wanglab/gogpt-training-data huggingface dataset:
Protein: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1) (mSAMHD1) (Q60710)
Organism: Mus musculus (Mouse)
Function: Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (By similarity). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells. Likewise, suppresses LINE-1 retrotransposon activity. In addition to virus restriction, dNTPase activity acts as a regulator of DNA precursor pools by regulating dNTP pools (By similarity). Phosphorylation at Thr-634 acts as a switch to control dNTPase-dependent and -independent functions: it inhibits dNTPase activity and ability to restrict infection by viruses, while it promotes DNA end resection at stalled replication forks (By similarity). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication (By similarity). Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation (By similarity). Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity (By similarity). Enhances immunoglobulin hypermutation in B-lymphocytes by promoting transversion mutation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}. Chromosome {ECO:0000250|UniProtKB:Q9Y3Z3}. Note=Localizes to sites of DNA double-strand breaks in response to DNA damage. {ECO:0000250|UniProtKB:Q9Y3Z3}.
Interaction partners:
- DDB1- and CUL4-associated factor 1
- Ribonuclease H2 subunit A
- Ribonuclease H2 subunit C
- Ribonuclease H2 subunit B
- DNA dC->dU-editing enzyme APOBEC-3
- Three-prime repair exonuclease 1
- Double-stranded RNA-specific adenosine deaminase
- DNA damage-binding protein 1
- Cullin-4A
- Serine incorporator 5
Sequence:
MDSLLGCGVSAAAREPVPRYLTSQPRVSEVAMQSAPLEQPAKRPRCDGSPRTPPSTPPATANLSADDDFQNTDLRTWEPEDVCSFLENRGFREKKVLDIFRDNKIAGSFLPFLDEDRLEDLGVSSLEERKKMIECIQQLSQSRIDLMKVFNDPIHGHIEFHPLLIRIIDTPQFQRLRYIKQLGGGYYVFPGASHNRFEHSLGVGYLAGCLVRALAEKQPELQISERDILCVQIAGLCHDLGHGPFSHMFDGRFIPRARPEKKWKHEQGSIEMFEHLVNSNELKLVMKNYGLVPEEDITFIKEQIMGPPITPVKDSLWPYKGRPATKSFLYEIVSNKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFIKFARICEVEYKVKEDKTYIRKVKHICSREKEVGNLYDMFHTRNCLHRRAYQHKISNLIDIMITDAFLKADPYVEITGTAGKKFRISTAIDDMEAFTKLTDNIFLEVLHSTDPQLSEAQSILRNIECRNLYKYLGETQPKREKIRKEEYERLPQEVAKAKPEKAPDVELKAEDFIVDVINVDYGMEDKNPIDRVHFYCKSNSKQAVRINKEQVSQLLPEKFAEQLIRVYCKKKDGKSLDAAGKHFVQWCALRDFTKPQDGDIIAPLITPLKWNNKTSSCLQEVSKVKTCLKF
Protein: Phosphodiesterase (EC 3.1.4.-) (Q9GQU6)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MTHNGGRHLLEAVTLCGSILTRYKRSNMKLDEAEVRALKELFEKYQDILVDGSPGLPTHASGPMIQPPVTNMVAPYDSPTDTIVKFVEGTINLQRPIVEVLHVMNEHLSLVLRAKNTHVFYVDPVNNLLYDPIHGVAAALDESSPIGKAIVSGERLNVAGTLYIPIISEGMPLGCVLSPCGRADYHASTMLESSLRVISTSLKNIIQAEKLNWNKEKAEAMLRMATQLARDNLEETVLASSIMNTVKSLTESARCSLFLVRGDVLEAHFEDGNVVTIPRGAGIAGYVAQTGETVNIVDAYADDRFNREVDKATGYRTKTILCMPVMYEGTIVAVAQLINKLDLTTESGLRLPRVFGKRDEELFQTFSMFAGASLRNCRINDRLLKEKKKSDVILDVVTVLSNTDIRDVDGIVRHALHGAKKLLNADRSTLFLVDKERNELCSRMADSVAGKEIRFPCGQGIAGTVAASGVGENIQDAYQDPRFNREVDKQLGYRTQTILCEPIILNGEILAVVQLVNKLDTSGEVTVFTEDDRETFRVFSLFAGISINNSHLLEFAVKAGREVMELNEHRATLFNKNVPSRAVKRVTAITKVEREAVLVCELPSFDVTDVEFDLFRARESTDKPLDVAAAIAYRLLLGSGLPQKFGCSDEVLLNFILQCRKKYRNVPYHNFYHVVDVCQTIYTFLYRGNVYEKLTELECFVLLITALVHDLDHMGLNNSFYLKTESPLGILSSASGNTSVLEVHHCNLAVEILSDPESDVFGGLEGAERTLAFRSMIDCVLATDMAKHGSALEAFLASAADQSSDEAAFHRMTMEIILKAGDISNVTKPFDISRQWAMAVTEEFYRQGDMEKERGVEVLPMFDRSKNMELAKGQIGFIDFVAAPFFQKIVDACLQGMQWTVDRIKSNRAQWERVLETRLSTSSGNNSSTR
Protein: Large ribosomal subunit protein uL1 (50S ribosomal protein L1) (BL1) (Q06797)
Organism: Bacillus subtilis (strain 168)
Function: Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
Interaction partners:
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein bL36
- Large ribosomal subunit protein bL27
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL15
Sequence:
MAKKGKKYVEAAKLVDRSKAYDVSEAVALVKKTNTAKFDATVEVAFRLGVDPRKNDQQIRGAVVLPNGTGKTQRVLVFAKGEKAKEAEAAGADFVGDTDYINKIQQGWFDFDVIVATPDMMGEVGKIGRVLGPKGLMPNPKTGTVTFEVEKAIGEIKAGKVEYRVDKAGNIHVPIGKVSFEDEKLVENFTTMYDTILKAKPAAAKGVYVKNVAVTSTMGPGVKVDSSTFNVK
Protein: Oxytocin-neurophysin 1 (OT-NPI) [Cleaved into: Oxytocin (Ocytocin); Neurophysin 1] (P01175)
Organism: Bos taurus (Bovine)
Function: Neurophysin 1 specifically binds oxytocin.
Subcellular location: Secreted.
Interaction partners:
- Oxytocin receptor
- Vasopressin-neurophysin 2-copeptin
- Vasopressin V1a receptor
- Pro-thyrotropin-releasing hormone
- Placental prolactin-related protein 1
- Placental prolactin-related protein 4
- Placental prolactin-related protein 3
- Pro-opiomelanocortin
- Prolactin-related protein IX
- Prolactin-related protein 14
Sequence:
MAGSSLACCLLGLLALTSACYIQNCPLGGKRAVLDLDVRTCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCSPDGCHEDPACDPEAAFSQH
Protein: Cellulose synthase-like protein D4 (EC 2.4.1.-) (OsCslD4) (Q2QNS6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UDP-glucuronate decarboxylase
- Probable UDP-arabinose 4-epimerase 2
- Probable UDP-arabinose 4-epimerase 3
- Probable UDP-arabinose 4-epimerase 1
- UDP-glucuronate decarboxylase
- UDP-D-apiose/UDP-D-xylose synthase
- Os04g0563801 protein
- UDP-glucuronate decarboxylase
- Os07g0674100 protein
- UDP-glucuronate decarboxylase
Sequence:
MSRRLSLPAGAPVTVAVSPVRSPGGDAVVRRGSGLTSPVPRHSLGSSTATLQVSPVRRSGGSRYLGASRDGGADESAEFVHYTVHIPPTPDRATASVASEAEAAAEAEEVHRPQRSYISGTIFTGGLNCATRGHVLNFSGEGGATAASRAAASGNMSCKMRGCDMPAFLNGGRPPCDCGFMICKECYAECAAGNCPGCKEAFSAGSDTDESDSVTDDDDDEAVSSSEERDQLPLTSMARKFSVVHSMKVPGAAANGNGKPAEFDHARWLFETKGTYGYGNALWPKDGHAHSGAGFVAADEPPNFGARCRRPLTRKTSVSQAILSPYRLLIAIRLVALGFFLAWRIRHPNPEAVWLWAMSVACEVWFAFSWLLDSLPKLCPVHRAADLAVLAERFESPTARNPKGRSDLPGIDVFVTSADPEKEPPLVTANTILSILAADYPVEKLACYLSDDGGALLSFEALAETASFARTWVPFCRKHGVEPRCPEAYFGQKRDFLKNKVRVDFVRERRKVKREYDEFKVRVNSLPEAIRRRSDAYNAGEELRARRRQQEEAAAAAAAGNGELGAAAVETAAVKATWMSDGSHWPGTWTCPAADHARGDHAGIIQAMLAPPTSEPVMGGEAAECGGLIDTTGVDVRLPMLVYVSREKRPGYDHNKKAGAMNALVRTSAIMSNGPFILNLDCDHYVHNSSALREGMCFMLDRGGDRVCFVQFPQRFEGVDPSDRYANHNLVFFDVSMRAMDGLQGPMYVGTGCVFRRTALYGFSPPRATEHHGWLGRRKIKLFLTKKKSMGKKTDRAEDDTEMMLPPIEDDDGGADIEASAMLPKRFGGSATFVASIPVAEYQGRLLQDTPGCHHGRPAGALAVPREPLDAATVAEAIGVISCFYEEKTEWGRRIGWIYGSVTEDVVTGYRMHNRGWRSVYCVTPRRDAFRGTAPINLTDRLHQVLRWATGSVEIFFSRNNALFASPRMKLLQRVAYFNAGMYPFTSVFLLAYCLLPAVSLFSGKFIVQRLSATFLAFLLVITLTLCLLALLEIKWSGITLHEWWRNEQFWVIGGTSAHPAAVLQGLLKVIAGVDISFTLTSKPGNGGGDGGVGGEGNDDEAFAELYEVRWSYLMVPPVTIMMVNAVAIAVAAARTLYSEFPQWSKLLGGAFFSFWVLCHLYPFAKGLLGRRGRVPTIVFVWSGLISMIISLLWVYINPPAGARERIGGGGFSFP
Protein: Metaxin-1 (Mitochondrial outer membrane import complex protein 1) (Q4KLN2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
RCSRGHVQFGKSPQRPLSRTRCPSSKPCLSPAVRGYARQRHRESPKRAWTAALLPYGGRLRTSPRRSSEGQCSTSSSAAASPAARSHASLDLKLRVATQAETRGCSSWREKADAYERVLPGQRMCKMAAPMELFCWSGGWGLPSVDLDSLAVLTYTRFTCAPLKVHKISNPWQSPSGTLPALRTSSGKVITEPHKIITHLRKEKYNADYDLSARQGADTLAFISLLEEKLLPMLIHTFWIDAKNYVEVTRKWYAEAMPFPLNFFLPGRMQRRHMERLQLLCGEHRLESEEELEKELYQEARECLTLLSHRLGSRKFFFGDAPASLDAFVFSHLVLLLQAKLPSGKLQAHLRGLQNLCVYCTHILNLYFPRDATDVPPPPCQTPAGPETEEEPYRRRTQILSVLAGLAAMVGYALLSGIVSIQRASPARAPCTQALDLAEEDEED
Protein: Retinal guanylyl cyclase 1 (Guanylate cyclase 2E) (Guanylyl cyclase GC-E) (EC 4.6.1.2) (P52785)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors. Plays an essential role in phototransduction, by mediating cGMP replenishment. May also participate in the trafficking of membrane-asociated proteins to the photoreceptor outer segment membrane.
Subcellular location: Photoreceptor outer segment membrane {ECO:0000269|PubMed:21598940}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Guanylyl cyclase-activating protein 1
- Guanylyl cyclase-activating protein 2
- Neurocalcin-delta
- Retinal guanylyl cyclase 2
- Guanylate cyclase D
- Bis
- Inosine triphosphate pyrophosphatase
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
Sequence:
MSAWLLPAGGLPGAGFCVPARQSPSSFSRVLRWPRPGLPGLLLLLLLPSPSALSAVFKVGVLGPWACDPIFARARPDLAARLAANRLNRDFALDGGPRFEVALLPEPCLTPGSLGAVSSALSRVSGLVGPVNPAACRPAELLAQEAGVALVPWGCPGTRAAGTTAPAVTPAADALYVLLRAFRWARVALITAPQDLWVEAGRALSTALRARGLPVALVTSMETSDRSGAREALGRIRDGPRVRVVIMVMHSVLLGGEEQRYLLEAAEELALTDGSLVFLPFDTLHYALSPGPEALAAFVNSSQLRRAHDAVLTLTRRCPPGGSVQDSLRRAQEHQELPLDLNLKQVSPLFGTIYDAVFLLAGGVKRARTAVGGGWVSGASVARQVREAQVSGFCGVLGRTEEPSFVLLDTDASGEQLFATHLLDPVLGSLRSAGTPMHFPRGGPAPGPDPSCWFDPDVICNGGVEPGLVFVGFLLVIGMGLTGAFLAHYLRHRLLHMQMASGPNKIILTLEDVTFLHPPGGSSRKVVQGSRSSLATRSASDIRSVPSQPQESTNVGLYEGDWVWLKKFPGEHHMAIRPATKTAFSKLRELRHENVALYLGLFLAGTADSPATPGEGILAVVSEHCARGSLHDLLAQREIKLDWMFKSSLLLDLIKGMRYLHHRGVAHGRLKSRNCVVDGRFVLKVTDHGHGRLLEAQRVLPEPPSAEDQLWTAPELLRDPSLERRGTLAGDVFSLAIIMQEVVCRSTPYAMLELTPEEVIQRVRSPPPLCRPLVSMDQAPMECIQLMTQCWAEHPELRPSMDLTFDLFKSINKGRKTNIIDSMLRMLEQYSSNLEDLIRERTEELEQEKQKTDRLLTQMLPPSVAEALKMGTSVEPEYFEEVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGAHDVYKVETIGDAYMVASGLPQRNGQRHAAEIANMSLDILSAVGSFRMRHMPEVPVRIRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVNMSTVRILRALDQGFQMECRGRTELKGKGIEDTYWLVGRLGFNKPIPKPPDLQPGASNHGISLQEIPPERRKKLEKARPGQFTGK
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) (RAD2 homolog nuclease 1) (RTH1 nuclease) (Structure-specific endonuclease RAD27) (P26793)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Subcellular location: Nucleus, nucleolus. Nucleus, nucleoplasm. Mitochondrion. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
Interaction partners:
- DNA ligase 1
- Proliferating cell nuclear antigen
- DNA polymerase delta catalytic subunit
- DNA replication ATP-dependent helicase/nuclease DNA2
- ATP-dependent helicase SGS1
- DNA repair protein RAD51
- Telomere length regulation protein ELG1
- DNA repair and recombination protein RAD52
- Crossover junction endonuclease MUS81
- ATP-dependent DNA helicase SRS2
Sequence:
MGIKGLNAIISEHVPSAIRKSDIKSFFGRKVAIDASMSLYQFLIAVRQQDGGQLTNEAGETTSHLMGMFYRTLRMIDNGIKPCYVFDGKPPDLKSHELTKRSSRRVETEKKLAEATTELEKMKQERRLVKVSKEHNEEAQKLLGLMGIPYIIAPTEAEAQCAELAKKGKVYAAASEDMDTLCYRTPFLLRHLTFSEAKKEPIHEIDTELVLRGLDLTIEQFVDLCIMLGCDYCESIRGVGPVTALKLIKTHGSIEKIVEFIESGESNNTKWKIPEDWPYKQARMLFLDPEVIDGNEINLKWSPPKEKELIEYLCDDKKFSEERVKSGISRLKKGLKSGIQGRLDGFFQVVPKTKEQLAAAAKRAQENKKLNKNKNKVTKGRR
Protein: Smooth, isoform M (A0A0B4K852)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYNGASNGSGASGAGGGGATIVVTEGPQNKKIRTGVQQPGENDVHMHARSTPQQNQQQALMNKSNDDLRRKRPETTRPNHILLFTIINPFYPITVDVLHKICHPHGQVLRIVIFKKNGVQAMVEFDNLDAATRARENLNGADIYAGCCTLKIDYAKPEKLNVYKNEPDTSWDYTLSTGEILPIKEIGNGRSPLLQEPLYEPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN
Protein: Slit homolog 1b (Drosophila) (Slit homolog 1b isoform X1) (A0A0R4IU60)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPDTERSRPSSGLWIWALLLSLFLSGRSGACPPHCSCTGSTVDCHGLAFKSVPRNIPKTTERLDLNANNLTHIGKDDFAGLKHLRILHLMDNQIVSIDRGAFSDLKELDRLRLNRNRLQQLPELLFLKNPALSRLDLSENNIQMIPRRAFRGATDIKNLQLDKNHISCIEDGAFRAMRVLEVLTLNNNNISAIPISSFNHMPKLRTFRLHWNSLRCDCHLSWLSQWLRQRPALGLYTQCSSPAHLHGLNLAELQKKDFTCAGALDSSPQPCGLASGSCPPMCSCTNNIVDCRGKGLTAIPANMPESMTEIRLEQNGIKSVPPGAFSSYKRLRRIDLSNNQISEIAPDAFHGLRSLNSLVLYGNKITDLPRGVFDGLSALELLLLNANKIHCVRVNVFQDLENLSLLSLYDNKIQTLAKGTFAPLKSIQTLHLAQNPFVCDCGLKWLADFLRSNPIETSGARCSSPRRLANKRISQIKSKKFRCSAKEQYYIPGSEDTRMNKDCNSKPVCPPKCRCEATVVDCSNLRLTKFPEHLPLSTTELRLNNNDLSILEATGLFRPLTHLKKINLSNNKITEIEDGAFDGASSVVELHLTANLLVSVRGGMFRGMDGLRMLMLRNNHIRCVHNSSFSGLQNVRLLSLYDNQLTTIMPGAFDSLPNLSTLNLLANPFSCDCRLSWLGEWLRSRQIVTGNPRCQNPAFLREIPLQDVAKPDFICDKDVLEQDVSCIPKPQCPEQCTCVDSVVRCSNKHLSALPRGVPLNVTELYLDGNVFVSIPQELSAFRQLQLLDLSNNKISSLTNTSFTNMSQLTTLILSYNALRCIPPLVFGGLSSLRLLSLHGNNISELHQQIFRDAASLSHLAIGANPLYCDCRLRWLSDWVKSGYKEPGIARCAGPQGMEGKLLLTTPGNTFQCTGPVDASVSGKCSPCSSNPCQNQGRCHNDPLHQYKCSCPQGYKGRNCELSISACEANPCVNGGTCRPEESRRGFRCVCPLGFEGLFCELDVDDCVDHQCVNGTICVDGVGNYSCVCAQPFSGQKCEEYEEDLCYPGQNPCQRGSTCIPTVSGPKCICPPGFVGDDCSVDYNECEGHYCQNGARCVDHVAGYTCVCPAGYSGRLCEASVSACDLLQCVNGAPCEEISGTAVCQCLPGFNGLRCEKLLSVNFIDRDSYLLLLRDATQSTHNNITLQVSTAEDNGILLYNGVNEHIAVELHDGHVKVTYDAGRQPGSTIYSSEIVNDGQFHTVELVTYERMVNLSIDGGLPTTLDSSGHIQPLTRDAPLYVGGMPENAKSLSSNHWPPVNGSSFQGCIRNLYINNELQDFTQTQMKPGVVPGCQACQELLCVNGLCQPDSAIGPVCHCQPGWGGKHCDQILLTAAAATNPCQKHKCVHGVCVAVDLQSYRCECVEGFHGQLCSQQDPCTALSCQHGLCQISPTGQPQCVCDSGYSGQLCDIVSPCQGEPVRDFHRVQRGDVQCRSTLPMSWTECRGGCRADSGLCCVGLRVRRRRYGFECDDGTTFTQEVEKTVECGCGKCV
Protein: Translocase of chloroplast 34 homolog, chloroplastic (Cr-TOC34) (TOC34p) (EC 3.6.5.-) (A8HYJ1)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis (By similarity). Functions as an essential component of the outer chloroplast membrane translocon (TOC) complex, which, in turn, catalyzes the import of nucleus-encoded precursor polypeptides from the cytoplasm to the chloroplast.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000250|UniProtKB:Q38906}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAQPPRPAEEYDDDVQEDEDELKEGELDDDESHEAASEGGEAAAGDEEAEDDEQDEEDGDEDSQPWAGLNRLPERDDMLDILNELRAEGRKQLTVLLLGKSSVGKSSLINSLLGEAVVRVQAFKLQADTDITTTVVRQVAVGNSEVDGFRLKLIDTCGLEDPEAGDTVNLGALSKIAEDVRGVGIDVVLYCDRLDLYRVDPLDKAIIDAISSTFGRGIWRRTVVALTHANLVQTPPGTDYDSFVNGRVRLIRGAVRGPLFFRPSLPVALVENSETCPVSSESGFRVLPDGEPWLVALVSQLVDMAAARRRPYKYHPRLSSKPSHRFRWLLPVAIAAEVLFYRRFLHPRLDDNQRRVEREEERVWALRGQQRRALGLHRPHRPDKDAAWRLEQMYDDD
Protein: cAMP-dependent protein kinase catalytic subunit 1 (PKA C) (EC 2.7.11.11) (Protein kinase DC0) (P12370)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine/threonine-protein kinase involved in memory formation. Promotes long-term memory by phosphorylating meng and by regulating CrebB protein stability and activity. As part of ethanol response in the glia, mediates ethanol-induced structural remodeling of actin cytoskeleton and perineurial membrane topology when anchored to the membrane.
Interaction partners:
- cAMP-dependent protein kinase type II regulatory subunit
- cAMP-dependent protein kinase type I regulatory subunit
- Protein smoothened
- Kinesin-like protein costa
- Suppressor of fused homolog
- Transcriptional activator cubitus interruptus
- Serine/threonine-protein kinase fused
- Forkhead box protein O
- Presenilin homolog
- Protein kinase shaggy
Sequence:
MGNNATTSNKKVDAAETVKEFLEQAKEEFEDKWRRNPTNTAALDDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKRYGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPRCKGPGDTSNFDDYEEEALRISSTEKCAKEFAEF
Protein: Down syndrome cell adhesion molecule 1, isoform AZ (Q0E9M1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVPQSYTVNVMDESILRGNSAILKCHIPSFVADFIVVDSWVEDEERVIYPQEDIAESDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPIGSVSPKISNSDDLKHVKVKRLLSLSLLCPAQAYPQPISRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVAPKIAPFDFGDEPSNFGESASVQCLVTSGDFPVSFAWLFNGREINENVYDVSMVKLGKKISALSIDIVRDHHAGNYTCVAVNRATSVNFTAELVVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Probable ATP-dependent DNA helicase CHR12 (EC 3.6.4.12) (Protein CHROMATIN REMODELING 12) (AtCHR12) (Protein MINUSCULE 1) (F4J9M5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable chromatin-remodeling factor that is functionally redundant with CHR23 in root and shoot stem cell initiation, and root apical meristem (RAM) and shoot apical meristem (SAM) maintenance. Plays an important role in mediating the temporary plant growth arrest induced upon perception of stress. May promote seed maturation and repress initiation of germination.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Chromatin structure-remodeling complex protein BSH
- SWI/SNF complex subunit SWI3A
- SWI/SNF complex subunit SWI3B
- SWI/SNF complex subunit SWI3D
- SWI/SNF complex subunit SWI3C
- Actin-related protein 4
- At3g01890
- SWI/SNF complex component SNF12 homolog
- Actin-related protein 7
- Chromatin remodeling factor18
Sequence:
MVAQQLQERCGGTSQEDPVETTKSLICALNYISRDLPLPPHLFTAVSSIYHGASSSSLSDSDVSPPLPTSPPANKAPYGADLMGEFEDALLKQRPDCESGSRLIQLLDNRNKSHIQRRLSELEELPSTRGEDLQAKCLLELYGLKLRELQGKVRTAVSSEFWLRLNCADVSSQVFDWGMMRLPRPFYGVGDPFAMEADDQFRKKRDAERLSRLEEEEKNLIETAKRKFFAEVLNAVREFQLQIQATQKRRRQRNDGVQAWHGRQRQRATRAEKLRLMALKSDDQEAYMKLVKESKNERLTTLLEETNKLLANLGAAVQRQKDAKLPEGIDLLKDSESDLSELDAPRSEPLQDLLPDQDIDITESDNNDDSNDLLEGQRQYNSAIHSIQEKVTEQPSLLEGGELRSYQLEGLQWMVSLFNNNLNGILADEMGLGKTIQTISLIAYLLENKGVPGPYLIVAPKAVLPNWVNEFATWVPSIAAFLYDGRLEERKAIREKIAGEGKFNVLITHYDLIMRDKAFLKKIEWYYMIVDEGHRLKNHESALAKTLLTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSVQNFEEWFNAPFADRGNVSLTDEEELLIIHRLHHVIRPFILRRKKDEVEKFLPGKTQVILKCDMSAWQKVYYKQVTDMGRVGLQTGSGKSKSLQNLTMQLRKCCNHPYLFVGGDYNMWKKPEIVRASGKFELLDRLLPKLRKAGHRILLFSQMTRLIDVLEIYLTLNDYKYLRLDGTTKTDQRGLLLKQFNEPDSPYFMFLLSTRAGGLGLNLQTADTVIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSVGSVEEVILERAKQKMGIDAKVIQAGLFNTTSTAQDRREMLEEIMRKGTSSLGTDVPSEREINRLAARSEDEFWMFERMDEERRRKENYRARLMQEQEVPEWAYTTQTQEEKLNNGKFHFGSVTGKRKRKEIVYSDTLSELQWLKAVESGEDLSKLSMRYNRREENASNTKTSTSKKVIESIQTVSDGTSEEDEEEQEEERAKEMSGKQRVDKSEEEEEEGEEENDGKAIFKWNTHKKKRSRYSFTCSSSDSRAQSSNGSRRK
Protein: Ceramide synthase LOH1 (CS1) (CSII) (EC 2.3.1.-) (Protein LONGEVITY ASSURANCE GENE ONE HOMOLOG 1) (LAG One Homolog 1) (LAG1 homolog 1) (LAG1 longevity assurance homolog 1) (Q9LDF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for plant growth, promotes cell division in root meristems. Catalyzes the biosynthesis of ceramide sphingolipids with C(16) to C(28) fatty acids, structural membrane lipids involved in membrane trafficking (e.g. early endosomes) and cell polarity (e.g. polar auxin transport related proteins); mostly active with t18:0 and saturated very long saturated fatty acids (C24:0 and C26:0), such as long-chain base (LCB) phytosphingosine (t18:0), lignoceroyl- and hexacosanoyl-CoAs. Mediates resistance to sphinganine-analog mycotoxins (SAMs, e.g. fumonisin B(1)) by restoring the sphingolipid biosynthesis (By similarity). Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure (By similarity). May prevent precocious cell death by delaying PR1 accumulation during aging. Contributes to hypoxic conditions tolerance (e.g. submergences), especially in the dark, by promoting the formation of very-long-chain (VLC) ceramide species (22:1, 24:1 and 26:1) and of VLC unsaturated ceramides, which are modulating CTR1-mediated ethylene signaling leading to endoplasmic reticulum (ER)-to-nucleus translocation of EIN2 and EIN3.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8C172}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- TTF-type zinc finger protein with HAT dimerization domain-containing protein
- Uncharacterized CRM domain-containing protein At3g25440
- Ceramide kinase
- 3-dehydrosphinganine reductase TSC10B
- Long chain base biosynthesis protein 2b
- Phosphatidylinositol:ceramide inositolphosphotransferase 2
- 3-dehydrosphinganine reductase TSC10A
- N-alpha-acetyltransferase 40
- Bromodomain transcription factor
- Transcription initiation factor TFIID subunit 8
Sequence:
MGLFESVKSIDWEQESFPTYQDLGFLPLFAVFFPTIRFLLDRFVFEKLASLVIYGRMSTNKSDNIKDRKKNSPKVRKFKESAWKCIYYLSAELLALSVTYNEPWFSNTLYFWIGPGDQIWPDQPMKMKLKFLYMFAAGFYTYSIFALVFWETRRSDFGVSMGHHITTLVLIVLSYICRLTRAGSVILALHDASDVFLEIGKMSKYCGAESLASISFVLFALSWVVLRLIYYPFWILWSTSYQIIMTVDKEKHPNGPILYYMFNTLLYFLLVLHIFWWVLIYRMLVKQVQDRGKLSEDVRSDSESDDEHED