wanglab/gogpt-training-data huggingface dataset:
Protein: CbrB (G3XCK7)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MAHILIVEDETIIRSALRRLLERNQYQVSEAGSVQEAQERYTIPSFDMVVSDLRLPGAPGTELIKLAEGIPVLIMTSYASLRSAVDSMKMGAVDYIAKPFDHDEMLQAVARILKDRQENRSAAPVSANGGKAGGERGASPAVADGEIGIIGSCAPMQELYSKIRKVAPTDSTVLIQGESGTGKELVARALHNLSKRAKAPLISVNCAAIPETLIESELFGHEKGAFTGASAGRAGLVEAADGGTLFLDEIGELPLEAQARLLRVLQEGEIRRVGSVQSQKVDVRLIAATHRDLKTLAKTGQFREDLYYRLHVISLKLPALRERGNDVMEIARAFLARQCTRMGRAPLSFAHDAEQAIRHYPWPGNVRELENAIERAVILSESQEIHADLLGIDIELDDLEDDFAADLGLGPAGAAASNHEPTEDLSLEDYFQHFVLEHQDHMTETELARKLGISRKCLWERRQRLGIPRRKSGASADS
Protein: Runt-related transcription factor (Q9DEA0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009374}.
Interaction partners:
Sequence:
MHIPVDPSTSRRFTPPSASFPCAKVTESQSMSAPGPLRSGRPVESRSVVDVLADHAGELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGDVPDGTLVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVFTGPPQVATYHRAIKVTVDGPREPRRHRVKPDDPHKQFSDRLSDIERFQRASLRMNPGNGTTRPHQTHYSPSSTTQIPGLWPDQIDPPTLKTCKVEDDLRWTSTDLFQQRTSFPSLSPLTAPRFSDSHMHYPSHFTYSANPSSTGIGGLSVAGMPTSSRYHTYLPPPYPGNQNQNSHFQTNSSPYHLYYGTGSGSYQFSMIPTGGSGSGGDRSPTRMLTSCTAAGGAAGNTGNNNLINANLGNQSDGVDADGSHSNSPTAMSASTRIDESVWRPY
Protein: Opsin (Q401Q0)
Organism: Pieris rapae (Small white butterfly) (Artogeia rapae)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MFDTVNATADGGAIAYAFKMVSSEVQENMLGFNIPPEHQDLVHEHWRNFPAVDKFWHYMLALIYTMLMVSSLCGNGIVVWIFSTSKSLRSASNMFIVNLALFDLVMMIEMPHLIMNSFFQKMLGYQLGCDIYATLGSVSGIGAAITNAVIAYDRYKTISCPIDGRINKVQAIILIVFTWFWTLPFTILPLTRVWGKFVPEGFLTTCSFDSFTDDSDTRVFVACIFVWSYVIPMVLICFFYSKLFSAVRLHEKMLREQAKKMNVKSLASNKDDAGKSVEIRIAKVAFTIFFLFVCAWTPYAVVTMIGTFGDRNLLTPHVTMIPAVFAKSVSCIDPWVYAINHPRYRAELEKRLPWMGIREPSAETQSTNASTATQSASADA
Protein: Sulfite reductase (Q9I2Q7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Bifunctional enzyme CysN/CysC
- Adenosine 5'-phosphosulfate reductase
- DUF934 domain-containing protein
- Sulfate adenylyltransferase subunit 2
- Probable oxidoreductase
- Sulfate transport system permease protein CysW
- Sulfate-binding protein
- Sulfate/thiosulfate import ATP-binding protein CysA
- Cysteine synthase
- Probable 3-mercaptopyruvate sulfurtransferase
Sequence:
MYVYDEYDQRIVEDRVKQFRDQTRRYLAGELTGEEFRPLRLQNGLYIQRYAPMLRIAVPYGLLSSRQLRKLAQIARDYDKGYAHISTRQNVQFNWPELEDVPEILAELATVQMHAIQTSGNCIRNTTTDQFAGVARDELVDPRPWCEIIRQWSTFHPEFAHLPRKFKIAVNGAVSDRAAIEVHDIGLEAVKNEAGELGFRVSVGGGLGRTPIVGSFINEFLPWQHLLGYLDAILRVYNRYGRRDNKYKARIKILVKALTPEVFAERVEAEWANLKDGPSTLTEAEVQRVAAHFVDPAYKALDDLDESLARLDAEHPGFARWRARNTFAHKKPGYVAVTLSLKPTGTAPGDVTDKQLEAIADLADRYSFGEVRNSHNQNIILADVEQGELFALWGELRELGFATPNVGLLTDIICCPGGDFCSLANAKSIPIAEAIQRRFDNLDYLFDIGDIDLNISGCMNACGHHHVGHIGILGVDKKGAEFYQVSLGGSSARDASLGQILGPSFAQEQMADVIDKIIQVYVERRTEEEPFIDTFRRIGIDPFKERVYAANH
Protein: N-acetylglucosamine-6-sulfatase (EC 3.1.6.14) (Glucosamine-6-sulfatase) (Q5M918)
Organism: Rattus norvegicus (Rat)
Subcellular location: Lysosome {ECO:0000256|PIRNR:PIRNR036666}.
Interaction partners:
Sequence:
MRLPSAAGPGPGCPSRLPALLLLPLLSGCLGLVGAARRPNVLLLLTDDQDAELGGMTPLKKTKALIGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPYTFPAILKLVCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTLSINGKARRHGENYSVDYLTDVLANLSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFPNVIAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIKFLDDAFRRRWQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQMDGTSLLPILKGDGNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTLSSMWNLQYCEFDDQEVFVEVYNITADPDQITNIAKSIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPG
Protein: Uncharacterized protein (Q387K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSKSIDSMMEKAVTTSPKFFSDMNAVEGVKQRKKAIRKERKESASTLTQWYGMKKSKLGAEERQELELLKYRNLINPELKHKTPKNNTGTSGFVEFGYFAGTGRNKRRRLKSFADEWMEENPEVQQIVQRRLKQNVRLNRKAKERMAKKAARDAEREKEKKSSKRLKKRDMML
Protein: DMOA farnesyltransferase nvfB (EC 2.5.1.-) (Novofumigatonin biosynthesis cluster protein B) (A0A2I1BT09)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: DMOA farnesyltransferase; 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:
- Flavin prenyltransferase PAD1, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Farnesyl-pyrophosphate synthetase
- isopentenyl-diphosphate Delta-isomerase
- Phosphatidate cytidylyltransferase
Sequence:
MGGKAQNGEDEARGKVLSSLPPSLVPYAELMRVHRPLGYYLNTSPYVVGVVFGAAVAPTKLPATILLDRLLILVLWSLFLRSAGCVWNDVIDMDLDRQIARTRLRPLPRGAVSSWNAVMLTAGIFACGGSLLSFLPRECAIEALIEIFFALLYPFGKRFTDFPQLILVNIGWAIPMSMHSLGLDPLAYKKPTFFMFLFIALVIVMIDVVYSRQDTEEDMKVGVKSMAVRFKHSIELLSYAFFYASTGALLAAGYYSGLGIPFTVLSVGGHFGGFLYFLKTTGVGKAPQVESYAKLACLIASLFWVVGLFVEYYLRV
Protein: Proteasome subunit alpha type-7 (Proteasome subunit RC6-1) (Proteasome subunit alpha-4) (alpha-4) (Q9Z2U0)
Organism: Mus musculus (Mouse)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14818}. Nucleus {ECO:0000250|UniProtKB:O14818}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:O14818}.
Interaction partners:
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-4
- Proteasome subunit beta type-6
- Proteasome subunit beta type-8
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-6
- Proteasome subunit beta type-9
- Proteasome subunit beta type-2
Sequence:
MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDDAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQPLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS
Protein: Acetate transporter protein patA (Patulin biosynthesis cluster protein A) (A0A075TRL0)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: Acetate transporter protein; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. May be involved in the uptake of acetate, a substrate for the synthesis of 6-methylsalicylic acid by the polyketide synthase patK (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Multi-pass membrane protein {ECO:0000269|PubMed:30680886}.
Interaction partners:
Sequence:
MKLSAEGTVMASSEEAAQLSCDTSSSHARNSKEQDFQPTQQIGSPTALGMGAFAIAFTTLSMSLMEWRSAAITNAYIGNCFFTAGMGLVLVAQWELVRGNSFGHTVFGGFGLFNLAFGAINAPAFGVADAFKDDPAALNNAIGYFLLVWGIFVLFFTVAAMPMNLVYTGMLGTSQITYTLLAASYFSFADDHASAGLALKKAAGAFGFVSGLFAWYTVGHLMCQDALLFSFPLGDTSPLYARLQRKKRH
Protein: Protease HtpX (EC 3.4.24.-) (Heat shock protein HtpX) (P23894)
Organism: Escherichia coli (strain K12)
Function: Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12081643}; Multi-pass membrane protein {ECO:0000269|PubMed:12081643}. Note=Bioinformatics programs predict 4 transmembrane helices, however PhoA and Bla fusions as well as other experiments only confirm the first 2. {ECO:0000269|PubMed:12081643}.
Interaction partners:
- ATP-dependent zinc metalloprotease FtsH
- Modulator of FtsH protease YccA
- Protein GrpE
- Chaperone protein ClpB
- Murein DD-endopeptidase MepM
- Inner membrane protein YebE
- Chaperone protein DnaK
- Chaperone protein HtpG
- ATP-dependent protease ATPase subunit HslU
- Periplasmic chaperone Spy
Sequence:
MMRIALFLLTNLAVMVVFGLVLSLTGIQSSSVQGLMIMALLFGFGGSFVSLLMSKWMALRSVGGEVIEQPRNERERWLVNTVATQARQAGIAMPQVAIYHAPDINAFATGARRDASLVAVSTGLLQNMSPDEAEAVIAHEISHIANGDMVTMTLIQGVVNTFVIFISRILAQLAAGFMGGNRDEGEESNGNPLIYFAVATVLELVFGILASIITMWFSRHREFHADAGSAKLVGREKMIAALQRLKTSYEPQEATSMMALCINGKSKSLSELFMTHPPLDKRIEALRTGEYLK
Protein: ABC transporter domain-containing protein C20G4.01 (Q7Z991)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- General negative regulator of transcription subunit 3
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- General negative regulator of transcription subunit 1
- General negative regulator of transcription subunit 2
- Cell differentiation protein rcd1
- Mitochondrial division protein 1
- Putative general negative regulator of transcription C16C9.04c
- Poly
- Uncharacterized protein C16C4.16c
- Uncharacterized mitochondrial carrier C1604.04
Sequence:
MEVTVSNLSYTFSPKQPLSLDHVTLDLPKGSRTLLVGANGAGKSTLLKLLSGKSLAKAGHISVGGKDPFRESSSAFVYLGTEWVNNPVIHRDMSVARLIASVGGDKFAERRDFLISILDIDLRWRMHAVSDGERRRVQLCMGLLRPFEVLLLDEVTVDLDVLARADLLNFLQEETEVRNATIVYATHIFDGLAEWPTHLVHLSLGRIVDYGPISKFGALMTRSSTGNSALLETCLEWLKEDKKNRGTREEEKRSTWDDVQESLKVGTDVFTDYFKISRAK
Protein: Cas scaffolding protein family member 4 (HEF-like protein) (HEF1-EFS-p130Cas-like protein) (HEPL) (Q9NQ75)
Organism: Homo sapiens (Human)
Function: Docking protein that plays a role in tyrosine kinase-based signaling related to cell adhesion and cell spreading. Regulates PTK2/FAK1 activity, focal adhesion integrity, and cell spreading.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18256281}. Cell junction, focal adhesion {ECO:0000269|PubMed:18256281}.
Interaction partners:
- Thioredoxin domain-containing protein 3
- Zinc finger CW-type PWWP domain protein 1
- Fermitin family homolog 2
- Protein-tyrosine kinase 2-beta
- Sortilin-related receptor
- CD2-associated protein
- Ras and Rab interactor 3
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
- Sodium/potassium/calcium exchanger 4
- Phosphatidylinositol-binding clathrin assembly protein
Sequence:
MKGTGIMDCAPKALLARALYDNCPDCSDELAFSRGDILTILEQHVPESEGWWKCLLHGRQGLAPANRLQILTEVAADRPCPPFLRGLEEAPASSEETYQVPTLPRPPTPGPVYEQMRSWAEGPQPPTAQVYEFPDPPTSARIICEKTLSFPKQAILTLPRPVRASLPTLPSQVYDVPTQHRGPVVLKEPEKQQLYDIPASPKKAGLHPPDSQASGQGVPLISVTTLRRGGYSTLPNPQKSEWIYDTPVSPGKASVRNTPLTSFAEESRPHALPSSSSTFYNPPSGRSRSLTPQLNNNVPMQKKLSLPEIPSYGFLVPRGTFPLDEDVSYKVPSSFLIPRVEQQNTKPNIYDIPKATSSVSQAGKELEKAKEVSENSAGHNSSWFSRRTTSPSPEPDRLSGSSSDSRASIVSSCSTTSTDDSSSSSSEESAKELSLDLDVAKETVMALQHKVVSSVAGLMLFVSRKWRFRDYLEANIDAIHRSTDHIEESVREFLDFARGVHGTACNLTDSNLQNRIRDQMQTISNSYRILLETKESLDNRNWPLEVLVTDSVQNSPDDLERFVMVARMLPEDIKRFASIVIANGRLLFKRNCEKEETVQLTPNAEFKCEKYIQPPQRETESHQKSTPSTKQREDEHSSELLKKNRANICGQNPGPLIPQPSSQQTPERKPRLSEHCRLYFGALFKAISAFHGSLSSSQPAEIITQSKLVIMVGQKLVDTLCMETQERDVRNEILRGSSHLCSLLKDVALATKNAVLTYPSPAALGHLQAEAEKLEQHTRQFRGTLG
Protein: Aquaporin PIP2-4 (Plasma membrane intrinsic protein 2-4) (ZmPIP2-4) (ZmPIP2;4) (Q9ATM6)
Organism: Zea mays (Maize)
Function: Water channel required to facilitate the transport of water across cell membrane. Active as homomers. Increased activity when heteromerization with PIP1-2.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAKDIEASGPEAGEFSAKDYTDPPPAPLIDAEELTQWSLYRAVIAEFIATLLFLYITVATVIGYKHQTDASASGPDAACGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLVRALLYIIAQCLGAICGVGLVKGFQSAYYVRYGGGANELSDGYSKGTGLAAEIIGTFVLVYTVFSATDPKRSARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSLGAAVIYNKDKAWDDQWIFWVGPLIGAAIAAAYHQYVLRASATKLGSYRSNA
Protein: Aquaglyceroporin (Tonoplast intrinsic protein (Tipa)) (Aquaporin TIP4-1-like) (Aquaporin TIP4-1t) (Q9XG70)
Organism: Nicotiana tabacum (Common tobacco)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAKIAVGSSREAIQPDCIQALIVEFICTFLFVFAGVGSAMAANKLNGDPLVSLFFVAMAHALVVAVTISAGFRISGGHLNPAVTLGLCMGGHITVFRSILYWIDQLLASVAACALLNYLTAGLETPVHTLANGVSYGQGIIMEVILTFSLLFTVYTTIVDPKKGILEGMGPLLTGLVVGANIMAGGPFSGASMNPARSFGPAFVSGIWTDHWVYWVGPLIGGGLAGFICENFFIVRTHVPLPSDESF
Protein: Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 (EC 2.4.99.-) (GalNAc alpha-2,6-sialyltransferase VI) (ST6GalNAc VI) (ST6GalNAcVI) (Sialyltransferase 7F) (SIAT7-F) (Q9JM95)
Organism: Mus musculus (Mouse)
Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside). Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Alpha-2,8-sialyltransferase 8E
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
Sequence:
MACSRPPSQCDPTTLPPGPPAGRWPLPFSRRRREMSSNKEQRSAVFVILFALITILILYSSNSANEVFHYGSLRGRTRRPVNLKKWSFSSAYFPILGNKTLPSRCNQCVIITSSSHLLGTKLGPEIERAECTIRMNDAPTSGYSADVGNKTTFRVVAHSSVFRVLRKPQEFVNRTPETVFIFWGPPNKMQKPQGSLLRVIQRAGLMFPNMEAYAVSPARMQQFDDLFRGETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPDYCSQRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWAQLYGITFSHPSWT
Protein: Tetratricopeptide repeat protein 29 (TPR repeat protein 29) (Protein TBPP2A) (Testis development protein NYD-SP14) (Q8NA56)
Organism: Homo sapiens (Human)
Function: Axonemal protein which is implicated in axonemal and/or peri-axonemal structures assembly and regulates flagella assembly and beating and therefore sperm motility.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:31735292, ECO:0000269|PubMed:31735294, ECO:0000269|PubMed:37934199}.
Interaction partners:
- Cilia- and flagella-associated protein 43
- A-kinase anchor protein 14
- Cilia- and flagella-associated protein HOATZ
- Dynein axonemal heavy chain 1
- Coiled-coil domain-containing protein 40
- Tetratricopeptide repeat protein 21A
- Cilia- and flagella-associated protein 91
- Cilia- and flagella-associated protein 47
Sequence:
MTTLPPLPMTRPKLTALARQKLPCSSRKIPRSQLIKEKDDIDHYLEVNFKGLSKEEVAAYRNSYKKNICVDMLRDGYHKSFTELFALMERWDALREAARVRSLFWLQKPLEEQPDKLDYLYHYLTRAEDAERKESFEDVHNNLYALACYFNNSEDKWVRNHFYERCFKIAQLIKIDCGKKEAEAHMHMGLLYEEDGQLLEAAEHYEAFHQLTQGRIWKDETGRSLNLLACESLLRTYRLLSDKMLENKEYKQAIKILIKASEIAKEGSDKKMEAEASYYLGLAHLAAEEYETALTVLDTYCKISTDLDDDLSLGRGYEAIAKVLQSQGEMTEAIKYLKKFVKIARNNFQSLDLVRASTMLGDIYNEKGYYNKASECFQQAFDTTVELMSMPLMDETKVHYGIAKAHQMMLTVNNYIESADLTSLNYLLSWKESRGNIEPDPVTEEFRGSTVEAVSQNSERLEELSRFPGDQKNET
Protein: Protein transport protein Sec31A (SEC31-like protein 1) (SEC31-related protein A) (D6RHZ5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}.
Interaction partners:
Sequence:
MKLKEVDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPYKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQNDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVIQMWDLRFASSPLRVLENHARGILAIAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASFDGRISVYSIMGGSTDGLRQKQVDKLSSSFGNLDPFGTGQPLPPLQIPQQTAQHSIVLPLKKPPKWIRRPVGASFSFGGKLVTFENVRMPSHQGAEQQQQQHHVFISQVVTEKEFLSRSDQLQQAVQSQGFINYCQKKIDASQTEFEKNVWSFLKVNFEDDSRGKYLELLGYRKEDLGKKIALALNKVDGANVALKDSDQVAQSDGEESPAAEEQLLGEHIKEEKEESEFLPSSGGTFNISVSGDIDGLITQALLTGNFESAVDLCLHDNRMADAIILAIAGGQELLARTQKKYFAKSQSKITRLITAVVMKNWKEIVESCDLKNWREALAAVLTYAKPDEFSALCDLLGTRLENEGDSLLQTQACLCYICAGNVEKLVACWTKAQDGSHPLSLQDLIEKVVILRKAVQLTQAMDTSTVGVLLAAKMSQYANLLAAQGSIAAALAFLPDNTNQPNIMQLRDRLCRAQGEPVAGHESPKIPYEKQQLPKGRPGPVAGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQRK
Protein: alpha-amylase (EC 3.2.1.1) (Q8N0Q5)
Organism: Drosophila kikkawai (Fruit fly)
Interaction partners:
Sequence:
MFLTKSIVCLAILALASAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAADGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIAEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGRLKNLNTDHGFSSGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKDQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFNSDNSCSGGWVCEHRWRQIYNMVAFRNAVGSDAIQNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGTKNGSSCTGKTVTVGSDGRASIYLGNSEDDGVLAIHVNAKL
Protein: Even-skipped homeobox 1 (Homeobox even-skipped homolog protein 1) (A0A0R4IVI8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Potassium channel, subfamily K, member 5b
Sequence:
MDSAKEIMMRAEGSQVGTLSAKTGSNLTEAPGDPLRKLPDKPITQNRLSPLPYSQSSVDDATKGHRSAKYGDVTLSSKPSLPDIDLSDIPNKDASSSDAESDLYEEIDVSCTPESMDYPNGQGLAMGSPKHGKEVGVDKIGSVPGSLNYGSDQMRRYRTAFTREQIARLEKEFYRENYVSRPRRCELAAALNLPETTIKVWFQNRRMKDKRQRLAMTWPHPADPAFYTYMMSHAAATGSLPYPFQSHLPLPYYSPLSSVTAGSATATAGPFSNPLRSLDSFRVLSHPYPRPELLCAFRHPSLYPSPGHGLGPGGSPCSCLACHASSQTNGLQHRSNNAEFSCSPTTRTEAFLTFSPAVISKSSSVSLDQREEVPLTR
Protein: cAMP-dependent protein kinase catalytic subunit beta (PKA C-beta) (EC 2.7.11.11) (P22694)
Organism: Homo sapiens (Human)
Function: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:P05131}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. {ECO:0000250|UniProtKB:P05131}.
Interaction partners:
- cAMP-dependent protein kinase type II-beta regulatory subunit
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- A-kinase anchor protein 1, mitochondrial
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- Ezrin
- A-kinase anchor protein 5
- cAMP-dependent protein kinase type I-beta regulatory subunit
- Cyclic AMP-responsive element-binding protein 1
- Ryanodine receptor 2
- A-kinase anchor protein 9
Sequence:
MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPTQNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCAKEFGEF
Protein: Stress-induced protein sti1, putative (Q57ZX0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Chaperone protein DNAJ, putative
- Chaperone protein DnaJ, putative
- ATP-dependent Clp protease subunit, heat shock protein 100
- Telomerase-associated protein, putative
- Heat shock protein 70
Sequence:
MDATELKNKGNQEFSSGRYREAAEFFSQAINLDPSNHVLYSNRSACFASLHQYAQALSDAEKCVSLKPDWVKGYVRHGAALHGLRRYDEAAAVYKKGLTVDPSSTACSEGIASVEKDKAASAMQNPFAKLFTPEAVKKIQSHRKLSLFMMQPDYVRMIDEVIKDPSNIQRYLEDQRFMMTCLVLSGMNIPVDDDDEEEERPKPEAPKKNEEPKKAAAVELSAEAKEALRAKEEGNALYKQRKFDEALAKYDEASSLDPTNTVYLLNITAVFYEKGEYELCMEKCENALEHGRENKCDYTVIAKLMTRQALCLQKLKRFDEAIALFKKALVEHRNPDTLAKLNACEKEKAKFEADAYIDPAIAQEKKDEGNSLFKQDKFPEAVAAYTESIKRNPMEHTTYSNRAAAYLKLGAYNEALADAEKCIEIKPDFVKAHARRGHAFFWTKQYNKAMQAYDEGLKYDKENAECKDGRMRTMMKIQEMASGQSEDGDEVAKRAMADPEVAAIMQDSYMQLVLNEMQRDPTRIKDYMRDPTLAKKINTLVSAGIIRFGQ