wanglab/gogpt-training-data huggingface dataset:
Protein: Pre-mRNA cleavage complex II Clp1-like, conserved (Q585W7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Suppressor of forked domain-containing protein
- Cleavage and polyadenylation specificity factor subunit, putative
- C3H1-type domain-containing protein
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor-like protein, putative
Sequence:
MSSNCRTEEFNLERKELKIRFRSSGYVVLTDGAATIFGAPLKKNTRYDFSMCSIPVVSPVACRLHVGGDFTSVVTYIRTDVYDIHAVLDFARHEASKRGVPSLNDTNPGGTSSNSLKEGPWGPRVLVVGDVNTGKSSLCRSLANMAVASQVHGVALVDVDVGQQGITCPGSVATAFVDNYLPIDEGFNTVMPLTAFFGDKTVNASTRGRYLDLCASLARGIISFSLATPKFAAGGVIVNTMGWVTDMGLDLLFQLLSVFSITHVVVCGSGNKLTETLRNAVIDEKIIFLKYPKQTGVFKRKGNVRDSWRAEQIVSYFQGTKRTPLLSYRAVCYVKDVHFIHALKLEPLSWKDVEPLSLAAVSWTDSLEAVNDINVAGFIVLLEVGETFFSFLSPVAGTLPKPFILVSPTIRLPRDKVPPLQAP
Protein: DNA primase (EC 2.7.7.101) (P9WNW0)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Interaction partners:
Sequence:
MSGRISDRDIAAIREGARIEDVVGDYVQLRRAGADSLKGLCPFHNEKSPSFHVRPNHGHFHCFGCGEGGDVYAFIQKIEHVSFVEAVELLADRIGHTISYTGAATSVQRDRGSRSRLLAANAAAAAFYAQALQSDEAAPARQYLTERSFDAAAARKFGCGFAPSGWDSLTKHLQRKGFEFEELEAAGLSRQGRHGPMDRFHRRLLWPIRTSAGEVVGFGARRLFDDDAMEAKYVNTPETLLYKKSSVMFGIDLAKRDIAKGHQAVVVEGYTDVMAMHLAGVTTAVASCGTAFGGEHLAMLRRLMMDDSFFRGELIYVFDGDEAGRAAALKAFDGEQKLAGQSFVAVAPDGMDPCDLRLKCGDAALRDLVARRTPLFEFAIRAAIAEMDLDSAEGRVAALRRCVPMVGQIKDPTLRDEYARQLAGWVGWADVAQVIGRVRGEAKRTKHPRLGRLGSTTIARAAQRPTAGPPTELAVRPDPRDPTLWPQREALKSALQYPALAGPVFDALTVEGFTHPEYAAVRAAIDTAGGTSAGLSGAQWLDMVRQQTTSTVTSALISELGVEAIQVDDDKLPRYIAGVLARLQEVWLGRQIAEVKSKLQRMSPIEQGDEYHALFGDLVAMEAYRRSLLEQASGDDLTA
Protein: Protein lin-36 (Abnormal cell lineage protein 36) (P34427)
Organism: Caenorhabditis elegans
Function: Required to negatively regulate vulval development. Antagonizes Ras-mediated vulval induction. Acts cell autonomously.
Subcellular location: Nucleus {ECO:0000269|PubMed:10393123}.
Interaction partners:
- Protein lin-15A
- Protein lin-15B
- Retinoblastoma-like protein homolog lin-35
- Protein lin-9
- Transcription factor dpl-1
- Uncharacterized protein
- RING-type domain-containing protein
Sequence:
MSEELLSTRPSKRDYNDIEEPEDSHVTVHSVEQDSQHSGEESSTVDALQETEGDVDVIGEDEDEHDIPVMPTVTSSGEVLDESQVTPTKQASSSQPREEIIHGKGESVYSSFPCQVIPETLSRMTRTPPDGEHLEVYRMSNGRLRIYVVDHFKKFSPYSNLTHKPCTVCNRVMKSGEMHLNFPADLDRRRIWANLLGFKYKDILRSKMGPVSFSIAAGPICTEHFAEECFRNHNFNKSAIEAFGVPVAISPDVKTTPSKKSSRVPWVCTVCEFHSCSVVELQTHLLNHTEEMLKKKDNVLDVPEAGFMCPFCRKCTYGYKTISGYRRHLNAGPIHHCHLRRIYEFAKMNCRATELDPAESWDNWTRRNVYVAYHGCEPPANEIVLTPSPTKKAYVQNPEERTKMVHDEEKRKKAVRTLSFVGKEGGTSVNDLNVMQRQVFLQLRREAEINTKAEESAQGTKEQESSQKKHAEEESDDVSELTSHQSPQAPMGSGERRKATRLATSATNSPIKKVAKHEVPATAPSTPAKKRKISHEEEHDPTPESVEREPTVSPNDPRERLRLKERDEQFAKMVQKRSQQVKRLINAKQFKKQEAATKKPRKALAYNLAKGIAATSSTEPEDKVTSSEQTPEPTTSQKFIARNTRSKTKESAVQKVEKPATPVAKPAPVEKEPEERPLKSMLARSFVAGVRPSMAKYQIPLESFTATASLGGGRSLSSGVISRPPTSSSPGGIFSQRVMGAVAQEKGPAKRPSVLSRRPLILSPRKKTSTPRPTLSHHESSPNFSASSPVVVSDEYLIPATDMEVEMVEEVIDSMGNSSSEDVATSSTSSERQPMLTLAEALEMDGSSGTVKDQDMEEISKEMMKDAHYYRAMEDAIKCRTVTKMRADMRLSRHCIRQIEAARARARLFGERTEDYQIFYSNDGAQVLTKKDPKWRELQQQQQQQQQQQEQFPGQGSSDSQQ
Protein: Spermatid perinuclear RNA-binding protein (Q91WM1)
Organism: Mus musculus (Mouse)
Function: Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth (By similarity). Binds to double-stranded DNA and RNA (By similarity). Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA (By similarity). Binds also to single-stranded poly(G) RNA (By similarity). Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA.
Subcellular location: [Isoform 2]: Cytoplasm, cytoskeleton. Note=Microtubule-associated that localizes to the manchette in developing spermatids.
Interaction partners:
Sequence:
MRSIRSFANDDRHVMVKHSTIYPSPEELEAVQNMVSTVECALKHVSDWLDETNKGTKPEGETEVKKDEAVENYSKDQGGRTLCGVMRIGLVAKGLLIKDDMDLELVLMCKDKPTETLLNTVKDNLPIQIQKLTEEKYQVEQCINEASIIIRNTKEPTLTLKVILTSPLIRDELEKKDGENVMMKDPPDLLDRQKCLNALASLRHAKWFQARANGLKSCVIVLRILRDLCNRVPTWAPLKGWPLELICEKSIGTCNRPLGAGEALRRVMECLASGILLPGGPGLHDPCERDPTDALSYMTTQQKEDITHSAQHALRLSAFGQIYKVLEMDPLPSSKPFQKYSWSVTDKEGAGSSALKRPFEDGLGDDKDPNKKMKRNLRKILDSKAIDLMNALMRLNQIRPGLQYKLLSQSGPVHAPVFTMSVDVDGTTYEASGPSKKTAKLHVAVKVLQAMGYPTGFDADIECISSDEKSDNESKNDTVSSNSSNNTGNSTTETSSTLEVRTQGPILTASGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFRGAGPNKKVAKASAALAALEKLFSGPNAANNKKKKIIPQAKGVVNTAVSAAVQAVRGRGRGTLTRGAFVGATAAPGYIAPGYGTPYGYSTAAPAYGLPKRMVLLPVMKFPTYPVPHYSFF
Protein: Sodium-dependent glucose transporter SGLT-I (Q95JG8)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
LTGFAFHEVGGYGAFVTKYINAIPTVTSYGNTTIKAECYTPRADSFHIFRDPLKGDLPWPGLIFGLTIISLWYWCTDQVIVQRCLSAKNMSHVKAGCIMCGYLKLLPMFLMVMPGMISRILFTEKVACTVPSECENYCGTKVGCTNIAYPTLVVELMPNGLRGLMLSVMLASLMSSLTSIFNSA
Protein: NADH:ubiquinone oxidoreductase core subunit V1 (cDNA FLJ57949, highly similar to NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial) (cDNA, FLJ79021, highly similar to NADH-ubiquinone oxidoreductase 51 kDa subunit, mitochondrial) (B4DE93)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNKPSDGRPKYLVVNADEGEPGTCKDREILRHDPHKLLEGCLVGGRAMGARAAYIYIRGEFYNEASNLQVAIREAYEAGLIGKNACGSGYDFDVFVVRGAGAYICGEETALIESIEGKQGKPRLKPPFPADVGVFGCPTTVANVETVAVSPTICRRGGTWFAGFGRERNSGTKLFNISGHVNHPCTVEEEMSVPLKELIEKHAGGVTGGWDNLLAVIPGGSSTPLIPKSVCETVLMDFDALVQAQTGLGTAAVIVMDRSTDIVKAIARLIEFYKHESCGQCTPCREGVDWMNKVMARFVRGDARPAEIDSLWEISKQIEGHTICALGDGAAWPVQGLIRHFRPELEERMQRFAQQHQARQAAS
Protein: Periplasmic protein (Q8ZPI6)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Interaction partners:
- Potassium binding protein Kbp
- Outer membrane porin protein OmpD
- Cytoplasmic protein
Sequence:
MKLQVAAFLSFLIMPYALADDQGGLKKDVAPPPPHAIEDGYRGTDDAEKMTIEQAKTLHDGATVSLRGNLIDHKGDDRYVFRDKSGEINVIIPSAVFDGREVQPDQMININGSLDKKAKEPLVRVNRLQK
Protein: LysM-domain receptor-like kinase (G7KAT5)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Interaction partners:
Sequence:
MHLFPFIPFFIFNLFFFFFVSNISIILGQQPYIGLATNACPRKGDSKSIRGYTCNGKTQTCQAYLTFRTQPIYSSVSTISSLLGSNPSQLAEINSVSLNETFETNKMVIVPVNCSCSGNYYQANTSYVFQNTDTYFIVANNTFEGLSTCQALMHENHNPGDVYPGRKLLVPLRCACPTKNQTQKNIKYLLSYLVDWGDSVSFISDKFGVNFRTTLEANTLSLTQSTIYPFTTLLVPLFDKPSSSQIQTHHSPSSSPPLSSSSSTDKKSKKTWVYVVVGVLGGVVIVALILFLYAFISFKKGKKKNDFLVSVSESTIFEEKEKPMKKEDEKLSEIICGIAQSFKVYDFEEIKVATDNFSPSCRVKGTVYRGLIKGDLAAIKKTEGDVSKEIQILNKVNHSNVIRLSGVSFNQGHWYLVYEYAANGALSDWLFSNKKMDDGNILSWIRRIKIALDVAIGVEYLHSFTSPPHIHKDLKCSNILLDSDFKAKVANLRHVRCVEEVENDEEFVATRHIVGTRGYMAPEYLENGLVSTKLDVYAFGILMLEIITGKEVGFMISKDNENLLDVLSGILGEKSGDEKLKEFMDPSLQGNYPFELAMFVIEIIQNCLNKDPGNRPAMDEIVPVLSRTLNSSLSWEM
Protein: Large ribosomal subunit protein uL10 (50S ribosomal protein L10) (P56036)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
Interaction partners:
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL22
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL16
Sequence:
MQKQHQRQHKVELVANLKSQFADAKALLICDYKGLSVRKLEALRNKARNQGIKVQVIKNTLAHIAMKETGYSDLDLKETNVFLWGGDQIALSKLVFDFQKEHKDHFVLKAGLFDKESVSVAHVEAVSKLPSKEELMGMLLSVWTAPARYFVTGLDNLRKAKEEN
Protein: WD repeat-containing protein 89 (Q9D0R9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEKIEDQFASLHIVRRSSEPKEPTYLLGIDTSKTVQADKGGLVAVLCSNGSIRIYDKETLHLLREFGGSPGLLSGVSFANSCDSVYSASTDGTVKCWDARGASEKPVQLFKGYPSCSFISFDVNCKDHVICAGAEKVDEDALLVFWDARFTSQDLSTRDPLGAYSETHSDDITQVRFHPSNPNLVVSGSTDGLVNVFDLSADKEEDALVATCNSVSSVSCIGWCGKDYKQIYCMTHDEGFCWWDLNHLDTDEPITCLNIQDVREITDVKDGHLDYLIGGLYHEKMDRLFVIGGTNTGKIHLLSCTSAGLTHVTSLHGGHAATVRSFCWNVSEDSLLTGGEDAQLLLWKPGAMEKTFTKKDSLKIASSVQQRVRVHSSDSYKKRKQQ
Protein: Serotonin N-acetyltransferase 2, chloroplastic (OsSNAT2) (EC 2.3.1.87) (Q6Z1Y6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. Catalyzes in vitro the N-acetylation of tryptamine to produce N-acetyltryptamine, 5-methoxytryptamine to produce melatonin and tyramine to produce N-acetyltyramine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27121038}. Plastid, chloroplast {ECO:0000269|PubMed:27121038}.
Interaction partners:
- Tryptophan decarboxylase 2
- Serotonin N-acetyltransferase 1, chloroplastic
- Os10g0400500 protein
- Tryptophan decarboxylase 1
- Tyrosine decarboxylase
- Os10g0380800 protein
- Os05g0510600 protein
- Os08g0140500 protein
- Acetylserotonin O-methyltransferase 1
- GCN5-related N-acetyltransferase, putative, expressed
Sequence:
MQMQAARPRVGVRPRGGIRPFPLPTLSFNNNSNRSACACACAVSVSDSELAARGFAVRRSSTGLDVGALNEVFARVGFPRRQEERLRRALEHSEVVWLEDSASSSAGRPVAFARAAGDGVFNAVVWDVVVEPSCQGLGLGRAVMERLVADLRGKGVSNIALYAEPRVVGFYRLLGFAMDPDAIRGMAFYRSRQQIQNTSS
Protein: Golgi brefeldin A resistant guanine nucleotide exchange factor 1 (F1M8X9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
- ADP-ribosylation factor 1
- ADP-ribosylation factor 4
- ADP-ribosylation factor GTPase-activating protein 1
- Ras-related protein Rab-1B
- small monomeric GTPase
- Coatomer subunit gamma-1
- Coatomer subunit beta
- Coatomer subunit alpha
- ADP-ribosylation factor 3
- ADP-ribosylation factor 5
Sequence:
MVDKNIYIIQGEINIVVGAIKRNARWSTHIPLDEERDPLLHSFSHLKEVLNSGTELSEIEPNVFLRPFLEVIRSEDTTGPITGLALTSVNKFLSCALIDPTHEGTAEGMENMADAVTHARFVGTDPASDEVVLMKILQVLRTLLLTPVGTHLTNESVCEIMQSCFRICFEMRLSELLRKSAEHTLVDMVQLLFTRLPQFKEEPKSYVGTNLKKLKMRAGGMSDSSKWKKQKRSPRPPRHTTKVMPGSELPTPNGAALSSNLTGGMPFIEAPTSISSASSEAASTVVSPCTDSGLELSSQATSKEDLTDLEQAGSPREITTTEPGSTEIGVSDQLDPQQEGAHVEKAQSASVESIPEVLEECTSPTDHSDSASVHDMDYVNPRGVRFTQSSQKEGTALVPYGLPCIRELFRFLISLTNPHDRHNSEVMIHMGLHLLTVALESAPVAQCQTLLGLIKDEMCRHLFQLLSVERLNLYAASLRVCFLLFESMREHLKFQLEMYIKKLMEIITVENPKMPYEMKEMALEAIVQLWRIPSFVTELYINYDCDYYCSNLFEDLTKLLSKNAFPVSGQLYTTHLLSLDALLTVIDSTEAHCQAKVLNTLNQQEKKETARPGFEAVDGSPDTYKSERAASDGKATGVPSDAPGLHFSSGGWLSTEHGKPGCSDLEEAGDSGVDKKTTRKPPRFSCLLPDPRELIEIKNKKKLLITGTEQFNQKPKKGIQFLQEKGLLTIPMDNTEVAQWLRENPRLDKKMIGEFVSDRKNMDLLESFVSTFSFQGLRLDEALRLYLEAFRLPGEAPVIHRLLEVFTEHWRSCNGSPFANSDACFALAYAVIMLNTDQHNHNVRKQNAPMTLEEFRKNLKGVNGGKDFEQDILEDMYHAIKNEEIVMPEEQTGLVRENYVWSVLLHRGATPEGIFLRVPPGSYDLDLFTMTWGPTIAALSYVFDKSLEETIIQKAISGFRKCAMISAHYGLSDVFDNLIISLCKFTALSSESIENLPSVFGSNPKAHIAAKTVFHLAHRHGDILREGWKNIMEAMLQLFRAQLLPKAMVEVEDFVDPNGKISLQREETPSNRGESTVLSFVSWLTLSGPEQSSVRGPSTENQEAKRVALDCIKQCDPEKMITESKFLQLESLQELMKALVSVTPDEETYDEEDAAFCLEMLLRIVLENRDRVGCVWQTVRDHLYHLCVQAQDFCFLVERAVVGLLRLAIRLLRREEISGQVLLSLRILLLMKPSVLSRVSHQVAYGLHELLKTNAANIHSGDDWATLFTLLECIGSGVKPPDALQATARADAPDAGAQSDSELPSYHQNDVSLDRGYTSDSEVYTDHGRPGKMHRSATDADMANSGWLVVGKDDIDNSKPAAGLSRPGPSPLVNQYSLTVGLDLGPHDTKSLLKCVESLSFIVRDAAHITPDNFELCVKTLRIFVEASLNGGCKSQDKRGKSHKYDSKGNRFKKKPKEGSMLRRPRASSQHATRAGHSDEEEDEGVPASYHTVSLQLLDLMHTLHTRAASIYSSWAEEQRHLETGGRKIEADSRTLWAHCWCPLLQGIACLCCDARRQVRMQALTYLQRALLVHDLQKLDALEWESCFNKVLFPLLTKLLENISPADVGGMEETRMRASTLLSKVFLQHLSPLLSLSTFAALWLTILDFMDKYMHAGSSDLLSEAVPESLKNMLLVMDTAEIFHSADARGGSPSALWEITWERIDCFLPHLRDELFKQTVIQDPMPTEPHSQKPLASTHLTPAAGDPRMPGHPPPPEIPSEVGACDPEKPESTRAASSSSPGSPVASSPSKQSPAPEGPPPLAQPPLILQPLTSPLQVGVPPMTLPIILNPALIEATSPVPLLATPRPTDPIPTSEVN
Protein: Ribulose-5-phosphate-3-epimerase, chloroplastic (R5P3E) (EC 5.1.3.1) (Pentose-5-phosphate 3-epimerase) (Protein EMBRYO DEFECTIVE 2728) (Q9SAU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein required during embryogenesis. Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate (By similarity). Essential for the early steps of nematode feeding sites (NFS, multinucleated root cells) formation induced by the root-knot nematodes Heterodera schachtii, Meloidogyne incognita, M.javanica and M.hapla.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:Q43157}.
Interaction partners:
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Phosphoribulokinase, chloroplastic
- Probable ribose-5-phosphate isomerase 3, chloroplastic
- Probable ribose-5-phosphate isomerase 2
- Probable ribose-5-phosphate isomerase 4, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Probable ribose-5-phosphate isomerase 1
- 6-phosphogluconate dehydrogenase, decarboxylating 3, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic
Sequence:
MSTSAASLCCSSTQVNGFGLRPERSLLYQPTSFSFSRRRTHGIVKASSRVDRFSKSDIIVSPSILSANFAKLGEQVKAVELAGCDWIHVDVMDGRFVPNITIGPLVVDALRPVTDLPLDVHLMIVEPEQRVPDFIKAGADIVSVHCEQQSTIHLHRTVNQIKSLGAKAGVVLNPGTPLSAIEYVLDMVDLVLIMSVNPGFGGQSFIESQVKKISDLRKMCAEKGVNPWIEVDGGVTPANAYKVIEAGANALVAGSAVFGAKDYAEAIKGIKASKRPAAVAV
Protein: Vermiform, isoform H (Q9VW31)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MARWWPILSVVCLCLAVAHGQDKLEGVDVEEVCADRPADEYFRLETDGDCREVYRCDSAGEDGTWRLAPIRCAGGLAFDVLRQLCDWKSNVKSCDVLEKPRKAKPILKTDEPICPEGKLSCGDGECLDKELFCNGKSDCKDESDENACSVDEDPNRAPECDPTQCALPDCFCSADGTRIPGGIEPQQVPQMITITFNGAVNVDNIDLYEDIFNGQRQNPNGCSIKGTFFVSHKYTNYSAVQDLHRRGHEISVFSLTHKDDPNYWTGGSYDDWLAEMAGSRLIVERFANITDGSIIGMRAPYLRVGGNKQFEMMADQFFVYDASITASLGRVPIWPYTLYFRMPHKCNGNAHNCPSRSHPVWEMVMNELDRRDDPTFDESLPGCHMVDSCSNVASGDQFARLLRHNFNRHYNSNRAPLGLHFHASWLKSKKEYRDELIKFIEEMLGRNDVFFVTNLQVIQWMQNPTELNSLRDFQEWKEKCDVKGQPYCSLPNACPLTTRELPGETLRLFTCMECPNNYPWILDPTGDGFSV
Protein: Sorbin and SH3 domain-containing protein 1 (Ponsin) (SH3 domain protein 5) (SH3P12) (c-Cbl-associated protein) (CAP) (Q62417)
Organism: Mus musculus (Mouse)
Function: Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions.
Subcellular location: Cell junction, adherens junction. Cell membrane. Cytoplasm, cytoskeleton. Cell junction, focal adhesion {ECO:0000250}. Nucleus. Nucleus matrix. Note=Colocalized with PXN at focal adhesions during myogenic differentiation (By similarity). Colocalizes with actin stress fibers. Also detected at the plasma membrane and in neuronal intranuclear inclusions. Colocalizes with the Ten-1 ICD form of TENM1 in the nucleus. {ECO:0000250}.
Interaction partners:
Sequence:
MSSECDVGSSKAVVNGLASGNHGPDKDMDPTKICTGKGTVTLRASSSYRGTPSSSPVSPQESPKHESKSGLEPEDPSADEWKLSSSADTNGNAQPSPLAAKGYRSVHPSLSADKPQGSPLLNEVSSSHIETDSQDFPPTSRPSSAYPSTTIVNPTIVLLQHNRDPASERRAGEQDPVPTPAELTSPGRASERRAKDASRRVVRSAQDLSDVSTDEVGIPLRNTERSKDWYKTMFKQIHKLNRDDDSDVHSPRYSFSDDTKSPLSVPRSKSEMNYIEGEKVVKRSATLPLPARSSSLKSSPERNDWEPLDKKVDTRKYRAEPKSIYEYQPGKSSVLTNEKMSRDISPEEIDLKNEPWYKFFSELEFGRPTNLEKDLSFCQAELEADLEKVETVNKSPSANSPQSSAVSPTPDITSEPPGYIYSSNFHAVKRESDGTPGGLASLENERQIYKSVLEGGDIPLQGLSGLKRPSSSASTKVDRKGGNAHMISSSSVHSRTFHTSNALGPGCKHKKPLSAAKACISEILPSKFKPRLSAPSALLQEQKSVLLPSEKAQSCENLCVSLNDSKRGLPLRVGGSIENLLMRSRRDYDSKSSSTMSLQEYGTSSRRPCPLSRKAGLHFSMFYRDMHQINRAGLSLGSISSSSVRDLASHFERSSLTLARGELGASQEGSEHIPKHTVSSRITAFEQLIQRSRSMPSLDFSGRLSKSPTPVLSRSGLTSARSAESLLESTKLRPREMDGMDSGGVYASPTCSNMADHALSFRSLVPSEPLSICSDELDHCSNVSNDSREGSGGSVHGDFPKHRLNKCKGTCPASYTRFTTIRKHEQQSSRQSDWRSDSRGDKNSLLRNIHLMSPLPFRLKKPLQQHPRQPPPSDSSESPAGQKADLPCHDPQDQPHSAGKPQVPTRLSSRHTMARLSHNSEPPLDRPAGLEDCTRAINNGNPVPYSDHGLDRNNNPQSELAAAHGDSESPRHFIPADYLESTEEFIRRRHDDKEKLLADQRRLKREQEEADIAARRHTGVIPTHHQFITNERFGDLLNIDDTAKRKSGLEMRPARAKFDFKAQTLKELPLQKGDVVYIYRQIDQNWYEGEHHGRVGIFPRTYIELLPPAEKAQPRKLAPVQVLEYGEAIAKFNFNGDTQVEMSFRKGERITLLRQVDENWYEGRIPGTSRQGIFPITYVDVLKRPLVKTPVDYIDLPYSSSPSRSATVSPQQPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL
Protein: RNA-binding protein 4B (RNA-binding motif protein 30) (RNA-binding motif protein 4B) (RNA-binding protein 30) (Q8VE92)
Organism: Mus musculus (Mouse)
Function: Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 2A
Sequence:
MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKASTKLHVGNISPTCTNQELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPVDRTGRVADFTEQYNEQYGAVRTPYTMGYGESMYYNDAYGALDYYKRYRVRSYEAVAAAAAASAYNYAEQTMSHLPQVQSSAVPSHLNSTSVDPYDRHLLQNSGSAATSAAMAAAASSSYYGRDRSPLRRNAAVLPAVGEGYGYGPESEMSQASAATRNSLYDMARYEREQYVDRTRYSAF
Protein: Transcription factor Toy (Q9XZC2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MMLTTEHIMHGHPHSSVGQSTLFGCSTAGHSGINQLGGVYVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIKPRAIGGSKPRVATTPVVQKIADYKRECPSIFAWEIRDRLLSEQVCNSDNIPSVSSINRVLRNLASQKEQQAQQQNESVYEKLRMFNGQTGGWAWYPSNTTTAHLTLPPAASVVTSPANLSGQADRDDVQKRELQFSVEVSHTNSHDSTSDGNSEHNSSGDEDSQMRLRLKRKLQRNRTSFSNEQIDSLEKEFERTHYPDVFARERLADKIGLPEARIQVWFSNRRAKWRREEKMRTQRRSADTVDGSGRTSTANNPSGTTASSSVATSNNSTPGIVNSAINVAERTSSALISNSLPEASNGPTVLGGEANTTHTSSESPPLQPSAPRLPLNSGFNTMYSSIPQPIATMAENYNSSLGSMTPSCLQQRDAYPYMFHDPLSLGSPYVSAHHRNTACNPSAAHQQPPQHGVYTNSSPMPSSNTGVISAGVSVPVQISTQNVSDLTGSNYWPRLQ
Protein: Non-specific lipid-transfer protein 4 (LTP 4) (Q9LLR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity).
Interaction partners:
- Uncharacterized protein
- F-box protein, putative
- At5g55460
- Alpha/beta-Hydrolases superfamily protein
- Defensin-like protein 195
- Dehydrin Xero 2
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Protein OXIDATIVE STRESS 3 LIKE 1
- 50S ribosomal protein L7/L12
- Protein kinase superfamily protein
Sequence:
MAFALRFFTCFVLTVFIVASVDAAITCGTVASSLSPCLGYLSKGGVVPPPCCAGVKKLNGMAQTTPDRQQACRCLQSAAKGVNPSLASGLPGKCGVSIPYPISTSTNCATIK
Protein: Gamma-aminobutyric acid type A receptor subunit alpha5 (G3V408)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDNGMFSGFIMIKNLLLFCISMNLSSHFGFSQMPTSSVKDETNDNITIFTRILDGLLDGYDNRLRPGLGERITQVRTDIYVTSFGP
Protein: Acid phosphatase PHO11 (EC 3.1.3.2) (P56) (P35842)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Inorganic phosphate transporter PHO84
- Repressible acid phosphatase
- Acid phosphatase PHO12
- Repressible alkaline phosphatase
- Constitutive acid phosphatase
- Putative cyclin-dependent kinase inhibitor SPL2
- Thiamine pyrophosphokinase
- Phosphate system positive regulatory protein PHO81
- Phosphate permease PHO89
- Thiamine biosynthetic bifunctional enzyme
Sequence:
MLKSAVYSILAASLVNAGTIPLGKLSDIDKIGTQTEIFPFLGGSGPYYSFPGDYGISRDLPESCEMKQVQMVGRHGERYPTVSKAKSIMTTWYKLSNYTGQFSGALSFLNDDYEFFIRDTKNLEMETTLANSVNVLNPYTGEMNAKRHARDFLAQYGYMVENQTSFAVFTSNSNRCHDTAQYFIDGLGDKFNISLQTISEAESAGANTLSAHHSCPAWDDDVNDDILKKYDTKYLSGIAKRLNKENKGLNLTSSDANTFFAWCAYEINARGYSDICNIFTKDELVRFSYGQDLETYYQTGPGYDVVRSVGANLFNASVKLLKESEVQDQKVWLSFTHDTDILNYLTTIGIIDDKNNLTAEHVPFMENTFHRSWYVPQGARVYTEKFQCSNDTYVRYVINDAVVPIETCSTGPGFSCEINDFYDYAEKRVAGTDFLKVCNVSSVSNSTELTFFWDWNTKHYNDTLLKQ
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic (EC 2.3.1.51) (EC 2.3.1.n4) (Lysophosphatidyl acyltransferase 1) (Protein EMBRYO DEFECTIVE 1995) (Q8GXU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plastidial enzyme of the prokaryotic glycerol-3-phosphate pathway that converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at position sn-2. Utilizes palmitoyl-ACP (16:0-ACP) to produce phosphatidic acid containing a saturated group at position sn-2, which is characteristic of lipids synthesized by the prokaryotic pathway. In vitro, can use 16:0-CoA as acyl donor. Essential for embryo development during the transition from the globular to the heart stage when chloroplasts begin to form.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:15169931}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase 3
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
- Lysophospholipid acyltransferase 1
- Lysophospholipid acyltransferase 2
- Glycerol-3-phosphate acyltransferase 9
- Glycerol-3-phosphate acyltransferase, chloroplastic
- Triacylglycerol lipase SDP1
- Lysophospholipid acyltransferase LPEAT2
Sequence:
MDVASARSISSHPSYYGKPICSSQSSLIRISRDKVCCFGRISNGMTSFTTSLHAVPSEKFMGETRRTGIQWSNRSLRHDPYRFLDKKSPRSSQLARDITVRADLSGAATPDSSFPEPEIKLSSRLRGIFFCVVAGISATFLIVLMIIGHPFVLLFDPYRRKFHHFIAKLWASISIYPFYKINIEGLENLPSSDTPAVYVSNHQSFLDIYTLLSLGKSFKFISKTGIFVIPIIGWAMSMMGVVPLKRMDPRSQVDCLKRCMELLKKGASVFFFPEGTRSKDGRLGSFKKGAFTVAAKTGVAVVPITLMGTGKIMPTGSEGILNHGNVRVIIHKPIHGSKADVLCNEARSKIAESMDL
Protein: Actin-like protein 7B (Actin-like-7-beta) (Testis-specific actin-1) (T-actin-1) (Q9QY83)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Dynactin subunit 2
Sequence:
MATKNSPSPKPMGTAQGDPGEAGTLPAPEAAGIRDTGSTQLKTKPKKIRKIKALVIDLGSQYCKCGYAGEPRPTYFISSTVGKRSAEMAADAGDNFKETYVGHELLNMEASLKLVNPLKHGVVVDWDCIQNIWEYIFHTAMKIMPEEHAVLVSDPPLSPTSNREKYAELLFETFGIPAMHVTSQALLSIYSYGKTSGLVVESGHGVSHVVPISEGDLLPGLPSRVDYAGCDLTNYLMQLLNEAGHKFSDDHLHIIEHIKKKCCYAALLPEEEMSLGLDELHVDYELPDGKIITIGQERFRCSEMLFKPSLVGCTQPGLPELTATCLARCQGTGFKEEMAANVLLCGGCTMLDGFPERFQRELSLLCPGDSPTVAAAPERKTSVWTGGSILASLQAFQQLWVSKEEFEERGCAAIYSKC
Protein: 3-hydroxy-3-methylglutaryl coenzyme A reductase 1 (HMG-CoA reductase 1) (Hydroxymethylglutaryl-CoA reductase) (PgHMGR1) (EC 1.1.1.34) (A0A0A1C3I2)
Organism: Panax ginseng (Korean ginseng)
Function: Catalyzes the synthesis of mevalonate, the specific precursor of all isoprenoid compounds present in plants (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Promotes triterpenes accumulation in roots.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24569845}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in intracellular vesicles. {ECO:0000269|PubMed:24569845}.
Interaction partners:
Sequence:
MDVRRRLPPKLRRPLPITESSHHHRKTPFPADVDRSPSPTPKASDALPLPLYLTNGIFFTLFFSVAYYLLHRWRDKIRSSTPLHIVTLSELAAIVSLIASFIYLLGFFGIDFVQSFVSRADVDVDIDVEPDILEADRRPCSKLMDQPPPPPVVMSSEEDEEIVKSVVSGKTPSYSLESKLGDCYRAASIRREAVQRTTGRSLLGLPLDGFDYESILGQCCEMPIGYVQIPVGIAGPLLLNGCEYVVPMATTEGCLVASTNRGCKAIYACGGATGILLKDGMTRAPVVRFSTAKRASDLKFFLEDPLNFDTLAVVFNKSSRFARLQSIQCSMAGKNLYIRFCCSTGDAMGMNMVSKGVQNVLEFLQSDFPDMDVIGISGNFCSDKKPAAVNWIEGRGKSVVCEAIITDDVVKKVLKTTVPALVELNMLKNLAGSAVAGALGGFNAHAANIVSAVFIATGQDPAQNIESSHCITMMEAINNGKDLHISVTMPSIEVGTVGGGTQLASQSACLNLLGVKGANKESHGSNSRLLATIVAGSVLAGELSLMSAIAAGQLVRSHMKYNRSSRDMSKIGS