wanglab/gogpt-training-data huggingface dataset:
Protein: cAMP-binding protein (Q7M7I9)
Organism: Vibrio vulnificus (strain YJ016)
Interaction partners:
- Adenylate cyclase
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit omega
Sequence:
MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERTAWVRAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMASRLQVTSQKVGDLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVVYGTR
Protein: tRNA pseudouridine(31) synthase (EC 5.4.99.42) (Pseudouridine synthase 6) (Pseudouridylate synthase 6) (Uracil hydrolyase) (tRNA pseudouridine 31 synthase) (PSI31 synthase) (P53294)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of pseudouridine at position 31 in the psi GC loop of tRNAS.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11406626}. Mitochondrion {ECO:0000269|PubMed:11406626}.
Interaction partners:
- Multisubstrate pseudouridine synthase 7
- 21S rRNA pseudouridine
- tRNA pseudouridine synthase 4
- tRNA pseudouridine
- tRNA pseudouridine synthase 1
- tRNA pseudouridine
- tRNA modification GTPase MSS1
Sequence:
MSTIKVIEVYTQNGLRKVRPYYNRRSAFVKGRWLGKLLIDVLVSEFKLRPRAYYLDQIRKGTYRLIRDGVPLVPDHLMTTIIKNHDVLETTTHKHEPPVKQWCSQEVEAEDLPGRIAGFNIVFEDESILVIDKPSGIPVHPTGQFYQNTITELLKLHGVDALPCYRLDKITSGLLILAKNSQSAGEIQKSIRSRDMIKIYLARVKGRFPHSELILDNENAAETTFEDTSKVTVEMTPIYSIDPKRQFPVGLSTSKDAITKFYPIRYFSHADETVVACKPITGRTHQIRIHLARLGHPIVNDSVYCSHITKYPERLKFITQFPRWENQQDLDAEELKVRFQKFVDETKNNCRTMETFCPECHTVDLKDPVLSDLELWLHAWKYEEINGKFKFKTDLPKWAQLDNS
Protein: Sodium/potassium/calcium exchanger 2 (Na(+)/K(+)/Ca(2+)-exchange protein 2) (Retinal cone Na-Ca+K exchanger) (Solute carrier family 24 member 2) (Q9UI40)
Organism: Homo sapiens (Human)
Function: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+). Required for learming and memory by regulating neuronal Ca(2+), which is essential for the development of synaptic plasticity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26631410}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDLQQSTTITSLEKWCLDESLSGCRRHYSVKKKLKLIRVLGLFMGLVAISTVSFSISAFSETDTQSTGEASVVSGPRVAQGYHQRTLLDLNDKILDYTPQPPLSKEGESENSTDHAQGDYPKDIFSLEERRKGAIILHVIGMIYMFIALAIVCDEFFVPSLTVITEKLGISDDVAGATFMAAGGSAPELFTSLIGVFIAHSNVGIGTIVGSAVFNILFVIGMCALFSREILNLTWWPLFRDVSFYIVDLIMLIIFFLDNVIMWWESLLLLTAYFCYVVFMKFNVQVEKWVKQMINRNKVVKVTAPEAQAKPSAARDKDEPTLPAKPRLQRGGSSASLHNSLMRNSIFQLMIHTLDPLAEELGSYGKLKYYDTMTEEGRFREKASILHKIAKKKCHVDENERQNGAANHVEKIELPNSTSTDVEMTPSSDASEPVQNGNLSHNIEGAEAQTADEEEDQPLSLAWPSETRKQVTFLIVFPIVFPLWITLPDVRKPSSRKFFPITFFGSITWIAVFSYLMVWWAHQVGETIGISEEIMGLTILAAGTSIPDLITSVIVARKGLGDMAVSSSVGSNIFDITVGLPLPWLLYTVIHRFQPVAVSSNGLFCAIVLLFIMLLFVILSIALCKWRMNKILGFIMFGLYFVFLVVSVLLEDRILTCPVSI
Protein: TATA-box-binding protein (TATA sequence-binding protein) (TATA-binding factor) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit) (P53360)
Organism: Mesocricetus auratus (Golden hamster)
Function: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (pre-initiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P20226}.
Interaction partners:
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor IIB
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
Sequence:
MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQREQQQQQQQQQQQQQQAVATAAASVQQSTSQQSTQGASGQTPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT
Protein: Transducer of Cdc42-dependent actin assembly protein 2 homolog (Q9XUS7)
Organism: Caenorhabditis elegans
Function: Plays a role in protein trafficking, actin organization and embryonic morphogenesis. Potentially acts as cdc-42 effector. May play a role in egg laying. Together with toca-1, is required for protein trafficking regulating yolk protein clathrin-mediated endocytosis by oocytes during oogenesis and retrograde recycling and the sorting of recycling endosome cargo proteins such as mig-14. Also, together with toca-2, controls the distribution of actin at cell junctions.
Subcellular location: Cell junction {ECO:0000269|PubMed:19798448}. Cell membrane {ECO:0000269|PubMed:19798448}; Peripheral membrane protein {ECO:0000269|PubMed:19798448}; Cytoplasmic side {ECO:0000269|PubMed:19798448}. Cytoplasmic vesicle {ECO:0000269|PubMed:19798448}. Cytoplasm {ECO:0000269|PubMed:19798448}. Recycling endosome {ECO:0000269|PubMed:25775511}. Note=Diffuse cytoplasmic localization (PubMed:19798448). Localizes to the rachis, which is the central core of the cytoplasm connecting developing oocytes in the syncytial gonad (PubMed:19798448). Co-localizes with toca-1 on recycling endosomes (PubMed:25775511). {ECO:0000269|PubMed:19798448, ECO:0000269|PubMed:25775511}.
Interaction partners:
- CRIB domain-containing protein
- Unconventional myosin-Ie
- DreBriN 1/DreBriN-like family homolog
- Cell division control protein 42 homolog
- Wiskott-Aldrich syndrome protein family member
- Transducer of Cdc42-dependent actin assembly protein 1 homolog
- tRNA-intron lyase
- WH1 domain-containing protein
- Cdc-42 Related Protein
- Major sperm protein
Sequence:
MIPVSRFFTVQDPSNALLSYTQKGIDFFEKLGQFSKEKAAIEEEYSTKLRSLAKKYAKKSEEDDEILKSVSYTSSFNSFLQQLDQIATRHQTSAEHIRGGVVSYVASKTCQMRSSRKNAINDLKTINDKLEDQINEMCKSGKCYLKSFKDAENSYQKFYKADKNLEISRLELEKARALANARNEACELAKQDYSALVRKTNAEQKRYHVELLPVIFARLKAVDKECIADMRQVLQKIVSFDDSLADSTEECRKIMQREVGKIDAEGDAQLVLKSVEATIEQPAPFEIEDLGDPKNCDSRTNDSADGSGGKLLKSSPSKNRIIRNFLGILKEKEADEKPEASNNDQLMYTDKSKPAHVRLSCLRSKIRDMEKQLEQAIQGREGITRLQQAYYTNPQHGNPSACTEPLISYAKKIEKLKMDIHNLKEFYAMLEMSVEEGQERSFGGRDTPDTTRSMSGSSTNQSSSKTIEDVLSGEAGNSSSADDSSKNILRQLFTTPKRLISSPKTSKSSTPTPLRRRAEISSPKILRSSFSGAIRKSLSTPDSVKVETAVTVTALFEFAKSSAETMSIEQGEILLVLEHDHGDGWTRTKNCRKHNEESGFVPTSYLQFPQ
Protein: Lipase lipl-5 (EC 3.1.1.-) (Lipase-like 5) (O61866)
Organism: Caenorhabditis elegans
Function: Lipase involved in lipid homeostasis. Regulates mitochondrial lipid composition, in particular cardiolipins and coenzyme Q-9 levels, in response to nutrient availability. Does not affect global triglyceride levels in response to nutrient availability. However, in coelomocytes, specifically promotes triglyceride catabolism and lifespan extension in response to nutrient deprivation.
Subcellular location: Lysosome lumen {ECO:0000269|PubMed:31340142}. Secreted {ECO:0000269|PubMed:31340142}. Note=Localizes to lysosomes in coelomocytes. {ECO:0000269|PubMed:31340142}.
Interaction partners:
- Delta
- Lipase lipl-1
- Delta
- Fatty acid synthase
- C-type lectin domain-containing protein
Sequence:
MWRFAVFLAAFFVQDVVGSHGDPELHMTTPQIIERWGYPAMIYTVATDDGYILEMHRIPFGKTNVTWPNGKRPVVFMQHGLLCASSDWVVNLPDQSAGFLFADAGFDVWLGNMRGNTYSMKHKDLKPSHSAFWDWSWDEMATYDLNAMINHVLEVTGQDSVYYMGHSQGTLTMFSHLSKDDGSFAKKIKKFFALAPIGSVKHIKGFLSFFANYFSLEFDGWFDIFGAGEFLPNNWAMKLAAKDICGGLKVEADLCDNVLFLIAGPESDQWNQTRVPVYATHDPAGTSTQNIVHWMQMVHHGGVPAYDWGTKTNKKKYGQANPPEYDFTAIKGTKIYLYWSDADWLADTPDVPDYLLTRLNPAIVAQNNHLPDYNHLDFTWGLRAPDDIYRPAIKLCTDDYLGK
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC1 (RNA polymerases I, II, and III subunit ABC1) (DNA-directed RNA polymerase II subunit E) (RPB5 homolog) (Q80UW8)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P19388}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P19388}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MDDEEETYRLWKIRKTIMQLCHDRGYLVTQDELDQTLEEFKAQFGDKPSEGRPRRTDLTVLVAHNDDPTDQMFVFFPEEPKVGIKTIKVYCQRMQEENITRALIVVQQGMTPSAKQSLVDMAPKYVLEQFLQQELLINITEHELVPEHVVMTKEEVTELLARYKLRESQLPRIQAGDPVARYFGIKRGQVVKIIRPSETAGRYITYRLVQ
Protein: Repressor of RNA polymerase III transcription MAF1 (Q9TZN2)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037240}.
Interaction partners:
- DNA-directed RNA polymerase subunit
- Transcription elongation factor 1 homolog
- DNA-directed RNA polymerase subunit beta
- B-related factor 1
- DNA-directed RNA polymerase III subunit RPC3
- Probable DNA-directed RNA polymerase III subunit RPC6
- Neural retina-specific leucine zipper protein
- RNB domain-containing protein
- DNA-directed RNA polymerase III subunit
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MKFLESSEMDVFSQTLVTGAIDCVIDFKLETYSSKMVTSEKKQWKSNDKSVIWGERQPLGSYEEMVMSASPSVGHNHRLRHLSERSCSGGSDNDFDVNDYLIKDSISRKKLYDLTQVLNCSFPDHDFSNANSEAFALVNYSDLSRLVDMKLETIVRDYHVRREELWGIIDEAIVPGDCQIYSFKSQFEDDPFTEDGCIWALAFIFYNKGLKRFVLLTIRCLSKQADTSIEIFPDFSEDEAEPQEK
Protein: Homeobox protein vnd (Homeobox protein NK-2) (Protein ventral nervous system defective) (P22808)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable transcriptional regulator involved in the regulation of the proneural AS-C genes and the neurogenic genes of the enhancer of split complex. Could specifically activate proneural genes in the ventral-most neuroectoderm.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein groucho
- Dorsal-ventral patterning protein Sog
- Brinker
- Achaete-scute complex protein T5
- Protein twist
- Achaete-scute complex protein T4
Sequence:
MTTSASLERTPSKRDRDRERDNSSGLGSAGSLPASPQSAITVSPSSPATPKRPLRTSTPSLERKREREDREDREDRKERQERHERDRDHERFAAVFSTASTTVPTNTSSSSGLAPEQLRIPTGAAAFSGFPGLHSMSSLMLPSSAAVAAAAAAPFLPWSPILLPPWNHALLPAAFYPAALRNALPGLFDAKVPSSQRSGFHISDILNLEGSELKNAAAAAAAAAHHGSDLSHHSASESTSGHRGQGSHTSPSALSPTPAGVSADEHHNGSGTGGGAGEADHHSTTEHHAPPSHPQQQHPHHQQHHHPHLLLPQQHHQQAVAPLPLAHHQSGEAQSHAHANAAAAHLLASHNAAAAAAVAAGQYLPNLPKNFPGSFGDEMSSYHHMAQTMLQHSGRSAWIKENELYGTQQPASPDSTSPVTSEVSYTYIGSNCQTSPALSGDYKSYSRSADSDALSVGDALHTLHGSSGNGSAGGAPTAHALHNNNNNTTNNNNHSLKAEGINGAGSGHDDSLNEDGIEEDIDDVDDADGSGGGDANGSDGLPNKKRKRRVLFTKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKTKRAQNEKGYEGHPGLLHGHATHPHHPSALPSPRRVAVPVLVRNGKPCLGDSSKLGADCVSVSSATATAMQNAAAHHLVALNGAAAYQHAAAAAAGLHAHAHAHAHAHGHGHPHAHAQRAAWWP
Protein: Ubiquitin-conjugating enzyme E2 4 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 4) (Ubiquitin carrier protein 4) (Ubiquitin-protein ligase 4) (P46595)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Mediates ubiquitination of PEX5.
Interaction partners:
- Ubiquitin-activating enzyme E1 1
- Polyubiquitin
- Anaphase-promoting complex subunit 11
- RING-box protein pip1
- Ubiquitin-ribosomal protein eL40A fusion protein
- Ubiquitin-ribosomal protein eS31A fusion protein
- Ubiquitin-ribosomal protein eL40B fusion protein
- Cullin-1
- Anaphase-promoting complex subunit 5
- Ubiquitin-ribosomal protein eS31B fusion protein
Sequence:
MALKRINRELADLGKDPPSSCSAGPVGDDLFHWQATIMGPADSPYAGGVFFLSIHFPTDYPFKPPKVNFTTRIYHPNINSNGSICLDILRDQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHVYKTDRSRYELSAREWTRKYAI
Protein: Multidrug resistance-like ATP-binding protein MdlB (EC 7.6.2.2) (P0AAG5)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Multidrug resistance-like ATP-binding protein MdlA
- Spermidine/putrescine import ATP-binding protein PotA
- Probable iron export ATP-binding protein FetA
- Thiamine import ATP-binding protein ThiQ
- Putrescine transport ATP-binding protein PotG
- L-cystine transport system ATP-binding protein TcyN
- Glutamine transport ATP-binding protein GlnQ
- Glutamate/aspartate import ATP-binding protein GltL
- DNA-binding transcriptional activator DecR
- Glycine betaine/proline betaine transport system ATP-binding protein ProV
Sequence:
MRSFSQLWPTLKRLLAYGSPWRKPLGIAVLMMWVAAAAEVSGPLLISYFIDNMVAKNNLPLKVVAGLAAAYVGLQLFAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSEFDTQPVGQVISRVTNDTEVIRDLYVTVVATVLRSAALVGAMLVAMFSLDWRMALVAIMIFPVVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEIINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSSLILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPLIELTTQQAMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGTIEVDNVSFAYRDDNLVLKNINLSVPSRNFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSALRQGVAMVQQDPVVLADTFLANVTLGRDISEERVWQALETVQLAELARSMSDGIYTPLGEQGNNLSVGQKQLLALARVLVETPQILILDEATASIDSGTEQAIQHALAAVREHTTLVVIAHRLSTIVDADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREEESLSA
Protein: Protocadherin 9 isoform 4 (Q2TJI3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
RCRHASRFKAAQRSKQGAEWMSPNQENKQNKKKKRKKRKSPKSSLLNFVTIEESKPDDAVHEPINGTISLPAELEEQGIGRFDWGPAPPTTFKPNSPDLAKHYKSASPQPAFHLKPDTPVSVKKHHVIQELPLDNTFVGGCDTLSKRSSTSSDHFGASECSSQGGFKTKGPLHTRQPQDEFYDQASPDKRTEADGNSDPNSDGPLGPRGLAEATEMCTQECLVLGHSDNCWMPPGLGPYQHPKSPLSTFAPQKEWIKKDKLVNGHTLTRAWKEDTNRNQFNDRKQYGSNEGHFNNGGHMADIPLANLKSYKQAGGTIESPKEHQL
Protein: Keratin-associated protein 4-12 (Keratin-associated protein 4.12) (Ultrahigh sulfur keratin-associated protein 4.12) (Q9BQ66)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MVNSCCGSVCSDQGCGLENCCRPSCCQTTCCRTTCCRPSCCVSSCCRPQCCQSVCCQPTCCRPSCCQTTCCRTTCCRPSCCVSSCCRPQCCQSVCCQPTCCRPSCCQTTCCRTTCCRPSCCVSSCCRPQCCQSVCCQPTCCRPSCCISSSCCPSCCESSCCRPCCCLRPVCGRVSCHTTCYRPTCVISTCPRPLCCASSCC
Protein: Deoxyhypusine synthase regulatory subunit (Inactive deoxyhypusine synthase) (Q4GZD1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Required for the activation and stability of deoxyhypusine synthase DHSc. Required for cell growth and survival.
Interaction partners:
- Eukaryotic translation initiation factor 5A
- Deoxyhypusine synthase
- Deoxyhypusine hydroxylase
- S-adenosylmethionine decarboxylase proenzyme-like, putative
- S-adenosylmethionine decarboxylase proenzyme
Sequence:
MSGVPFPSRVIGDLDYSNLLNIGQEEAIRCVLNAYPNIGLEATNLGRARRIVQRALNDNGMDGNKVMLAYTSNLISSGLRDTFACLARENRIGAVVTTAGGVEEDVIKCLGDTLVGDFALNDHALRNNGLNRVGNLLVPNDNYRNFEDFFVPLLRRLHEQQRDSRWTTKTTPSQIIAEIGAALESVRPNDCGSSLIYWCYRNDIPVFSPAFTDGSMGDMIYFYNYSRKGLVVDPVPDVRRLRQLGCKSTNVGRITCIVLGAGLPKHHLLRNVQADAVVYVTTGSDADGCESSCNVMADRANGLLSPNCDVVRVHGDATIISPLLLLRSSDGKEKVGVREDGN
Protein: N(6)-L-threonylcarbamoyladenine synthase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (Q8IJ99)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03180}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03180}.
Interaction partners:
- non-specific serine/threonine protein kinase
- EKC/KEOPS complex subunit CGI121
- Threonylcarbamoyl-AMP synthase
Sequence:
MFDNMEVDKKNGKKKYILGIEGSANKLGISIINEDMNILVNMRRTYISEIGCGFIPREISAHHKYYIIDMIKSCLKKVNIKISDITLICYTKGPGIGSALYIGYNIAKILYSYFNIPVVGVNHCIAHIEMGIFITKLYNPIVLYVSGSNTQIIYYNDHKKKYEIIGETLDIAIGNVIDRSARILKISNAPSPGYNVELLARKKYLLNIMKRNNNKNKNNITKEQEMKDNDFNPNELNDEQINDNKKMEDFTELLFFPYTIKGMDISFSGYDFYITKYFSKYMNKKSKTLNKLEKQTTNQGCNEKRKDNQYDNKIKCNQKKQQQEKEKDTYSNINKKCKIENVSQQTIESNQNNNNMYNQNKLGKETFKNIEPLKDNYKNDYVKVKEDIRDNHNGTVQNINDDNNSSNNYQKSNKLFYVAGLKGNSYYEDNIIFESEHKENYGENDEYIDDNCSIETASDFYEKSVNEEGEGEGEEDVIDLTEEEKRKIQICYSLQHHIFSMLIEITERAIAFTNSKEVIIVGGVGCNLFLQNMMKKMAKQKNIKIGFMDHSYCVDNGAMIAYTGYLEYLHAKNKDIYNFNNITIHQRYRTDDVFVTWK
Protein: Glutamate-rich protein 2 (A1L162)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METVNEPETGEVSKDAVIVKQEKNNEYCLQDIDDKLSESAEDDGEDDTNDEDDDEDSNPKKNTQAPLELMAEFLRAEMAREYQLAKKLCQMILIYEPENPEAKEFFTLIEEMLLMEKTQNHEQDGENSDEDSSGESKGESDEELSDESSDEGEDGS
Protein: Protein SOC1 (A0A509AHT1)
Organism: Plasmodium berghei (strain Anka)
Interaction partners:
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Shewanella-like protein phosphatase 2, putative
- Shewanella-like protein phosphatase 1
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
Sequence:
MDWKFKSESSVFELSKYIETQDLESILNYECLLHEIKSENYELINYIVKDDNLKKIISYIIDEFYDKNNYDRYYRFPYKCHQIISSENKLITDSIVYNNNLMKYFWSFILNKNQLNEVLAGYFSRCAIAIYNKNSKEVVNFLKKKKELYLKGFLYHFYSRNITELFKVLLFVKIPYLTIFENKNIIYLILSNLNGNFSDNEYIISDREDNIACLIRDLFVRKTEIYYFNYFIIDLSSQISFLYLIKCVFSECPYTVSAAITIISDLLHYTVLAKSYNQIDFYECLDIYNKEEEAKKKEELKEFEILQKKKETKKKKKKRKSIKLLEENIFVSKTHLISNQGYQTIVEDNLFLQNSNIDANSDFATIETVQNEYEEKEENEEKEENEEKCERVKREIEKIEIEQSNDINKDTQLNHISKKIKEEKNIPIQTICNGDINETLVTSELSNQNILADGFENPNNLIYTDITIEKNINFNDNVDNNQTINYNDIKNERCNSDGFSFASDFSSDYSTNDDNIEHLKKIKFEDVLNKMKNIATIKKVSQYQSEYKLNKEVEVLSWNSISQNDNIPQLNHQNVQNLQNEFICSDITNNTNNIYNEMTVEANKMEMVDIETGHEFIQNDQDNNSLQNNNSNNIKTTFNIFQKEEREPTITLEKWVEYLENTLFIDICFLGYIKDIMNIYIKNIKKNKDKNILGFTTLEIIQLIKTLIKTKSKNILTEIIDEGFFDISIDIFFKFKWNNLLHISVCDLLQTIIFKENEYSYVLYYILALTTFLPKCLRYFDVVRRCRNIKKKKKKKKLEALIDCGYKAHLLHICQILSNKSLEIKWLSNFLVTVSGWNDIIIEELNHYSLYFNDSNYINDKKIEDTNQTQLLQNNNQNISQITDFNKIQNSENNNLLIHPQNVQISKDIENPQISSEILDNPLTPNDQNNQNDQNNQNDQNSQNDQNSQNDQNSQNDQNSQNDQNSQNDQNSQNDQNNQNSSDINFSNYSNAIDILFDENKNVYSKYEDEFQDNKNSFNFENYNQFTSIDNTQNNNTNFADNKNNYLYEDNANEQNN
Protein: Proline-serine-threonine phosphatase interacting protein 1 isoform 3 (A0A0S2Z528)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAGLSAARV
Protein: F420-dependent glucose-6-phosphate dehydrogenase (FGD) (G6PD) (EC 1.1.98.2) (A0QQJ4)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. Appears to have a role in resistance to oxidative stress, via its consumption of G6P that serves as a source of reducing power to combat oxidative stress in mycobacteria. Cannot use NAD, NADP, FAD or FMN instead of coenzyme F420 as an electron acceptor. Exhibits nearly no activity with D-mannose-6-phosphate or D-fructose-6-phosphate as substrate.
Interaction partners:
- Phosphoenolpyruvate transferase
- Deazaflavin-dependent nitroreductase family protein
- Bifunctional F420 biosynthesis protein FbiB
- Phosphoenolpyruvate guanylyltransferase
- FO synthase
- Nitroreductase
- Deazaflavin-dependent nitroreductase family protein
- Pyridoxine/pyridoxamine 5'-phosphate oxidase
- Nitroreductase
- Pyridoxamine 5'-phosphate oxidase-related, FMN-binding
Sequence:
MAELKLGYKASAEQFAPRELVELAVLAESAGMDSATVSDHFQPWRHEGGHAPFSLAWMTAVGERTKNLVLGTSVLTPTFRYNPAVIAQAFATMGCLYPGRIFLGVGTGEALNEIATGYAGEWPEFKERFARLRESVRLMRELWLGDRVDFDGEYYRTKGASIYDVPEGGIPVYIAAGGPVVAKYAGRAGDGFICTSGKGEELYAEKLIPAVKEGAAAADRDADAIDRMIEIKISYDTDPELALENTRFWAPLSLTAEQKHSIDDPIEMEKAADALPIEQVAKRWIVASDPDEAVEKVGQYVKWGLNHLVFHAPGHDQRRFLELFKRDLEPRLRKLA
Protein: Rough deal protein (O96695)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWSNFEASSLEDETISNIFSSRGIFQISSEEEVNKYPDVMASVQCGKMVIGIDKSLLLLEDELVAKCSFLAFGAAIEAIAISSSGNLIVCGLSDGEVHGVFIKGLLLFSVAVNLEDVSLTGGTFRSIHQLDQRFYFTCKNGSIYSLSDIDETCLETLGNMSLNENETIACEKALLEDVTIQRLSKGRSSCSVDCAVLLKRLLTGNISAENNQDDLEAQPGLVITGDQSTMNFRNAANDVTRINLPAQYGSLKQIFNLEHYIIALTDSGHLVEICPYTRTVYMCQTTQQKNLLIEDLLVMECSEDNIELLVLTKSTAEGRFIKIVEYPTLNVKNEVEVPDHAWLVRHAKCAVNLYYLAAKEVNQSSIPSVVEMMLVSETDPSDRFKKLICKGRLEEAEEFGKQFELCLQPIYEAKAKRILVELCNSNSQNVDTKFQDLLQLLSQVESKAFIKSHRMINLNSRHILERYLHEVKKRLTFEDDEEDMLEIDEQLHRLKTLAIIDPYECNTDWQKFIYDNNLVRMVKSLFNTDMPTACLIWRRHSSSILPLLNEDELRTLLGFIPSNTKPFNVVQWLRQFIPMVSNTHPSIMPFITDWSIEMTRNLQYSPHWPDIGLEFCTKILDIFEEIQFTYSDVRRQQERNVGKLRDLVNALQDLSVLKTNYNMGFTLDNYMQDSIDATALSILQHVQLDKLQRLVKNFMYPIFQEKGRQPLDVIKQYISQLVASRLSSSSWLDRAMACIELLHNEDSRLECALSVLQNAPVPWPDTLAPLIRLRASTHPLAVKINAEYEIQVIKIMKVKYGWPADSSDINLELFMMRIVKLNLPDMLDDISALTKAAPELSTSANFNCCYQMARRGQVEMAYEFFKKLNGEKNSKSAKEVVEIMANILENSSSASFESDIKVQEHLNVLELFKLFLPHVESVYERRYLVIKHRFRLRKFGILLSCSSELIPLHRRHCLLDEAIERIIERAQATLNVSAFIASEISELCTALGLPKVFGLHRICQRIGCLPLSCALAYHVVSFVDCVPANAGEFVNLALELLVQQIESAKGKNQETASSLQLINENDPLSFYLAYELLASALLHESSRRHDLVELIKYIRVAVIHYPLDAIKSHYDGKEQAVNEHICRALDGISVALGETTINFSCALNGSFDVKTLTVPTTTKKRYSVSMFDEVEVQPIQQQPQKKSVGGRMAIVKFLARTLLLMVIETEPNNSLLMQVRNELPENTKADVESVCADFFLSLEHLTKVKEHDAWYVMSQYLLDFQKQNCRTKRIINEGFITLQLRRIFRNAMGSKDVNFIELFTMLVVDSEALALLEKLSVEVKTDLQKINFLTLSAMYHEHIEDLDSVQMIRTKRLKLFYYLEFCQQDHRIKGKFNADMDNIEDLLKEFHNKQLDVQLLERMSRLWVRLPKDSYYPDTKHIERPGVALRGEEGYFGDEELVMLSSAQEMRDMCQPYINEINNVELFTSKLKHFIEDINIYFYELYMCVINILMYFDSAPKEMEIWMNILHFLRHKMITRRRNRPGQVETDTWLKSQRENGVMPKISRYRLPFKPIVEQPLKDILDSELNVDNCQSWFPLIQMYTALKGSKDSSQNCDYFCMSAVKNSISEYKSKNDSESWSLHPTNNAFLQSILRLVEKVNNPNKAFLILYFVSNYARDGADQVEASYECWKFVKEKGHLITDPKSREQVAKVKRRYPIQKTQHLLYVYGLTDEKLLRQVENPTELIQALYHHELILKSSKVDINALVAEIAKLHDLCLATIQYRLLQKWLALTMESAGDGTILEETFMEEQNWPEQATAESSNSQDASENVNRAFYILSSWPKAEAVKFLVGLIFKGGSVNTSTQLQMYECYSKLNDGSNSFTNTISQRQFISIKCVHELKALGYKSNLEKFSDDHCNKIDILKMIWQRNAQNPLSLEVMANICLGFDIHLPQIWNGILKRMVMFHMVRDVNALLDVLSCRPHLLHLDGLAQAWDYVLCHPLQNAVELRSFKQEELLHKTLLRLQGCPVVHALNLLQFAQLCIVVHRPHMAASLLSFCQSSEQRQKIKKMIHSHPVENLRQQILDLEDAGILPVALNFALKELNLVSVEIWILLFP
Protein: GATA factor d (Q9BPQ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLDIQSHLRSEEDFQNYSITINQVGGSDFKSKAPKASTGSLLDSGDSSDSHKLEMDITSSINDRKTPDSLSSDHATDAATTQLWQALARSAAKSKEDNPASQIFRNMMSQPFAFPVPSTVSFTKVPEEPIALLKDLSEAQSSKSKPCRRKQSFPTKTDCIDVVNENVTDTYTTSEATPDDKKDKRNINLFNAIPGAQKDMSCSNCGTLTTTIWRRSVRGEMVCNACGLYFKLHGVNRPHSMRRDTIHTRRRRPKELERSKKKHKQMSSCSSIETTKQDFLTARESLAISGLVLNKFKKEIDDTETPAAAALKDILSRRKKSNSLPAFNDTCESADLSAPLNLVSSENNAKLT