wanglab/gogpt-training-data huggingface dataset:
Protein: Single-stranded DNA-binding protein, mitochondrial (Q84J78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to ss-DNA.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Eukaryotic translation initiation factor 4C
- Eukaryotic translation initiation factor 4C
- Nucleic acid-binding, OB-fold-like protein
- At5g02050
- Large ribosomal subunit protein bL21m
- Single-stranded DNA-binding protein WHY2, mitochondrial
- Putative DNA-binding protein At1g48610
- At5g12410
- DNA-directed primase/polymerase protein
Sequence:
MNSLAIRVSKVLRSSSISPLAISAERGSKSWFSTGPIDEGVEEDFEENVTERPELQPHGVDPRKGWGFRGVHRAIICGKVGQAPLQKILRNGRTVTIFTVGTGGMFDQRLVGATNQPKPAQWHRIAVHNEVLGSYAVQKLAKNSSVYVEGDIETRVYNDSISSEVKSIPEICVRRDGKIRMIKYGESISKISFDELKEGLI
Protein: (R)-citramalyl-CoA lyase (EC 4.1.3.46) (A9WGE2)
Organism: Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Function: Involved in the glyoxylate assimilation cycle used to regenerate acetyl-CoA and produce pyruvate as universal precursor for biosynthesis. Catalyzes the cleavage of (R)-citramalyl-CoA to yield acetyl-CoA and pyruvate.
Interaction partners:
- Enoyl-CoA hydratase/isomerase
- Acetaldehyde dehydrogenase
- Succinyl-CoA--D-citramalate CoA-transferase
- GntR domain protein
- Ketol-acid reductoisomerase
- Propionyl-CoA carboxylase
- Dihydroxy-acid dehydratase
- Isocitrate/homoisocitrate dehydrogenase
- 3-isopropylmalate dehydrogenase
Sequence:
MEAVTIVDVAPRDGLQNEPDVLEPATRVELIERLLAAGVPRIEIGSFVNPRQVPQMAGIDQIARMLIERGHNLAARTTNDLFRFTALVPNQRGYELAAAAGLRHVRLVLAASDGLNRANFKRTTAESLIEFSRFALNIRRDGLTFGVAIGAAFGCPFDGYVSPERVRAIAEHAVDIGAGEIILADTTGMAVPTQVAALCRTILDRIPDVTVTLHLHNTRNTGYANAFAAWQVGIRSFDAALGGIGGCPFAPRAVGNIASEDLVHLFNGLGVPTGIDLSALIAASDWLSATLGRPLPALVGKAGPVYPQVVSMAPYLS
Protein: Protein FAM9C (Q8IZT9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:12213195}.
Interaction partners:
Sequence:
MAAKDQLEVQVMAAQEMELAGKDPVSHEHEERKPVTETKEGDVTDEHGERGSFAETDEHTGVDTKELEDIAADIKEHLAAKRKRIEKIAKACSEIKNRIKNVLRTTQLKRQKRDYRISLKLPNVLEEFITDEQKDEEGDGEKEEQIKIFQEQQKRWQQDGKGTERD
Protein: Spliceosome RNA helicase DDX39B (EC 3.6.4.13) (56 kDa U2AF65-associated protein) (ATP-dependent RNA helicase p47) (DEAD box protein UAP56) (HLA-B-associated transcript 1 protein) (Q13838)
Organism: Homo sapiens (Human)
Function: Involved in nuclear export of spliced and unspliced mRNA. Assembling component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May undergo several rounds of ATP hydrolysis during assembly of TREX to drive subsequent loading of components such as ALYREF/THOC and CHTOP onto mRNA. Also associates with pre-mRNA independent of ALYREF/THOC4 and the THO complex. Involved in the nuclear export of intronless mRNA; the ATP-bound form is proposed to recruit export adapter ALYREF/THOC4 to intronless mRNA; its ATPase activity is cooperatively stimulated by RNA and ALYREF/THOC4 and ATP hydrolysis is thought to trigger the dissociation from RNA to allow the association of ALYREF/THOC4 and the NXF1-NXT1 heterodimer. Involved in transcription elongation and genome stability.
Subcellular location: Nucleus. Nucleus speckle. Cytoplasm. Note=Can translocate to the cytoplasm in the presence of MX1. TREX complex assembly seems to occur in regions surrounding nuclear speckles known as perispeckles.
Interaction partners:
- THO complex subunit 5
- THO complex subunit 6
- SAP domain-containing ribonucleoprotein
- THO complex subunit 4
- Chromatin target of PRMT1 protein
- THO complex subunit 2
- THO complex subunit 3
- Eukaryotic initiation factor 4A-III
- THO complex subunit 1
- THO complex subunit 7
Sequence:
MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDISSYIEQTR
Protein: Materazzi (Q9W0L3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRFIGCAFLGFMCLVAFPSATPAILAPIRPYGQNGTLAQQNNFALELKSVIRQIPVDNIEKLVQTYLLNDIEFQGVIRAINSLPAYRFYRQLINQPEVRQLQQWITQQLILSGGGPKIFDYLELEIKILNKYPYWSQIVNGIQGFQAEFVQIYPVQLIRSFLEPSATQTSPQLSELWRRLVALRPVYERVLATPPGKAITAELQRLGVDVGGVDALIRYQFGWSNVTFPSYDYTDYLY
Protein: Transcriptional regulator QRICH1 (Glutamine-rich protein 1) (Q3UA37)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that acts as a mediator of the integrated stress response (ISR) through transcriptional control of protein homeostasis under conditions of ER stress. Controls the outcome of the unfolded protein response (UPR), an ER-stress response pathway that either promotes recovery of ER homeostasis and cell survival, or triggers the terminal UPR which elicits programmed cell death when ER stress is prolonged and unresolved. ER stress induces QRICH1 translation by a ribosome translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced QRICH1 regulates a transcriptional program associated with protein translation, protein secretion-mediated proteotoxicity and cell death during the terminal UPR (By similarity). May cooperate with ATF4 transcription factor signaling to regulate ER homeostasis which is critical for cell viability (By similarity). Up-regulates CASP3/caspase-3 activity in epithelial cells under ER stress. Central regulator of proteotoxicity associated with ER stress-mediated inflammatory diseases in the intestines and liver. Involved in chondrocyte hypertrophy, a process required for normal longitudinal bone growth.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q2TAL8}. Cytoplasm {ECO:0000250|UniProtKB:Q2TAL8}. Cell membrane {ECO:0000250|UniProtKB:Q2TAL8}.
Interaction partners:
- Glutamine-rich protein 2
- GMP synthase
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MNNSLENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQTATTTMVYQQGGNCIYTDSTEVAGSLLELACPVTTSVQPQTQQEQQIQVQQPQQVQVQVQVQQSPQQVSAQQLSPQFTVHQPAEQPIQVQVQIQGQAPQSAAPSIQTPSLQSPSPSQLQAAQIQVQHVQAAQQIQAAEIPEEHIPHQQIQAQLVAGQSLAGGQQIQIQTVGALSPPPSQQGSPREGERRVGTASVLQPVKKRKVDMPITVSYAISGQPVATVLAIPQGQQQSYVSLRPDLLTVDSAHLYSATGTITSPTGETWTIPVYSAQPRGDPQQQSITHIAIPQEAYNAVHVSGSPKALAAVKLEDDKEKMVGTTSVVKNSHEEVVQTLANSLFPAQFMNGNIHIPVAVQAVAGTYQNTAQTVHIWDPQQQPQQQTAQEQTPPPQQQQQQLQVTCSAQTVQVAEVEPQSQPQPSPELLLPNSLKPEEGLEVWKNWAQTKNAELEKDAQNRLAPIGRRQLLRFQEDLISSAVAELNYGLCLMTREARNGEGEPYDPDVLYYIFLCIQKYLFENGRVDDIFSDLYYVRFTEWLHEVLKDVQPRVTPLGYVLPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKSPSNPKDKSTSIRYLKALGIHQTGQKVTDDMYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQMLTRILVIREIQEAIAVANATTMH
Protein: Ethylene-responsive transcription factor 7 (AtERF7) (Ethylene-responsive element-binding factor 7) (EREBP-7) (Q9LDE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of gene expression by abscisic acid, stress factors and by components of stress signal transduction pathways. Transcription factor that binds to the GCC-box pathogenesis-related promoter element. Part of a transcriptional repressor complex including a histone deacetylase.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:15994908}.
Interaction partners:
- Paired amphipathic helix protein Sin3-like 3
- Histone deacetylase 19
- Paired amphipathic helix protein Sin3-like 2
- Histone deacetylase complex subunit SAP18
- Histone deacetylase HDT3
Sequence:
MRKGRGSSVVGPALPVTAGGSVKEPRYRGVRKRPWGRFAAEIRDPLKKSRVWLGTFDSAVDAARAYDTAARNLRGPKAKTNFPIDCSPSSPLQPLTYLHNQNLCSPPVIQNQIDPFMDHRLYGGGNFQEQQQQQIISRPASSSMSSTVKSCSGPRPMEAAAASSSVAKPLHAIKRYPRTPPVAPEDCHSDCDSSSSVIDDGDDIASSSSRRKTPFQFDLNFPPLDGVDLFAGGIDDLHCTDLRL
Protein: 40S ribosomal protein S6 (Q38CL9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S13, putative
- 40S ribosomal protein S24
- 40S ribosomal protein S33, putative
- 40S ribosomal protein S18, putative
- 40S ribosomal protein S25
- 40S ribosomal protein S17, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S27, putative
- 40S ribosomal protein S15, putative
Sequence:
MKLNVAYPRNGTVKQVEVTDEVLRRVNLGDYRLGNEVDGAIFGEAFRGYTFKLRGGSDKEGFPMVQGVMAPSRVSLLVKRGAVGFNTFRGYQGERRRKSLRGCILGSDIAVLNVTVEKVGEQPIEGVTDVSVPRRLGPKRANKIRKLFNLGRTDDVRKYVIRRKVTKEGKKDRFKAPKIQRLITSTIRARRAKKVRVAIDKVRKSAAERREYLRLVGARRRAARQRKAARHHSSRVNAQRKEVDAFKARK
Protein: DNA topoisomerase 2 (EC 5.6.2.2) (DNA topoisomerase II) (P08096)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks.
Subcellular location: Nucleus.
Interaction partners:
- DNA topoisomerase 1
- Structural maintenance of chromosomes protein 2
- Structural maintenance of chromosomes protein 6
- Structural maintenance of chromosomes protein 4
- Structural maintenance of chromosomes protein 5
- Probable tyrosyl-DNA phosphodiesterase
- DNA topoisomerase 3
- Separin
- Double-strand break repair protein rad32
- Condensin complex subunit 2
Sequence:
MSIDADFSDYEDEASGDENVLPNTTTKRKASTTSSKSRAKKASTPDLRQTSLTSMTASEQIPLVTNNGNGNSNVSTQYQRLTPREHVLRRPDTYIGSIEPTTSEMWVFDSEKNKLDYKAVTYVPGLYKIFDEIIVNAADNKVRDPNMNTLKVTLDPEANVISIYNNGKGIPIEIHDKEKIYIPELIFGNLLTSSNYDDNQKKVTGGRNGYGAKLCNIFSTEFVVETADKERMKKYKQTWYDNMSRKSEPVITSLKKPDEYTKITFKPDLAKFGMDKIDDDMVSIIKRRIYDMAGTVRETKVYLNNERISISGFKKYVEMYLASDTKPDEEPPRVIYEHVNDRWDVAFAVSDGQFKQVSFVNNISTIRGGTHVNYVANKIVDAIDEVVKKENKKAPVKAFQIKNYVQVFVNCQIENPSFDSQTKETLTTKVSAFGSQCTLSDKFLKAIKKSSVVEEVLKFATAKADQQLSKGDGGLRSRITGLTKLEDANKAGTKESHKCVLILTEGDSAKSLAVSGLSVVGRDYYGVFPLRGKLLNVREASHSQILNNKEIQAIKKIMGFTHKKTYTDVKGLRYGHLMIMTDQDHDGSHIKGLIINYLESSYPSLLQIPGFLIQFITPIIKCTRGNQVQAFYTLPEYEYWKEANNNGRGWKIKYYKGLGTSDHDDMKSYFSDLDRHMKYFHAMQEKDAELIEMAFAKKKADVRKEWLRTYRPGIYMDYTQPQIPIDDFINRELIQFSMADNIRSIPSVVDGLKPGQRKVVYYCFKRNLVHETKVSRLAGYVASETAYHHGEVSMEQTIVNLAQNFVGSNNINLLMPNGQFGTRSEGGKNASASRYLNTALSPLARVLFNSNDDQLLNYQNDEGQWIEPEYYVPILPMVLVNGAEGIGTGWSTFIPNYNPKDITANLRHMLNGEPLEIMTPWYRGFRGSITKVAPDRYKISGIINQIGENKVEITELPIRFWTQDMKEYLEAGLVGTEKIRKFIVDYESHHGEGNVHFNVTLTEAGMKEALNESLEVKFKLSRTQATSNMIAFDASGRIKKYDSVEDILTEFYEVRLRTYQRRKEHMVNELEKRFDRFSNQARFIHMIIEGELVVSKKKKKDLIVELKEKKFQPISKPKKGHLVDLEVENALAEEEQSGDVSQDEDSDAYNYLLSMPLWSLTYERYVELLKKKDEVMAELDALIKKTPKELWLHDLDAFEHAWNKVMDDIQREMLEEEQSSRDFVNRTKKKPRGKSTGTRKPRAIAGSSSSTAVKKEASSESKPSTTNRKQQTLLEFAASKEPEKSSDINIVKTEDNSHGLSVEENRISKSPGLDSSDSGKSRKRSQSVDSEDAGSKKPVKKIAASASGRGRKTNKPVATTIFSSDDEDDLLPSSLKPSTITSTKASAKNKGKKASSVKKQSPEDDDDDFIIPGSSSTPKASSTNAEPPEDSDSPIRKRPTRRAAATVKTPIYVDPSFDSMDEPSMQDDSFIVDNDEDVDDYDESD
Protein: AT3g51730/T18N14_110 (Saposin B domain-containing protein) (Q9SCT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pulmonary surfactant-associated protein B)
- Aspartic proteinase A2
- Cysteine proteinase RD21A
- Probable calcium-binding protein CML14
- 2-thiocytidine tRNA biosynthesis protein, TtcA
- Uncharacterized protein T9L24.31
Sequence:
MGLKAGTFVLLLLGLILVSDARSFVDSTISEKVSNKEDVCTLCEEYVTDALSYLEKNVTQAEIIEDLHDRCSQLRGYSQQCISLVDYYVPLFFLQLESFQPHYFCKRMNLCGKVVALVEEARQDSCGVCHRTVSEILIKLQDPDTQLDIVELLIKGCKSLKNYEKKCKTLVFEYGPLILVNAEEFLVKNDVCTLLRACPPEKSVLRQPELADS
Protein: Glycosyl-phosphatidylinositol-anchored molecule-like protein (Q99445)
Organism: Homo sapiens (Human)
Function: May play a role in the apoptotic pathway or cell-cycle regulation induced by p53/TP53 after DNA damage.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MLLFALLLAMELPLVAASATMRAQWTYSLRCHDCAVINDFNCPNIRVCPYHIRRCMTISIRINSRELLVYKNCTNNCTFVYAAEQPPEAPGKIFKTNSFYWVCCCNSMVCNAGGPTNLERDMLPDEVTEEELPEGTVRLGVSKLLLSFASIIVSNILP
Protein: Adrenodoxin, mitochondrial (Ferredoxin 1) (E7F7J1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Cysteine desulfurase
- Si:ch211-191d15.2
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Frataxin.
- LYR motif-containing protein 4
- Cholesterol 7-desaturase nvd
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- Cytochrome P450 27C1
Sequence:
MSACVLRAFLQRAAVMRQAAQQTISQTRAFPQSYTHIRGINTYANSLRAEEKVTVHFLNRDGKRITVKASIGESLLDVVVDRDLDIDGFGACEGTLACSTCHLIFEEDVYKKLGPVSDEEMDMLDLAYGLTDTSRLGCQVCLRKDLDGMILRVPDVISDARADSEKESSTAPPKI
Protein: G-protein alpha subunit (G5EC80)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGCNFSSQSKVSDVPAACDKPIPEPDVIGKEENIEPIEHSAEKEVVEKKESTPVPPPSISPQVALQVPEIRASRSITPASQKSEDPYSHIRLLLLGSAESGKTTVLEQVRLLYKQHFTESEYFHRRAFIYHNIFKSIKALCRAMRMSDIQFADPINMGRAQSIIADEHGHYGLFSKDLAEKIKHIWNDKSMQKLYARRSQFNLNDSASYFLNNIDKINMVDYKPSERDLIMAYVPTCGVQNVIFTACNQSFQLFDIGGQKIDRRKWALQYEGIDAIFFCIAISEYDQVMSEDMVTNRLDDALNLLQSISEDPAFATTPIYLFLNEIDVFCEKLSVIPLSKYKPDFKGGDQDDAIDFMENLACEALGKRDRSLYRVYRCIAIDTQMMAELLSTVFKDIAKRKK
Protein: J domain-containing protein (Q5A1E4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MGIPFPDIDPYETLGVSKDCSPLEIKKTYKKLCLKYHPDKLRQNNNDNDKDKQQEMFTKIQFAFSILNDPVKRKRYDNTGSLADYDLEDEGFDWKDYFESINEKITVEMVEEDRLKYQGSEEEKYDILNNFIYYDGDFLKLFELIPHLEFTESEEQRVYKIIDKELNNLQVNDSVRKSWEKYTKSRKTKVKQMLKKLAKEAKQAEELQQLLQNKPKKGQDLTSLIKSRQANRLDDLINNLESKYKDKKGKKRSPKDIDEDEFERIQNEIMKKKK
Protein: Stress-activated map kinase-interacting protein 1 (SAPK-interacting protein 1) (dSin1) (Q9V719)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of a multiprotein complex that phosphorylates Akt1, a protein that regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes.
Interaction partners:
- FI03615p
- LOBE
- Protein LST8 homolog
- Serine/threonine-protein kinase mTor
- Raptor, isoform B
- Ribosomal protein S6 kinase
- Serine/threonine-protein kinase Smg1
- RAC serine/threonine-protein kinase
- GTP-binding protein Rheb homolog
- Gigas, isoform A
Sequence:
MATYSNQHWLLSHIRNSFISTDDTGMCETVMLSDDMPKHYLRKFGNSGAGGDHYHWRRAHKTPPTGGGTTPERNTRHPDAPLQEVDFICYPGLDLSDDEEDMSTHSFDIQMYPEVGAHRFRSNTAQKLEKLDIAKRRAARIKSVNYQEEVQPPESDDFFKRKELPLSKAERVKNEPKANDDDLSDEGVQSQLTEQLAKSPKQAQNRFIEFARFDGTSQVGMQTKRINVFLNMLPEPDRNYPLKICVVATAKIQEVIGFVCYRTSLQYPDVPLKSLQHYALYMTEDNDDMEDFPPLDNREPCSKFGFSQLTLAERRPLAPVTRVDYHSQLGSKSMTSVEDKTALSDAAVKALQNISLNGGTSDPGGGGGGGDSPHDNVKEYEKRLLNHNDMLEAPMHRTFRLNIIDKRFFKSDVTLGISGERIEIDQCKNAKFWPQKKPVSTPIDFVAHCEILERRHLKALLRIWLKSNSSSPSFSTGCTSAPINASVTTLNAGSGSGGIAHSPSSPGHSSGLFSSSNIRFKHYDFDTDTHTAEQIHNKLNCILEMRSSDLRREFLLQRDRKQEKRQLKL
Protein: Putative RNA-binding protein 15B (One-twenty two protein 3) (HsOTT3) (HuOTT3) (RNA-binding motif protein 15B) (Q8NDT2)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Plays a key role in m6A methylation, possibly by binding target RNAs and recruiting the WMM complex. Involved in random X inactivation mediated by Xist RNA: acts by binding Xist RNA and recruiting the WMM complex, which mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA and promoting transcription repression activity of Xist. Functions in the regulation of alternative or illicit splicing, possibly by regulating m6A methylation. Inhibits pre-mRNA splicing. Also functions as a mRNA export factor by acting as a cofactor for the nuclear export receptor NXF1.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:16129689}. Nucleus speckle {ECO:0000269|PubMed:19586903}. Nucleus envelope {ECO:0000269|PubMed:19586903}. Note=Colocalizes with BMLF1 in the nucleus. Localized in the nucleoplasm with a granular staining pattern and excluded from the nucleoli. {ECO:0000269|PubMed:16129689}.
Interaction partners:
- N
- N
- Pre-mRNA-splicing regulator WTAP
- RNA-binding protein 15
- Protein virilizer homolog
- Zinc finger CCCH domain-containing protein 13
- E3 ubiquitin-protein ligase Hakai
- RNA N
- Microtubule-associated protein RP/EB family member 2
- mRNA export factor RAE1
Sequence:
MKRQSERDSSPSGRGSSSSAKRPREREREAEAGGRRAAHKASGGAKHPVPARARDKPRGSGSGGGGHRDGRGTGDANHRASSGRSSGSGAGGGGRGGKASGDPGASGMSPRASPLPPPPPPPGAEPACPGSSAAAPEYKTLLISSLSPALPAEHLEDRLFHQFKRFGEISLRLSHTPELGRVAYVNFRHPQDAREARQHALARQLLLYDRPLKVEPVYLRGGGGSSRRSSSSSAAASTPPPGPPAPADPLGYLPLHGGYQYKQRSLSPVAAPPLREPRARHAAAAFALDAAAAAAVGLSRERALDYYGLYDDRGRPYGYPAVCEEDLMPEDDQRATRNLFIGNLDHSVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMSGRVIGRNPIKIGYGKANPTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDHVKGDSFAYIQYESLDAAQAACAKMRGFPLGGPDRRLRVDFAKAEETRYPQQYQPSPLPVHYELLTDGYTRHRNLDADLVRDRTPPHLLYSDRDRTFLEGDWTSPSKSSDRRNSLEGYSRSVRSRSGERWGADGDRGLPKPWEERRKRRSLSSDRGRTTHSPYEERSRTKGSGQQSERGSDRTPERSRKENHSSEGTKESSSNSLSNSRHGAEERGHHHHHHEAADSSHGKKARDSERNHRTTEAEPKPLEEPKHETKKLKNLSEYAQTLQLGWNGLLVLKNSCFPTSMHILEGDQGVISSLLKDHTSGSKLTQLKIAQRLRLDQPKLDEVTRRIKQGSPNGYAVLLATQATPSGLGTEGMPTVEPGLQRRLLRNLVSYLKQKQAAGVISLPVGGSKGRDGTGMLYAFPPCDFSQQYLQSALRTLGKLEEEHMVIVIVRDTA
Protein: Homoserine dehydrogenase (HDH) (HSD) (EC 1.1.1.3) (P29365)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Threonine synthase
- Homoserine kinase
- Aspartate-semialdehyde dehydrogenase
- Homoserine O-succinyltransferase
- Methionine synthase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Phosphoserine phosphatase ThrH
- Dihydrodipicolinate synthase family protein
- Aspartokinase
- Probable dihydrodipicolinate synthetase
Sequence:
MKPVKVGICGLGTVGGGTFNVLERNAEEIARRAGRGIEVAQIAARRPNPKCDTGATPITADIFDVACNPEIDVVVELIGGYTLAHELVLKAIENGKHVVTANKALIAVHGNEIFAKAREKGVIVAFEAAVAGGIPVIKAIREGLSANRINWLAGIINGTGNFILSEMREKGRTFPDVLAEAQALGYAEADPTFDVEGIDAAHKLTILASIAFGIPLQFDKAYTEGISKLTSADVNYADALGYRIKHLGVARRTESGFELRVHPTLIPSDRLIANVNGVMNAVMVNGDAVGSTLYYGAGAGMEPTASSVVADLVDVVRAMTSDPENRVPHLAFQPDALSDHPILPIEACESAYYLRIQAKDHPGVLAQVATILSERGINIESIMQKEAEEQDGLVPMILVTHRVIEQRINDAIAALEALEGVSGPVVRIRVEQLN
Protein: Hemocyanin subunit 1 (P83174)
Organism: Cancer pagurus (Rock crab)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
DSPGGASDTQKQHXVNSXXXKXY
Protein: Proline-rich family protein (F4K7R6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKTTKGGKVMNPTDAYRKQIRKREIKRVNSFAVAKKVKMRFLPSCSIGVSLSNKKERQKVREVGILKKDPEQIKDQIRKLDMSKAEGALDKARKHKKRQLEDTLKMVEYDEKKKEQGEATTSVMFSHLPPQRRLTGEEDLKPEDSVYYHPTLNPTGAPPPGKPPMYNSSIGLAISSDGASSSSAALSSITESEDSVLVNPPPLPPLPDGDNALSASLPLPPLPPLPPTTGLTLPHSPFPPPPPGPPPKEQDFVRPPLPPPPQLPQSSQPPPPGLSGSQGDGRFPESSDFTFDNRMNANITSVPLLPPPGIPSNESESRPAESNASSFQNANLSKMVAPPPPAPLHQQHQSTFAGAAASLTNFQPDVHPPPGMLRFPPPPPPLDMHPPHPGMFVGHLIPRPPYGPPPGPPPMMRPPLPPGPPPSSFQDGQAMIRPYVPNKPSFVKSAAPTVVRRPLAQHTPELTSMVPASVRVRRESATVTKPKPKTSIASSLSFTPRAMASAATVKVEPAKTSAASKPQSIDDSYTAFLEDMKALGALDG
Protein: Late embryogenesis abundant protein (LEA) family protein (Q9SUB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Late embryogenesis abundant protein
- Late embryogenesis abundant protein At3g53040
- Reticulon-like protein B13
- Oleosin 21.2 kDa
- 12S seed storage protein CRA1
- Aquaporin TIP3-1
Sequence:
MAAMQLTRTALVGLSKAFPGIKAPATLAASSRKVSRICFATSVSQNEGRDPLDNARDSRADSAYGSKKWREDTGEYYAQAAKDKANEGASKAADKAYETKEQAKDKAYETKEKAKDTAYNAKEKAKDYAERTKDKVNEGAYKAADKAEDTKEKAKDYAEDTMDNAKEKARHAKEKVKEYGEDTKEKAEGFKETVKGKAEELGEKTKETVKGAWESTKNAAQTVTEAVVGPEEDAEKARADMNKGVEDHRKKKAEKDQKEDDFITFN
Protein: Core histone macro-H2A.1 (Histone macroH2A1) (mH2A1) (Histone H2A.y) (H2A/y) (Medulloblastoma antigen MU-MB-50.205) (O75367)
Organism: Homo sapiens (Human)
Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9634239}. Chromosome {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin (PubMed:15621527, PubMed:15897469, PubMed:9634239). Recruited to DNA damage sites in an APLF-dependent manner (PubMed:21211722, PubMed:29905837). {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:9634239}.
Interaction partners:
- Histone H4
- Poly [ADP-ribose] polymerase 1
- Histone H3.1
- Histone H2B type 1-J
- Histone H3.2
- Speckle-type POZ protein
- Histone H2B type 3-B
- Histone H2A type 1-B/E
- Histone deacetylase 1
- Histone deacetylase 2
Sequence:
MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
Protein: Protein SIS1 (O96212)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Heat shock 70 kDa protein
- Heat shock 70 kDa protein
- Endoplasmic reticulum chaperone GRP170
- Heat shock protein 110
- Endoplasmic reticulum chaperone BIP
- Heat shock protein 70
- HSP40, subfamily A
- Heat shock protein 90
- Heat shock protein 90, putative
- Endoplasmin, putative
Sequence:
MGKDYYSILGVSRDCTTNDLKKAYRKLAMMWHPDKHNDEKSKKEAEEKFKNIAEAYDVLADEEKRKIYDTYGEEGLKGSIPTGGNTYVYSGVDPSELFSRIFGSDGQFSFTSTFDEDFSPFSTFVNMTSRKSRPSTTTNINTNNYNKPATYEVPLSLSLEELYSGCKKKLKITRKRFMGTKSYEDDNYVTIDVKAGWKDGTKITFYGEGDQLSPMAQPGDLVFKVKTKTHDRFLRDANHLIYKCPVPLDKALTGFQFIVKSLDNRDINVRVDDIVTPKSRKIVAKEGMPSSKYPSMKGDLIVEFDIVFPKSLTSEKKKIIRETLANTF
Protein: Hemopexin (A0A0A1HAN6)
Organism: Carassius carassius (Crucian carp)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKLIQMLTLCLALSLSLAAPSHHKEDHVQQDEPQGHQHELHHGANLDRCGGMEFDAIAVNEEGIPYFFKGDHLFKGFHGQAELSNETFPELDEHHHLGHVDAAFRMHSEDSPEHHDHQFFFLDTKVFSYYKHKLEKDYPKDISELFPGIPDHLDAAVECPKPDCANDTIIFFKGDEIYHFDMKTKKVDEKEFKSMPNCTGAFRYMDHYYCFHGHQFSKFDPITGEVQGKYPKETRDYFMRCPHFGQKTTDEHIEREQCSRVQLDAITSDDDGSVYAFRGHHFLSITGDKFHSDTIESAFKELHSEVDAVFSYEGHLYMIKDNEVFVYKVGEPHTHLEGYPKPLKEVLGIEGPVDAAFVCADHHIAHIVKGQTVYDVDLKATPRVPVKEGSIAHLKKIDAAMCGPKGVTAVIGNHYYQFGSPMIMMMAKIMPEQHRVSQGLFGCDH