wanglab/gogpt-training-data huggingface dataset:
Protein: 14-3-3-like protein GF14 omega (General regulatory factor 2) (Q01525)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P48349}. Cytoplasm {ECO:0000250|UniProtKB:P48349}. Note=Translocates from the cytosol to the nucleus when phosphorylated. {ECO:0000250|UniProtKB:P48349}.
Interaction partners:
- Growth-regulating factor 6
- Probable E3 ubiquitin-protein ligase RHC2A
- AT3g15090/K15M2_24
- DEAD-box ATP-dependent RNA helicase 28
- Dual specificity phosphatase Cdc25
- ATPase 5, plasma membrane-type
Sequence:
MASGREEFVYMAKLAEQAERYEEMVEFMEKVSAAVDGDELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNDDHVTAIREYRSKIETELSGICDGILKLLDSRLIPAAASGDSKVFYLKMKGDYHRYLAEFKTGQERKDAAEHTLAAYKSAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDAADEIKEAAAPKPTEEQQ
Protein: Uncharacterized protein C685.03 (Q9Y7L5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MQFFGSLFVSLLGAAGLANALPSPGIPSNDKDLAIYPPVDANNTTSQDVVIDVVLFNGTEWISSRERFSLVSPGWASIYGPSGQSSVGSVLYSPILDYIDNAQLLVLDDVSFGVFSSLANSVTGYASNYTQSSSNSTSTMNSTGSVSGGSVYPTNSTTNSSISWNSSTSAATNTSSSSSSSSQSSVVSVNSEIFSYFGLSQQYVNYSTSRLCVVGTPRANMSTVSVTNNGSAVSNYTVNTNGWTSSNFKCVDDVVANIFGLDFYTAAVLSEVSILRSFALCNATTSSSLFRQIASYGVYGSFHFSSSESGSFANLIGTNNYFMTDVKSSSVVIVQSETSCSINSASMSSNTTYFYWNSTSSLSSSVFTNTTSSSNSTNSSIPTTYPSNSTTYQNITTSYPWSQPVVNITDYLSDNGDGHFVLAGDGNQTIGDFYVMNWTTIASGEYLVPFNY
Protein: Cyclic AMP-dependent transcription factor ATF-6 alpha (cAMP-dependent transcription factor ATF-6 alpha) (Activating transcription factor 6 alpha) (ATF6-alpha) [Cleaved into: Processed cyclic AMP-dependent transcription factor ATF-6 alpha] (F6VAN0)
Organism: Mus musculus (Mouse)
Function: Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane. Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22682248}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P18850}; Single-pass type II membrane protein {ECO:0000255}. Note=Translocates from the endoplasmic reticulum to the Golgi, where it is processed. {ECO:0000250|UniProtKB:P18850}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-dependent transcription factor ATF-6 alpha]: Nucleus {ECO:0000269|PubMed:22682248}. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus (PubMed:22682248). THBS4 promotes its nuclear shuttling (PubMed:22682248). {ECO:0000269|PubMed:22682248}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- DNA damage-inducible transcript 3 protein
- Vesicle-associated membrane protein-associated protein B
- X-box-binding protein 1
- Wolframin
- Membrane-bound transcription factor site-1 protease
- Cyclic AMP-dependent transcription factor ATF-5
- Serine/threonine-protein kinase/endoribonuclease IRE1
- Cyclic AMP-dependent transcription factor ATF-4
- CCAAT/enhancer-binding protein beta
Sequence:
MESPFSPVLPHGPDEDWESTLFAELGYFTDTDDVHFDAAHEAYENNFDHLNFDLDLMPWESDLWSPGSHFCSDMKAEPQPLSPASSSCSISSPRSTDSCSSTQHVPEELDLLSSSQSPLSLYGDSCNSPSSVEPLKEEKPVTGPGNKTEHGLTPKKKIQMSSKPSVQPKPLLLPAAPKTQTNASVPAKAIIIQTLPALMPLAKQQSIISIQPAPTKGQTVLLSQPTVVQLQSPAVLSSAQPVLAVTGGAAQLPNHVVNVLPAPVVSSPVNGKLSVTKPVLQSATRSMGSDIAVLRRQQRMIKNRESACQSRKKKKEYMLGLEARLKAALSENEQLKKENGSLKRQLDEVVSENQRLKVPSPKRRAVCVMIVLAFIMLNYGPMSMLEQESRRVKPSVSPANQRRHLLEFSAKEVKDTSDGDNQKDSYSYDHSVSNDKALMVLSEEPLLYMPPPPCQPLINTTESLRLNHELRGWVHRHEVERTKSRRMTNSQQKARILQGALEQGSNSQLMAVQYTETTSISRNSGSELQVYYASPGSYQGFFDAIRRRGDTFYVVSFRRDHLLLPATTHNKTTRPKMSIVLPAININDNVINGQDYEVMMQIDCQVMDTRILHIKSSSVPPYLRDHQRNQTSTFFGSPPTTTETTHVVSTIPESLQ
Protein: Large ribosomal subunit protein eL33 (60S ribosomal protein L35a) (A0A8L2QK69)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLFPPSWRLWRPAGNRTSKKTSMSGRLWCKAIFAGYKRGLRNQREHTALLKIEGVYARDETEFYLGKRCAYVYKAKNNTVTPGGKPNKTRVIWGKVTRAHGNSGMVRAKFRSNLPAKAIGHRIRVMLYPSRI
Protein: Cyclin dependent kinase 13 (A0A2R8YF61)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
IVGKESKSAATKEESVSLKEKTKPLTPSIGAKEKEQHVALVTSTLPPLPLPPMLPEDKEADSLRGNISVKAVKKEVEKKLRCLLADLPLPPELPGGDDLSKSPEEKKTATQLHSKRRPKICGPRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELIRASLCCQAGVQWRNLGSLQPLPPRFNRICGSPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPDLPLWQDCHELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDSRTNTPQGVLPSSQLKSQGSSNVAPGEKQTDPSTPQQESSKPLGGIQPSSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEASLQLRPPPEPSTPVSGQDDLIQHQDMRILELTPEPDRPRILPPDQRPPEPPEPPPVTEEDLDYRTENQHVPTTSSSLTDPHAGVKAALLQLLAQHQPQDDPKREGGIDYQAGDTYVSTSDYKDNFGSSSFSSAPYVSNDGLGSSSAPPLERRSFIGNSDIQSLDNYSTASSHSGGPPQPSAFSESFPSSVAGYGDIYLNAGPMLFSGDKDHRFEYSHGPIAVLANSSDPSTGPESTHPLPAKMHNYNYGGNLQENPSGPSLMHGQTWTSPAQGPGYSQGYRGHISTSTGRGRGRGLPY
Protein: Transmembrane protein 218 (A2RU14)
Organism: Homo sapiens (Human)
Function: May be involved in ciliary biogenesis or function.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9CQ44}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000250|UniProtKB:Q9CQ44}.
Interaction partners:
- Transmembrane protein 17
- Transmembrane protein 231
Sequence:
MAGTVLGVGAGVFILALLWVAVLLLCVLLSRASGAARFSVIFLFFGAVIITSVLLLFPRAGEFPAPEVEVKIVDDFFIGRYVLLAFLSAIFLGGLFLVLIHYVLEPIYAKPLHSY
Protein: Inner kinetochore subunit MCM21 (CENP-O homolog) (Chromosome transmission fidelity protein 5) (Constitutive centromere-associated network protein MCM21) (Minichromosome maintenance protein 21) (Q06675)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-associated proteins and the outer kinetochore. COMA interacts with other inner kinetochore proteins to form the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:29046335}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:29046335}.
Interaction partners:
- Inner kinetochore subunit CTF3
- Inner kinetochore subunit CTF19
- Inner kinetochore subunit AME1
- Inner kinetochore subunit OKP1
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit IML3
- Inner kinetochore subunit NKP2
- Inner kinetochore subunit MCM16
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit NKP1
Sequence:
MSRIDDLQQDIESLLSEINSLEESREKLKAKIKDKRKNEESANPIVQEFEDLFDQFPQLNNFLFNEHPELEETDDKDISRAQADIPATPIPYEPKKRAKLENEEILPEQEWVLKTQPMVQHQMFDPGVADLLDTDILTSPSKRKRKLKIDDISTSDRSELEDYIVLENVYRMFGITFFPLVDPIDLKIKDASGEIFVDREMLGIRLEVFSERTSQFEKPHYVLLKKRIKSNSWFLFKHTIPSFIDVQGIFDDTNGGLVISHDDAYLFAKRVFLQLVEVQKRRQIFKDLEAKKIIHDLDLDLESSMVSFFVKDIKVELFVKQNEIVSCSILDDIHDFSQNNKSKWEIALLGSLDDLELKLNHSFATIFK
Protein: Interferon-induced GTP-binding protein Mx (B5X1G2)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNYTLNQHYEEKVRPCIDLIDSLRSLGVEKDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLELKMKRKKEGEEWHGKIRYQDREEEIEDPSDVEKKIRKAQDEMAGVGVGISDDLISLEIGSPDVPDLTLIDLPGIARVAVKGQPENIGEQIKNLIRKFITKQETINLVVVPCNVDIATTEALKMAQEVDPQGGRTLGILTKPDLVDKGTEEMVVDIVHNEVIHLTKGYMIVKCRGQKEIMEQVSLTEATEREKAFFKEHLHLSTLYDEGHATIPKLAEKLTLELVQHIEKSMPRLKEQIEEKLEETRTTLEKCGTGPPEDPKERQYFLIDKVTLFTQDVINLSTGEELKSGDINIFSTLRTEFGKWKAQLDRSGKNFNKKIEKEVADYEKTYRGRELPGFINYKTFEVMVKDQIKQLEEPAVKKLKELSDVARKAFILLAQNSFTGFPILLKTAKTKIETIKQEKESTAESMLRTQFKMELIVYTQDITYSSSLRKRKREEEELEEGELVKNPSLSFGSQKVLSVFSVRSTVNGHDNHAALREMMLHLKSYYNIASQRLADQIPMVIRYLVLQEFASQLQREMLQTLQEKDNIEQLLKEDIDIGSKRASLQSKLKRLMKARSYLVEF
Protein: Cinnamyl alcohol dehydrogenase (C1IC55)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MGSLETERTTTGWAARDPSGVLSPYTYTLRNTGPEDVFVKVMCCGICHTDLHQAKNDLGMSNYPMVPGHEVVGEVLEVGSDVSKFRVGDIVGVGCLVGCCRNCRPCDSDNEQYCLKKIWSYNDVYTDGKPTQGGFAGSMVVDQKFVVKIPEGMAPEQVAPLLCAGVTVYSPLNHFGLMGSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKKVEALEHLGADDYLVSSDAEGMQKAADSLDYIIDTVPVFHPLEPYLSLLKFDGKLILTGVINTPLQFVSPMVMLGRKSITGSFIGSMKETEEMLNFCKEENLTSMIEVVKMDYINTAMERLEKNDVRYRFVVDVAGSKLDQ
Protein: Valine--tRNA ligase, mitochondrial (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (P07806)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: [Isoform Cytoplasmic]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.
Interaction partners:
- U3 small nucleolar RNA-associated protein 8
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Elongation factor 1-gamma 2
- Elongation factor 1-gamma 1
- Cysteine--tRNA ligase
- Histidine--tRNA ligase, mitochondrial
Sequence:
MNKWLNTLSKTFTFRLLNCHYRRSLPLCQNFSLKKSLTHNQVRFFKMSDLDNLPPVDPKTGEVIINPLKEDGSPKTPKEIEKEKKKAEKLLKFAAKQAKKNAAATTGASQKKPKKKKEVEPIPEFIDKTVPGEKKILVSLDDPALKAYNPANVESSWYDWWIKTGVFEPEFTADGKVKPEGVFCIPAPPPNVTGALHIGHALTIAIQDSLIRYNRMKGKTVLFLPGFDHAGIATQSVVEKQIWAKDRKTRHDYGREAFVGKVWEWKEEYHSRIKNQIQKLGASYDWSREAFTLSPELTKSVEEAFVRLHDEGVIYRASRLVNWSVKLNTAISNLEVENKDVKSRTLLSVPGYDEKVEFGVLTSFAYPVIGSDEKLIIATTRPETIFGDTAVAVHPDDDRYKHLHGKFIQHPFLPRKIPIITDKEAVDMEFGTGAVKITPAHDQNDYNTGKRHNLEFINILTDDGLLNEECGPEWQGMKRFDARKKVIEQLKEKNLYVGQEDNEMTIPTCSRSGDIIEPLLKPQWWVSQSEMAKDAIKVVRDGQITITPKSSEAEYFHWLGNIQDWCISRQLWWGHRCPVYFINIEGEEHDRIDGDYWVAGRSMEEAEKKAAAKYPNSKFTLEQDEDVLDTWFSSGLWPFSTLGWPEKTKDMETFYPFSMLETGWDILFFWVTRMILLGLKLTGSVPFKEVFCHSLVRDAQGRKMSKSLGNVIDPLDVITGIKLDDLHAKLLQGNLDPREVEKAKIGQKESYPNGIPQCGTDAMRFALCAYTTGGRDINLDILRVEGYRKFCNKIYQATKFALMRLGDDYQPPATEGLSGNESLVEKWILHKLTETSKIVNEALDKRDFLTSTSSIYEFWYLICDVYIENSKYLIQEGSAIEKKSAKDTLYILLDNALKLIHPFMPFISEEMWQRLPKRSTEKAASIVKASYPVYVSEYDDVKSANAYDLVLNITKEARSLLSEYNILKNGKVFVESNHEEYFKTAEDQKDSIVSLIKAIDEVTVVRDASEIPEGCVLQSVNPEVNVHLLVKGHVDIDAEIAKVQKKLEKAKKSKNGIEQTINSKDYETKANTQAKEANKSKLDNTVAEIEGLEATIENLKRLKL
Protein: L-lactate dehydrogenase (EC 1.1.1.27) (Q8BVP2)
Organism: Mus musculus (Mouse)
Interaction partners:
- Putative aspartate aminotransferase, cytoplasmic 2
- Pyruvate kinase PKLR
- Pyruvate kinase PKM
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Probable D-lactate dehydrogenase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- NADP-dependent malic enzyme, mitochondrial
Sequence:
MAWATSILRASRRVSTTRVDFKGFGIALWPSQVQRVPPNRAWWSLTPTSSMATVKGELIQHISSEEPVLHNKVSIVGTGSVGMACAIGIIAKGLTDELALVDNNEEKMKGETMDLQHGSVFMKMPNIVCSKDFRVTANSEVVIITAGARQEKNETRLNLVQRNVTIFKAMVAEIIKHSPRCKIIVVSNPVDILTFVTWKLSGFPKNRIIGSGCNLDTARFRYMLGQRLGIHSESCHGWVLGEHGDSSVPVWSGVNIAGVPLRELNSAIGTSKDPEKWGDVHKEVIASAYNIIKMKGYTSWAIGLSVTDIAESILKNLRKTHPVTTKIQGLYGIKEEVFLSVPCILGESGISDIIKVKLSPTEEAQMVKSAETIWKIQKDIKF
Protein: Non-catalytic caspase homolog csp-3 (G5ECW5)
Organism: Caenorhabditis elegans
Function: Non-catalytic caspase homolog which does not contain the region necessary for caspase activity. Acts as an inhibitor of caspase ced-3 zymogen autoactivation and delays ced-4-induced ced-3 processing. Has no effect on active ced-3. Probably by preventing ced-3 activation, protects cells, whose fate is to live, from apoptosis during embryonic and larval development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18776901}.
Interaction partners:
- Cell death protein 4
- Apoptosis regulator ced-9
- Cell death protein 3
- RING-type domain-containing protein
Sequence:
MFFGKLGGFAFFLQRAVRCDGFIDNFFDRIPKFFQFMKSKFPSHQTSSSQADLLVSFSTSPGFLSFKDETKDTWYIQELYRVIIENAKDTHLADLLTETNRRVVEKYEADKVVFVCKQAPEFWSRFTKQLFFMSRNDVF
Protein: Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) (Q8VDG3)
Organism: Mus musculus (Mouse)
Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (By similarity). Also able to recognize poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to leading to microRNAs degradation or snoRNA increased stability (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95453}. Cytoplasm {ECO:0000250|UniProtKB:O95453}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O95453}. Note=Some nuclear fraction is nucleolar. {ECO:0000250|UniProtKB:O95453}.
Interaction partners:
- Symplekin
- Poly
- m7GpppN-mRNA hydrolase
- Far upstream element-binding protein 2
- Poly
- Cytoplasmic polyadenylation element-binding protein 1
- Poly
- Poly
- Poly
- Neuroguidin
Sequence:
MEIIRSNFKINLHKVYQAIEEADFFAIDGEFSGISDGPSVTALTSGFDTPEERYQKLKKHSMDFLLFQFGLCAFKYDHTDSKHVTKSFNFYVFPKPFSRSSPDVKFVCQSSSIDFLASQGFDFNKVFCSGIPYLNQEEERQLREQFDEKRSQANGAGALAKCPVTIPEDQKKFIDQVIEKIEDFLQSEEKRSLELDPCTGFQRKLIYQTLSWKYPKGIHVETLETDKKERHIVISKVDEEERKRREQEKYTKEQEELNDAVGFSRVIHAIANSGKLVVGHNMLLDVMHTIHQFYCPLPADLNEFKEMAICVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFDPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSLLSPPKMCVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVQIAVNTSKYAESYRIQTYAEYVGKKQEGKQVKRKWTEDSWKEVDRKRPHMQGPCYHSNSFTAAGVLGKRTLSPDPREAALEDRESEEVSDSELEQTDSCTDPLPEGRKKSKKLKRMKKELSLAGSVSDSPAVLFEVPDTW
Protein: M cell-type agglutination protein mam3 (Adhesin mam3) (Q9HDY9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: M cell-type specific protein involved in agglutination during conjugation.
Subcellular location: Cell surface {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mating-type M-specific polypeptide Mc
Sequence:
MSIALAFFILVLLGFSWASPSALDDTFNVSRSVGLISSSNLESCQSSPLEVGNIYNSTSASEILSTLDAKYITIIGVIGSSNSSIQDLIDSVGNSNNAASSNPTSTVTEYVDRVQTVTEYVTLSCGQAFTSTVDISSSTSSSVINSPTGTAVSSQISTLSMSPSSTPVFSPSASVSSKVASSVSYVSSEPSDSSSSTNTVILTTSVNSPAVSSSETLTSVSITSTESAYTSSSVDIAASTTASSTLPVSTSEATVSFSTDIPATPSTLSSPASSSSSYLVETSSTLTDSVFTTVTATSDSSVITYTLINSVTSSSETTNLPSSSSSLVTIGESSFPSSLLSLLTQSFSTVRSTSSSSTDQLTSASPISSSVISPSVSSPTSSILTNSGSIKSGDHQIVTTSFVQTTTHGSQVETLTYVTTLTETILTTTYDSHTFLTTITPSPSNSISYTNNTFIPSSSIKSSIVYSVTPTSAENYTSSEAFSTSSSLVVIPPVNSSLVTSSTSFTKFSSLSSSQLSTENFTSASSSLSLTNAKSSLSTPSTTIPTSNSSVSLQTSSSLIISSPIISSSLTATSTSTPALTHSITPSNTSYTSSLIPSSSTDYSSSLITVCSNVTSEISSTSLASLISTLTSQQISSNKSSEFVGQTTTEYTTSGSVGFTTTLATQSGSVPGTVLVDVPTPSWITETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSIGFTTTIATPIGSTAGTVLVDVPTPSWVTETVTSGSVGFTTTIATPIGSTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVVVDVPTPSWVTETVTSGSVGFTTTIATPIGSTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPQQHATTTTTTTFDGFSGYTSSYTGSITETIVIGTPHHSVVDVS
Protein: Zinc finger protein, multitype 2 (D4A0R1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor GATA-4
- Transcription factor GATA-6
- Similar to Transcription factor GATA-5
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Erythroid transcription factor
Sequence:
MSRRKQSKPRQIKRPLEDAIEDEEEECPVEEADVIAKGDFPLEESFPTGFESENLSCEEVEFFCNKGDDEGIQEPAESDGDSHSDKPGQPGVETDDWDGPGELEVFQRDGERKIQSRQQLPVGTTWGPFAGKMDLNNNSLKTKAQVSMVLTAGPKWLLDVTWQGVEDSKNNCIVYSKGGQLWCTTTKAISEGEELIAFVVDFDSRLQTASQMTLTEGMYPARLLDSIQLLPQQAAMASILPTAIVNKDIFPCKSCGIWYRSERNLQAHLMYYCSGRQREAAPVSEENEDSTHQISSLCPFPQCTKSFSNARALEMHLTSHSGVKMEEFLPPGASLKCTVCSYTADSVINFHQHLFSHLTQAAFRCNHCHFGFQTQRELLQHQELHVPGGKLPRESDMEHSPSGTEDSLQPATDLLARSDLSQSQKAMPTKDASSDTELDKCEKKTQLFLTNQRPEMQPAANKQNFSYTKIKSEPSSPRLASSPVQPNLGPSFPVGPFLSQFAFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECNITFNNLDNYLVHKKHYCSSRWQQMAKSPEFPSVSEKIPEALSPNTGQTSINLLNPAAHPPDPENPLLQTSCINSSTVLDLIGPNGKGHEKDFSTQAKKLPTSNNNDDKINGKPVDVKNPSGPLVDGESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRPPLVQQRFLDVANLSNPCSSTQEPTEGLGECYHPRCDIFPGIVSKHLETSLAINKCVPVPKCDTTHSSVSCLEMDVPIDLSKKCLSQSERTTASPKRLLDYHECTVCKISFNKVENYLAHKQNFCPVTAHQRNDLGQLDGKVFPNPESERNSPEVSFERNMIKCEKNGNPKQPSPNGNLFSSHLATLQGLKVFSEAAQLIATKEENKHLFLPQCLYPGAIKKTKGADQLSPYYGIKPSDYIAGSLVIHNTDVEQNTNTENESPKGQASSNGCAVPKKDSLPLLPKNRGMVIVNGGLKQDERPTANPQQENISQNAQHEDGHKSPSWISENPLAANENVSPGIPCAEEQLSSIAKGVNGSTQAPSSGKYCRLCDIQFNNLSNFITHKKFYCSSHAAEHVK
Protein: Thermosome subunit alpha (Chaperonin subunit alpha) (Thermophilic factor 55 alpha) (TF55-alpha) (Thermosome subunit 1) (Q9V2S9)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
Interaction partners:
- Thermosome subunit beta
- Translation initiation factor 5A
- Thermosome subunit gamma
- TATA-box-binding protein
- Probable translation initiation factor IF-2
- Prefoldin subunit alpha
- Large ribosomal subunit protein uL4
- Proteasome subunit alpha
- Prefoldin subunit beta
- Flap endonuclease 1
Sequence:
MAAPVLLLKEGTSRTTGRDALRNNILAAKTLAEMLRSSLGPKGLDKMLIDSFGDVTITNDGATIVKDMEIQHPAAKLLVEAAKAQDAEVGDGTTSAVVLAGALLEKAESLLDQNIHPTIIIEGYKKAYNKALELLPQLGTRIDIKDLNSSVARDTLRKIAFTTLASKFIAEGAELNKIIDMVIDAIVNVAEPLPNGGYNVSLDLIKIDKKKGGSIEDSVLVKGLVLDKEVVHPGMPRRVTKAKIAVLDAALEVEKPEISAKISITSPEQIKAFLDEESKYLKDMVDKLASIGANVVICQKGIDDIAQHFLAKKGILAVRRVKRSDIEKLEKALGARIISSIKDATPEDLGYAELVEERRVGNDKMVFIEGAKNLKAVNILLRGSNDMALDEAERSINDALHALRNILLEPVILPGGGAIELELAMKLREYARSVGGKEQLAIEAFADALEEIPLILAETAGLEAISSLMDLRARHAKGLSNTGVDVIGGKIVDDVYALNIIEPIRVKSQVLKSATEAATAILKIDDLIAAAPLKSEKKGGEGSKEESGGEGGSTPSLGD
Protein: Signiferin-3.1 (P86135)
Organism: Crinia signifera (Common eastern froglet)
Function: Inhibits the formation of NO by neuronal nitric oxide synthase with an IC(50) of 81 ug/ml.
Subcellular location: Secreted {ECO:0000269|PubMed:15317042}.
Interaction partners:
Sequence:
GIAEFLNYIKSKA
Protein: DNA repair protein REV1 (EC 2.7.7.-) (A1L461)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR036573}.
Interaction partners:
Sequence:
MRRGGWRKRAENDGWETWGGYMAAKVQKLEEQFRSDAAMQKDGTSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSYIPYQLYTKQSSMQKGLSFNPVCRPEDPLPGPSNIAKQLNNRVNHIVKKIETENEVKVNGMNSWNEEDENNDFSFVDLEQTSPGRKQNGIPHPRGSTAIFNGHTPSSNGALKTQDCLVPMVNSVASRLSPASSQEEDKAEKSSTDFRDCTLQQLQQSTRNTDALRNPHRTNSFSLSPLHSNTKINGAHHSTVQGPSSTKSTSSVSTFSKAAPSVPSKPSDCNFISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKLKKMKTGRSALVVTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRAPLRPGANPQLEWQYYQNKILKGKADIPDSSLWENPDSAQANGIDSVLSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQLVPTNLNPSTCPSRPSVQSSHFPSGSYSVRDVFQVQKAKKSTEEEHKEVFRAAVDLEISSASRTCTFLPPFPAHLPTSPDTNKAESSGKWNGLHTPVSVQSRLNLSIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQAESHGDKKKEPVNGCNTGILPQPVGTVLLQIPEPQESNSDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQRQGENSTHQQSASASVPKNPLLHLKAAVKEKKRNKKKKTIGSPKRIQSPLNNKLLNSPAKTLPGACGSPQKLIDGFLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
Protein: Ubiquitin-like domain-containing protein (Q381L8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEVADFSDSADEWEATPKGPVDDAEEAANGKPKPKRPQIDQLTGEERELAGELLKLVFHLPDGSVQHREHFMGQTVSYLKAQLEDVDGLPYERTTLFFEDRQLLDPLSLNDLPFSVDGENHITVRLSN
Protein: Phosphoglycerate mutase 1 (EC 5.4.2.11) (EC 5.4.2.4) (BPG-dependent PGAM 1) (Phosphoglycerate mutase isozyme B) (PGAM-B) (Q9DBJ1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate. Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate.
Interaction partners:
- Phosphoglycerate kinase 1
- Alpha-enolase
- Gamma-enolase
- Triosephosphate isomerase
- Phosphoglycerate mutase 2
- Fructose-bisphosphate aldolase A
- Phosphoglycerate kinase 2
- Glucose-6-phosphate isomerase
- Beta-enolase
- D-3-phosphoglycerate dehydrogenase
Sequence:
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKVKK
Protein: tRNA-aminoacylation cofactor ARC1 (Acyl-RNA-complex protein 1) (GU4 nucleic-binding protein 1) (G4p1 protein) (P42) (tRNA-interacting factor ARC1) (P46672)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11726524, ECO:0000269|PubMed:15710377, ECO:0000269|PubMed:17131041, ECO:0000269|PubMed:8895587}. Note=Largely excluded from the nucleus.
Interaction partners:
- Glutamate--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Putative proline--tRNA ligase YHR020W
Sequence:
MSDLVTKFESLIISKYPVSFTKEQSAQAAQWESVLKSGQIQPHLDQLNLVLRDNTFIVSTLYPTSTDVHVFEVALPLIKDLVASSKDVKSTYTTYRHILRWIDYMQNLLEVSSTDKLEINHDLDLPHEVIEKKKKAPAGGAADAAAKADEDVSKKAKKQDHPRGKPDEETLKKLREEAKAKKAAKKAANAKQQQEQQNKAPEKPKPSAIDFRVGFIQKAIKHPDADSLYVSTIDVGDEEGPRTVCSGLVKHFPLDAMQERYVVVVCNLKPVNMRGIKSTAMVLCGSNDDKVEFVEPPKDSKAGDKVFFEGFGDEAPMKQLNPKKKIWEHLQPHFTTNDGLEVIFKDEEEKDHPVRKLTNAKGESFKVASIANAQVR