wanglab/gogpt-training-data huggingface dataset:
Protein: Signal transducing adaptor molecule (B5DF55)
Organism: Rattus norvegicus (Rat)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004469}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004469}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004469}.
Interaction partners:
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- STAM-binding protein
- Signal transducing adapter molecule 2
- Tumor susceptibility gene 101 protein
- Tyrosine-protein kinase JAK3
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- Polyubiquitin-C
- Vacuolar protein sorting-associated protein 28 homolog
Sequence:
MPLFATNPFDQDVEKATSELNTAEDWGLILDICDKVGQSRTGPKDCLRSIMRRVNHKDPHVAMQALTLLGACVSNCGKIFHLEVCSRDFASEVSNVLNKGHPKVCEKLKALMVEWTDEFKNDPQLSLISAMIKNLKEQGVTFPAIGSQAAEQAKASPALVAKDPGTVATKKEEEDLAKAIELSLKEQRQQAAPLSTLYPSTSSLLTNHQHEGRKVRAVYDFEAAEDNELTFKAGEVITVLDDSDPNWWKGETHQGMGLFPSNFVTADLTAEPEMIKTEKKTVQFSDDVQIETIEPEPEPEPAFIDEDKMDQLLQMLQSTDPSDNQPDLPELLHLEAMCHQMGPLIDEKLEDIDRKHSELSELNVKVMEALSLYTKLMNEDPVYSVYAKSQSQQYYVQASGVSAPQVYPGPAQSGAYLVAGNAQMTHLQSYSLPPEQLASISQGAVPPSATPALPNQQAQASYPNAMVSSVQGNSYPSQASIYSPAAAAAAVAVTAVPVPADVTIYQNPGPNMSQVPNYTLTSSTLPHTGGSQQPPQPQQAYSQKALL
Protein: Vitamin B6 transporter TPN1 (Transport of pyridoxine protein 1) (P53099)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine.
Subcellular location: Membrane {ECO:0000269|PubMed:12649274}; Multi-pass membrane protein {ECO:0000269|PubMed:12649274}.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit SNZ1
- Thiamine-repressible mitochondrial transport protein THI74
Sequence:
MNRDNMDTTKRKEDHTKHTTDVIEFYEEGTAASSLNIATEKANSSPSILRRIINRAAWLSKKVDAMGVESTGIQRISPYERGTSKKQFLHVAGLWLSATGGLSSMSSFLLGPLLFGLSFRESVASSLISVTIGCLIAAYCSIMGPQSGCRQMVTARYLFGWWFVKLVALASIIGVMGWSVVNSVVGGEMLAAISNDKVPLWVGIVIVTVCSFLVAIFGIKQVIKVETYLSVPVLTAFLLLYISSSDKYSFVNAYVSKGNLDSSTRKGNWMSFFSLCYSITATWGSITADYYILFPEDTPYIQIFCLTFFGTFLPTCFVGILGLLLASVAMSYKPWSVEYDSHGMGGLLWAGFQRWNGFGKFCVVVLVFSLVSNNIINTYSAAFSIQLSSVFCAKIPRWFWSIVCTIICLVCALIGRNHFSTILGNFLPMIGYWISMYFILLFEENLVFRRFFLHLYTKEFPTVTGEINGPELVGSSKEVEKDAVTNIHLLKRKHKVTKHRYNWDKWEDYEVLTHGYAATFAFIVGVAGVVVGMAQAYWIGPIAAKFGEYGGDVAMWLSMAFSGVVYPPCRYLELRKFGR
Protein: RING-box protein HRT1 (RING-box protein 1) (E3 ubiquitin-protein ligase complex SCF subunit HRT1) (High level expression reduces Ty3 transposition protein 1) (Regulator of cullins protein 1) (Q08273)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. Recruits the E2 ubiquitin-conjugating enzyme CDC34/UBC3 to the complex and brings it into close proximity to the substrate. Also stimulates CDC34/UBC3 autoubiquitination and promotes the neddylation of CDC53 and RTT101. Component of the SCF(CDC4) ubiquitin ligase required for ubiquitination of the cyclin-dependent kinase inhibitor SIC1 and for the G1-to-S phase transition. Component of the RTT101(MMS1-MMS22) ubiquitin ligase that promotes fork progression through damaged DNA or natural pause sites. Component of the CRL3(ELA1) ubiquitin ligase required for ubiquitination of RPB1, the largest subunit of RNA polymerase II (Pol II), which targets Pol II for proteasomal degradation in DNA-damaged cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10880467}. Nucleus {ECO:0000269|PubMed:10880467}.
Interaction partners:
- Suppressor of kinetochore protein 1
- Cell division control protein 4
- Ubiquitin-conjugating enzyme E2-34 kDa
- Cullin-8
- Cullin-3
- Cell division control protein 53
- Elongin-C
- NEDD8-conjugating enzyme UBC12
- Defective in cullin neddylation protein 1
- F-box protein MET30 subunit MET30)
Sequence:
MSNEVDRMDVDEDESQNIAQSSNQSAPVETKKKRFEIKKWTAVAFWSWDIAVDNCAICRNHIMEPCIECQPKAMTDTDNECVAAWGVCNHAFHLHCINKWIKTRDACPLDNQPWQLARCGR
Protein: Neuroendocrine secretory protein 55 (NESP55) [Cleaved into: LHAL tetrapeptide; GPIPIRRH peptide] (O95467)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine secretory granules. {ECO:0000250}.
Interaction partners:
Sequence:
MDRRSRAQQWRRARHNYNDLCPPIGRRAATALLWLSCSIALLRALATSNARAQQRAAAQQRRSFLNAHHRSGAQVFPESPESESDHEHEEADLELSLPECLEYEEEFDYETESETESEIESETDFETEPETAPTTEPETEPEDDRGPVVPKHSTFGQSLTQRLHALKLRSPDASPSRAPPSTQEPQSPREGEELKPEDKDPRDPEESKEPKEEKQRRRCKPKKPTRRDASPESPSKKGPIPIRRH
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP1 (EC 2.7.4.24) (Probable protein QUANTITATIVE VITAMIN E-7) (Protein VIP HOMOLOG 2) (VIP1 homolog protein 1) (Arabidopsis homolog protein of yeast VIP1 1) (AtVIP1) (F4J8C6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Probably involved in vitamin E homeostasis via the regulation of gamma-tocopherol biosynthesis. Catalyzes the conversion of InsP7 to InsP8. Regulates jasmonic acid (JA) perception and plant defenses against herbivorous insects (e.g. P.rapae) and necrotrophic fungi (e.g. M.brassicae, B.cinerea and A.brassicicola) by triggering the production of jasmonate-induced pools of InsP8 and subsequent activation of SCF(COI1) E3 ubiquitin ligase complexes with JAZ proteins (e.g. TIFY10A/JAZ1).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O43314}.
Interaction partners:
- Inositol-pentakisphosphate 2-kinase
- Inositol-pentakisphosphate 2-kinase
- Inositol-pentakisphosphate 2-kinase
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase VIP2
- Inositol-tetrakisphosphate 1-kinase 1
- Inositol-tetrakisphosphate 1-kinase 2
- Inositol polyphosphate multikinase alpha
- Inositol polyphosphate multikinase beta
- SPX domain-containing protein 1
- Protein PHR1-LIKE 1
Sequence:
MEMEEGASGVGEKIKIGVCVMEKKVFSAPMGEILDRLQSFGEFEILHFGDKVILEDPIESWPICDCLIAFHSSGYPLEKAQAYAALRKPFLVNELDPQYLLHDRRKVYEHLEMYGIPVPRYACVNRKVPNQDLHYFVEEEDFVEVHGERFWKPFVEKPVNGDDHSIMIYYPSSAGGGMKELFRKIGNRSSEFHPDVRRVRREGSYIYEEFMATGGTDVKVYTVGPEYAHAEARKSPVVDGVVMRNTDGKEVRYPVLLTPAEKQMAREVCIAFRQAVCGFDLLRSEGCSYVCDVNGWSFVKNSYKYYDDAACVLRKMCLDAKAPHLSSTLPPTLPWKVNEPVQSNEGLTRQGSGIIGTFGQSEELRCVIAVVRHGDRTPKQKVKLKVTEEKLLNLMLKYNGGKPRAETKLKSAVQLQDLLDATRMLVPRTRPGRESDSDAEDLEHAEKLRQVKAVLEEGGHFSGIYRKVQLKPLKWVKIPKSDGDGEEERPVEALMVLKYGGVLTHAGRKQAEELGRYFRNNMYPGEGTGLLRLHSTYRHDLKIYSSDEGRVQMSAAAFAKGLLDLEGQLTPILVSLVSKDSSMLDGLDNASIEMEAAKARLNEIVTSGTKMIDDDQVSSEDFPWMTDGAGLPPNAHELLRELVKLTKNVTEQVRLLAMDEDENLTEPYDIIPPYDQAKALGKTNIDSDRIASGLPCGSEGFLLMFARWIKLARDLYNERKDRFDITQIPDVYDSCKYDLLHNSHLDLKGLDELFKVAQLLADGVIPNEYGINPQQKLKIGSKIARRLMGKILIDLRNTREEALSVAELKESQEQVLSLSASQREDRNSQPKLFINSDELRRPGTGDKDEDDDKETKYRLDPKYANVKTPERHVRTRLYFTSESHIHSLMNVLRYCNLDESLLGEESLICQNALERLCKTKELDYMSYIVLRLFENTEVSLEDPKRFRIELTFSRGADLSPLRNNDDEAETLLREHTLPIMGPERLQEVGSCLSLETMEKMVRPFAMPAEDFPPASTPVGFSGYFSKSAAVLERLVNLFHNYKNSSSNGRS
Protein: ATP synthase subunit b-delta [Includes: ATP synthase subunit b (ATP synthase F(0) sector subunit b 2) (ATPase subunit I 2) (F-type ATPase subunit b 2) (F-ATPase subunit b 2); ATP synthase subunit delta (ATP synthase F(1) sector subunit delta) (F-type ATPase subunit delta) (F-ATPase subunit delta)] (P9WPV3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- ATP synthase subunit b
- ATP synthase gamma chain
- ATP synthase subunit alpha
- ATP synthase subunit beta
- ATP synthase epsilon chain
- ATP synthase subunit c
- ATP synthase subunit a
- Uncharacterized protein Rv1507c
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL4
Sequence:
MSTFIGQLFGFAVIVYLVWRFIVPLVGRLMSARQDTVRQQLADAAAAADRLAEASQAHTKALEDAKSEAHRVVEEARTDAERIAEQLEAQADVEAERIKMQGARQVDLIRAQLTRQLRLELGHESVRQARELVRNHVADQAQQSATVDRFLDQLDAMAPATADVDYPLLAKMRSASRRALTSLVDWFGTMAQDLDHQGLTTLAGELVSVARLLDREAVVTRYLTVPAEDATPRIRLIERLVSGKVGAPTLEVLRTAVSKRWSANSDLIDAIEHVSRQALLELAERAGQVDEVEDQLFRFSRILDVQPRLAILLGDCAVPAEGRVRLLRKVLERADSTVNPVVVALLSHTVELLRGQAVEEAVLFLAEVAVARRGEIVAQVGAAAELSDAQRTRLTEVLSRIYGHPVTVQLHIDAALLGGLSIAVGDEVIDGTLSSRLAAAEARLPD
Protein: Hexose transporter HXT17 (P53631)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable glucose transporter.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
Sequence:
MQSSTESDRDIQDGPDADIHVAPPVEKEWSDGFDDNEVINGDNVEPPKRGLIGYLVIYLLCYPISFGGFLPGWDSGITAGFINMDNFKMNFGSYKHSTGEYYLSNVRMGLLVAMFSIGCAIGGLIFARLADTLGRRLAIVIVVLVYMVGAIIQISSNHKWYQYFVGKIIYGLGAGGCSVLCPMLLSEIAPTDLRGGLVSLYQLNMTFGIFLGYCSVYGTRKYDNTAQWRVPLGLCFLWTLIIIIGMLLVPESPRYLIECERHEEARASIAKINKVSPEDPWVLKQADEINAGVLAQRELGEASWKELFSVKTKVLQRLITGILVQTFLQLTGENYFFFYGTTIFKSVGLTDGFETSIVLGTVNFFSTIIAVMVVDKIGRRKCLLFGAAGMMACMVIFASIGVKCLYPHGQDGPSSKGAGNAMIVFTCFYIFCFATTWAPVAYIVVAESFPSKVKSRAMSISTACNWLWQFLIGFFTPFITGSIHFYYGYVFVGCLVAMFLYVFFFLPETIGLSLEEIQLLYEEGIKPWKSASWVPPSRRGIPSEESKTEKKDWKKFLKFSKGSD
Protein: Uncharacterized protein (Q38DP5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MASLEDKVARLQEQNAALQRKVRIQASIISRLSIRESQLKQVRRIPVLQHRLNAARGECEELLCELAERRDREARLSEELRVLRKFVALDAKTETAEVARLCARYEVMQEELKTLHERLKTTYDEREEYRKRTLMLCDEVEYYRQGWRSLLDETRKPEGCVTGEETKGNIVVEGCRFPVEDRTSEARAIGGGCSAETVRAARTLPQCVDDYEPPSSEATLSEASVEAVDVLREQPVESQVEPCHDQTVVASDIACGEPVASGGAKVPAVVKSLRRQLCLSEGMCSLLEDRWNALSEENKSLLRRLRDEEAAGASLRRQLRDVCRECEHLKQIFADLSRVRLSLS
Protein: Stretchin-Mlck, isoform N (EC 2.7.11.17, EC 2.7.11.18) (A0A0B4JCU1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRDVTASRSGEICLQVKHPQAEFRRIPTTRTYTSLLVLPAIRGNSSSSSLAARSCILTRPEDCTALIGGHVRLSVRYEPFPGTKVIWYKACHPIVESSNVTIRTTSQQSTLYITDISADDSGKYTVEVMNDYGVEAAAASVAVEGPPEPPSGQPSVSLGPDRVAVAWCGPPYDGGCMITGFIIEMQTIGDENCDEDSWQQVTRVVDSLAYTVKNLQPERQYRFRVRAENIHGRSAPGQASELVQITNTPQRSTSSDASDRFGQATVSVQSGGDFKSRFEIIEELGKGRFGIVYKVQERGQPEQLLAAKVIKCIKSQDRQKVLEEISIMRALQHPKLLQLAASFESPREIVMVMEYITGGELFERVVADDFTLTEMDCILFLRQVCDGVAYMHGQSVVHLDLKPENIMCHTRTSHQIKIIDFGLAQRLDTKAPVRVLFGTPEFIPPEIISYEPIGFQSDMWSVGVICYVLLSGLSPFMGDTDVETFSNITRADYDYDDEAFDCVSQEAKDFISQLLVHRKEDRLTAQQCLASKWLSQRPDDSLSNNKICTDKLKKFIIRRKWQQRSREGAVEAHPVYPAKASHPRCVPCPALRCLSDPLRRRG
Protein: Disease resistance protein RPS6 (EC 3.2.2.6) (Resistance to Pseudomonas syringae 6) (F4KHH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Disease resistance (R) protein that specifically recognizes the hopA1 type III effector avirulence protein from Pseudomonas syringae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth.
Interaction partners:
- Protein kinase superfamily protein
- Pentatricopeptide repeat-containing protein At5g46460
- Protein EDS1
- Transmembrane emp24 domain-containing protein p24delta4
- Suppressor of RPS4-RLD 1
Sequence:
MASSSSSSSRNWSYHVFPSFSGEDVRNTFLSHFLKELDRKLIISFKDNEIERSQSLDPELKHGIRNSRIAVVVFSKTYASSSWCLNELLEIVKCKKEFGQLVIPIFYNLDPSHVRKQTGDFGKIFEKTCRNKTVDEKIRWKEALTDVANILGYHIVTWDNEASMIEEIANDILGKMNISPSNDFEDLVGIEDHITKMSSLLHLESEEVRMVGIWGPSGIGKTTIARALFSRLSCQFQSSVFIDKVFISKSMEVYSGANLVDYNMKLHLQRAFLAEIFDKKDIKIHVGAMEKMVKHRKALIVIDDLDDQDVLDALADQTQWFGSGSRIIVVTENKHFLRANRIDHIYKVCLPSNALALEMFCRSAFKKNSPPDDFLELSSEVALRAGNLPLGLNVLGSNLRGINKGYWIDMLPRLQGLDGKIGKTLRVSYDGLNNRKDEAIFRHIACIFNGEKVSDIKLLLANSNLDVNIGLKNLVDRSLICERFNTLEMHSLLQELGKEIVRTQSNQPGEREFLVDLKDICDVLEHNTGTKKVLGITLDIDETDELHIHESSFKGMHNLLFLKIYTKKLDQKKKVRWHLPERFDYLPSRLRLLRFDRYPSKCLPSNFHPENLVKLQMQQSKLEKLWDGVHSLAGLRNMDLRGSRNLKEIPDLSMATNLETLKLSSCSSLVELPSSIQYLNKLNDLDMSYCDHLETIPSGVNLKSLDRLNLSGCSRLKSFLDIPTNISWLDIGQTADIPSNLRLQNLDELILCERVQLRTPLMTMLSPTLTRLTFSNNPSFVEVPSSIQNLYQLEHLEIMNCRNLVTLPTGINLDSLISLDLSHCSQLKTFPDISTNISDLNLSYTAIEEVPLSIEKLSLLCYLDMNGCSNLLCVSPNISKLKHLERADFSDCVELTEASWNGSSSEMVKLLPADNFSTVKLNFINCFKLDLTALIQNQTFFMQLILTGEEVPSYFTHRTSGDSISLPHISVCQSFFSFRGCTVIDVDSFSTISVSFDIEVCCRFIDRFGNHFDSTDFPGYFITTKLGGHLVVFDCYFPFNEEFTTFLDGQFNYDHVDIQFRLTNDNSQLKLKGCGILLSEDVPSLDNRPCSPNILPGVCEDSALERRSFRTKMRMMRMRLLKKLLNR
Protein: Rac GTPase activating protein 1 (F8VWY4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSDISFDKTDESLDWDSSLVKT
Protein: Dyslexia-associated protein KIAA0319 (Q5VV43)
Organism: Homo sapiens (Human)
Function: Involved in neuronal migration during development of the cerebral neocortex. May function in a cell autonomous and a non-cell autonomous manner and play a role in appropriate adhesion between migrating neurons and radial glial fibers. May also regulate growth and differentiation of dendrites.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18063668, ECO:0000269|PubMed:19419997}; Single-pass type I membrane protein {ECO:0000269|PubMed:18063668}. Early endosome membrane {ECO:0000269|PubMed:19419997}; Single-pass type I membrane protein {ECO:0000269|PubMed:18063668}. Note=Low-abundance isoforms lacking the transmembrane domain have been described; these are secreted. {ECO:0000269|PubMed:18063668}.
Interaction partners:
- Doublecortin domain-containing protein 2
- Dynein axonemal assembly factor 4
- Acyl-coenzyme A thioesterase 13
- Tyrosyl-DNA phosphodiesterase 2
- Intron Large complex component GCFC2
- AP-2 complex subunit mu
- Roundabout homolog 1
- Large ribosomal subunit protein bL19m
- Calcium-transporting ATPase type 2C member 2
Sequence:
MAPPTGVLSSLLLLVTIAGCARKQCSEGRTYSNAVISPNLETTRIMRVSHTFPVVDCTAACCDLSSCDLAWWFEGRCYLVSCPHKENCEPKKMGPIRSYLTFVLRPVQRPAQLLDYGDMMLNRGSPSGIWGDSPEDIRKDLTFLGKDWGLEEMSEYSDDYRELEKDLLQPSGKQEPRGSAEYTDWGLLPGSEGAFNSSVGDSPAVPAETQQDPELHYLNESASTPAPKLPERSVLLPLPTTPSSGEVLEKEKASQLQEQSSNSSGKEVLMPSHSLPPASLELSSVTVEKSPVLTVTPGSTEHSIPTPPTSAAPSESTPSELPISPTTAPRTVKELTVSAGDNLIITLPDNEVELKAFVAPAPPVETTYNYEWNLISHPTDYQGEIKQGHKQTLNLSQLSVGLYVFKVTVSSENAFGEGFVNVTVKPARRVNLPPVAVVSPQLQELTLPLTSALIDGSQSTDDTEIVSYHWEEINGPFIEEKTSVDSPVLRLSNLDPGNYSFRLTVTDSDGATNSTTAALIVNNAVDYPPVANAGPNHTITLPQNSITLNGNQSSDDHQIVLYEWSLGPGSEGKHVVMQGVQTPYLHLSAMQEGDYTFQLKVTDSSRQQSTAVVTVIVQPENNRPPVAVAGPDKELIFPVESATLDGSSSSDDHGIVFYHWEHVRGPSAVEMENIDKAIATVTGLQVGTYHFRLTVKDQQGLSSTSTLTVAVKKENNSPPRARAGGRHVLVLPNNSITLDGSRSTDDQRIVSYLWIRDGQSPAAGDVIDGSDHSVALQLTNLVEGVYTFHLRVTDSQGASDTDTATVEVQPDPRKSGLVELTLQVGVGQLTEQRKDTLVRQLAVLLNVLDSDIKVQKIRAHSDLSTVIVFYVQSRPPFKVLKAAEVARNLHMRLSKEKADFLLFKVLRVDTAGCLLKCSGHGHCDPLTKRCICSHLWMENLIQRYIWDGESNCEWSIFYVTVLAFTLIVLTGGFTWLCICCCKRQKRTKIRKKTKYTILDNMDEQERMELRPKYGIKHRSTEHNSSLMVSESEFDSDQDTIFSREKMERGNPKVSMNGSIRNGASFSYCSKDR
Protein: pyridoxal 5'-phosphate synthase (EC 1.4.3.5) (Q7KSW3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSQGASEVPLSALRLKYCERKDAFLEDNIKVKNPFCVFRDWLELALKTPEILEPNAAALATVSAEGRPSNRYVLVKEATAEGFTFFTNYGSRKAEDIKSNPYVAISFYWLPLRRSVRIEGVAEKISVEDSLKYFHQRPRASQIGAAASPQSQRIPSRSYLDDVEAAIKLELGPDGEVPLPNWGGYLVRPDLIEFWQGQTDRLHDRIRFRRGGGVESEVDSKLVHKGEDGWVYERLAP
Protein: Ribonuclease G (RNase G) (EC 3.1.26.-) (Cytoplasmic axial filament protein) (CafA protein) (P0A9J0)
Organism: Escherichia coli (strain K12)
Function: An endonuclease that acts in the processing of the 5'-end of precursors of 16S rRNA, generates a precursor with 3 extra nucleotides at its 5'-end (which is matured by Rnm). It prefers 5'-monophosphorylated over 5'-OH or 5'-triphosphorylated substrates and cleaves single-stranded sites rich in A and U residues; contributes to RNA turnover. 5'-monophosphate-assisted cleavage requires at least 2 and preferably 3 or more unpaired 5'-terminal nucleotides for cleavage. The optimal spacing between the 5' end and the scissile phosphate appears to be 6 nucleotides. Any sequence of unpaired nucleotides at the 5'-end is tolerated. Processes the 5'-end precursors of 23S rRNA. Participates in processing of tRNA(Pro) (proK and proM). Also involved in metabolism of some mRNAs. Cells overproducing this protein form chains of cell with cytoplasmic axial filaments. Could be involved in chromosome segregation and cell division. It may be one of the components of the cytoplasmic axial filaments bundles, or merely regulate the formation of this structure (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22509045, ECO:0000305|PubMed:14622423}. Cell inner membrane {ECO:0000269|PubMed:22509045}; Peripheral membrane protein {ECO:0000305|PubMed:22509045}. Cytoplasm, cytoskeleton {ECO:0000303|PubMed:8300545}. Note=Possible cytoskeletal location is upon overproduction. {ECO:0000303|PubMed:8300545}.
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- dTTP/UTP pyrophosphatase
- Ribonuclease 3
- Ribonuclease R
- Exoribonuclease 2
- Endoribonuclease YbeY
- Ribonuclease BN
- RNA pyrophosphohydrolase
- Cell shape-determining protein MreC
- ATP-dependent RNA helicase RhlB
Sequence:
MTAELLVNVTPSETRVAYIDGGILQEIHIEREARRGIVGNIYKGRVSRVLPGMQAAFVDIGLDKAAFLHASDIMPHTECVAGEEQKQFTVRDISELVRQGQDLMVQVVKDPLGTKGARLTTDITLPSRYLVFMPGASHVGVSQRIESESERERLKKVVAEYCDEQGGFIIRTAAEGVGEAELASDAAYLKRVWTKVMERKKRPQTRYQLYGELALAQRVLRDFADAELDRIRVDSRLTYEALLEFTSEYIPEMTSKLEHYTGRQPIFDLFDVENEIQRALERKVELKSGGYLIIDQTEAMTTVDINTGAFVGHRNLDDTIFNTNIEATQAIARQLRLRNLGGIIIIDFIDMNNEDHRRRVLHSLEQALSKDRVKTSVNGFSALGLVEMTRKRTRESIEHVLCNECPTCHGRGTVKTVETVCYEIMREIVRVHHAYDSDRFLVYASPAVAEALKGEESHSLAEVEIFVGKQVKVQIEPLYNQEQFDVVMM
Protein: GDP-polyphosphate phosphotransferase (EC 2.7.4.-) (Polyphosphate kinase PPK2) (O05877)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP. In addition, modulates nucleotide triphosphate synthesis catalyzed by the nucleoside diphosphate kinase (Ndk) in favor of GTP production over CTP or UTP. Plays an important role in survival of M.tuberculosis in macrophages.
Interaction partners:
- Polyphosphate kinase
- Conserved protein
- Inorganic pyrophosphatase
- Exopolyphosphatase 1
- Exopolyphosphatase 2
- Probable diacyglycerol O-acyltransferase tgs3
- Possible triacylglycerol synthase
- Probable transcriptional regulatory protein Rv2603c
- NADPH oxidoreductase
- NAD kinase
Sequence:
MDIPSVDVSTATNDGASSRAKGHRSAAPGRRKISDAVYQAELFRLQTEFVKLQEWARHSGARLVVIFEGRDGAGKGGAIKRITEYLNPRVARIAALPAPTDRERGQWYYQRYIAHLPAKGEIVLFDRSWYNRAGVEKVMGFCTPQEYVLFLRQTPIFEQMLIDDGILLRKYWFSVSDAEQLRRFKARRNDPVRQWKLSPMDLESVYRWEDYSRAKDEMMVHTDTPVSPWYVVESDIKKHARLNMMAHLLSTIDYADVEKPKVKLPPRPLVSGNYRRPPRELSTYVDDYVATLIAR
Protein: Phytochrome-associated serine/threonine-protein phosphatase 3 (AtFyPP3) (EC 3.1.3.16) (Protein EMBRYO DEFECTIVE 2736) (Q9LHE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of protein phosphatase 6 (PP6) (Probable). Dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms. Plays a major role in the photoperiodic control of flowering time in long days by modulating phytochrome signals in flowering time control. Involved in the regulation of polar auxin transport in roots. Dephosphorylates directly the auxin efflux carriers PIN1 and PIN2, thus promoting their proper polar localization in root cell plasma membrane. Acts antagonistically with the protein kinase PID to regulate the reversible phosphorylation of PIN and polar targeting, subsequently impacting polar auxin transport and plant development. Involved in the regulation of abscisic acid (ABA) signaling during seed germination and postgermination seedling growth. Functions as negative regulator of ABA signaling through direct dephosphorylation and destabilization of ABI5 protein. Acts antagonistically with the protein kinase SRK2E/SNRK2.6 to regulate ABI5 phosphorylation and ABA responses. Involved in the regulation of phosphorylation status in hypocotyl phototropism. Involved in the negative regulation of photomorphogenesis by controlling the stability and transcriptional activity of PIF3 and PIF4 proteins in the dark, via the regulation of their phosphorylation status.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12468726}.
Interaction partners:
- PP2A regulatory subunit TAP46
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine-protein phosphatase PP2A-4 catalytic subunit
- SIT4 phosphatase-associated family protein
- At1g07990/T6D22_5
- SIT4 phosphatase-associated family protein
- SIT4 phosphatase-associated family protein
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 4 regulatory subunit-like protein
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MDLDQWISKVKDGQHLSEDELQLLCEYVKEILIEESNVQPVNSPVTVCGDIHGQFHDLMKLFQTGGHVPDTNYIFMGDFVDRGYNSLEVFTILLLLKARYPANITLLRGNHESRQLTQVYGFYDECQRKYGNANAWRYCTDVFDYLTLSAIIDGTVLCVHGGLSPDVRTIDQIRLIERNCEIPHEGPFCDLMWSDPEDIETWAVSPRGAGWLFGSRVTTEFNHINKLDLVCRAHQLVQEGLKYMFQDKGLVTVWSAPNYCYRCGNVASILSFNDNMEREVKFFTETEENNQMRGPRTGVPYFL
Protein: Deoxycytidine kinase 2 (GgdCK2) (EC 2.7.1.74) (Deoxyadenosine kinase 2) (EC 2.7.1.76) (Deoxyguanosine kinase 2) (EC 2.7.1.113) (Q5ZJM7)
Organism: Gallus gallus (Chicken)
Function: Phosphorylates the deoxyribonucleosides deoxyadenosine, deoxycytidine and deoxyguanosine. Shows highest activity against deoxyguanosine followed by deoxycytidine and then deoxyadenosine. Shows only very minor activity against deoxyuridine and deoxythymidine.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27707}.
Interaction partners:
- Cytidine deaminase
- Deoxycytidylate deaminase
- UMP-CMP kinase 2, mitochondrial
- Uncharacterized protein.
- Adenylosuccinate lyase
- UMP-CMP kinase
- Pribosyltran domain-containing protein.
- Adenylate kinase 5
- Adenylate kinase isoenzyme 1
- AMP deaminase
Sequence:
MSAPAKRRCRGPAADLDSSFQKRLRKISIEGNIAAGKSTLVRLLEKHSDEWEVIPEPIAKWCNIQTSEDECKELSTSQKSGGNLLQMLYDKPTRWAYTFQTYACLSRVRAQLKPISAKLHEAEHPVQFFERSVYSDRYVFASNLFESGNINETEWAIYQDWHSWLLNQFQSEIELDGIIYLRTTPQKCMERLQKRGRKEEEGIDLEYLENLHYKHETWLYEKTMRVDFENLKEIPILVLDVNEDFKNDKIKQEYLIDEIKSFLTS
Protein: Tyrosine-protein kinase Src64B (Dsrc64) (EC 2.7.10.2) (P00528)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in the development of neural tissue and smooth muscle.
Interaction partners:
- Tyrosine-protein kinase
- Downstream of kinase
- Raf homolog serine/threonine-protein kinase Raf
- Ras-like protein 1
- RE45833p
- Segmentation protein Runt
- Uncharacterized protein, isoform B
- Mitogen-activated protein kinase p38b
- Epidermal growth factor receptor
- Tyrosine-protein kinase hopscotch
Sequence:
MGNKCCSKRQDQELALAYPTGGYKKSDYTFGQTHINSSGGGNMGGVLGQKHNNGGSLDSRYTPDPNHRGPLKIGGKGGVDIIRPRTTPTGVPGVVLKRVVVALYDYKSRDESDLSFMKGDRMEVIDDTESDWWRVVNLTTRQEGLIPLNFVAEERSVNSEDWFFENVLRKEADKLLLAEENPRGTFLVRPSEHNPNGYSLSVKDWEDGRGYHVKHYRIKPLDNGGYYIATNQTFPSLQALVMAYSKNALGLCHILSRPCPKPQPQMWDLGPELRDKYEIPRSEIQLLRKLGRGNFGEVFYGKWRNSIDVAVKTLREGTMSTAAFLQEAAIMKKFRHNRLVALYAVCSQEEPIYIVQEYMSKGSLLDFLREGDGRYLHFEDLIYIATQVASGMEYLESKQLIHRDLAARNVLIGENNVAKICDFGLARVIADDEYCPKQGSRFPVKWTAPEAIIYGKFSIKSDVWSYGILLMELFTYGQVPYPGMHSREVIENIERGFRMPKPTNHYFPDNIYQLLLQCWDAVPEKRPTFEFLNHYFESFSVTSEVPYREVQD