wanglab/gogpt-training-data huggingface dataset:
Protein: Ral GTPase-activating protein subunit alpha-2 (250 kDa substrate of Akt) (AS250) (p220) (P86411)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of the heterodimeric RalGAP2 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q2PPJ7}.
Interaction partners:
- Rho GTPase activating protein 4
Sequence:
MFSRRSHGDVKKSTQKVLDPKKDVLTRLKHLRALLDNVDASDLKQFFETNYSQIYFIFYENFITLENSLKLKGNNKSQREELDSILFLFEKILQFLPERIFFRWHYQSIGSTLKKLLHTGNSIKIRCEGIRLFLLWLQALQTNCAEEQVLIFACLVPGFPAVLSSRGPCTLETLINPSPSVVDAKIYPEEITPLLPAVSGEKIAEDQTCFFLQILLKYMVIQAASLEWKNKENQDTGFKFLFTLFRKYYLPHLFPSFTKLTNIYKPVLEIPHLRPKPLYVTVTRDNETIYSTKIPYMAARVVFIKWIVTFFLEKKYLTATQNTKNGVDVLPKIIQTVGGGAIQEKVPELDGAGATEQDKSHSNSSTLSDRRLSNSSLCSIEEEHRTVYEMVQRILLSTRGYVNFVNEVFRQAFLLPSCEISITRKVVQVYRKWILQNKPVFMEEPDKKDVAEEDADKLGLSETDSKEVSSESSGHKRSSSWGRTYSFTSAMSRGCVTEEDNTNVKAGAQAMLQVFLTNAANVFLLEPCVEVPMLLREQVDACKAVLIIFRRMIMELTMNQKTWEQMLQILLRITEAVMQKPKDKLVQDSFARSLAGLLFRTLIVAWIRANLCVYISRELWDDFLRVLSSLTEWEELITEWSNIMDSLTAVLARTVYGVEMTNLPLDKLSEQKEKKQRGKGCVLEPQKGTAVGRSFSLSWRSHPDVTEPMRFRSATTSGAPGVEKARNTVRQKATEVEEFQQAESTAAADCDYLVVGQQPVPRSSSTSDITERLYSDSSQGQKVENSQNLSSSEPKSVQESKGHVTHEHEGVTILVRRSSSPAELDLKEESQQTHGRCRERQKSESTGSDMAVGYSNEAELPVSPWQTCEEDPELSTPTDAVADSDARHWLQLSPTDASNLTESRECLADDCSIIAGGNLTGWHPDSAAVLWRRVLGILGDVNNIQSPKIHAKVFSYLYELWYKLAKIRDNLAISLDNQSSPSPPLLIPPLRMFASWLFKATTLPNEYKEGKLQAYKLICAMMTRRQDVLPNSDFLVHFYLVMHLGLTSEDQDVLNTIIKNCSPRFFSLGLPGFSMLVGDFITAAARVLSTDMLAAPRSEALTLLGSLVCFPNTYQEIPLLQSVPEVSDVVTGAEDVKHYLINILLKNATEEPNECARCIAICSLGVWICEELAQCASHPQVKDAINVIGVTLKFPNKIVAQVACDVLQLLVSYWEKLQMFETALPRKMAEILVATIAFLLPSAEYSSVETDKKFIVSLLLCLLDWCMALPVSALLHPVSTAVIEELHPSRAPLLDYIYRVLHCCVCGSSTYTQQSHYTLTLADLSSTDYDPFLPLANVRNSEPVQYHSSADLGNLLTVEEEKKRRSVELIPLTARMVMAHLVNHLGHYPLSGGPAVLHSLVSENHDNAHVEGTELSSEVFRSPNLQLFVFNDSTLISYLQTPAEGPAGGTSGGSLSDVRVIVRDISGKYSWDGKVLYGPLEGRLAPSGRNPSFQISGWHHHTCGPQSNLFHGEEGDDVLDKLLENIGHTSPECLLPSQLNLNEPSPTPSAMNCDQEKEIIEVILRQSTQEDEYVQRCHSNSAVKVTSQGQPSPVEPRGPFYFCRLLLDDLGMNSWDRRKNFHLLKKNSKLLRELKNLDSRQCRETHKIAVFYIAEGQEDKCSILANERGSQAYEDFVAGLGWEVDLSTHCGFMGGLQRNGSTGQTAPYYATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHSRDYRRGIIPTAFGDVSIIIYPMKNHMFFITITKKPEVPFFGPLFDGAIVSGKLLPSLICATCINASRAVKCLIPLYQSFYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSLSGTD
Protein: Autophagy-related 16, isoform B (Q9VAF9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKKRLLKSFSFSYNSQDENRRLLERLMQYKSKDADKLNEENESIIRKRSAKLKRDLEDAVREPSSSSNAASSPGAASLQRNSSPAQFVGGLIGDEDFDEAAINGAMEAIGLDDNEYISARFTAGEIAENSRASIDTLKATGYLGQANPTKILMKFEAHENESHAVRWSPVERMVATGGADRKVKLWDIGKNSTEPRAVLSGSSAGINSVDFDSTGAYILGTSNDYGARVWTVMDNRLRHTLTGHSGKVMAAKYVQEPIKVVTGSHDRTLKIWDLRSIACIETKFAGSSCNDLVTTDSLGSTIISGHYDKKIRFWDIRTEKQADDVLMPAKITSLDLSKDCNYLICSVRDDTIKLLDLRKNQVISTFTNEHFKISCDFARASFNSSGLKIACGSADGAIYIWNVNGFLEATLKGHSTAVNAVSWSPNNNMLASVGKNKRCTIYSES
Protein: V-type proton ATPase 116 kDa subunit a 4 (V-ATPase 116 kDa isoform a 4) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4) (Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform) (Q9HBG4)
Organism: Homo sapiens (Human)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Involved in normal vectorial acid transport into the urine by the kidney.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:10973252}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q920R6}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the apical surface of alpha-intercalated cells in the cortical collecting ducts of the distal nephron (PubMed:10973252). Localizes to the basolateral surface of beta-intercalated cells in the cortical collecting ducts of the distal nephron (By similarity). {ECO:0000250|UniProtKB:Q920R6, ECO:0000269|PubMed:10973252}.
Interaction partners:
- V-type proton ATPase subunit d 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit F
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase subunit E 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit H
Sequence:
MVSVFRSEEMCLSQLFLQVEAAYCCVAELGELGLVQFKDLNMNVNSFQRKFVNEVRRCESLERILRFLEDEMQNEIVVQLLEKSPLTPLPREMITLETVLEKLEGELQEANQNQQALKQSFLELTELKYLLKKTQDFFETETNLADDFFTEDTSGLLELKAVPAYMTGKLGFIAGVINRERMASFERLLWRICRGNVYLKFSEMDAPLEDPVTKEEIQKNIFIIFYQGEQLRQKIKKICDGFRATVYPCPEPAVERREMLESVNVRLEDLITVITQTESHRQRLLQEAAANWHSWLIKVQKMKAVYHILNMCNIDVTQQCVIAEIWFPVADATRIKRALEQGMELSGSSMAPIMTTVQSKTAPPTFNRTNKFTAGFQNIVDAYGVGSYREINPAPYTIITFPFLFAVMFGDCGHGTVMLLAALWMILNERRLLSQKTDNEIWNTFFHGRYLILLMGIFSIYTGLIYNDCFSKSLNIFGSSWSVQPMFRNGTWNTHVMEESLYLQLDPAIPGVYFGNPYPFGIDPIWNLASNKLTFLNSYKMKMSVILGIVQMVFGVILSLFNHIYFRRTLNIILQFIPEMIFILCLFGYLVFMIIFKWCCFDVHVSQHAPSILIHFINMFLFNYSDSSNAPLYKHQQEVQSFFVVMALISVPWMLLIKPFILRASHRKSQLQASRIQEDATENIEGDSSSPSSRSGQRTSADTHGALDDHGEEFNFGDVFVHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVMNSGLQTRGWGGIVGVFIIFAVFAVLTVAILLIMEGLSAFLHALRLHWVEFQNKFYVGDGYKFSPFSFKHILDGTAEE
Protein: 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 2 (AtDHNAT2) (DHNA-CoA thioesterase 2) (EC 3.1.2.-) (Q9FI76)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of the thioester bond of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) in peroxisomes, a necessary step to form the naphthoquinone ring of phylloquinone (vitamin K(1)). Displayed also slight thioesterase activity towards benzoyl-CoA. Is not active on phenylacetyl-CoA, succinyl-CoA and palmitoyl-CoA thioesters.
Subcellular location: Peroxisome {ECO:0000269|PubMed:22372525}.
Interaction partners:
- 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal
- 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1
- 3-hydroxyacyl-CoA dehydrogenase family protein
- 2-succinylbenzoate--CoA ligase, chloroplastic/peroxisomal
- Chorismate synthase, chloroplastic
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- 3-dehydroquinate synthase, chloroplastic
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
Sequence:
MDPKSPEFIIDQPLKILGFVFDELSATRVSGHLTLTEKCCQPFKVLHGGVSALIAEALASLGAGIASGFKRVAGIHLSIHHLRPAALGEIVFAESFPVSVGKNIQVWEVRLWKAKKTETPDNKIMVSTSRVTLFCGLPIPDHVKDAPDELKKVISKL
Protein: Probable peptidyl-tRNA hydrolase 2 (PTH 2) (EC 3.1.1.29) (O13830)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Interaction partners:
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase C18B5.05c
Sequence:
MKVPFVNFMISSFPAAVLVGAVVGFMIGRKYSVADASRGYSSKNANKASNPEKESPVSVSNDEDSESETELLDMLKGNSSLAALALAEGQTKMVLVVRTDLGMTKGKIAAQCAHAALACYKIASAVDPDLVRIWENAGQAKITLQAQTEETLELLQAQAMSLGLCARVIHDAGRTQIASGSATVLGIGPGPVSVINEVTGSLKLF
Protein: Acetyl-coenzyme A synthetase (EC 6.2.1.1) (Q57XD7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Citrate synthase
- Aldehyde dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta
- Acetyl-CoA carboxylase, putative
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase, putative
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Succinate--CoA ligase subunit beta, mitochondrial
- Enoyl-CoA hydratase/Enoyl-CoA isomerase/3-hydroxyacyl-CoA dehydrogenase, putative
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MRDTGRCSGHNDDVVDPVTSNGAMSHVGPDLAHRQALYEESVRDPVAFWEQAAADFHWERTWPKDKSPLEYNFHKSNGSIFVKWFDGAESNMCYNALDRHLPKHKDRVCYHWEGNDEGESRDVTYGEMFEEVVRIAAVLKHRYNVKKGDVVTIYLPMIPFAAQVMLAVARLGAVTSVVFAGFSSQAVASRLTDARSKLIITADSFWRGTKTLLLKELSDAALAICEAEGHNVQCLVYDRSKRENVPMTEGRDAWYSDVVETLTASELADCPIVWIGAEDPLFLLYTSGSTGKPKAILHTLGGYMVYAGVTFKYSFDYHESDVSFCTADIGWITGHSYALYGPMLNAATSVLFEGMPTHPTPSRWWDLVDKYRVTIFYTAPTAIRALMQCGDEHLQSTTRGTLRILGSVGEPINAEAWQWFYEVVGKRRADVIDTWWQTETGGHLITPLPGCTPMKAGSATLPFFGIVPALLHPTTNAVVEGEGEGLLAMQTPWPGIARTIFGDHNRYEQAYFAVDGFYLTGDGARRDKDGYYWITGRVDDVLNVSGHRIGTSEVEEAVNSHPDVAESAAVGIPHDVKGECIYVFVTFNNNVTVDATLLKRVRETVRRVIGPFAAPDYVQAAQCGLPKTRSGKIMRRILRKIASGLHEELGDTSTLLDPSVVQNLIEGRKQTVG
Protein: GTP-binding nuclear protein Ran-2 (Ras-related nuclear protein 2) (P41917)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17530257}. Nucleus envelope {ECO:0000269|PubMed:17530257}. Note=Localized in the perinuclear region with the highest concentration at the nuclear envelope at the interphase.
Interaction partners:
- Exportin-T
- Protein EXPORTIN 1A
- Protein EXPORTIN 1B
- Protein HASTY 1
- Ran-binding protein 1 homolog a
- Ran-binding protein 1 homolog b
- Ran-binding protein 1 homolog c
- Elongation factor 1-alpha 1
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 2
Sequence:
MALPNQQTVDYPSFKLVIVGDGGTGKTTFVKRHLTGEFEKKYEPTIGVEVHPLDFFTNCGKIRFYCWDTAGQEKFGGLRDGYYIHGQCAIIMFDVTARLTYKNVPTWHRDLCRVCENIPIVLCGNKVDVKNRQVKAKQVTFHRKKNLQYYEISAKSNYNFEKPFLYLARKLAGDQNLHFVESPALAPPEVHLDIAAQQQNEADLAAAAAQPLPDDDDDAFE
Protein: L-dopachrome isomerase (EC 5.3.2.1) (EC 5.3.3.12) (L-dopachrome tautomerase) (Phenylpyruvate tautomerase) (F4KAK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Probable aminotransferase TAT4
- Tyrosine aminotransferase
- Probable aminotransferase TAT1
- Tyrosine transaminase family protein
- Probable aminotransferase TAT2
- Probable aminotransferase TAT3
- 4-hydroxyphenylpyruvate dioxygenase
- Aspartate aminotransferase, cytoplasmic isozyme 1
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic isozyme 2
Sequence:
MPTLNLFTNIPVDAVTCSDILKDATKAVAKIIGKPESYVMILLNSGVPIAFAGTEEPAAYGELISIGGLGPGVNGKLSETISEILQIKLSIDSSRFYIKFYDSPVSPLLLQIQSFA
Protein: Permeases of the major facilitator superfamily (Q8NRB5)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Permeases of the major facilitator superfamily
- glycogen phosphorylase
- Phytoene dehydrogenase and related proteins
- Predicted transcriptional regulators
- Rifampin ADP-ribosyltransferase domain-containing protein
- Hypothetical membrane protein
- Permeases of the major facilitator superfamily
Sequence:
MLTQKIELEAKPKIPEEIWVLVVAAFIIALGYGLIAPILPQFVVGFDVSFAAASAVVSIFAGARLLFAPMSGSLIDKIGSRRVYLTGLLTVAITTGLVALAQEYWQILLLRGIAGIGSTMFTVSAMGLIVKMAPVEIRGRCSSVYASSFLFGNIIGPVVGAAMSGLGMRWPFAIYGASVGLAALVVWWRMPKTNDSLRKADSNSVPALRFAEAIKDSAYRSALFSAFANGWSNFGVRVAVLPLFAAAAFSNGGAIAGFAMAAFAAGNALCLQFAGDLSDRIGRKPMIISGLIVNAVFTAMIGFGTEVWILITVSALAGAGAGLLNPSQQAVLADVIDSRPGGKVLANFQMAQDFGAIVGPILVGMIAEQAGFQIGFMLCGVISLLAAVAWIFGRETLPTAKVEQV
Protein: Virion protein (Membrane) (Q77CD2)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Subcellular location: Host nucleus inner membrane {ECO:0000256|ARBA:ARBA00043948}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00043948}.
Interaction partners:
Sequence:
MHGRERDCDGEGEGEGSSRSLMARIRLLVAGNLQCGEGDVPQPWDPRRPPARCVFQFNGQDGSNESFPLEYILRLMASWAQTDCDPYVRVQNTGVSVLFQGYFSRPPGAPLAAITAEQNNATLASTQSTGLSLSALEKIKARGGIDPRPFRAMMSVSCFVRMPRVQLSFRFMGPGDSHRTGRLLDRAVRERLSERDVRSRRASACGHSERELEPAGGAGNVAHYAGALLTARRQKMAALATLVGGVCGILAILRLFWAPS
Protein: LIM domain containing preferred translocation partner in lipoma (A0A087WZF1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METTHSFGNPSISVSTQQPPKKFAPVVAPKPKYNPYKQPGGEGDFLPPPPPPLDDSSALPSISGNFPPPPPLDEEAFKVQGNPGGKTLEERRSSLDAEIDSLTSILADLECSSPYKPRPPQSSTGSTASPPVSTPVTGHKRMVIPNQPPLTATKKSTLKPQPAPQAGPIPVAPIGTLKPQPQPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAAPSSGQIYGSGPQGYNTQPVPVSGQCPPPSTRGGMDYAYIPPPGLQPEPGYGYAPNQGRYYEGYYAAGPGYGGRNDSDPTYGQQGHPNTWKREPGYTPPGAGNQNPPGMYPVTGPKKTYITDPVSAPCAPPLQPKGGHSGQLGPSSVAPSFRPEDELEHLTKKMLYDMENPPADEYFGRCARCGENVVGEGTGCTAMDQVFHVDCFTCIICNNKLRGQPFYAVEKKAYCEPCYINTLEQCNVCSKPIMERILRATGKAYHPHCFTCVMCHRSLDGIPFTVDAGGLIHCIEDFHKKFAPRCSVCKEPIMPAPGQEETVRIVALDRDFHVHCYRCEDCGGLLSEGDNQGCYPLDGHILCKTCNSARIRVLTAKASTDL
Protein: Mono(ADP-ribosyl)transferase SpvB (mADPRT) (mART) (EC 2.4.2.31) (65 kDa virulence protein) (NAD(+)--arginine ADP-ribosyltransferase) (Toxin SpvB) (P21454)
Organism: Salmonella typhimurium
Function: Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylates all actins tested, has more activity on nonmuscle beta/gamma-actin than on muscle alpha-actin. Prefers monomeric G-actin but can weakly ADP-ribosylate F-actin. ADP-ribosylation prevents the polymerization of G-actin to F-actin, causing actin filament depolymerization, destruction of the cytoskeleton and cytotoxicity. Does not possess NAD(+)-glycohydrolase activity, unlike most mART enzymes.
Subcellular location: Secreted. Note=Secreted via the type III secretion system 2 (SPI-2 T3SS). {ECO:0000305}.
Interaction partners:
Sequence:
MLILNGFSSATLALITPPFLPKGGKALSQSGPDGLASITLPLPISAERGFAPALALPYSSGGGNGPFGVGWSCATMSIARRTSHGVPQYNDSDEFLGPDGEVLVQTLSTGDAPNPVTCFAYGDVSFPQSYTVTRYQPRTESSFYRLEYWVGNSNGDDFWLLHDSNGILHLLGKTAAARLSDPQAASHTAQWLVEESVTPAGEHIYYSYLAENGDNVDLNGNEAGRDRSAMRYLSKVQYGNATPAADLYLWTSATPAVQWLFTLVFDYGERGVDPQVPPAFTAQNSWLARQDPFSLYNYGFEIRLLRLCRQVLMFHHFPDELGEADTLVSRLLLEYDENPIRTQLCAARTLAYEGDGYRRAPVNNMMPPPPPPPMMGGNSSRPKSKWAIVEESKQIQALRYYSAQGYSVINKYLRGDDYPETQAKETLLSRDYLSTNEPSDEEFKNAMSVYINDIAEGLSSLPETDHRVVYRGLKLDKPALSDVLKEYTTIVNIIIDKAFMSTSPDKAWINDTILNIYLEKGHKGRILGDVAHFKGEAEMLFPPNTKLKIESIVNCGSQDFASQLSKLRLSDDATADTNRIKRIINMRVLNS
Protein: Transposon Ty1-DR4 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q07793)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKHKTSSDKNI
Protein: Urease accessory protein G (AtUREG) (E0ZS47)
Organism: Oryza sativa subsp. indica (Rice)
Function: Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.
Interaction partners:
Sequence:
MASHDHDHHHHHHHSHDDGDHHHSHHQDGSHGGGGGSWVGEDGRVWHSHDGLAPHSHEPIYSPGDFSKRAPPLISRRFAERAFTVGIGGPVGTGKTALMLALCRSLREKYSLAAVTNDIFTKEDGEFLIKHGALPEERIRAVETGGCPHAAIREDISINLGPLEELSNLYKADLLLCESGGDNLAANFSRELADYIIYIIDVSGGDKIPRKGGPGITQADLLIINKTDLAPAVGADLAVMERDALRMREGGPFVFAQVKHGVGVEEIVNHILQAWEIATGNKRR
Protein: DNA-directed RNA polymerases IV and V subunit 4 (Protein RNA-DIRECTED DNA METHYLATION 2) (RNA polymerase II, Rpb4, core protein) (Q6DBA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. Required for the de novo DNA methylation directed by the RdDM pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:19204117}. Note=Detected as small foci dispersed throughout the nucleoplasm.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerase V subunit 7
- DNA-directed RNA polymerase IV subunit 1
- DNA-directed RNA polymerase V subunit 5A
- DNA-directed RNA polymerase V subunit 1
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerase IV subunit 7
Sequence:
MSEKGGKGLKSSLKSKDGGKDGSSTKLKKGRKIHFDQRTPPANYKILNVSSDQQPFQSSAAKCGKSDKPTKSSKNSLHSFELKDLPENAECMMDCEAFQILDGIKGQLVGLSEDPSIKIPVSYDRALAYVESCVHYTNPQSVRKVLEPLKTYGISDGEMCVIANASSESVDEVLAFIPSLKTKKEVINQPLQDALEELSKLKKSE
Protein: Protein CRAC (P35401)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Couples activated G protein to adenylyl cyclase signal transduction from surface cAMP receptor. Pianissimo a cytosolic regulator and CRAC, are both essential for activation of the enzyme adenylyl cyclase. Pianissimo and CRAC do not function redundantly. Both proteins are integral components of the adenylyl cyclase activation pathway.
Subcellular location: Cytoplasm.
Interaction partners:
- phosphatidylinositol N-acetylglucosaminyltransferase
Sequence:
MGKTERKKELLELFEYEKIKGDVSYSSIMKKAGGNGKGFLDRYFALHRNYILYYKLGKSSLKPDDKQEPQGYINLMDCNPDDTKEIAPLMFQISHKHRTYIVKAKDESSMKQFLTLLIARIRSLEKIDIDKLGCTVVVLTKVKKFREVLTNPLILPDRVSPEMAEEWVKQMKNYNASFNLADPFIKQVEQISEFCRGEVKEYIDWFGGPEGPRLAMIRCEETVLSNWVEYINKTSSEITTYQDNRFFREDFKDIAVHLKNMTTFIDCYNDYMIHCRKYNNNKPNTKFLEEKQTFKEYIEKFIPKVASCNDVSLNQFYDRSLIQSSDGIVTINTSGIKKTLINQSNIISITSTTTTTTTTTTTTCSMPNMSNLIHSLDHTNLNIIDLNHSKSQQQLHPPPSPHHQHLHHQIVSNSKDFNISVSSNNFNDGNSEFPNLDINCDFDLTSASNLSSPILSSEVPSNVVDPIGSGQGGGGSGGGGVTAVTEEAINEKWHFDCNTSMIFKPPSEDGRNEGSNMSTSSITSKMSLSLNGGFDMKWVYQCGYFKSKNMGSISWNGKHWCWSHPRTSYKIKYIWDPTKQSFLNIPFKSRVGATGGGSVPSSQSTNNLQSSTSSMSSLSSSSTSTTKRSHPTTLYPDYQFKDNLLTPIIIEGRHQPSLTLIDSPLTIPNACLLTIAMTQYIQDALIHLSLGPKVLSSK
Protein: Dual specificity phosphatase 28 (EC 3.1.3.16) (EC 3.1.3.48) (Q4G0W2)
Organism: Homo sapiens (Human)
Function: Has phosphatase activity with the synthetic substrate 6,8-difluoro-4-methylumbelliferyl phosphate (in vitro). Has almost no detectable activity with phosphotyrosine, even less activity with phosphothreonine and displays complete lack of activity with phosphoserine. The poor activity with phosphotyrosine may be due to steric hindrance by bulky amino acid sidechains that obstruct access to the active site.
Interaction partners:
Sequence:
MGPAEAGRRGAASPVPPPLVRVAPSLFLGSARAAGAEEQLARAGVTLCVNVSRQQPGPRAPGVAELRVPVFDDPAEDLLAHLEPTCAAMEAAVRAGGACLVYCKNGRSRSAAVCTAYLMRHRGLSLAKAFQMVKSARPVAEPNPGFWSQLQKYEEALQAQSCLQGEPPALGLGPEA
Protein: Hypothetical membrane-bound beta-hydroxylase (Lipid A hydroxylase LpxO) (A0A0H3NVJ7)
Organism: Salmonella typhimurium (strain SL1344)
Interaction partners:
Sequence:
MFAAIIIGIFIISVIYAHSRGVEKQKLSRQLFDHSTFMAPINMFMTRFSTLPAKQPYFDTTAFPELQKLTENWQVIREEALQLQHHIKAAQANNDAGFNTFFKRGWKRFYLKWYSDAHPSAETLCPITTKLVNSIPSIKAAMFAELPPGAYLGKHRDPYAGSVRYHLGLSTPNDDRCFIEVDRQRHSWRDGKAVIFDETYVHWAENKTEQTRIILFCDIERPMKWRWAQSVNHWVGASLMSAASSPNDENDRTGAINRIFKYVHAARDAGQRLKKKNRTLYYALKYLVIAAIFAAIILFSLL
Protein: Testis-specific Y-encoded-like protein 5 (TSPY-like protein 5) (Q86VY4)
Organism: Homo sapiens (Human)
Function: Involved in modulation of cell growth and cellular response to gamma radiation probably via regulation of the Akt signaling pathway. Involved in regulation of p53/TP53. Suppresses p53/TP53 protein levels and promotes its ubiquitination; the function is dependent on USP7 and independent on MDM2. Proposed to displace p53/TP53 from interaction with USP7.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 7
Sequence:
MSGRSRGRKSSRAKNRGKGRAKARVRPAPDDAPRDPDPSQYQSLGEDTQAAQVQAGAGWGGLEAAASAQLLRLGEEAACRLPLDCGLALRARAAGDHGQAAARPGPGKAASLSERLAADTVFVGTAGTVGRPKNAPRVGNRRGPAGKKAPETCSTAGRGPQVIAGGRQKKGAAGENTSVSAGEEKKEERDAGSGPPATEGSMDTLENVQLKLENMNAQADRAYLRLSRKFGQLRLQHLERRNHLIQNIPGFWGQAFQNHPQLASFLNSQEKEVLSYLNSLEVEELGLARLGYKIKFYFDRNPYFQNKVLIKEYGCGPSGQVVSRSTPIQWLPGHDLQSLSQGNPENNRSFFGWFSNHSSIESDKIVEIINEELWPNPLQFYLLSEGARVEKGKEKEGRQGPGKQPMETTQPGVSQSN
Protein: Zinc import ATP-binding protein ZnuC (EC 7.2.2.20) (Q9HT73)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01725}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01725}.
Interaction partners:
- High-affinity zinc uptake system membrane protein ZnuB
- Transcriptional regulator np20
- High-affinity zinc uptake system protein ZnuA
- Probable permease of ABC transporter
- High-affinity zinc uptake system protein ZnuA
- Lipoprotein
- DUF2796 domain-containing protein
- Probable ATP-binding component of ABC transporter
- DNA gyrase inhibitor YacG
Sequence:
MDNALVRLTQVGVSFNGQAVLSDVDLAIEPGQIVTLIGPNGAGKTTLVRSVLGLLKPHVGEVWRRPRLTIGYMPQKLHVDATLPLSVLRFLRLVPGVKREQALAALREVGAAHVLERPLQSISGGELQRVLLARALLRKPELLVLDEPVQGVDVAGQAELYRLIGKLRDRYGCGVLMVSHDLHLVMSATDQVVCLNRHVCCSGHPEQVSGDPAFVELFGQDARSLAIYHHHHDHAHDLHGEVVKAGPGALPPGTRFTPVHKHGPDCNHG
Protein: Cyclin Y (Cyclin-Y isoform X4) (A0A286Y7Z8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGNSTSCCVSSSPKLRRNAHSRLEPYRPEPELSREDTGCNLQHISDRENIDELNMEYNPSDHPRASTIFLSKSQTDVREKRKSLYVNHQHPSGPMRRKYSSCSTIFLDDSTVSQPNLKYTIKCVALAIYYHIKNRNVDGRMLLDIFDEKLHPLSKSEVPSDYDKHDPEQKQIYRFVRTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPANWKRIVLGAILLASKVWDDQAVWNVDYCQILKDITVEDMNELERQFLELLQFNINVPSSVYAKYYFDLRSLSEANNLSFPLEPLSRDKAQKLEAISRLCDDKYKDLRKAAKKRSVSADNLSVVRWSPAIIS