wanglab/gogpt-training-data huggingface dataset:
Protein: LLGL scribble cell polarity complex component 2 (J3QRV5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRRFLRPGHDPVRERLKRDLFQFNKTVEHGFPHQPSALGYSPSLRILAIGTRSGAIKLYGAPGVEFMGLHQENNAVTQIHLLPGQCQLVTLLDDNSLHLWSLKVKGGASELQEDESFTLRGPPGAAPSATQITVVLPHSSCELLYLGTESGNVFVVQLPAFRALEDRTISSDAVLQRLPEEARHRRVFEMVEALQEHPRDPNQILIGYSRGLVVIWDLQGSRVLYHFLSSQQLENIWWQRDGRLLVSCHSDGSYCQWPVSSEAQQPEPLRSLVPYGPFPCKAITRILWLTTRQGLPFTIFQGGMPRASYGDRHCISVIHDGQQTAFDFTSRVIGFTVLTEADPAATFDDPYALVVLAEEELVVIDLQTAGWPPVQLPYLASLHCSAITCSHHVSNIPLKLWERIIAAGSRQNAHFSTMEWPIDGGTSLTPAPPQRDLLLTGHEDGTVRFWDASGVCLRLLYKLSTVRVFLTDTDPNENFSAQGEDEWPPLRKVGSFDPYSDDPRLGIQKIFLCKYSGYLAVAGTAGQVLVLELNDEAAEQAVEQVEADLLQDQEGYRWKGHERLAARSGPVRFEPGFQPFVLVQCQPPAVVTSLALHSEWRLVAFGTSHGFGLFDHQQRRQVFVKCTLHPSDQLALEGPLSRVKSLKKSLRQSFRRMRRSRVSSRKRHPAGPPGEAQEGSAKAERPGLQNMELAPVQRKIEARSAEDSFTGFVRTLYFADTYLKDSSRHCPSLWAGTNGGTIYAFSLRVPPAERRMDEPVRAEQAKEIQLMHRAPVVGILVLDGHSVPLPEPLEVAHDLSKSPDMQGSHQLLVVSEEQFKVFTLPKVSAKLKLKLTALEGSRVRRVSVAHFGSRRAEDYGEHHLAVLTNLGDIQVVSLPLLKPQVRYSCIRREDVSGIASCVFTKYGQGFYLISPSEFERFSLSTKWLVEPRCLVDSAETKNHRPGNGAGPKKAPSRARNSGTQSDGEEKQPGLVMERALLSDERVLKEIQSTLEGDRGSGNWRSHRAAVGCSLSNGGE
Protein: Non-histone chromosomal protein HMG-14 (High mobility group nucleosome-binding domain-containing protein 1) (P05114)
Organism: Homo sapiens (Human)
Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity).
Subcellular location: Nucleus. Cytoplasm. Note=Cytoplasmic enrichment upon phosphorylation. The RNA edited version localizes to the nucleus.
Interaction partners:
- Non-histone chromosomal protein HMG-17
- Ubiquitin-like protein FUBI
- Transcription elongation factor A protein 1
- DNA excision repair protein ERCC-6
- High mobility group nucleosome-binding domain-containing protein 5
- Histone acetyltransferase p300
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS19
Sequence:
MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD
Protein: Conjugal transfer protein (Q48B14)
Organism: Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6))
Interaction partners:
Sequence:
MASNEVLKRLTFESYNAMSRPAMFWNIPIMPMVGLLMGGLVFGVAATFLLSWVWGLVAAAPFLIALIALRVVGLIDPQYLRRIRFARRRLWLNLKYGKPLLLTPFNPQWSEFYGARFSQKRYAPGKESAIDALSGPRTHGDTARQPPGESDPVERGFQRNPQ
Protein: F-actin-uncapping protein LRRC16A (CARMIL homolog) (Capping protein regulator and myosin 1 linker protein 1) (Capping protein, Arp2/3 and myosin-I linker homolog 1) (Capping protein, Arp2/3 and myosin-I linker protein 1) (Leucine-rich repeat-containing protein 16A) (Q5VZK9)
Organism: Homo sapiens (Human)
Function: Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments. Plays a role in lamellipodial protrusion formations and cell migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19846667}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6EDY6}. Cell membrane {ECO:0000269|PubMed:26578515}. Cell projection, lamellipodium {ECO:0000269|PubMed:19846667}. Note=Found on macropinosomes (PubMed:19846667). Colocalized with heterodimeric capping protein (CP) and F-actin in lamellipodia but not with F-actin in stress fibers (PubMed:19846667). {ECO:0000269|PubMed:19846667}.
Interaction partners:
- Tropomodulin-4
- F-actin-capping protein subunit alpha-2
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha-1
- Scinderin
- Unconventional myosin-Ic
- Gelsolin
- CD2-associated protein
Sequence:
MTEESSDVPRELIESIKDVIGRKIKISVKKKVKLEVKGDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGTCLRKIFPGLSPVRIMKKVSMEPSERLASLQALWDSQTVAEQGPCGGFSQMYACVCDWLGFSYREEVQWDVDTIYLTQDTRELNLQDFSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLSNTECSLDMVCGALLRGCLQYLAVLNLSRTVFSHRKGKEVPPSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKGVSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNLVQMIQDEESPLQSLSLADSKLKTEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDASQALKTNPEKTEDALQKIENYLLRNHETRKYLQEQAYRLQQGIVTSTTQQMIDRICVKVQDHLNSLRNCGGDAIQEDLKSAERLMRDAKNSKTLLPNLYHVGGASWAGASGLLSSPIQETLESMAGEVTRVVDEQLKALLESMVDAAENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLADHFSRRGKTLPQQESLEIELAEEKPVKRSIITVEELTEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEMEFDLDKALEEVPIHIEDPPFPSLRQEKRSSGFISELPSEEGKKLEHFTKLRPKRNKKQQPTQAAVCAANIVSQDGEQNGLMGRVDEGVDEFFTKKVTKMDSKKWSTRGSESHELNEGGDEKKKRDSRKSSGFLNLIKSRSKSERPPTILMTEEPSSPKGAVRSPPVDCPRKDTKAAEHNGNSERIEEIKTPDSFEESQGEEIGKVERSDSKSSPQAGRRYGVQVMGSGLLAEMKAKQEKRAACAQKKLGNDAVSQDSSSPALSGVERSDGGGAVPKLHPGLPENRFGLGTPEKNTKAEPKAEAGSRSRSSSSTPTSPKPLLQSPKPSLAARPVIPQKPRTASRPDDIPDSPSSPKVALLPPVLKKVPSDKERDGQSSPQPSPRTFSQEVSRRSWGQQAQEYQEQKQRSSSKDGHQGSKSNDSGEEAEKEFIFV
Protein: T-cell surface glycoprotein CD3 epsilon chain (E9PSH8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MQSGTHWRVLGLCLLSVGVWGQDGNEEMAYKVSISGTTVILTCPQYPGSEILWQHNDKNIGGDEDDKNIGSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDANFYLYLRARVCENCMEMDVMSVATIVIVDICITGGLLLLVYYWSKNRKAKAKPVTRGAGAGGRQRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRRI
Protein: At1g64405 (Q3ECI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Peroxidase 66
- Polygalacturonase ADPG1
Sequence:
MGNCMERWMQGEGEEGKIEVTERAKESFKLDGDDNEDGHGGMKVKIVLTRHELDMFLLQMNRSHDGNLMITKDVMVELEKRIIRASSFSSLSSSPSSIAWEPALESILECPEVQEMDR
Protein: Probable 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) (5,10-methenyl-tetrahydrofolate synthetase) (MTHFS) (Methenyl-THF synthetase) (Q9P7W2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Methylenetetrahydrofolate dehydrogenase [NAD
- C-1-tetrahydrofolate synthase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Phosphoribosylglycinamide formyltransferase
- Probable serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
Sequence:
MSLKKNQLRAILNSSLGKLADHIIDSQSISICKQVVELPEWKRCKNVCLYMNMPKKEVRTRCLIDVAFKEGKNVFIPKCIGSHVMEMYQVFEKTESLTINKWGIAEPNGESRKIMDDETDCELIIVPGVAFDEKLSRLGHGKGYYDNYISKYQSWALQKESRANMFKVGICLKEQILPNREIPMDTRDQKLDALVTPEKVIRNI
Protein: Uncharacterized protein Rv2577 (P9WL81)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0090
Sequence:
MGADLKQPQDADSPPKGVSRRRFLTTGAAAVVGTGVGAGGTALLSSHPRGPAVWYQRGRSGAPPVGGLHLQFGRNASTEMVVSWHTTDTVGNPRVMLGTPTSGFGSVVVAETRSYRDAKSNTEVRVNHAHLTNLTPDTDYVYAAVHDGTTPELGTARTAPSGRKPLRFTSFGDQSTPALGRLADGRYVSDNIGSPFAGDITIAIERIAPLFNLINGDLCYANLAQDRIRTWSDWFDNNTRSARYRPWMPAAGNHENEVGNGPIGYDAYQTYFAVPDSGSSPQLRGLWYSFTAGSVRVISLHNDDVCYQDGGNSYVRGYSGGEQRRWLQAELANARRDSEIDWVVVCMHQTAISTADDNNGADLGIRQEWLPLFDQYQVDLVVCGHEHHYERSHPLRGALGTDTRTPIPVDTRSDLIDSTRGTVHLVIGGGGTSKPTNALLFPQPRCQVITGVGDFDPAIRRKPSIFVLEDAPWSAFRDRDNPYGFVAFDVDPGQPGGTTSIKATYYAVTGPFGGLTVIDQFTLTKPRGG
Protein: Chondroitin sulfate synthase sqv-5 (EC 2.4.1.174) (EC 2.4.1.175) (EC 2.4.1.226) (Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N- acetylgalactosaminyltransferase 1) (Glucuronylgalactosylproteoglycan 4-beta-N- acetylgalactosaminyltransferase) (N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1) (Squashed vulva protein 5) (Q7Z1Z1)
Organism: Caenorhabditis elegans
Function: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. The beta-1,3-glucuronic acid transferase activity is controversial as it is not detected using the purified recombinant enzyme. Adds the first N-acetylgalactosamine(GalNAc) to initiate the chondroitin chain. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and GalNAc from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Together with mig-22, required for chondroitin synthesis. Plays a role in early embryonic development by controlling cell division and cytokinesis. In addition, involved in vulva morphogenesis and in the directed migration of gonadal distal tip cells and hermaphrodite specific neurons. May be required for nunc6/netrin-mediated dorsal guidance of distal tip cells.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305|PubMed:12761549}; Single-pass type II membrane protein {ECO:0000305|PubMed:12761549}. Note=Localizes in punctate foci in the cytoplasm. Co-localizes with sqv-1. {ECO:0000269|PubMed:12761549}.
Interaction partners:
- Chondroitin sulfate synthase mig-22
- UDP-glucuronate decarboxylase
- UDP-sugar transporter sqv-7
- Xylosylprotein 4-beta-galactosyltransferase
- Exostosin-like-3 homolog
- Probable syndecan
- E3 ubiquitin-protein ligase marc-3
- Xylosyltransferase sqv-6
- Beta-1,3-galactosyltransferase sqv-2
Sequence:
MRVFQRSTCRMPVSRATVTILLGILFGFSITYYLTALKSLTNPIICGPEQQIGGFDYLDVISQRADADVFTRSQSLPGHRRGLILVAIMTAAKYVDTRAYNVWKTWAQHIPGRVLIFVAEGTESVHEDMPLIRLKGVDDTYPPQKKSFAMVKWLAENMADEYDWFLRADDDLYIRGEELALFLRSVDSSKAHIIGQAGLGNSAEYGLLALGSTDNYCMGGPGIVMSRDTLLKVSPHLESCLQHMLTSHEDVELGRCIRKHVGVACTWNYEMQKLFHNNQSAIKESYAKNMKELKDAITLHPIKDPAVMRKVHLRNREIKLREARAKRSLLSSELSTAKAQTLVRMTPNRTNDLTPWEYINNNKILFCADRVNCPRHTVDLSIRTEMADTITQLFDEFNTNARQRGRVLQFQSLQYGYMRVEPTKGVDYVLDMLLWFKKFRPPNRTTISVRRHAYVQQTFGKLRSLSEGVFRSNMRANSTLIEDPTLHMIMPLRGRAAIFARFAQHLKSICARGGDDLAVSLTIVLYSSEDEMENRETIEMLRASFIPVTVIEMGDVSFSRGVALMRGAETLPANALLFFTDVDMLFTCDALKRIKSNTILNAQIYFPIVFSEFSHESWSENDKLLADAFHYGRGRGYFRHFGYGLAAMYKADLMDVGGFDTKIEGWGKEDVDLFEKAIKNGRLRVIRVPEPGLVHIYHPIHCDENMPTAQKDMCHGSKAASLASIDTLVEQIAQYT
Protein: ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit) (A1KI97)
Organism: Mycobacterium bovis (strain BCG / Pasteur 1173P2)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00815}.
Interaction partners:
Sequence:
MAATLRELRGRIRSAGSIKKITKAQELIATSRIARAQARLESARPYAFEITRMLTTLAAEAALDHPLLVERPEPKRAGVLVVSSDRGLCGAYNANIFRRSEELFSLLREAGKQPVLYVVGRKAQNYYSFRNWNITESWMGFSEQPTYENAAEIASTLVDAFLLGTDNGEDQRSDSGEGVDELHIVYTEFKSMLSQSAEAHRIAPMVVEYVEEDIGPRTLYSFEPDATMLFESLLPRYLTTRVYAALLESAASELASRQRAMKSATDNADDLIKALTLMANRERQAQITQEISEIVGGANALAEAR
Protein: Purine permease (Q2USE7)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Dihydroorotate dehydrogenase
- allantoinase
- Xanthine/uracil/vitamin C permease
- Purine-cytosine permease
- Orotate phosphoribosyltransferase
- Uncharacterized protein
- Orotidine 5'-phosphate decarboxylase
- C6 transcription factor
- Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase
- Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial
Sequence:
MDGPDQIGPDLRPKRTWADKARRIVKTFTTRDGLIGDYDYAYLFTPNIPFMQQTRRTAPFFGLDDRVPVVLALILGLQHSLAMLAGVISPPILLGGSSGANLGEDDYQYLVSTSLIVSGLLSALQMLRFRIYKTPYSIGTGLISVVGTSFSIITVASGTFTQMYSSGYCPVDAQGNRLPCPAGYGALLGTSCLCSLLQIGLSFISSKVLKRVFPPLVTGPTVLLIGASLLETGMKDWAGGSGSCGSDPSARALCPSADAPHALPWGSAEFIGLGFLVFVTIILCERFGSPIMKSCAVVVGLLVGCIVAGACGYFDRSTIDAAPVVSFIWVRTFPLTIYAPLILPLLAVYIVIMMESIGDITATCDVSQVEVQGPDFDSRIRGGVLGNGLTCLLAGLCTITPMSVFAQNNGVIALTKCANRKAGYCCCFFLVIMGIFAKFAAALVAIPSSVLGGMTTFLFSSVAVSGIRIISSIPFTRRNRFILTASFAIGMAATLVPDWFDYFFTYSGDNHALQGLLDAVTLVMTNGFAVTAVLGLILNLLIPEDPEEEAAIVDARGSEVRSESEETKGTSESSHFKTAEAGPAIV
Protein: Cysteine desulfurase, mitochondrial (EC 2.8.1.7) (Q9VKD3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9Y697}. Nucleus {ECO:0000250|UniProtKB:Q9Y697}.
Interaction partners:
- LYR motif-containing protein 4 homolog
- Iron-sulfur cluster assembly enzyme IscU
- Frataxin homolog, mitochondrial
- Adenylyltransferase and sulfurtransferase MOCS3
- Adrenodoxin-like protein 2, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Adrenodoxin-like protein 1, mitochondrial
- GH14121p
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Sulfurtransferase
Sequence:
MQKVLGRIQAQVLRSRATNALANVVRHEATSSRTAAKPAATSKEFRERQVRFNIKNEQTEGRPLYLDAQATTPMDPRVLDAMLPYLTNFYGNPHSRTHAYGWETESAVEKAREQVATLIGADPKEIIFTSGATESNNIAVKGVARFYGTKKRHVITTQTEHKCVLDSCRALENEGFKVTYLPVLANGLIDLQQLEETITSETSLVSIMTVNNEIGVRQPVDEIGKLCRSRRVFFHTDAAQAVGKVPLDVNAMNIDLMSISGHKIYGPKGVGALYVRRRPRVRLEPIQSGGGQERGLRSGTVPAPLAVGLGAAAELSLREMDYDKKWVDFLSNRLLDRISSALPHVIRNGDAKATYNGCLNLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTVEEVDYTADKCIKHVERLREMSPLWEMVQEGIDLKTIQWSQH
Protein: Zinc finger protein 174 (AW-1) (Zinc finger and SCAN domain-containing protein 8) (Q15697)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor.
Subcellular location: Nucleus.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 32
- G-patch domain and KOW motifs-containing protein
- Zinc finger protein 24
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger and SCAN domain-containing protein 1
- Zinc finger protein 396
- Zinc finger and SCAN domain-containing protein 20
- Zinc finger protein 18
- Zinc finger protein 397
- PiggyBac transposable element-derived protein 1
Sequence:
MAAKMEITLSSNTEASSKQERHIIAKLEEKRGPPLQKNCPDPELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLVEDFHRASKKPKQWVAVCMQGQKVLLEKTGSQLGEQELPDFQPQTPRRDLRESSPAEPSQAGAYDRLSPHHWEKSPLLQEPTPKLAGTEAPRMRSDNKENPQQEGAKGAKPCAVSAGRSKGNGLQNPEPRGANMSEPRLSRRQVSSPNAQKPFAHYQRHCRVEYISSPLKSHPLRELKKSKGGKRSLSNRLQHLGHQPTRSAKKPYKCDDCGKSFTWNSELKRHKRVHTGERPYTCGECGNCFGRQSTLKLHQRIHTGEKPYQCGQCGKSFRQSSNLHQHHRLHHGD
Protein: Dihydroneopterin triphosphate diphosphatase (EC 3.6.1.67) (Dihydroneopterin triphosphate pyrophosphatase) (dATP pyrophosphohydrolase) (P0AFC0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of dihydroneopterin triphosphate to dihydroneopterin monophosphate and pyrophosphate. Required for efficient folate biosynthesis. Can also hydrolyze nucleoside triphosphates with a preference for dATP.
Interaction partners:
- Probable transcriptional regulatory protein YebC
- Aspartate--tRNA ligase
- GTP cyclohydrolase 1
- Crossover junction endodeoxyribonuclease RuvC
- Alkaline phosphatase
- Dihydroneopterin triphosphate 2'-epimerase
- 6-carboxy-5,6,7,8-tetrahydropterin synthase
- Bifunctional NAD
- Holliday junction branch migration complex subunit RuvA
Sequence:
MKDKVYKRPVSILVVIYAQDTKRVLMLQRRDDPDFWQSVTGSVEEGETAPQAAMREVKEEVTIDVVAEQLTLIDCQRTVEFEIFSHLRHRYAPGVTRNTESWFCLALPHERQIVFTEHLAYKWLDAPAAAALTKSWSNRQAIEQFVINAA
Protein: Putative transferase caf17, mitochondrial (EC 2.1.-.-) (Q09929)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Iron-sulfur assembly protein 2
- NifU-like protein C1709.19c
- Iron-sulfur assembly protein 1
- Protein isd11
- Lipoyl synthase, mitochondrial
- Iron sulfur cluster assembly protein 1, mitochondrial
- Probable aminomethyltransferase, mitochondrial
- Monothiol glutaredoxin-5
- Probable cysteine desulfurase, mitochondrial
- GrpE protein homolog
Sequence:
MNRFTVRSKFIKFSFQLFRNYSVCLNSSKSLIRVEGVDAVKFLQGLTTNKITLDNPVYTGFLNTQGRVLFDSFIYPKVSNNGTENERSDELYVEIDKVAESDFLKHLKKYNLRSRCSIAKIPSEELSIKVIWDVKEESRLKDTVAYAKDPRFSKQRLLRMIVPTSTCTSSSSGSLDDYKVFRYRNGIPEGPQEIIPSISFPLESNMDWMKGIDFHKGCYLGQELTVRTYYTGVTRKRIFPFIIPNYEDNPSQVIEPSAPLSIVAKQGEPVSRRSPGKIIAILGKVGLALVRLQYLKSDLACNGIPIQLNTSIWLDELSSTPSENS
Protein: Poly(rC) binding protein 2 (A0A8I6AP00)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLESPPKGVTIPYRPKPSSSPVIFAGGQAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWAGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
Protein: Serine/threonine-protein kinase BSK1-2 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 1-2) (OsBSK1-2) (Q336V9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable serine/threonine kinase that functions as a positive regulator of plant immunity. May be involved in the regulation of pattern-triggered immunity (PTI). Does not seem to be involved in responses to brassinosteroid (BR) signaling.
Subcellular location: Cell membrane {ECO:0000255}; Lipid-anchor {ECO:0000255}.
Interaction partners:
- Brassinosteroid LRR receptor kinase BRI1
- 4-coumarate--CoA ligase
- Nuclear pore protein
- Os02g0732700 protein
- non-specific serine/threonine protein kinase
- Mediator of RNA polymerase II transcription subunit 10
- Os06g0217500 protein
- Os01g0296000 protein.
- non-specific serine/threonine protein kinase
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MGCCGSSLRVGSHAPEKPPRRARPPPPPPQPHHPRRPSFTLNAHQAAASSSAASAAPAPAFAEFSLAELREATGGFAAANIVSESGEKAPNLVYRGRLQGAGGGGRAIAVKKFGKLAWPDPKQFAEEARGVGKLRHRRMANLIGYCCDGDERLLVAEFMPNDTLAKHLFHWENKAIEWAMRLRVAYNIAEALEYCSNEERPLYHDLNAYRVLFDENGDPRLSCFGLMKNSRDGKSYSTNLAYTPPEYLRNGRVTLESVVFSFGTILIDLLSGKRIPPTLALDMIRSRSIQAIMETNLEGKYSIEEATTLVDLASKCLQYEPRDRPDIKKLVSILQPLQTKSEVPSYVMLGVPKPEEVPKAPPAPQHPLSPMGEACSRMDLTAIHQILVSTHYRDDEGTNELSFQEWTQQMRDMLDARKRGDFAFRDKNFKQAIDCYTQFVDVGTMVSPTVYARRSLCHLMCDQPDAALRDAMQAQCVYPDWPTAFYMQAVALSKLNMQSDSLDMLNEASQLEEKRQKSIKGP
Protein: Small nuclear ribonucleoprotein SmD1a (AtSmD1-a) (Q9SSF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in splicing regulation. Facilitates post-transcriptional gene silencing (PTGS) by limiting the degradation of transgene aberrant RNAs by the RNA quality control (RQC) machinery, thus favoring their entry into cytoplasmic siRNA bodies where they can trigger PTGS. Does not participate in the production of small RNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:26842463}. Nucleus speckle {ECO:0000250|UniProtKB:Q9SY09}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9SY09}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D2
- Probable small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein G
- Sm protein F
- Small nuclear ribonucleoprotein SmD3b
- Small nuclear ribonucleoprotein SmD3a
- Small nuclear ribonucleoprotein E
- Sm-like protein LSM8
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
Sequence:
MKLVRFLMKLNNETVSIELKNGTVVHGTITGVDVSMNTHLKTVKMSLKGKNPVTLDHLSLRGNNIRYYILPDSLNLETLLVEDTPRVKPKKPVAGKAVGRGRGRGRGRGRGRGR
Protein: 17-beta-hydroxysteroid dehydrogenase type 6 (17-beta-HSD 6) (17-beta-HSD6) (EC 1.1.1.105) (EC 1.1.1.209) (EC 1.1.1.239) (EC 1.1.1.53) (EC 1.1.1.62) (3-alpha->beta-hydroxysteroid epimerase) (3-alpha->beta-HSE) (Oxidative 3-alpha hydroxysteroid dehydrogenase) (O54753)
Organism: Rattus norvegicus (Rat)
Function: NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro) (By similarity). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro).
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14756}; Lumenal side {ECO:0000250|UniProtKB:O14756}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14756}; Peripheral membrane protein {ECO:0000250|UniProtKB:O14756}; Lumenal side {ECO:0000250|UniProtKB:O14756}.
Interaction partners:
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Polyprenal reductase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Testosterone 17-beta-dehydrogenase 8)
- UDP-glucuronosyltransferase 2B37
- Aromatase
- Aldo-keto reductase family 1 member D1
Sequence:
MWFYLVTLVGLYYLLRWYRERQVVSHLHDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELKSKTSDRLETVILDVTNTDSISAATQWVKEHVGDKGLWGLVNNAGVFQAFAYIEWCRPEDCMSIFQVNLIGLAQVTLSMLFLVKKARGRIVNVSSVLGRVALFGGFYSCSKYGVEAFSDVLRREIRDFGVKVSIIEPGSFKTRMTDAELIIEKTKKTWEATPEHIRESYGQQFFDDFCNTTRRELKKCSTNLSLVTDCMEHALTSKYPRTRYSAGWDARLFFIPLSYLPTSLVDCLLAISRRKPAQAV
Protein: Protein Tax-1 (Protein X-LOR) (Trans-activating transcriptional regulatory protein of HTLV-1) (P0C222)
Organism: Human T-cell leukemia virus 1 (isolate Melanesia mel5 subtype C) (HTLV-1)
Function: Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to three 21 bp repeat elements located within the LTRs, referred to as Tax-responsive elements (TRE). Binding to TRE requires the interaction with CREB1 and CREBBP. Also induces chromatin remodeling of proviral LTR-mediated gene expression by recruiting the histone acetyl transferases CREBBP and EP300 to the chromatin, which results in histone acetylation. Via its interaction with IKK regulatory subunit IKBKG, Tax-1 persistently stimulates I-kappa-B kinase (IKK), resulting in constitutive activation of the transcription factor NF-kappa-B. Induction of the nuclear expression of members of the NFkB family of transcription factors, which leads to up-regulated expression of many gene promoters containing NFkB motifs. These genes include those encoding IL2, IL15, IL2RA and IL15RA, leading to autocrine IL2/IL2RA and IL15/IL15RA loops. The resulting T-cell proliferation leads to malignant transformation and to the development of adult T-cell leukemia (ATL). IL13, known to be linked to leukemogenesis, is also up-regulated by Tax-1. Interaction with PDZ domain-containing proteins induce IL2-independent growth, which may be a factor in multi-step leukemogenesis. Inhibits the action of at least three cellular tumor suppressors p53/TP53, RB1 and DLG1, and suppresses their abilities to dictate apoptosis in primary cells. Required for viral replication (By similarity).
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03409}. Host cytoplasm {ECO:0000250|UniProtKB:P03409}. Note=Shuttles from the host nucleus to the cytoplasm. Found predominantly in the nucleus, where it is equally distributed between the nucleoplasm and the nuclear matrix. {ECO:0000250|UniProtKB:P03409}.
Interaction partners:
Sequence:
MAHFPGFGQSLLYGYPVYVFGDCVQGDWCPISGGLCSARLHRHALLATCPEHQITDPIDGRVIGSALQFLIPRLPSFPTQRTSKTLKVLTPPTTHTTPNIPPSFFQAVRQHSPFRNGCMEPTLGQQLPSLSFPDPGLRPQNLYTLWGSSVVCMYLYQLSPPITWPLLPQVIFCHPGQLGAFLTNVPYKRMEELLYKIFLNTGALIILPEGCLPTTLFQPIRAPATLTAWQNGLLPFQSTLTTPGLIWTFSDGTPMISGPCPKDGQPSLVLQSSSFIFHKFQTKAYHPSVLLSHGLIQYSSFHSLHLPFEEYTNIPISLLFNKREADDTDYGPRIPPGGLEPPSEKHFHETEV