head and to a lesser extent, the midpiece of the tail. {ECO:0000269|PubMed:8025165}.
Interaction partners:
- Phosphoacetylglucosamine mutase
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
- UDP-N-acetylhexosamine pyrophosphorylase-like protein 1
- UDP-glucose 4-epimerase
- Glucosamine 6-phosphate N-acetyltransferase
- Glutamine--fructose-6-phosphate aminotransferase 1
- Glutamine--fructose-6-phosphate aminotransferase 2
- N-acetylgalactosamine kinase
- Phosphoglucomutase-1
- UDP-glucose 6-dehydrogenase
Sequence:
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQCEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI
Protein: Ig-like domain-containing protein (Q8BVF6)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAQLARATRSPLSWLLLLFCYALRKAGGDIRVLVPYNSTGVLGGSTTLHCSLTSNENVTITQITWMKKDSGGSHALVAVFHPKKGPNIKEPERVKFLAAQQDLRNASLAISNLSVEDEGIYECQIATFPRGSRSTNAWLKVQARPKNTAEALEPSPTLILQDVAKCISANGHPPGRISWPSNVNGSHREMKEPGSQPGTTTVTSYLSMVPSRQADGKNITCTVEHESLQELDQLLVTLSQPYPPENVSISGYDGNWYVGLTNLTLTCEAHSKPAPDMAGYNWSTNTGDFPNSVKRQGNMLLISTVEDGLNNTVIVCEVTNALGSGQGQVHIIVREKPENMQQNTRLHLGYIFLIVFVLAVVIIIAALYTIRRCRHGRALQSNPSERENVQYSSVNGDCRLNMEPNSTR
Protein: Guanylate kinase 1 (AtGK1) (EC 2.7.4.8) (GMP kinase 1) (P93757)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for recycling GMP and indirectly, cGMP. Required for normal development of the gametophyte and embryo, in association with GK2.
Interaction partners:
- GMP synthase
- Hypoxanthine phosphoribosyltransferase
- Adenine phosphoribosyltransferase 5
- Adenine phosphoribosyltransferase 4
- Adenine phosphoribosyltransferase 1, chloroplastic
- Adenine phosphoribosyltransferase 3
- Adenine phosphoribosyltransferase 2
- Nucleoside diphosphate kinase II, chloroplastic
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
- Nucleoside diphosphate kinase 1
Sequence:
MGEAPAVLVDHPENGHSNGVCVKSEPENTEITVDVGDRIFLIGGTHERNNFSIGVQIYDKISNNWFSPIVLGTGPKPSKGYSAFVLEQGRILVIKKGSPRNDSIWFLEVDSPYVREQKKLLRKEVVAWSKGVRGNAEKPIVISGPSGVGKGTLISMLMKEFPSMFGFSVSHTTRSPRSMEMDGVHYHFADKKVMEKEIKDGKFLEFASVHGNLYGTSIESVEAVTDSGKRCILDIDVQGARSVRASSLDAIFIFVCPPSMKELEDRLRARGTETEEQIQKRLRNAEAEIKEGISSGIFGLILYNDNLEECYKKLKNLLGLDGLAHVNGVEIEGINLPIEYAVSKMEDKIIIQETGKETRNKIVVDISSLNGGAPGRTRGILVDAIKF