wanglab/gogpt-training-data huggingface dataset:
Protein: Lysine-specific histone demethylase 2 (EC 1.14.99.66) (Flavin-containing amine oxidase domain-containing protein 1) (Lysine-specific histone demethylase 1B) (Q8NB78)
Organism: Homo sapiens (Human)
Function: Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of GLYR1 to achieve such activity, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes.
Subcellular location: Nucleus {ECO:0000269|PubMed:30664650}. Chromosome {ECO:0000269|PubMed:30664650}. Note=Found in actively RNAPolII-transcribed gene bodies. {ECO:0000305|PubMed:30970244}.
Interaction partners:
Sequence:
MATPRGRTKKKASFDHSPDSLPLRSSGRQAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF
Protein: Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) (A0A8I6AJH7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
SRCCSPPGRVYYFNHITNASQWERPSGGSTVGGGSKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRSKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
Protein: Nuclear pore complex protein Nup155 (155 kDa nucleoporin) (Nucleoporin Nup155) (P140) (P37199)
Organism: Rattus norvegicus (Rat)
Function: Essential component of nuclear pore complex. Could be essessential for embryogenesis (By similarity). Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:15703211}. Nucleus membrane {ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}; Cytoplasmic side {ECO:0000269|PubMed:15703211}. Nucleus membrane {ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}; Nucleoplasmic side {ECO:0000269|PubMed:15703211}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis.
Interaction partners:
- Nucleoporin 205
- Nuclear pore complex protein Nup93
- Nucleoporin NUP35
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin NUP188
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup54
- Nuclear pore complex protein Nup85
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup88
Sequence:
MPSMLGSMMVASTSAPSLQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNSPTVSGMSDMDYPLQGPGLLSVPSLPEISTIRRVPLRLSWLNSLDTCSVTAMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANVQTGSGILNDSVCGGLQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPIVQIEIDNSRNILYTRSEKGVIQVYDLGHDGQGMSRVASVSQNAIVCAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHKALYSKGILLMTASENEDNDILWCVNHDTFPFQKPMMETQMTTRVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPATLPTPSNVGPILGSPMYSSSPVPTGSPYPNPSSLGTPSHGAQPPTMSTPMSAVGNPAMQAASLSGLTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERVFKSSNREITAIESSVPIQLLESVLQELKGLQEFLDRNSQFSGGPLGNPNTTAKVQQRLLGVMRPENGNTQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFTVIVGELQKEFQEQLKITTFKDLVIREKEVTGALIASLINCYIRDNAAVDGISLHLQDTCPLLYSTDDAVCSKANELLQRSRQVQSKSERERMLRESLKEYQKISNQVDLPSVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDVVGLQTFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLAQRSKDELFSIALYNWLIQADLADKLLQIASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSSAARVLSKLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAISQLDSELMDITKLYGEFADPFKLAECKLAIIHCAGYSDPILVHTLWQDIIEKELSDSVTLSSSDRMHALSLKLVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRVKSPLHLLDCIHVLLTRYVENPSLVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLH
Protein: Cell cycle regulator of non-homologous end joining (Cell cycle regulator of NHEJ) (Modulator of retrovirus infection homolog) (Q8BHZ5)
Organism: Mus musculus (Mouse)
Function: Cell-cycle-specific regulator of classical non-homologous end joining (NHEJ) of DNA double-strand break (DSB) repair, which can act both as an activator or inhibitor of NHEJ, depending on the cell cycle phase. Acts as a regulator of DNA repair pathway choice by specifically inhibiting classical NHEJ during the S and G2 phases, thereby promoting error-free repair by homologous recombination during cell cycle phases when sister chromatids are present (By similarity). Preferentially protects single-stranded overhangs at break sites by inhibiting classical NHEJ, thereby creating a local environment that favors homologous recombination (By similarity). Acts via interaction with XRCC5/Ku80 and XRCC6/Ku70 (By similarity). In contrast, acts as an activator of NHEJ during G1 phase of the cell cycle: promotes classical NHEJ in G1 phase cells via multivalent interactions that increase the affinity of DNA damage response proteins for DSB-associated chromatin. Also involved in immunoglobulin V(D)J recombination. May also act as an indirect regulator of proteasome (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BWK5}. Nucleus {ECO:0000250|UniProtKB:Q9BWK5}. Chromosome {ECO:0000269|PubMed:30017584}. Note=Nuclear localization may depend upon interaction with XRCC5/Ku80 and XRCC6/Ku70 heterodimer (By similarity). Localizes to DNA damage sites (PubMed:30017584). {ECO:0000250|UniProtKB:Q9BWK5, ECO:0000269|PubMed:30017584}.
Interaction partners:
- X-ray repair cross-complementing protein 6
- X-ray repair cross-complementing protein 5
Sequence:
METLKSKTKTRVLPSWMTAPVDERKVVSVKTATRKQTAAWAQRVGAATRAPATETVYCMNEAEMVDVALGILIEGRKQEKPWEQRSLEATDKLQLSPPCSSSPGSSSEEEDSRISSLAPGLSPPRGPEASDSPCSRSPEEEKEEEDALKYVREIFFS
Protein: BZIP domain-containing protein (F6Y6H6)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Interaction partners:
- Transcription factor protein
- Stress-activated protein kinase JNK
- Transcription factor protein
- Transcription factor protein
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
Sequence:
QNLYQVETTRDYCQAGYSDQRSLEYDFRNRNSELQGNVPQSEYQYAKTFEQPKNNDTGVLSEFRAPEEQSCISQESSVADERMTVHSSKTYTVLTSGRCASDTGYSGKNVSRGDRLLMTAMSQSLPMIRRDVRQQSPQHSIESNVLRRNSQCMNSQTQQPSSTSEGPMEPHSVATPMTAGDISQHHKMLEGVGHLKPFPHLILPPHVPSQLDQHQRILQSTSTYQRQSPKNDGYSHEMATGYDSAAILEHRRQPHIVSQAQPLQHQPTHEAQYFPQPYRPAGLPPVSTYGVYPLLPPQHHFMVKQEDSENQGNASTSHKRPSPSAAAYKATQLRDQYYLKPPPVDLDDLSDDERERMRVKRERNRVAAAKCRNRRRELLERLEKEAEQLEREQELLRESVKRLQSQKRKLGVMLDEHETSCTSKLEEETRKSPEDKTETVEAKTDDTDS
Protein: uroporphyrinogen-III synthase (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) (Q5XIF2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Porphobilinogen deaminase
- Uroporphyrinogen decarboxylase
- Delta-aminolevulinic acid dehydratase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Amine oxidase
- Ferrochelatase
- 5-aminolevulinate synthase, non-specific, mitochondrial
- Endonuclease V
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Mitochondrial glycine transporter
Sequence:
MKVLLLKDAKDDDSGQDPYIQELRLCGLEATLIPVLSFEFMSLPSLSEKLSHPEGFGGLIFTSPRAVEAVKLCLEKDNKTEAWEKSLKDRWNAKSVYVVGSATASLVNKIGLDAEGAGSGNAEKLAEYICSKPSSELPLLFPCGTIKGDTLPKMLRDKGIPMESMHVYQTIPHPGIQGSLESYYENQGIPASITFFSPSGLKYSLEYIQALSGGSFDQIKFVAIGPSTTRAMAAKGLPVSCTAESPTPQALAAGIRKALKPNSCC
Protein: FACT complex subunit POB3 (Facilitates chromatin transcription complex subunit POB3) (Q5ALL8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q04636}. Chromosome {ECO:0000250|UniProtKB:Q04636}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000250|UniProtKB:Q04636}.
Interaction partners:
- FACT complex subunit SPT16
- RNA polymerase-associated protein LEO1
- Cdc73p
- RNA polymerase-associated protein CTR9
- RNA polymerase II-associated protein 1
- Rtf1p
- Transcription elongation factor SPT5
- Transcription elongation factor SPT6
- Transcription elongation factor SPT4
- Histone H4
Sequence:
MVNTDFEKIYLNQSRAGGRMRIAESGLGWKASASSGSTSQPFLLPREEILIASWSRGSKGYELRVQTKNKGVVSLDGFDHDDFTQLKQELTRNFHINLEHREHSLRGWNWGKTDLARNELIFNVNNKPAFEIPYSDISNSNLTGKNEVALEFNLDNNKNGDEIVEMRFYVPGTIENETTIVKNETNGDVIEEAVVNETSAAQQFYEQLKDKADIGQVAGEAIVSFSDVLFLTPRGRYDIDMYPSSLRLRGKTYDYKIQYEQIERIFSLPKPDETHHLIVLQIDPPLRQGQTRYPFLVLQFVKDEETELELNVSDEDFEKKYKDRLKKTYDAPTNVVMSHCLRGLTERKLITPGAFQSRYLQAGVPCSVKASEGYLFPLDRCFLFVTKPTLYIPYSEISSVVMSRTGGGVSASRTFDLEVNVIGSNQPHVFSNIDREEQEFIESFCKEKGVKVKNEEKIAKARLAKALEQEANDDDDEDADMGSAGDEDEDEDVDFQSGSDSDVAEEFDSDAAPSSDDDEEMADSKETDDRPPKKKAKN
Protein: Glycine amidinotransferase, mitochondrial (EC 2.1.4.1) (L-arginine:glycine amidinotransferase) (Transamidinase) (Q9D964)
Organism: Mus musculus (Mouse)
Function: Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- Antizyme inhibitor 2
- Guanidinoacetate N-methyltransferase
- Serine hydroxymethyltransferase, cytosolic
- Arginase-2, mitochondrial
- Alanine--glyoxylate aminotransferase
- Arginase-1
- Glycine N-methyltransferase
- Nitric oxide synthase 3
- Sarcosine dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
Sequence:
MLRVRCLRGGSRGAEAVHYIGSRLGGSLTGWVQRTFQSTQAATASSRNSCAAEDKATHPLPKDCPVSSYNEWDPLEEVIVGRAENACVPPFTVEVKANTYEKYWPFYQKNGGLYFPKDHLKKAVAEVEEMCNILSMEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILMVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYDQNYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGPGLVLSNPDRPCHQIDLFKKAGWTIVTPPTPVIPDDHPLWMSSKWLSMNVLMLDEKRVMVDANEVPIQKMFEKLGISTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYFD
Protein: Dehydrin Rab18 (P30185)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Dehydrin family protein
- Low-temperature-induced 65 kDa protein
- At4g38410
- 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal
- Dehydrin HIRD11
- Aspartyl/glutamyl-tRNA
- RING-H2 finger protein ATL18
- Low-temperature-induced 78 kDa protein
- Late embryogenesis abundant protein 7
- Late embryogenesis abundant protein
Sequence:
MASYQNRPGGQATDEYGNPIQQQYDEYGNPMGGGGYGTGGGGGATGGQGYGTGGQGYGSGGQGYGTGGQGYGTGTGTEGFGTGGGARHHGQEQLHKESGGGLGGMLHRSGSGSSSSSEDDGQGGRRKKGITQKIKEKLPGHHDQSGQAQAMGGMGSGYDAGGYGGEHHEKKGMMDKIKEKLPGGGR
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (O77306)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Pre-mRNA-splicing factor CEF1, putative
- Serine/arginine-rich splicing factor 4
- RNA-binding protein, putative
- Splicing factor 1
- Protein serine/threonine kinase-1
- U1 small nuclear ribonucleoprotein 70 kDa homolog, putative
- Alternative splicing factor ASF-1, putative
- Serine/arginine-rich splicing factor 1
Sequence:
MSFSNTCSLSNNSNSSSSSEDATSGKLQYTESDDEGSDEYCEGGYHPVKINEIYNDRYRIEGKLGWGHFSTVWVATDLKSKPLKFVAIKIQKGSETYTESAKCEINYLNTVKVNSFDSSWVELKEQQRERLFHYNMTKGVVSFIDSFEHKGPNGTHICMVFEFMGPNLLSLIKHYDYKGIPLNLVRKIATHVLIGMQYLHDVCKIIHSDIKPENVLVSPLTTIPKPKDYTKDKLESNKSNQVEKKENDQNVDKKLITTMNNNINTNLSEKKKVINDTQKNDKNIEYDQKCTSSKENIEDNVSFVNDPSDPNQKNNLNNNITDNNIIPSNVQIEKQSTLSKNKKNEKDSYININNSLTNDDQNLKREDIKFNDKAEGITKYDMLNIKNNISIKEKINDCHSPNENKNKDNHNQCEDNSINICNNKNNNIQTNNINDNTVNEKINNTSKKDMLNNTQNNNDSEKNDVVIEQQLVNEDILKKKNKQTKKKKNINEPPYVKHKLRPSNSDPSLLTSYSNIHALQETLTRKPYHYNTYFLNNPEKYRDNKMNPYLHRLPNDCLKKIDQDDSDETEEEDDLSDVDQNKEQNKNQLEVNLPNNKYPNSNDVYKFFEKDINKFPIYCDMFNHLIHPEALRLHELYMKNKKNIDSNNTMNDLGNNQNSHKVVYINTEDGEYCIRPYDPSVYYHEKSCYKICDLGNSLWIDESRYAEIQTRQYRAPEVILKSGFNETADIWSFACMVFELVTGDFLFNPQKGDRYDKNEEHLSFIIEVLGNIPKHMIDAGYNSHKYFNKNNYRLKNIRNIKKYGLYKILKYKYNLPEKEISPLCSFLLPMLSVDPQTRPSAYTMLQHPWLNMVSLEEGDDMYINDESYSINNDRNMKNNSNSNNFIYDGHNSSKNKNSSNKKKIDVNYKIGNNGNNAYNDNYYNKNYKNNKNNKNFNDDVVEPSPDQYMHANYNNDIVHAVLYEKPYNSNNVISYTNNKGHKNNFDINYLQHRNDNNSNKQNISLTTNDYTFNSDYIANMMDHDTYRKQIIKNIPAHQISKLKDGKNFKAYNESIQYEMHDFQQYNEHDFEYKFNKRFEHAHHIKEMKHNDDDYEEEDEDEDDDDEDYESDVDYDDDDEYDEGQEHDADQDEKNNDNEKQQEQQNYGEKYNYEHYENNMGYNKNIQQLSYTNNNDDENNFCETQNIYILQNKRDINFKECTPRNNINKEIKSDKYQSSKVINQKDNYWNYKIKENTKLREHAKKQHYSNNNNINKNDNTNIMNQIDTKDQISKNLHDLSTNNNMDQKHGALQKMHMNEKTNQDKPLNDEEILIENRDDQNVNKINCKVINKKNSCAYT
Protein: Guanine nucleotide exchange factor MSS4 (Rab-interacting factor) (P47224)
Organism: Homo sapiens (Human)
Function: Guanine-nucleotide-releasing protein that acts on members of the SEC4/YPT1/RAB subfamily. Stimulates GDP release from both YPT1, RAB3A and RAB10, but is less active on these proteins than on the SEC4 protein. Might play a general role in vesicular transport.
Interaction partners:
- Ras-related protein Rab-8A
- Growth factor receptor-bound protein 2
- Son of sevenless homolog 1
- Lymphocyte cytosolic protein 2
- Cell division control protein 42 homolog
- Son of sevenless homolog 2
- Ras-related protein Rab-1B
- ADP-ribosylation factor 1
- Transforming protein RhoA
- Proto-oncogene DBL
Sequence:
MEPAEQPSELVSAEGRNRKAVLCQRCGSRVLQPGTALFSRRQLFLPSMRKKPALSDGSNPDGDLLQEHWLVEDMFIFENVGFTKDVGNIKFLVCADCEIGPIGWHCLDDKNSFYVALERVSHE
Protein: Endopolygalacturonase B (EC 3.2.1.15) (Pectinase B) (Polygalacturonase B) (P35335)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pectinesterase
- galacturonan 1,4-alpha-galacturonidasegalacturonohydrolase)
- Probable pectinesterase A
- Pectinesterase
- Probable pectate lyase A
- Probable endopolygalacturonase D
- galacturonan 1,4-alpha-galacturonidase
- Endopolygalacturonase I
- Pectate lyase
- galacturonan 1,4-alpha-galacturonidase
Sequence:
MQLLQSSVIAATVGAALVAAVPVELKARDSCTFTSAADAKSGKTSCSTITLSNIEVPAGETLDLTGLNDGTTVIFSGETTFGYKEWEGPLISVSGTNIKVQQASGAKIDGDGSRWWDGKGGNGGKTKPKFFYAHKLDSSSITGLQIYNTPVQGFSIQSDNLNITDVTIDNSAGTAEGHNTDAFDVGSSTYINIDGATVYNQDDCLAINSGSHITFTNGYCDGGHGLSIGSVGGRSDNTVEDVTISNSKVVNSQNGVRIKTVYDATGTVSNVKFEDITLSGITKYGLIVEQDYENGSPTGTPTNGIKVSDITFDKVTGTVESDATDIYILCGSGSCTDWTWSGVSITGGKTSSKCENVSTGASC
Protein: FI06461p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9VL01)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MILLNCLVICLCIFSCGAQDSSLDKLISDIFKTDETPKPSSPPPPVVNPKDSSGSTGSENGGSSSTQYQSCGDQKECVPRWLCANDTINTSGDGIIDIRLGTDAECKNYLDLCCDLPNKRKDPIFEFKPDHPEGCGYQNPNGVGFKITGAVNQEAEFGEFPWMLAILREEGNLNLYECGGALIAPNVVLTAAHCVHNKQPSSIVVRAGEWDTQTQTEIRRHEDRYVKEIIYHEQFNKGSLYNDVAVMLLESPFTLQENIQTVCLPNVGDKFDFDRCYATGWGKNKFGKDGEYQVILKKVDMPVVPEQQCETNLRETRLGRHFILHDSFICAGGEKDKDTCKGDGGSPLVCPIAGQKNRFKSAGIVAWGIGCGEVNIPGVYASVAKLRPWIDAKLKIWSIDPRHYTP
Protein: GEO10195p1 (IP03664p) (Q8IPA4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO10302p1
- E2 ubiquitin-conjugating enzyme
- trypsin
Sequence:
MRCLAFIAFCLSALLAMAVGQVFQYSCPCPRNYDPVCGSDSVTYSNQCVLDCLIKEGRSITVEKKGRC
Protein: Large ribosomal subunit protein uL2m (60S ribosomal protein L2, mitochondrial) (P92812)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion.
Interaction partners:
- Small ribosomal subunit protein uS14c
- 60S ribosomal protein L29
- Os06g0683200 protein
- Large ribosomal subunit protein uL5c
- Os08g0116500 protein
- Large ribosomal subunit protein bL27c
- Os01g0220300 protein
- Large ribosomal subunit protein bL33c
- Os04g0501000 protein
- Os01g0348700 protein
Sequence:
MRQSIKGRALRHFTLSTGKSAGRNSSGRITVFHRGGGSKRLQRKIDLKRSTSSIGIVERIEYDPNRSSRIALVRWIEGVLPGRQRKFKTIEEFALPRKILESTTATIFCLFSFSSLSSPLAQGETASLSFGSSLGFPRIAVAGAKPAFFAERMREKKIGKKTFSLCEIRKWRTHCVLWAHRIKRKAALSWQSLRQQKTLELVGAAEHNESKLKADQGSLLPRQVLAYALCSGRPSYLHASRSFYKALLPVEASRFGSLPAKPPIGEGPKDGAYKVDRAPVTYILASHQLEAGNMVINCDCSKPSKSGFLRPAQNAHTYLRFQELGRTVNKGRVEGGSQLAASWPRPPAYRHEILDLNSKVGNSIPLADIRMGTWVHDIECHPGQGAKLARAAGTYAKIIKEPASQCLVRLPSGVEKLIDSRCRATIGIVSNPNHGARKLRKAGQSRWSGRRPIVRGVAMNPVDHPHGGGEGRTKGGRPSVSPWGKPTKAGFRAGVGVGKRRI
Protein: Adiponectin (cDNA FLJ78108, highly similar to Homo sapiens adiponectin, C1Q and collagen domain containing (ADIPOQ), mRNA) (A8K660)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLLLGAVLLLLALPGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN
Protein: Exonuclease 3'-5' domain-containing protein 2 (EC 3.1.11.1) (3'-5' exoribonuclease EXD2) (EC 3.1.13.-) (Exonuclease 3'-5' domain-like-containing protein 2) (Q9NVH0)
Organism: Homo sapiens (Human)
Function: Exonuclease that has both 3'-5' exoribonuclease and exodeoxyribonuclease activities, depending on the divalent metal cation used as cofactor. In presence of Mg(2+), only shows 3'-5' exoribonuclease activity, while it shows both exoribonuclease and exodeoxyribonuclease activities in presence of Mn(2+). Acts as an exoribonuclease in mitochondrion, possibly by regulating ATP production and mitochondrial translation. Also involved in the response to DNA damage. Acts as 3'-5' exodeoxyribonuclease for double-strand breaks resection and efficient homologous recombination. Plays a key role in controlling the initial steps of chromosomal break repair, it is recruited to chromatin in a damage-dependent manner and functionally interacts with the MRN complex to accelerate resection through its 3'-5' exonuclease activity, which efficiently processes double-stranded DNA substrates containing nicks. Also involved in response to replicative stress: recruited to stalled forks and is required to stabilize and restart stalled replication forks by restraining excessive fork regression, thereby suppressing their degradation.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:29599527, ECO:0000269|PubMed:31127291}; Single-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:31127291}. Mitochondrion matrix {ECO:0000269|PubMed:29335528}. Nucleus {ECO:0000269|PubMed:26807646}. Chromosome {ECO:0000269|PubMed:26807646, ECO:0000269|PubMed:31255466}. Note=Mainly localizes to the mitochondrial outer membrane (PubMed:29599527, PubMed:31127291). May translocate to the nucleus in response to DNA damage; however mechanism that explain nuclear localization are unknown and require experimental evidences (PubMed:26807646). Recruited to replication forks following replication stress (PubMed:31255466). {ECO:0000269|PubMed:26807646, ECO:0000269|PubMed:29599527, ECO:0000269|PubMed:31127291, ECO:0000269|PubMed:31255466}.
Interaction partners:
- Transmembrane protein 214
- CCR4-NOT transcription complex subunit 2
- Protein transport protein Sec61 subunit beta
Sequence:
MSRQNLVALTVTTLLGVAVGGFVLWKGIQRRRRSKTSPVTQQPQQKVLGSRELPPPEDDQLHSSAPRSSWKERILKAKVVTVSQEAEWDQIEPLLRSELEDFPVLGIDCEWVNLEGKASPLSLLQMASPSGLCVLVRLPKLICGGKTLPRTLLDILADGTILKVGVGCSEDASKLLQDYGLVVRGCLDLRYLAMRQRNNLLCNGLSLKSLAETVLNFPLDKSLLLRCSNWDAETLTEDQVIYAARDAQISVALFLHLLGYPFSRNSPGEKNDDHSSWRKVLEKCQGVVDIPFRSKGMSRLGEEVNGEATESQQKPRNKKSKMDGMVPGNHQGRDPRKHKRKPLGVGYSARKSPLYDNCFLHAPDGQPLCTCDRRKAQWYLDKGIGELVSEEPFVVKLRFEPAGRPESPGDYYLMVKENLCVVCGKRDSYIRKNVIPHEYRKHFPIEMKDHNSHDVLLLCTSCHAISNYYDNHLKQQLAKEFQAPIGSEEGLRLLEDPERRQVRSGARALLNAESLPTQRKEELLQALREFYNTDVVTEEMLQEAASLETRISNENYVPHGLKVVQCHSQGGLRSLMQLESRWRQHFLDSMQPKHLPQQWSVDHNHQKLLRKFGEDLPIQLS
Protein: KIAA0007-like protein (WD repeat domain 43) (WD repeat-containing protein 43) (Q8JHG6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAADGGRAALPCAFSPKSHQFLALCAQDGRLRIWNTESKTLQQEYVPSAHLSAACTCVTWGPCRAVQEVPQRKRRKCDAASSAEQSDLLALGTAAGTILIYSTLKGDLHCTLDGGHSGPVNSVQWHPEDSVLYSGSDDTHIAEWDLKTGKVCCKWKADRSAISSLCISPDGKMLLSAGMTIKMWDLETKEVYRKFTGHSTMVTTLCFATTRPPDSNGMYFLSGAVHDRLLSVWQVRSDGKDKNSVVSFTLTDEPQHIDLQTSNSKDEAVRLAVVCKDGQLHLFEHFLNGQCKKPLSPACSLQVSTMKGESPVPVPLLAAALCADRQNLMLAYGHHLQPVMEKTPFNTSERHTCLNRDVHATLSLSVDTTVSKVKTPVVNQQSKVLIPGVPGHKAPIKLTPNEGEKRKKGASTTEVSIEERLEQIELSAGRKGADKGSSSLQTDSFAVLLVQGLESKDEKILNKIFQTKKETLIKNTVARLPPPAVLPLLEELSRRLQGHPYAALLIVHWFKAVLTQHTSYLSSLPDLVSQLGSIYQMIESRVKLYHQITRLHGKLYLLMTQVATSNSATKVGEIDHTAKLVYEEESSEDEDSGDEGRPEDDSDNWEEDEEAMEVTGDKKNHKDEEDQDMNEESKANGDSDLDPENESEEE
Protein: Probable pyridoxal 5'-phosphate synthase subunit SNZ2 (PLP synthase subunit SNZ2) (EC 4.3.3.6) (PDX1 homolog 2) (Pdx1.2) (P53824)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit SNZ1
- Probable pyridoxal 5'-phosphate synthase subunit SNO2
- Probable pyridoxal 5'-phosphate synthase subunit SNO3
- Pyridoxal 5'-phosphate synthase subunit SNO1
- Probable pyridoxal 5'-phosphate synthase subunit SNZ3
- Pyridoxamine 5'-phosphate oxidase
- Putative pyridoxal kinase BUD16
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI5
- Putative pyridoxal kinase BUD17
- Uncharacterized protein YGR017W
Sequence:
MSEFKVKTGLAQMLKGGVIMDVVTPEQAIIAERAGACAVMALERIPADMRKSGQVCRMSDPRMIKEIMEAVSIPVMAKVRIGHFVEAQILEELQVDYIDESEVLTPADWTHHIEKHNFKVPFVCGAKDLGEALRRINEGAAMIRTKGEAGTGDVSEAVKHITKIKAEIQQYKENLKTESDFAAKATELRVPVDLLKTTLSEGKLPVVNFAAGGVATPADAALLMQLGCEGVFVGSGIFKSSDPEKLACAIVEATTHYDNPAKLLQISSDLGDLMGGISIQSINEAGGKNGARLSEIGW