wanglab/gogpt-training-data huggingface dataset:
Protein: Hematopoietic lineage cell-specific protein (Hematopoietic cell-specific LYN substrate 1) (LckBP1) (p75) (P14317)
Organism: Homo sapiens (Human)
Function: Substrate of the antigen receptor-coupled tyrosine kinase. Plays a role in antigen receptor signaling for both clonal expansion and deletion in lymphoid cells. May also be involved in the regulation of gene expression.
Subcellular location: Membrane {ECO:0000269|PubMed:7682714}; Peripheral membrane protein {ECO:0000269|PubMed:7682714}. Cytoplasm {ECO:0000269|PubMed:7682714}. Mitochondrion {ECO:0000305|PubMed:7682714}.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Proto-oncogene tyrosine-protein kinase Src
- Dynamin-2
- Tight junction protein 1
- Actin nucleation-promoting factor WASL
- Cofilin-2
- Cofilin-1
- Paxillin
- Actin-related protein 2
- Protein deacetylase HDAC6
Sequence:
MWKSVVGHDVSVSVETQGDDWDTDPDFVNDISEKEQRWGAKTIEGSGRTEHINIHQLRNKVSEEHDVLRKKEMESGPKASHGYGGRFGVERDRMDKSAVGHEYVAEVEKHSSQTDAAKGFGGKYGVERDRADKSAVGFDYKGEVEKHTSQKDYSRGFGGRYGVEKDKWDKAALGYDYKGETEKHESQRDYAKGFGGQYGIQKDRVDKSAVGFNEMEAPTTAYKKTTPIEAASSGTRGLKAKFESMAEEKRKREEEEKAQQVARRQQERKAVTKRSPEAPQPVIAMEEPAVPAPLPKKISSEAWPPVGTPPSSESEPVRTSREHPVPLLPIRQTLPEDNEEPPALPPRTLEGLQVEEEPVYEAEPEPEPEPEPEPENDYEDVEEMDRHEQEDEPEGDYEEVLEPEDSSFSSALAGSSGCPAGAGAGAVALGISAVAVYDYQGEGSDELSFDPDDVITDIEMVDEGWWRGRCHGHFGLFPANYVKLLE
Protein: Plastid transcriptionally active 4 (A0A178W0D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNLFERFSRVVKSYANALISSFEDPEKILEQTVIEMNSDLTKMRQATAQVLASQKQLQNKYKAAQQSSDDWYKRAQLALAKGDEDLAREALKRRKSFADNATALKTQLDQQKGVVDNLVSNTRLLESKIQEAKAKKDTLLARARTAKTATKVQEMIGTVNTSGALSAFEKMEEKVMAMESEADALTQIGTDELEGKFQMLETSSVDDDLADLKKELSGSSKKGELPPGRSTVAASTRYPFKDSEIENELNELRRKANDF
Protein: Large ribosomal subunit protein P1A (P1A) (60S acidic ribosomal protein P1-alpha) (A1) (L12eIIA) (YP1alpha) (P05318)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL3
Sequence:
MSTESALSYAALILADSEIEISSEKLLTLTNAANVPVENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD
Protein: Complement C1q subcomponent subunit B (P31721)
Organism: Rattus norvegicus (Rat)
Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
Subcellular location: Secreted.
Interaction partners:
- Complement C1q subcomponent subunit A
- Complement C1q subcomponent subunit C
- Plasma protease C1 inhibitor
- Complement C1s subcomponent
- Complement C4
- Complement C1r subcomponent
- Complement C2
- Complement C4A
- Calreticulin
- Calreticulin
Sequence:
MKTQWSEILTPLLLLLLGLLHVSWAQSSCTGSPGIPGVPGIPGVPGSDGKPGTPGIKGEKGLPGLAGDHGELGEKGDAGIPGIPGKVGPKGPVGPKGAPGPPGPRGPKGGSGDYKATQKVAFSALRTVNSALRPNQAIRFEKVITNVNDNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNIVRGRDRDRMQKVLTFCDYAQNTFQVTTGGVVLKLEQEEVVHLQATDKNSLLGVEGANSIFTGFLLFPDMDV
Protein: Paxillin (A0A1B0GTU4)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDDLDALLADLESTTSHISKRPVFLSEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTILDPLDQWQPSSSRFIHQQPQSSSPVYGSSAKTSSVSNPQDSVGSPCSRVGEEEHVYSFPNKQKSAEPSPTVMSTSLGSNLSELDRLLLELNAVQHNPPGFPADEANSSPPLPGALSPLYGVPETNSPLGGKAGPLTKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSTQQQTRISASSATRELDELMASLSDFKTSSSTVALSAPGLSSSAPSSYCSLPPSPPPMPSVFLPPTTIPSPRGQGHTPEFPCTEQSGRGLLPPVAPSWLDLAGLGVMPDTFNSRSPSVEGSLWAVGTESQGRDWRHLPTITSELSGAPRCHTVPCAGSTALQEPGEPQGPPASPSCPEEALAATWEQPWASEVFGPERMPPSGAARSFQEVTEPAVVAVDRQAIFPDTWTLTEEHGLQQERPRPEPGRLGSSSPASVTTEQLGAKMTERGSVARPTQGPETPRSPEGTTEAATQDGKEQPELPCAMAMGTPSTTERISTSGQIRSVIRRSWESGHAHPMSREPSPRRRLDPATLSRTPSQEQLIAELQGRLGIQPEAEEPAEAAGPSAQDWLTEGVIITVQPRGKRAGGQLVEKVVFPPGSPIPLRRTISVLASPSVPLLQHRTDAAASSSSPLPSLLASSPLGPSAYTCGSSGVQSAGEEPHDEGVQGPALPIPAPHTMRSVGCQTDEDPLFPPMQIQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGGFMAQGKTGSSSPPGGPPKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC
Protein: Protein Wnt-6 (Q9Y6F9)
Organism: Homo sapiens (Human)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. Together with CAV1 may promote chemoresistance of gastric cancer cells to DNA-damaging anthracycline drugs through the activation of the canonical Wnt receptor signaling pathway.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Frizzled-2
- Protein-serine O-palmitoleoyltransferase porcupine
- Dickkopf-related protein 2
- Dickkopf-related protein 4
- Wnt inhibitory factor 1
- Dickkopf-related protein 1
- Palmitoleoyl-protein carboxylesterase NOTUM
- Frizzled-9
- Low-density lipoprotein receptor-related protein 5
- Frizzled-4
Sequence:
MLPPLPSRLGLLLLLLLCPAHVGGLWWAVGSPLVMDPTSICRKARRLAGRQAELCQAEPEVVAELARGARLGVRECQFQFRFRRWNCSSHSKAFGRILQQDIRETAFVFAITAAGASHAVTQACSMGELLQCGCQAPRGRAPPRPSGLPGTPGPPGPAGSPEGSAAWEWGGCGDDVDFGDEKSRLFMDARHKRGRGDIRALVQLHNNEAGRLAVRSHTRTECKCHGLSGSCALRTCWQKLPPFREVGARLLERFHGASRVMGTNDGKALLPAVRTLKPPGRADLLYAADSPDFCAPNRRTGSPGTRGRACNSSAPDLSGCDLLCCGRGHRQESVQLEENCLCRFHWCCVVQCHRCRVRKELSLCL
Protein: Asnovolin H synthase nvfL (EC 5.4.99.-) (Novofumigatonin biosynthesis cluster protein L) (Terpene cyclase nvfL) (A0A2I1BT01)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of novofumigatonin, a heavily oxygenated meroterpenoid containing a unique orthoester moiety. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase nvfA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then converted to farnesyl-DMOA by the farnesyltransferase nvfB. Epoxydation by FAD-dependent monooxygenase nvfK, followed by a protonation-initiated cyclization catalyzed by the terpene cyclase nvfL leads to the production of asnavolin H. The short chain dehydrogenase nvfC then as a 3-OH dehydrogenase of asnovolin H to yield chemesin D. There are two branches to synthesize asnovolin A from chemesin D. In one branch, chemesin D undergoes Baeyer-Villiger oxidation by nvfH, methylation by nvfJ, and enoyl reduction by the nvfM D enoylreductase that reduces the double bond between C-5'and C-6', to form respectively asnovolin I, asnovolin K, and asnovolin A. In the other branch, the methylation precedes the Baeyer-Villiger oxidation and the enoyl reduction to yield asnovolin A via the asnovolin J intermediate. Asnovolin A is further converted to fumigatonoid A by the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfI that catalyzes an endoperoxidation reaction. The alpha/beta hydrolase nvfD then acts as an epimerase that converts fumigatonoid A to its C-5' epimer, which then undergoes spontaneous or nvfD-catalyzed lactonization. The following step utilizes the ketoreductase nvfG to produce fumigatonoid B. The dioxygenase nvfE further converts fumigatonoid B into fumigatonoid C. Finally the Fe(II)/2-oxoglutarate-dependent dioxygenase nvfF catalyzes two rounds of oxidation to transform fumigatonoid C into the end product, novofumigatonin A.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDPWIALSSPLTSQTVEYVANTLRIMCAISWNISYMSMAYYSFRDKTYGNALIPLCNNIAWEFVYSFIHCPKLTFVRIENTGWFLLNIVVMYAAIKYSENEWKHAPLVQRNLPFIFAVGISAMIAGHLALAAQIGPRIAFVWSAKGCQLVLSTGALSQLLSRGSTRGGSYVVWLSRYLGTVFIDVMVTIRHVYRAAGPSWPSSPLLLWFMAVFHLLDWTYGFCFYHIRRQELVSEAAEKDKDK
Protein: Probable porin (Q9HZH0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- DUF485 domain-containing protein
- Cation/acetate symporter ActP
- Uncharacterized protein
- Acetyl-coenzyme A synthetase 1
Sequence:
MSMTPIARAVAFAALGSSITVPTLAHAEFIKDSKASIELRNFYFNRDFRQEGASQSKAEEWAQGFLLRYESGYTEGTIGFGVDAIGLLGVKLDSSPDRSGTGLLKRDRETGRAQDDYGEAGITAKLRASKSTLKIGTLTPKLPVIMPNDSRLLPQTFQGGALNSMEIDGLTLDAGRLKKVNQRDSSDNEDMTITGGGKRNIVVRSGLTSDKFDFAGGSYKWTDNLSTSYHYGKLDNFYKQHYLGLVHTLPIADKQSLKSDIRWARSTDDGSSNVDNKALNAMFTYSLGYHAFGVGYQKMSGDTGFAYINGADPYLVNFIQIGDFANKDEKSWQARYDYNFAGVGIPGLTFMTRYVKGDNIDLLTTSGEGKEWERDMDIAYVFQSGPLKNLGVKWRNATMRTNYTNDYDENRLIVSYTLPLW
Protein: Replication factor C subunit 1 (A0A0G2JVK8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR036578}.
Interaction partners:
Sequence:
MDIRKFFGVISSGKKPVNETVKKNEKTKPSEGTVKGKKGVKEAKVNNPCKEDASRPKQHNKKKRIIYDSDSESEETVQVKNAKKKSEKLPVSCKPGKISRKDPVTYISETDEDDDFLCKKAASKSKENGVSTNSYLGASNVKKNEENTKTKSKPLSPIKLTPTSVLDYFGTESVQRSGKKMVASKKKESSQTPDDSRLNDEAIAKQLQLDEDAELERQLHEDEEFARTLALLDEEPKTKKARKDSEEGESFSPAKAELSKAAKQKSPANEHFSIGRKTYSPAKYGKGRGSEGTKQPCRSAHQKEACSSLKASSKLALMKAQEENSYKETELLAAKRESAIEPKGEKTTPRKTKGSPTKRESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGAENCLEGLTFVITGVLESIEREEAKSLIERYGGKVTGNVSKKTSYLVMGRDSGQSKSDKAAALGTKILDEDGLLDLIRTMPGKKSKYEIAAEAEMKKEKSKLERTPQKNDQGKRKLSPTKRELEPKKSKLTPLKHSPRKAVKEEERVCPRGLDAKEPHGSHSASREECLLWVDKYKPTSLKNIIGQQGDQSCANKLLRWLRNWHKSSPEEKKHAAKFGKVASKDDGSSFKAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKNSLKAIVAESLNNTSIKGFYTSGASPSVSARHALIMDEVDGMAGNEDRGGIQELIGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKSAMLSIAFKEGLKIPPPAMNEIILGANQDVRQVLHNLSMWCAQSKVLTYDQAKADSQRAKKDIRLGPFDVTRKVFAAGEETAHMSLMDKSDLFFHDYSIAPLFVQENYLHVKPVAAGGDMKKHLMLLSRAADSICDGDLVDNQIRSKQNWSLLPTQAIYASVVPGELMRGYMSQFPSFPSWLGKHSSTGKHDRTVQDLSLHMSLRTYSSKRTVNMDYLSHIRDALVRPLTSQGVEGVQRVVTLMDTYYLVKEDFDNIMEVSSWGGKPSTFSKLDPKVKAAFTRAYNKEAHLTPYSLQVVKASRPSIGPALDSEYNEESQEDATQSDEKEQDALETDAMIKVVYSACPVRDLKKGKFLTCLFWLS
Protein: Ras-related protein Rab-3D (EC 3.6.5.2) (P35276)
Organism: Mus musculus (Mouse)
Function: Protein transport. Probably involved in vesicular traffic (By similarity). May be involved in the insulin-induced exocytosis of glut4-containing vesicles in adipocytes.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rab effector Noc2
- Geranylgeranyl transferase type-2 subunit alpha
Sequence:
MASASEPPASPRDAADQNFDYMFKLLLIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTVYRHDKRIKLQIWDTAGQERYRTITTAYYRGAMGFLLMYDIANQESFTAVQDWATQIKTYSWDNAQVILVGNKCDLEDERVVPAEDGRRLADDLGFEFFEASAKENINVKQVFERLVDIICDKMNESLEPSSSPGSNGKGPALGDTPPPQPSSCSC
Protein: Membrane-anchored ubiquitin-fold protein 3 (AtMUB3) (Membrane-anchored ub-fold protein 3) (ATGP4) (Q9SW27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May serve as docking site to facilitate the association of other proteins to the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16831869}; Lipid-anchor {ECO:0000269|PubMed:16831869}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 8
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- At5g40190
- Eukaryotic aspartyl protease family protein
- Transport/golgi organization-like protein
- Myosin heavy chain-like protein
- Ubiquitin system component Cue protein
- Transmembrane protein
- Myosin-binding protein 7
- Probable protein S-acyltransferase 13
Sequence:
MPEEESIDIKFRLYDGSDIGPFRYSAASTVDFLKQRVVSDWPKGKTVVPKGINEVKLISSGKILENNKTVGQCKTPFGDIAGGVIVMHVVVQPSLAKSKTEKKVDKAPKAVICTCTIL
Protein: Calcium/calmodulin-dependent protein kinase I, isoform I (EC 2.7.11.17) (A4V110)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPLFGKKDSGKKAKAKDLKELNKQVSIEEKYNLHGLLGTGAFSEVRLAESKDSPGEHFAVKIIDKKALKGKEESLENEIRVLRRLTHPNIVQLLETYEDKSKVYLVMELVTGGELFDRIVEKGSYTEKDASHLIRQILEAVDYMHEQGVVHRDLKPENLLYYSPDDDSKIMISDFGLSKMEDSGIMATACGTPGYVAPEVLAQKPYGKAVDVWSIGVISYILLCGYPPFYDENDANLFAQILKGDFEFDSPYWDEISESAKHFIKNLMCVTVEKRYTCKQALGHAWISGNEASSRNIHGTVSEQLKKNFAKSRWKQAYYAATVIRQMQRMALNSNSNANFDSSNSSNQDSTTPTAATGAWTSNVLSSQQSVQSHAQEMNKSGGSTNAASQ
Protein: Glycoprotein L (UL1) (Virion surface glycoprotein L) (Q77Q67)
Organism: Gallid alphaherpesvirus 2
Interaction partners:
Sequence:
MKIYRVLVHLSFVLGMFTKTNTVLAWSKYDLVHGFMRVANISSIMRLDCLPNLLSSNAGYAALPSDDIPTGIFIKVNCSIPEFILWYEQKAMAAWINPIMGTVLMMNDVLKSGLENSVKVGLLTFLKRIAEKGPNGPLRNRGSGCINLIAPADISCYGSTRLDRFNRDFEDDSRGMPCRAKAMRRTTSGSRRANA
Protein: D site-binding protein (Albumin D box-binding protein) (Albumin D-element-binding protein) (Tax-responsive enhancer element-binding protein 302) (TaxREB302) (Q10586)
Organism: Homo sapiens (Human)
Function: This transcriptional activator recognizes and binds to the sequence 5'-RTTAYGTAAY-3' found in the promoter of genes such as albumin, CYP2A4 and CYP2A5. It is not essential for circadian rhythm generation, but modulates important clock output genes. May be a direct target for regulation by the circadian pacemaker component clock. May affect circadian period and sleep regulation.
Subcellular location: Nucleus.
Interaction partners:
- Basic helix-loop-helix ARNT-like protein 1
- Circadian locomoter output cycles protein kaput
- Neuronal PAS domain-containing protein 2
- Nuclear receptor subfamily 1 group D member 1
- Pyridoxal kinase
- Period circadian protein homolog 3
Sequence:
MARPVSDRTPAPLLLGGPAGTPPGGGALLGLRSLLQGTSKPKEPASCLLKEKERKAALPAATTPGPGLETAGPADAPAGAVVGGGSPRGRPGPVPAPGLLAPLLWERTLPFGDVEYVDLDAFLLEHGLPPSPPPPGGPSPEPSPARTPAPSPGPGSCGSASPRSSPGHAPARAALGTASGHRAGLTSRDTPSPVDPDTVEVLMTFEPDPADLALSSIPGHETFDPRRHRFSEEELKPQPIMKKARKIQVPEEQKDEKYWSRRYKNNEAAKRSRDARRLKENQISVRAAFLEKENALLRQEVVAVRQELSHYRAVLSRYQAQHGAL
Protein: Adipocyte-specific protein 6 (Q920S4)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MRSCRRLDQLQAGLCLLLASLQLVSWTLAAEPVDVLEAWGVHRDQAGVAEGPGFCPLRIPQGDRAFRVGKSSLLSVPTWQLFPDGHFPENFSVLLTLRAQPANQSVLLSIYDEKGVRQLGLALGPALGLLGDSFRPLPKQVNIMDGRWHRVAVSISGNKVTLVVDCEPQPPTFGQGPRFISTAGLTVMGTQDTREESFEGDIQELLLIPDPQAAFQACESYLPGCETLDSTTTGAPKDDEPETPAPRRRKGKGKKKGRGRKGKGRKKNKETSELSPTPGAPENQTSLHIPETEKTVPHLPPTPTPLAITTTVTIGQNATVSKGLDSGTETEQRTPEMDATEEGEGGGPTMGPKFRAAEQSLQTEFQIFPGAGEKGAKGEPATVEQGQQFEGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGARGLPGTVIMMPFHFASSSMKGPPVSFQQAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEVGPQGPRGLQGPPGPPGREGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGRVGQPGPPGEDGVKGLQGPPGPTGQAGEPGPRGLIGPRGLPGPLGRPGVTGSDGAPGAKGNVGPPGEPGPPGQQGNHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPRGYPGLRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGPPGPRGEDGPEGQKGPGGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGPPGEKGLPGLQGPPGFPGPKGPPGPQGKDGISGHPGQRGELGFQGLTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEQGLPGIEGREGAKGELGPLGSVGKEGPPGPRGFPGPQGAPGDPGPIGLKGDKGPPGPVGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPVSVCWLTFSGET
Protein: C2H2-type domain-containing protein (O18064)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTCDDWNSYIQVNIYGKTIEGLQQQGVVLESLLNNVGCSKVWIMEGSVCTNPRPESSTHSEESTIEPVVPLSTTLATNKLPRFSTPAIGHSNNNSSKNFTLNLAEKLSEILSDDDKTDEFLENSHQSETSKDDVIKDLLEEMVQTVANSNKPPILLSTTLANVGVPRFSTPIKPQHALNRDFTMNMTEMISEIDSNYEGYELFDDSSNDCTTLTPNCQEVESSFYRALSEAASSIVPYQEGKRRSSRRLSTLSSLKETVKVEPAVSKLTKRRRLTPVECSSETMIPHSQPIPLDTCSDQPIFPNSTHNAIQSDGFSYEQPICEFGDSQLFLSAKSLCTEPNSSIAEDVKPVLTVSDSDITASNRNNIDDHNRVIELSTEHKTMGEFQYNFDDEDTVLIGNYEEVGTEIDEADEQHNEENSEDDEEDESPIPSKKRVSFAVPLVQSRSKQKDEMNKVHIIKCHFDKCNKSYNWRKKYGKLRLVDHAFTHVPHLKMKCNFCDYMCKGIRNIRLHHKKSHPDEQLTGFGIKSVVRTSKKGKDLAKVWDECFKKNRVLQHGSGTDSNLLHFSRQDKGSKRSQKSMDSGAKQKLDEARDEDVKPF
Protein: Transketolase, N-terminal subunit (A0A0H2US62)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MILSKNREDGLRKFATNIRLNTLRTLNHLGFGHYGGSLSIVEVLAVLYGEIMPMTPEIFAARDRDYFILSKGHGGPALYSTLYLNGFFDKEFLYSLNTNGTKLPSHPDRNLTPGIDMTTGSLGQGISVATGLAYGQRIRKSPFYTYAIVGDGELNEGQCWEAIQFASHQQLSNLIVFVDDNKKQLDGFTKDICNPGDFVEKFSAFGFESIRVKGSDIREIYEGIVQLKQSNNSSPKCIVLDTIKGQGVQELEEMKSNHHLRPTVEEKQMLTSVVERLSQELEETE
Protein: Inositol diphosphatase DSP1 (EC 3.6.1.52) (Inositol pyrophosphate phosphatase DSP1) (Protein PLANT AND FUNGI ATYPICAL DUAL-SPECIFICITY PHOSPHATASE 1) (AtPFA-DSP1) (Q9ZVN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses phosphotyrosine phosphatase activity in vitro. Hydrolyzes para-nitrophenyl phosphate in vitro. Hydrolyzes O-methylfluorescein phosphate in vitro. Hydrolyzes polyphosphate and ATP in vitro. Dephosphorylates the phosphoinositides PI(3,4,5)P3, PI(3,5)P2, but not PI(3)P, PI(3,4)P2 or PI(4,5)P2.
Interaction partners:
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- mRNA guanylyltransferase
- Photosystem I reaction center subunit IX
- Photosystem I subunit O
- ARM repeat superfamily protein
- acid phosphatase
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
Sequence:
MKLVEKTTTTEQDNGEDFCRTIIEVSEVNRNVFQAPGGEADPFRVVSGEELHLIPPLNFSMVDNGIFRSGFPDSANFSFLQTLGLRSIIYLCPEPYPESNLQFLKSNGIRLFQFGIEGNKEPFVNIPDHKIRMALKVLLDEKNHPVLIHCKRGKHRTGCLVGCLRKLQKWCLTSIFDEYQRFAAAKARVSDQRFMEIFDVSSFSHIPMSFSCSIR
Protein: Opine/polyamine ABC transporter, periplasmic substrate-binding protein (Q5LPZ5)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
- Opine/polyamine ABC transporter, permease protein
- Opine/polyamine ABC transporter, permease protein
- Polyamine ABC transporter, permease protein
- Polyamine ABC transporter, permease protein
- Opine/polyamine ABC transporter, ATP-binding protein
- Spermidine/putrescine import ATP-binding protein PotA
- Polyamine ABC trasnporter, periplasmic polyamine-binding protein
- Beta-lactamase, putative
- Acyl-CoA synthetase, putative
Sequence:
MQDKQFMKEMLTESAHAYKEGRMDRRTFLALCGASGIAMNAVLAGDAQAAADHVVMWNWGGQSVECHGSAIGEAFTAATGKGVKFDTSGPLEGKIKEMVDSGNVTADVADADLFNAVSLGPTGHLEPIDYSIVSKDKTLPGYALEHGVSVILYGYAFVYDTEAYGDNPPKDWKDFFDTANFPGTRSLYKWANGSLEAALMADGVAGDALYPLDMERALNKIKSIKDDSIYWGSGSEVHSMVVNGEVTMAMIWQNRGRNIENDTDGRFKLVNNQAMAMPGAYIVPKGNPAGREAVMQFIATAQEVPAQLMLLDCLGMTPSNPAAFGEIPEDQQPYAITSAMNIDKIVYNDPTWWGENGGDAVNAFLEAIS
Protein: Solute carrier family 25 member 43 (A2A3V2)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein FUBI
Sequence:
MATWRRDGRLTGSQRLLCAGLAGAFSLSLTAPLELATVLAQVGKVQSHSLGLWATGRRVWLSEGPRALWKGNGVACLRLFPCSMVQLAAYRKFVVLFMDDLGRISQWSSIVTGSLAGMVSTIVTYPTDLIKTRLMVQNVLEPSYRGLIHAFSTIYQQEGFLALYRGVSLTVLGAVPFSAGSLLVYMNLEKVWNGPRDRFSHLQNFANVCVAAAVSQTLSFPFDTVKRKMQAQSPYLPHYGGVDVHFSGAADCFRQIVKTQGVLGLWNGLTANLLKVVPYFGVMFSMFEFCKRIFLYQNGYTLSPLTYKLTPGVDQSLKPQELRELKKFFKRRKLHSKTPPW
Protein: Enhancer of split mgamma protein (E(spl)mgamma) (Split locus enhancer protein mB) (Q01070)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional repressor of genes that require a bHLH protein for their transcription. May serve as a transcriptional regulator of the Achaete-scute complex (AS-C) genes. Contributes to the neural-epidermal lineage decision during early neurogenesis. Part of the Notch signaling pathway, plays a role in neuroblasts proliferation in embryos and larvae. In the larval brain, together with other self-renewal transcriptional repressors such as klu and dpn, required for type II neuroblast self-renewal and for maintaining erm in an inactive state in intermediate neural progenitors (INP) derived from type II neuroblasts.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Enhancer of split mdelta protein
- Enhancer of split m7 protein
- Bearded
- Enhancer of split m4 protein
- Enhancer of split M2 protein
- Enhancer of split malpha protein
- Sphingosine-1-phosphate lyase
- BARBU
- Klumpfuss, isoform B
- Achaete-scute complex protein T4
Sequence:
MSSLQMSEMSKTYQYRKVMKPMLERKRRARINKCLDELKDLMVATLESEGEHVTRLEKADILELTVTHLQKMKQQRQHKRASGDESLTPAEGFRSGYIHAVNEVSRSLSQLPGMNVSLGTQLMTHLGQRLNQIQPAEKEVLPVTAPLSVHIANRDAYSVPISPISSYAGSPNSNTSSTSHSLLTTIDVTKMEDDSEDEENVWRPW
Protein: Major fimbrium subunit FimA type-1 (Fimbrillin) (Fimbrilin) (Major fimbrial subunit protein type I) (B2RH54)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Structural subunit of the major fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity.
Subcellular location: Fimbrium {ECO:0000269|PubMed:15165251, ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:17675496, ECO:0000269|PubMed:20530728, ECO:0000269|PubMed:9786913}. Cell outer membrane {ECO:0000269|PubMed:15165251}. Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein. {ECO:0000269|PubMed:15165251}.
Interaction partners:
Sequence:
MKKTKFFLLGLAALAMTACNKDNEAEPVTEGNATISVVLKTSNSNRAFGVGDDESKVAKLTVMVYNGEQQEAIKSAENATKVEDIKCSAGQRTLVVMANTGAMELVGKTLAEVKALTTELTAENQEAAGLIMTAEPKTIVLKAGKNYIGYSGTGEGNHIENDPLKIKRVHARMAFTEIKVQMSAAYDNIYTFVPEKIYGLIAKKQSNLFGATLVNADANYLTGSLTTFNGAYTPANYANVPWLSRNYVAPAADAPQGFYVLENDYSANGGTIHPTILCVYGKLQKNGADLAGADLAAAQAANWVDAEGKTYYPVLVNFNSNNYTYDSNYTPKNKIERNHKYDIKLTITGPGTNNPENPITESAHLNVQCTVAEWVLVGQNATW
Protein: Hemoglobin alpha, adult chain 2 (A0A8I6AWV0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLAAGSIHSPSYRLRKQSWCSLQMTKPTSRTAGGRLVAMVVNMARRPYRGEIRTLFFKDSRIQTGPGTQWAAPKCAFPWPQLISPSHRMFAAFPTTKTYFSHIDVSPGSAQVKAHGKKVADALAKAADHVEDLPGALSTLSDLHAHKLRVDPVNFKFLSHCLLVTLACHHPGDFTPAMHASLDKFLASVSTVLTSKYR