wanglab/gogpt-training-data huggingface dataset:
Protein: Virginiamycin B lyase (EC 4.2.99.-) (Streptogramin B lyase) (Q55557)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Sll0174 protein
Sequence:
MSPFPAKSLLIALVLSWPASFDAALAAPVPASTYKTSGIPAPEAIGNDASRYKVTIYPTVPGIGTRDVAPDPDGSVWFNGQWSGVIGHLNPKTGEVKLYPLGTGSHPHGVVMGPDGGLWICDESNAIRRFDRKTHEVKTFQLPPFSGSMGYGNLNTPVFDGEGILWFTAQNGYYGRLDPSTGDMKIFPAPQGFGPYGMTATPKGEVWYTSLAGNYIARIDTKTYLPEVFPIPDDKANGSRRIWSDSQGHIWITTWGNGALMRFNPQNKSWDSYKLPGLGPRGYSTYVDNQDRVWSSDFGTNSIHQFNPETMSFTVFPGNKQNVQTLQMNGVGDKIWAGQQGVDQIVLFERIP
Protein: Down syndrome cell adhesion molecule 1, isoform R (Q0E9I5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVAQYYDTDVNKAYVIRGNAAVLKCEIPSFVADFVSVVSWHTDQNEDFLPGSEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGSIGPRLTSGDESRILRVYLAASATLLCPAQAYPVPFFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMELPQVDQFHFNANGVNGGQAVRVMCMVSSGDLPIDIYWLKDGQPLLRSIYHKIDEYTLILSLRQTTIGDSGNYTCVASNAAGVASRWSILKVKVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Flavin prenyltransferase PAD1, mitochondrial (EC 2.5.1.129) (Phenylacrylic acid decarboxylase 1) (PAD) (P33751)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for the ferulic acid decarboxylase FDC1/ubiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN (By similarity). Involved in the decarboxylation of phenylacrylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives which play the role of aroma metabolites. Also involved in the degradation of the food preservative sorbic acid (2,4-hexadienoic acid) to a volatile hydrocarbon, 1,3-pentadiene. Not essential for ubiquinone synthesis. Can rescue Q biosynthesis in E.coli strains lacking UbiX. Has mRNA binding activity.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03197, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17054397}.
Interaction partners:
- Ferulic acid decarboxylase 1
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
Sequence:
MLLFPRRTNIAFFKTTGIFANFPLLGRTITTSPSFLTHKLSKEVTRASTSPPRPKRIVVAITGATGVALGIRLLQVLKELSVETHLVISKWGAATMKYETDWEPHDVAALATKTYSVRDVSACISSGSFQHDGMIVVPCSMKSLAAIRIGFTEDLITRAADVSIKENRKLLLVTRETPLSSIHLENMLSLCRAGVIIFPPVPAFYTRPKSLHDLLEQSVGRILDCFGIHADTFPRWEGIKSK
Protein: Nuclear pore complex interacting protein family member B7 (I3L0I5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTLRNPGSSGRKERPEAGTGSWLGRTRNQVINSLAVYRHRETDFGVGVRDHPGQHGKTPSPQKLDNLIIIIIGFLRRYTFNVLFCTSCLCVSFLKTIFWSRNGHDGSMDVQQRAWRSNRSRQKGLRSICMHTKKRVSSFRGNKIGLKDVITLRRHVETKVRAKIRKRKVTTKINRHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKPLCNWVRMAAAEHCHSSGLPYWLYLTAETLKNRMGRQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSVDDNIKECPLAPLPPSPLPPSVDDNLKECLFVPLPPSPLPPSVDDNLKECLFVPLPPSPLPPSVDDNLKTPPLATQEAEVEKPPKPKRWRVDEVEQSPKPKRQREAEAQQLPKPKRRRLSKLRTRHCTQAWAIRINP
Protein: mRNA-decapping enzyme 1B (EC 3.6.1.62) (Q3U564)
Organism: Mus musculus (Mouse)
Function: May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8IZD4}. Nucleus {ECO:0000250|UniProtKB:Q9NPI6}.
Interaction partners:
- Enhancer of mRNA-decapping protein 3
- Probable ATP-dependent RNA helicase DDX6
- m7GpppN-mRNA hydrolase
- Enhancer of mRNA-decapping protein 4
- mRNA-decapping enzyme 1A
- 5'-3' exoribonuclease 1
- Protein PAT1 homolog 1
- KIF-binding protein
- NAD
- Protein LSM14 homolog A
Sequence:
MAAAAAGGLPGKGHDISLAALRRHDPYISRIVDVASQVALYTFGHRANEWEKTGVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQLQNPFLLYRNGTLSIYGIWFYDKEECQRIAKLMKNLTQSEQLKACHGAGSSPVTLSSGEGQEVDILQMLTKAKDEYTKCKTCSEPKQMTNSSAICDNPKLIKPVPVRPSSSQRLQGPAPSKTSDPEPQHLSLTALFGKQDKAPCQETVKPSRTFAHHHHHHHQQQQETRPVHHGVACSLSCEEPRKLSLPVEKQLCPAIQKLMLGSPGLHPLPQHPEQWSCKSGSPSPAGGILPGPVQLGSPWNGRVAHCTQSTCRGHKLLEQLQGAPGAVHKYNPCAPTGPAVATQVAPGQSVAQSQLVYFSGPLQPPAPGHQALRKEQGALPAQAVSLSGSQESSPTVLPTQELLRKLQVVHQEQQAAPRPALAARFPVSAQGSGTEKPLEAWVSKTASMEKQAPLLQSTCAPLRETDNGLMALGGQELPAASSNLLLPLQNWESSTVASRPLTRLQLQEALLNLIQNDDNFLSIIYEAYLFSVTQAAMRTT
Protein: Serine/threonine-protein kinase BRSK2 (EC 2.7.11.1) (Brain-selective kinase 2) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 2) (BR serine/threonine-protein kinase 2) (Serine/threonine-protein kinase 29) (Serine/threonine-protein kinase SAD-A) (Q8IWQ3)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and axonogenesis, cell cycle progress and insulin secretion. Phosphorylates CDK16, CDC25C, MAPT/TAU, PAK1 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Plays a role in the regulation of the mitotic cell cycle progress and the onset of mitosis. Plays a role in the regulation of insulin secretion in response to elevated glucose levels, probably via phosphorylation of CDK16 and PAK1. While BRSK2 phosphorylated at Thr-174 can inhibit insulin secretion, BRSK2 phosphorylated at Thr-260 can promote insulin secretion. Regulates reorganization of the actin cytoskeleton. May play a role in the apoptotic response triggered by endoplasmic reticulum (ER) stress.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Detected at centrosomes during mitosis. Localizes to the endoplasmic reticulum in response to stress caused by tunicamycin.
Interaction partners:
- M-phase inducer phosphatase 2
- M-phase inducer phosphatase 3
- Wee1-like protein kinase
Sequence:
MTSTGKDGGAQHAQYVGPYRLEKTLGKGQTGLVKLGVHCVTCQKVAIKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVDAARRLTLEHIQKHIWYIGGKNEPEPEQPIPRKVQIRSLPSLEDIDPDVLDSMHSLGCFRDRNKLLQDLLSEEENQEKMIYFLLLDRKERYPSQEDEDLPPRNEIDPPRKRVDSPMLNRHGKRRPERKSMEVLSVTDGGSPVPARRAIEMAQHGQRSRSISGASSGLSTSPLSSPRVTPHPSPRGSPLPTPKGTPVHTPKESPAGTPNPTPPSSPSVGGVPWRARLNSIKNSFLGSPRFHRRKLQVPTPEEMSNLTPESSPELAKKSWFGNFISLEKEEQIFVVIKDKPLSSIKADIVHAFLSIPSLSHSVISQTSFRAEYKATGGPAVFQKPVKFQVDITYTEGGEAQKENGIYSVTFTLLSGPSRRFKRVVETIQAQLLSTHDPPAAQHLSDTTNCMEMMTGRLSKCGSPLSNFFDVIKQLFSDEKNGQAAQAPSTPAKRSAHGPLGDSAAAGPGPGGDAEYPTGKDTAKMGPPTARREQP
Protein: Interferon regulatory factor 9 (IRF-9) (IFN-alpha-responsive transcription factor subunit) (ISGF3 p48 subunit) (Interferon-stimulated gene factor 3 gamma) (ISGF-3 gamma) (Transcriptional regulator ISGF3 subunit gamma) (Q61179)
Organism: Mus musculus (Mouse)
Function: Transcription factor that plays an essential role in anti-viral immunity. It mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state.
Subcellular location: Nucleus.
Interaction partners:
- Signal transducer and activator of transcription 2
- Signal transducer and activator of transcription 1
- Non-receptor tyrosine-protein kinase TYK2
- Signal transducer and activator of transcription 3
- Signal transducer and activator of transcription
- Ubiquitin-like protein ISG15
- Signal transducer and transcription activator 6
- Tyrosine-protein kinase JAK1
- Signal transducer and activator of transcription 4
- Signal transducer and activator of transcription 5B
Sequence:
MASGKVRCTRKLRSWIVEQVESGHFPGVCWDDAAKTMFRIPWKHAGKQDFREDQDAAIFKAWALFKEKHKDGDIGHPAVWKTRLRCALNKSSEFEEVPERGRMDVAEPYKVYRILPAGTLPNQPRNQKSPCKRSISCVSPEREENMENGRTNGVVNHSDSGSNIGGGGNGSNRSDSNSNCNSELEEGAGTTEATIREDPVFLEHQLPLNSDYSLLLTFIYGGRVVGKTQVHSLDCRLVAERSDSESSMEQVEFPKPDPLEPTQHLLNQLDRGVLVASNSRGLFVQRLCPIPISWNAPEAPPGPGPHLLPSNKCVELFKTTYFCRDLAQYFQGQGPPPKFQATLHFWEESPGSSHSQENLITVQMEQAFARHLLEKIPEEEKAALFLLQHTEQSPSALGH
Protein: Colony stimulating factor 3 receptor (A0A8I6B3M3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MVGLGACNLTGVTLIVLLLPRSLEGCGQIRISPPIVHLGDPVLASCTISPNCSKLDRQPKILWRLQDEPNQPGDRQHHLPDGSQESIITLPHLNYTQAFLFCLVPWNNSFQVLDQAELRAGYPPASPSNLSCLMYLTTNSLVCQWEPGPETHLPTSFILKSFRSRTGCQYQGGTILDCMPKKRHSNCSIPRKHLLLYQNMVIWVQAENMLGSSESPKLCIDPMDVGRESLTTPPPAVKLEPPMLQALDIGHDIVSRQPGCLWLSWKPWKPSEFMEQECELRYQPQLEGANWTLVRPRKTSRWRWGMERGQAGFSVTPPTHQVSHLPSSTDRFELCSLHQAPVYTLQLRCIRSSLPGLWSSWSPGLQLRPTIKAPTIRLDTWWQKKHLDPETVRMQLFWKPTPLQKDSGQIQGYLLSWSCPDGQGRIMHLCNTTELSCTFHLPSEAQNVTLVAYNSAGTSSPTLVVFLEHEGPAVTSLHAMAQDLGSIWVDWEAPSLLPQGYLIEWGPDSHKYSNNSWRIEPNGNTTGILLEDNIHPFQLYRITVAPLYPGTVGPPVNVYTYSGEKALPHAPELYLKHVGRTWAQLEWVPETPWLGMIPLTNYTIFWTDARDHSFSVTLNISFHDFVLDHLKPASLYHVYLMATSRAGSTNSTGLTLMTMALDSSDVNIFLGILCFVLLSITCATAWFCCKQSRKTFFWPNVPDPAHSSLSAWVPTIMTEETFQLPSFWGSSVPSITKITELEEDKKPTHWDPSESSGTGSLPAVVQAYVLQGDPREISNQFQPPSSTNDQVLYGQVLGSPTSPEVVGYLRCDSTQPLLGGPTPSPKSYENIWFHSRPQETFIPQPPSQEDDCVFGPPFDFPLFQGLQVHGVEEQGGF
Protein: Antitoxin CcdA (LynA) (Protein H) (Protein LetA) (P62552)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system which inhibits the post-segregational killing (PSK) of plasmid-free cells, also referred to as a plasmid addiction system. Labile antitoxin with a half-life of about 1 hour in the presence of CcdB. Binds to and blocks the activity of CcdB; will also remove bound CcdB protein from the CcdB-GyrA complex by forming a CcdA-CcdB complex, a process termed rejuvenation. The N-terminal 36 residues are not required for rejuventation. Functions as a transcriptional corepressor for the ccdAB operon, repression also requires CcdB.
Interaction partners:
Sequence:
MKQRITVTVDSDSYQLLKAYDVNISGLVSTTMQNEARRLRAERWKAENQEGMAEVARFIEMNGSFADENRDW
Protein: Pyruvate kinase PKLR (EC 2.7.1.40) (L-PK) (Pyruvate kinase isozymes L/R) (P53657)
Organism: Mus musculus (Mouse)
Function: Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis.
Interaction partners:
- Alpha-enolase
- Glucose-6-phosphate isomerase
- Beta-enolase
- Phosphoenolpyruvate carboxykinase, cytosolic
- Enolase 4
- Gamma-enolase
- L-lactate dehydrogenase C chain
- L-lactate dehydrogenase A chain
- Pyruvate carboxylase, mitochondrial
- L-lactate dehydrogenase
Sequence:
MSVQENELPQQLWPWIFKSQKDLAKSALSGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVDRLKEMIKAGMNIARLNFSHGSHEYHAESIANIREAAESFATSPLSYRPVAIALDTKGPEIRTGVLQGGPESEVEIVKGSQVLVTVDPKFRTRGDAKTVWVDYHNITQVVAVGGRIYIDDGLISLVVRKIGPEGLVTEVEHGGFLGNRKGVNLPNAEVDLPGLSEQDLLDLRFGVEHYVDIIFASFVRKASDVVAVRDALGPEGRGIKIISKIENHEGVKKFDEILEVSDGIMMARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKARPTRAETSDVANAVLDGADCIMLSGETAKGSFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEASFKCCAAAIIVLTKTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLSRGVFPLLYREPPEAVWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLTIS
Protein: bZIP transcription factor 16 (AtbZIP16) (Q501B2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds to the G-box motif (5'-CACGTG-3') and other cis-acting elements with 5'-ACGT-3' core, such as Hex, C-box and as-1 motifs. Possesses high binding affinity to G-box, much lower affinity to Hex and C-box, and little affinity to as-1 element. G-box and G-box-like motifs are cis-acting elements defined in promoters of certain plant genes which are regulated by such diverse stimuli as light-induction or hormone control (Probable). Binds to the G-box motif 5'-CACGTG-3' of LHCB2.4 (At3g27690) promoter. May act as transcriptional repressor in light-regulated expression of LHCB2.4. Binds DNA as monomer. DNA-binding activity is redox-dependent.
Subcellular location: Nucleus {ECO:0000269|PubMed:18315949, ECO:0000269|PubMed:22718771}.
Interaction partners:
- bZIP transcription factor 53
- Basic leucine zipper 8
- Chlorophyll a-b binding protein 2.4, chloroplastic
- Pentatricopeptide repeat-containing protein At1g25360
- Pentatricopeptide repeat-containing protein At5g09450
- Pentatricopeptide repeat-containing protein At2g01740
- Pentatricopeptide repeat-containing protein At3g29290
- Pentatricopeptide repeat-containing protein At5g39350
- Pentatricopeptide repeat-containing protein At2g27610
Sequence:
MASNEMEKSSKEKEPKTPPPSSTAPPSSQEPSSAVSAGMATPDWSGFQAYSPMPPPHGYVASSPQPHPYMWGVQHMMPPYGTPPHPYVAMYPPGGMYAHPSMPPGSYPYSPYAMPSPNGMTEVSGNTTGGTDGDAKQSEVKEKLPIKRSRGSLGSLNMITGKNNEPGKNSGASANGAYSKSGESASDGSSEGSDGNSQNDSGSGLDGKDAEAASENGGSANGPQNGSAGTPILPVSQTVPIMPMTAAGVPGPPTNLNIGMDYWGAPTSAGIPGMHGKVSTPVPGVVAPGSRDGGHSQPWLQDDRELKRQRRKQSNRESARRSRLRKQAECDELAQRAEVLNEENTNLRAEINKLKSQCEELTTENTSLKDQLSLFPPLEGISMDNDHQEPDTNQTGAAERKVDSYKDST
Protein: Serine/arginine-rich splicing factor SR45a (At-SR45A) (AtSR45a) (Protein TRANSFORMER2-like) (atTra2) (Q84TH4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable splicing factor involved in constitutive and/or alternative splicing events. May bridge the 5' and 3' components of the spliceosome.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:17556373, ECO:0000269|PubMed:23132568}. Note=The phosphorylation status has no effect on the localization.
Interaction partners:
- Serine/arginine-rich splicing factor SR30
- U1 small nuclear ribonucleoprotein 70 kDa
- Pre-mRNA-splicing factor 38
- Serine/arginine-rich splicing factor RS2Z33
- Serine/arginine-rich splicing factor SR34B
- Nuclear protein-like
- Splicing factor U2af small subunit B
- Serine/arginine-rich splicing factor SR34A
- Splicing factor U2af large subunit A
- Serine/arginine-rich splicing factor RS2Z32
Sequence:
MGKREIHFTPVGRQVQRVLEYPLRLENRSPMSYSRRSRYSPSLSPYDKRRGRSVSRSLSRSPTRSVSSDAENPGNSLYVTGLSHRVTERDLEDHFAKEGKVTDVHLVLDPWTRESRGFGFISMKSVGDANRCIRSLDHSVLQGRVITVEKARRRRGRTPTPGKYLGLRTARGRHKSPSYSPRRSVSCSRSRSRSYSSDRGRSYSPSYGRRGRSSSYSPFYRRRRFYSPSRSPSPDDRYNRRRDRSYSPYYRRRDRSRSYSRNCRARDRSPYYMRRYRSRSRSYSPRYRARDRSCSPYYRGRDRSYSPHYQGRDRSYSPESRYYRRHRSVSGSVSPGGRSMSRSISPRKGRKESRSKSRRHDRQSSMCHSRSARSSTSRSVSP
Protein: Sporulation-specific protein 73 (P40031)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for spore wall assembly and ascus formation. Involved in the formation and elongation of prospore membranes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15590821}. Prospore membrane {ECO:0000269|PubMed:26605945, ECO:0000269|PubMed:27303688}; Peripheral membrane protein {ECO:0000305|PubMed:26605945, ECO:0000305|PubMed:27303688}. Note=Punctate location throughout the cytosol in meiosis II cells and peripheral punctate structures in the spore. {ECO:0000269|PubMed:15590821}.
Interaction partners:
- Autophagy protein 5
- Prospore membrane adapter protein SPO71
- Intermembrane lipid transfer protein VPS13
- Putative meiotic phospholipase SPO1
- Peroxisomal membrane protein PEX30
- Peroxisomal membrane protein PEX31
Sequence:
MGKNHFLKDFSALPEDVLIENERGITLLGYPLFSPKILLPHVDPPQFQRLNTENGSLIALSKNTISNFIELYPIDLSTERTAGSSSSQMTKWFVLMDYKEKYDIDDQGWCYSWNFNNSRWKSKNGLVRRRVWVRLPTTSHGLD
Protein: POU class 2 homeobox 3 (H0YLC5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
GDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAESSPSDPSVSTPSSYPSLSEVFGRKRKKRTSIETNIRLTLEKRFQDVSPSGSLGPLSVPPVHSTMPGTVTSSCSPGNNSRPSSPGSGLHASSPTASQNNSKAAVNSASSFNSS
Protein: Oxidoreductase, 2OG-Fe oxygenase family protein, expressed (cDNA clone:J013156L02, full insert sequence) (Q7XC81)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MNYYPPCLKADKVLGLSPHTDPGGLTLLLQVNDVQGLQINKDGKWFSVNALNGALIVNIGDTLEILSNGKFRSVEHRAVVHPSRERISAALFYYPCQDMVISPLPDFVKDGKVKYKTISYQDLLTEYFTAELDGRNRLKKMKLEP
Protein: Ammonium transporter 1 member 2 (LeAMT1;2) (O04161)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Ammonium transporter probably involved in ammonium uptake from the soil.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- PII protein
- PII-like protein
Sequence:
MASAMTCSAAELFPHLGSSANATAAAEFICSRFSAVSEYLTNTTYAVDTTYLLFSAYLVFAMQLGFAMLCAGSVRAKNTMNIMLTNVLDAAAGGFSYYLFGFAFAFGAPSNGFIGKHFFGLKEFPSQAFDYSYFLYQWAFAIAAAGITSGSIAERTQFVAYLIYSSFLTGFVYPIVSHWFWSGDGWASASKTDGNLLLRFGVIDFAGSGVVHMVGGIAGLWGAFIEGPRIGRFDRSGRSVALRGHSASLVVLGTFLLWFGWYGFNPGSFLTILKSYDHTIRGTYYGQWSAIGRTAVTTTLAGCTAALTTLFCKRLLVAHWNVVDVCNGLLGGFAAITSGCAVVEPWAAIVCGFIAAWVLIGFNALAAKLKYDDPLEAAQLHGGCGSWGIIFTGLFAKKEYVNEVYPGFPNRPYGLFMGGGGKLLGAQVIQVVVIIGWVSVTMGPLFYLLHKFKLLRISRDDETAGMDLTRHGGFAYIYHDEDEGSSMPGFKMTRVEPTNTSTPDHQNRSVNVVV
Protein: Probable 3-mercaptopyruvate sulfurtransferase (MST) (EC 2.8.1.2) (Q9USJ1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenylyltransferase and sulfurtransferase uba4
- Probable cysteine desulfurase, mitochondrial
- Cystathionine beta-lyase
- Aspartate aminotransferase, cytoplasmic
- Sulfite reductase subunit beta
- Aspartate aminotransferase, mitochondrial
- Probable phosphoadenosine phosphosulfate reductase
- Cytoplasmic tRNA 2-thiolation protein 1
- Probable sulfite reductase flavoprotein component
- Homocysteine synthase
Sequence:
MFSVGKKISFILPIKGVLQKLKDNAQKTVLLDATWYLPTDTKNGKKEYLESRLPGAQYFDIDEAKDHKNPLPHMLPPADEFASYVGKLGIDRNTNVIIYDRKGFFSSPRVFWTFKVFGHEHVFLFPNAFNAWKTEGLELETGEPRTPKPVVYEGAKLNKDLVASFDDIVKVIESPDAAGVHIVDARAHERFLGNVPESRPGLASGHIPTSINIPFTETTAAGITAPKPEEDLEKVFSSHGLTDKSVPIITSCGSGVTASVLFAALKECGFKDVRVYDESWSGYGKRANEDSSLLATGP
Protein: Transcription initiation factor TFIID subunit taf73 (Transcription initiation factor TFIID 73 kDa subunit) (TAFII-73) (O74319)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Regulates the genes involved in ubiquitin-dependent proteolysis during the progression of M-phase of mitosis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- TATA-box-binding protein
- Putative transcription initiation factor TFIID 111 kDa subunit
- Transcription initiation factor TFIID subunit 7
- SAGA complex/transcription factor TFIID complex subunit Taf6
- Transcription initiation factor TFIID subunit 4
- SAGA complex/transcription factor TFIID complex subunit Taf12
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 8
- SAGA complex/transcription factor TFIID complex subunit Taf10
- Transcription initiation factor TFIID subunit 11
Sequence:
MAQSSYSSGNSTSDLNKIVLDYLFKKGYSRTEAMLRLEISSVGAIPEEQQDWHIGASETYVQVYILLRDWIDGTLDLYKPKLQKVLYPIFVHSYLDLLQKNDPEMAIYFFESFRIEHEVLHGYDIRALAQLKIASDVEEIEIAQLYRKNKYRINFTRSTFDLLVQFLFENEVNGSGIIIRLLNQYIDIKITMPQVEGKEDPNVQAVYEMDEAKNEQTIISEQEGIPGHSEQLLDYNKQSIQLGLRPLSEEVVTTLKNLLEVKDKDVEGRNEALNKILHPAKNLVELLTEKENLINESTLESPSDPPLPPTKMKDIDYFVSLLESEQNSLILGKNATDPSVFMYTMHNTLSAVNCAAFSDDASMFALGCADSSIHLYSSTNNGPQPLVGSQNEPLQKSSLIGHTRPVFGVSISPQKEFILSCSEDGFTRLWSKDTKSTIVKYAGHNAPIWDVQFSPFGYYFATASHDQTARLWDVEHAAPLRVFVGHQNDVDCVSFHPNAAYLATGSSDHTTRMWDVRTGGTVRVFNAHHSPVSALCMSADGLSLASADESGIIKVWDLRSSNQHVSFVKHSSIVYSLSFSYDNKILVSGGADTDVNFWDLTYRNNLSDGEQSPLLFNFKTKNTIIQNLSFTRRNYCLALSSS
Protein: Fructosamine-3-kinase (EC 2.7.1.171) (Protein-psicosamine 3-kinase FN3K) (Protein-ribulosamine 3-kinase FN3K) (EC 2.7.1.172) (Q9ER35)
Organism: Mus musculus (Mouse)
Function: Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate. Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (By similarity). Involved in intracellular deglycation in erythrocytes and pancreatic islets. Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function. Also able to phosphorylate psicosamines and ribulosamines (By similarity).
Interaction partners:
- Sorting nexin-13
Sequence:
MEQLLRAQLHTTTLRAFGSSGGGCISEGYAYYTDSGPVFVKVNRRTQARQMFEGEMASLEALRNTGLVRVPKPMKVIDLPGGGAVFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKSKTRQNTVGCGAEGAEPQGVTKFGFHTVTCCGFIPQVNEWQEDWPTFFTRHRLQAQLDLIEKDYADRETQELWSRLQVKIPDLFAGIEIVPALLHGDLWSGNVAEDDQGPVIYDPASFYGHSEFELAIASMFGGFPRSFFTAYHRKIPKAPGFDKRLLLYQLFNYLNHWNHFGREYRSPSLGVMRKLLR
Protein: Synaptotagmin 7, isoform F (Q59DP7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTDMYLDSTDPSENVGQIHFSLEYDFQNTTLILKVLQGKELPAKDLSGTSDPYVRVTLLPDKKHRLETKIKRRTLNPRWNETFYFEGFPIQKLQSRVLHLHVFDYDRFSRDDSIGEVFLPLCQVDFAGKQSFWKALKPPAKDKCGELLSSLCYHPSNSILTLTLIKARNLKAKDINGKSDPYVKVWLQFGDKRVEKRKTPIFTCTLNPVFNESFSFNVPWEKIRECSLDVMVMDFDNIGRNELIGRILLAGKNGSGASETKHWQDMISKPRQTVVQWHRLKPE