wanglab/gogpt-training-data huggingface dataset:
Protein: Ketoreductase nvfG (EC 1.-.-.-) (Novofumigatonin biosynthesis cluster protein G) (A0A2I1BT56)
Organism: Aspergillus novofumigatus (strain IBT 16806)
Function: Ketoreductase; 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.
Interaction partners:
- Ribosomal protein S19
- Plectin/eS10 N-terminal domain-containing protein
- 40S ribosomal protein S7
- 40S ribosomal protein S3
- 40S ribosomal protein S10a
- 40S ribosomal protein S25
- Small ribosomal subunit protein eS1
- 40S ribosomal protein S29
- 40S ribosomal protein S19
- 40S ribosomal protein S16
Sequence:
MTQGKHCVPQGSTILVTGANGYLASAITKLLLELGYKVRGTVRAPKPWLNHYFEERYGSGNFETVIITDFQDTDTWDQALEGISGIAHVAHDMAWSSDPNIAVRGPVKAILNILDIASKHDSVKRIVLTSTIGAAPCIDINGNPATTPVNDDDWNDFAVEAAWSDSTPEEQRVYINHCAAKVEGDRKALQWVQDNQPGFDVNIVMPGFSVGRILHASITGQSMREIVGLLQGKPTKMFEFVPPWFINTEDVARLHVIALLKPEVSSQRIFACASPFTWKEVVSILRELDPSNTLIPDAPDENRRPCHVIPATEAERLIQDFFGRNGFTSLRDSLASAVTKSA
Protein: Tafazzin family protein (A0A8I5ZU36)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side {ECO:0000256|ARBA:ARBA00004137}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00024323}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00024323}; Intermembrane side {ECO:0000256|ARBA:ARBA00024323}.
Interaction partners:
Sequence:
MPLHVKWPFPAVPRLTWTLASSVVMGLVGTYSCFWTKYMNHLTVYNKEVLYELIENRGPATPLITVSNHQSCMDDPHLWGILKLRHIWNLKLMRWTPAAADICFTKELHSHFFSLGKCVPVCRGDGVYQKGMDFILEKLNHGDWVHIFPEGIGRLIAECHLNPIILPLWHVGMNDVLPNSPPYFPRFGQKITVLIGKPFSTLPVLERLRAENKSAVEMRKALTDFIQEEFQRLKMQAEQLHNHFQPGR
Protein: Doublecortin domain-containing protein (Q381W3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIETPDASSGVYPQIHQIREMIREVSGVLESDLQVVREGWDKLRKARETIMKGFLGTNIDSPSVHSPRDRGTILPEDVELSTMEDGESMNDMCISEDSASDNSHGEVENVGRDDAAPSSELPKKTFMGNGSGGSDASIMGEVSEQQEDASHIPEETHFDVGKRSGKLQTVYASIPCVHVIEACTRPHVHKKGSRCLFEKGTFCVPQSLSKKTPTTQPSNRKKVSAVNCQSRRPRRAAQTRVDRMISPSGPSYSPCRTSPDQTFWINVWPCFGSFSVRSCVPSRIAVYGNFFYVEDVIERAAAATKCRPAPRVLYEPHGRPVCSVKQLLPEHHYLIYPGGALYRRENIPEALLRELIWSAKAKLMECGTPPGKAASS
Protein: phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC 3.1.3.95) (G5EBF2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSSTPSSVTTPLSAWWNNMSLSGIYPSISTSTPSSSSSWSSHFVFGGHHHHTNNNTANTPQSTVPPSALSSGYTEDITVAGSLLKDKINGLVDSLMGRESVHSGCGYGEDGRIAMMVDKVCLVDRLGCQENLVGTVHVTTTHIIFRAENGSKELWLATGLISSVEKGTLTAAGCMLVIRCKHFQVITLLISRDKSCQDLYETLQRAAKPVSVNVTELLAFENREPVEDVRGWRRLDWNSEMTRQGITKSQWTESNINEGYTICDTYPNKLWFPTAASTSVLLGSCKFRSRGRLPVLTYFHQQTEAALCRCAQPLTGFSARCVEDEKLMELVGKANTNSDNLFLVDTRPRVNAMVNKVQGKGFEDERNYSNMRFHFFDIENIHVMRASQARLLDAVTKCRDVTEYWKTLEASGWLKHVRSVVECSLFLAESISRGTSCVVHCSDGWDRTSQVVALCQLLLDPYYRTIHGFQVLIEKDWLGFGHKFDDRCGHVGALNDEAGKEVSPIFTQWLDCIWQIMQQKPRAFQFNERYLIEMHEHVYSCQFGTFIGNCDKDRRDLNLSKRTKSLWTWMDARHDDYMNPFYSPTAHVALLDLDTRAARFTVWTAMYNRFDNGLQPRERLEDLTMAAMEHVGVLESHVAQLRTRLAELKTQQNQQITSTNTPTNMVDSGMSSATDDLKNLSLSHPLDPLSSTLPILERATSQESGVMDSSLYYPDEALTKYSLKWQPLRGADRCSNPACRGEFSSTIERRIHCHLCGMIFCRRCLKVSADERERVCDKCKTD
Protein: Serine-peptidase 212 (EC 3.4.21.-) (Q7KSK1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein, isoform I
Sequence:
MGLELIVIVSLIALAGAQLVPENSCPDYFRYVNDAFQGVQGEITLPSLMRGRNRIDIRFSQRGEQDASAVGSLIPYPDENAVRQLTGSAKFRIAVRPNSSNGLPKLTRLSYNEQILCSASEYRPPNSFFNRFYELDISGSLASFPSSVFNPFTRDGLDVNVQTVFYPTSSRGNDIWRGFTQPWTTVSNRSPAVVTPAPTPTEIFWNQPVPSVPITFAPPVPTITSSPAPAPPPPPPLPTPPAVVTVPPATPPPQRFDPRSQISSVVCGREGSTTPFIVRGNEFPRGQYPWLSAVYHKEVRALAFKCRGSLISSSIVISAAHCVHRMTEDRVVVGLGRYDLDDYGEDGAEMRNVMRLLWHPDYNTRSYSDADIALITIERPVTFNDIIAPICMWTVEASRTVSTTGFIAGWGRDEDSSRTQYPRVVEAEIASPTVCASTWRGTMVTERSLCAGNRDGSGPCVGDSGGGLMVKQGDRWLLRGIVSAGERGPAGTCQLNQYVLYCDLSKHINWISENIR
Protein: Probable cardiolipin-specific deacylase 1, mitochondrial (EC 3.5.1.-) (O14249)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial cardiolipin-specific phospholipase which deacylates de novo synthesized cardiolipin (CL). Part of the remodeling process of cardiolipin, which involves deacylation-reacylation of premature cardiolipin.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P53264}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53264}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53264}; Matrix side {ECO:0000250|UniProtKB:P53264}.
Interaction partners:
- Multifunctional tryptophan biosynthesis protein
Sequence:
MSQVKVAVRSEEAANSYTQTFGMSWRQWRQACSEEYAKQCEREVLHTVDFIRENEKDPERLVEVVDSKIYDNDGLVHEVCVSDKATGKANKRSIVYMHGYGAGLGFYFRNMDGLTKGVTKDFNSYFVDWLGMGNSSRPPFDIKGQTASEKVEETERFFTESLETWRIGHGIEKMILVGHSMGGYLSAVYAMQYPERVEKLLLVSPVAIPENPFASNDDAEVYNSVASSAVHAVMDEPPLSNVTNEVLQTQEETTGLEPSRPSKPKNPLPRFITFLWEQNVTPFSLLRLSGPLGPKLMSFWSSRRFSTLPPETFRALHNYCYSIFRLKGSSEYALGNLLAPGAFARRCIMNRLRMLKCRTIFMYGDKDWMDDVAGLEATNRLKEMNIEAEHHIISNAGHHCYLDNPEDFNEIVLKEIRMSLRSFSSISE
Protein: PSP1 C-terminal domain-containing protein (Q57VG4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- ESAG8-associated protein, putative
Sequence:
MSGSADILDGFFVGPEISSQGGGGSALWGSEQHQQHPDLRRQRQQLSNALQPHTPDNSVDVATTTSICSSTPNNGDKDISGLPGSRGEVDYKEAGGVAVVNLGMNGGIDRTGGVNQNSSSDVSNGNNNVNYVRVGVEPSISPVPSGTASNEAFAPLGSRYIPDVGQRLPHQVLHHQQPNIPVQLGPASLPKVDRVNEAGVPSTPALPRGDGMLDQLLSRLGESKIMATLLLMQTMHSSPQGSPAVAILDRVVATLEESITNITQSRDLLSPPTTNGGVPFHGMPNDVLLDPLHAPPLQAQPQHQQFQPNGGDMPYFPGPSAPGRYNDRAIWFPPQMPGSNGDGGNLMETGCPTVTVGAMHQPHPSPSQKQQNQKNQRRHRQQPHAPAVQGQRPFDSGMLPSNQMAPYINGGGPAAGAAYNNSNAPLLDMGDDSLPAYDTSADSGAALVDGSRGNHTGSSNNGVGGGVLGQGGDEIIRGPPHRPSELQLPPGSEEVESFLAFVEFKRGRIRKYECRIDIFPGQYVIVDGDRGRDCGLVVQTVKCKPDGNAAVCCMDGCNVNSDKIKLEKGRVLGVATTEEIDYIHHTMQRAERIALETCRKVCDDMGIRINLLDCEYQFDMEKVSFYFNSEHSVDFRPLVRELYRTFRVRIWMENTNPRVKNSMPTGGSGGGRRGSIKNSNNNNGDDSDGIGDDVSVLSDVADAVKRHEGGNGASGPNGGGKRRGCQRGFQRQKQAKRSSS
Protein: Translocation protein sec63 (Q9HGN7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon. sec63 may affect sec61-polypeptide interactions by increasing the affinity of targeting pathways for sec61 and/or by modifying sec61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Translocation protein sec62
- Translocation protein sec66
- ER protein translocation subcomplex subunit sec67
- Protein transport protein sec61 subunit alpha
- Protein transport protein sec61 subunit beta
- Probable protein transport protein Sec61 subunit gamma
- Uncharacterized protein C19G7.17
- Endoplasmic reticulum chaperone BiP
- Pre-mRNA-splicing factor brr2
- Uncharacterized protein C589.03c
Sequence:
MSSEYKYDEQGIFFPVFLLVGTSCCVLPLTYSTILGPSASKEKKNVRDPFQKYRPKDLKVQRKSIFRLRYIFLILGWLAIGFLSYKIANSRLKLNIWDPYEILGIAKGTSVDDVRRHYKRLSIKFHPDKVRNMVNTTREEVEKHYIEITNAYRALTDDKTRENYALYGTPDVPQHISVGIALPKWISESENSIYILGFYGLVFGIVLPYAVGKWWYGSRTYTRDHVHVDTVDEWFPKMETSLTLDELLSLFASSKELTSLVPNEKNPKEYILKLLFDHLNRKKTNNFNTHQILSQSDVVLNALLSVATAFGFANPVDNVLKLWQHIVQAIPLDAPFPLLQLPHLLMEDVKNLSIRNISSIPQFLSLSEEQTKDYLPNYSKNQLKEMREIANGIPRISVVAAKVLVDDDEYITVGAIANLILDLKCSYGTEVVPEVSTDGTETATKKDEEDAEKYHQSKDVVLGDVETLPYAWAPYFTQHHKTAWWIYVVDPRQNRVIVPPFSITDIPKTLRTFRIPFQVPPVAGTFSFQLHIMSNSYVGEDVISNLTMIVKDTSVLQEQLQEEAVSDLEDNSDIDESANAGKDFSDDENIGSDEEDESEYDPMDTDTSDGE
Protein: Protein RESISTANCE TO PHYTOPHTHORA 1, chloroplastic (AtRPH1) (Q9ZU82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a positive role in the immune response to the oomycetes P.brassicae, including induced oxidative burst (e.g. H(2)O(2)) and enhanced expression of defense-related genes.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19170932}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein TOM THREE HOMOLOG 1
- Probable disease resistance protein At5g45510
Sequence:
MSWSLCSTHGVSSSIALTYGFRHRRRSTFRIFATSDGLEPKDDPPESPLPSSSSALGKDLKKVVNKTAATFAPRASTASKNPALPGTTLYKVFEVQGYASMFLGGVLSFNLLFPSSEPDLWRLMGMWSIWMFTIPSLRARDCPSKEKEALNYLFLIVPLLNVAIPFFWKSFALVWSADTVAFFAMYAWKLGWLERTE
Protein: Casein kinase 1-like protein 7 (EC 2.7.11.1) (Protein CASEIN KINASE I-LIKE 7) (Q9FFH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16126836}.
Interaction partners:
- At3g49990
- non-specific serine/threonine protein kinase
- Bystin
- Serine/threonine-protein kinase RIO2
Sequence:
MDLVIGGKFKLGKKIGSGSFGELYLGVNVQTGEEVAVKLENVKTKHPQLHYESKLYMLLQGGSGIPNIKWFGVEGDYSVMVIDLLGPSLEDLFNYCNRKLTLKTVLMLADQLLNRVEFMHTRGFLHRDIKPDNFLMGLGRKANQVYIIDFGLGKKYRDLQTHKHIPYRENKNLTGTARYASVNTHLGVEQSRRDDLESLGYVLMYFLKGSLPWQGLKAGTKKQKYDRISEKKVSTPIEVLCKNQPSEFVSYFHYCRSLRFDDKPDYSYLKRLFRDLFIREGYQFDYVFDWTVLKYPQIGSSSGSSSRTRHHTTAKPGFNADPIERQERILGKETTRYKIPGAVEAFSRRHPTTTSSPRDRSRSRNSDDGPFSKQTHGDSERANSSSRYRASSSRKAVAASSSRPSSAGGPSESRTSSRLVSSSGGGGSGSGNGRPSTSQRVQAGYESKTLSFSRATAARNTREDQLRSFELLSLRK
Protein: Mad1-A protein (Mitotic arrest deficient 1 like 1 L homeolog) (Q6GPD1)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2A
- HORMA domain-containing protein.
- Uncharacterized protein.
- WD_REPEATS_REGION domain-containing protein.
- Dual specificity protein kinase TTK
- Uncharacterized protein.
- Uncharacterized protein.
- HORMA domain-containing protein.
- Cell division cycle protein 20 homolog
- Cell division cycle protein 20 homolog
Sequence:
MDDSEDNTTVISTLRSFNKFLSQPLEGTAPSLGTSTSTGASLQMQFQQRFLLEDQAAQIRSKSNLIQVEREKMQMELSHKRARIELEKAASTNAKNYEREADRNQGLHTRIKALEEKENEFQNKLQEQNEMIKSYKKTIEAQSKKLLEKEDKLSESNENISVLKGKASELQWKIMNQEMQIKTQETEKQELTEQLEIHRKKLQESNEKMQALHELQAQNADNEQKIKSLEQKLSAQEQDAAIVKSMKSDLTKLPKLERELQQLRDENAYHREMKENNALLKEEVEGLRRAAERFNKMKEDLVGSEIEKEQLVKKLKLWENLEHTTGLNIRTPDDFSRQIMAVQQRELKLKEENMTIHNSARMLETSRQQLQEELLKVQSGFLEEKKRREHQEALVRRLQKRVLLLTKERDGMRAILDSYDSELTPTEHSPQLSRRLKEAEDILQKVQDHNAEMETQLSEALEDAGIQKQKSELLTAELKVLKSQMGSSDQTMSFTNEAMSALRLKIEELEAERGRLEEENKILEMRLESLNLQGCYDPSRTKVIHLSLNPASKAKQQRTDTVRHLQEECDKLREIVRILEGGAQIPDKLEATGSPQSSQELAELKKQVESAELKNQRLREVFQTKIHEFRTACYMLTGYRIDITTENQYRLTSMYGEHKEDNLLFKASGSSGGKMQLLETDFSLTLRDFIDLHLHHQNSIPAFLSAVTLDLFSRQTFA
Protein: Epithelial cell adhesion molecule (Tumor-associated calcium signal transducer 1) (C9JKY3)
Organism: Homo sapiens (Human)
Subcellular location: Lateral cell membrane {ECO:0000256|ARBA:ARBA00004591}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004591}.
Interaction partners:
Sequence:
MAPPQVLAFGLLLAAATATFAAAQEGEARIGAELWSWAGLGGSGPRPSAPETGIIGRGPRGRAFQRGDRTVRPCSGSGPPRGRKRRGPSRGAASLRSFARLECVCENYKLAVNCFVNNNRQCQCTSVGAQNTVICSKLAAKCLVMKAEMNGSKLGRRAKPEGALQNNDGLYDPDCDESGLFKAKQCNGTSMCWCVNTAG
Protein: Sulfur carrier protein ThiS adenylyltransferase (EC 2.7.7.73) (P30138)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS.
Interaction partners:
- Sulfur carrier protein ThiS
- Thiamine-phosphate synthase
- Thiazole synthase
- Phosphomethylpyrimidine synthase
- 2-iminoacetate synthase
- tRNA sulfurtransferase
- Molybdopterin synthase catalytic subunit
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
- Molybdopterin synthase sulfur carrier subunit
- Cysteine desulfurase IscS
Sequence:
MNDRDFMRYSRQILLDDIALDGQQKLLDSQVLIIGLGGLGTPAALYLAGAGVGTLVLADDDDVHLSNLQRQILFTTEDIDRPKSQVSQQRLTQLNPDIQLTALQQRLTGEALKDAVARADVVLDCTDNMATRQEINAACVALNTPLITASAVGFGGQLMVLTPPWEQGCYRCLWPDNQEPERNCRTAGVVGPVVGVMGTLQALEAIKLLSGIETPAGELRLFDGKSSQWRSLALRRASGCPVCGGSNADPV
Protein: ACD shelterin complex subunit and telomerase recruitment factor (R4GMR6)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQVDRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSNAGLSLSQLLDEMREDQEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSSMLCISENDQLILSSLGPCQRTQGPELPPPDPALQDLSLTLIASPPSSPSSSGPELPGEPRSPALSGNPQRGIVMVLPSSMSMSHPARPSVLGSKLSGFLPSSWPGPCTF
Protein: Brefeldin A resistance protein (P41820)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Confers hyper-resistance to brefeldin A (BFA), an inhibitor of intracellular protein transport. Could serve as an efflux pump of various antibiotics.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Caffeine resistance protein 5
- Transporter mfs1
- AP-1-like transcription factor
- Heme A synthase-mitochondrial ferredoxin fusion protein
- Uncharacterized transcriptional regulatory protein C530.05
- Putative uncharacterized oxidoreductase C513.07
- Threonine synthase
- Uncharacterized transporter C36.03c
- ATP synthase subunit alpha
Sequence:
MNQNSDTTHGQALGSTLNHTTEVTRISNSSDHFEDSSSNVDESLDSSNPSSNEKASHTNEEYRSKGNQSYVPSSSNEPSPESSSNSDSSSSDDSSVDRLAGDPFELGENFNLKHYLRAYKDSLQRDDIITRSSGVCMRDHSVYGVGSGYEFLKTFPDIFLQPYRAITEKQVVEKAILSHCHALANAGELVMVLGQPGSGCSTFLRSVTSDTVHYKRVEGTTHYDGIDKADMKKFFPGDLLYSGENDVHFPSLTTAETLDFAAKCRTPNNRPCNLTRQEYVSRERHLIATAFGLTHTFNTKVGNDFVRGVSGGERKRVTISEGFATRPTIACWDNSTRGLDSSTAFEFVNVLRTCANELKMTSFVTAYQASEKIYKLFDRICVLYAGRQIYYGPADKAKQYFLDMGFDCHPRETTPDFLTAISDPKARFPRKGFENRVPRTPDEFEQMWRNSSVYADLMAEMESYDKRWTETTPASSEAPEKDNFGSDISATTKHELYRQSAVAEKSKRVKDTSPYTVTFSQQLWYCLARSWERYINDPAYIGSMAFAFLFQSLIIGSIFYDMKLNTVDVFSRGGVLFFSILFCALQSLSEIANMFSQRPIIAKHRASALYHPAADVISSLIVDLPFRFINISVFSIVLYFLTNLKRTAGGFWTYFLFLFIGATCMSAFFRSLAGIMPNVESASALGGIGVLAIAIYTGYAIPNIDVGWWFRWIAYLDPLQFGFESLMINEFKARQFECSQLIPYGSGYDNYPVANKICPVTSAEPGTDYVDGSTYLYISFNYKTRQLWRNLAIIIGYYAFLVFVNIVASETLNFNDLKGEYLVFRRGHAPDAVKAAVNEGGKPLDLETGQDTQGGDVVKESPDNEEELNKEYEGIEKGHDIFSWRNLNYDIQIKGEHRRLLNGVQGFVVPGKLTALMGESGAGKTTLLNVLAQRVDTGVVTGDMLVNGRGLDSTFQRRTGYVQQQDVHIGESTVREALRFSAALRQPASVPLSEKYEYVESVIKLLEMESYAEAIIGTPGSGLNVEQRKRATIGVELAAKPALLLFLDEPTSGLDSQSAWSIVCFLRKLADAGQAILCTIHQPSAVLFDQFDRLLLLQKGGKTVYFGDIGEHSKTLLNYFESHGAVHCPDDGNPAEYILDVIGAGATATTNRDWHEVWNNSEERKAISAELDKINASFSNSEDKKTLSKEDRSTYAMPLWFQVKMVMTRNFQSYWREPSILMSKLALDIFAGLFIGFTFYNQGLGVQNIQNKLFAVFMATVLAVPLINGLQPKFIELRNVFEVREKPSNIYSWVAFVFSAIIVEIPFNLVFGTLFFLCWFYPIKFYKHIHHPGDKTGYAWLLYMFFQMYFSTFGQAVASACPNAQTASVVNSLLFTFVITFNGVLQPNSNLVGFWHWMHSLTPFTYLIEGLLSDLVHGLPVECKSHEMLTINPPSGQTCGEYMSAFLTNNTAAGNLLNPNATTSCSYCPYQTADQFLERFSMRYTHRWRNLGIFVGYVFFNIFAVLLLFYVFRVMKLRSTWLGKKITGTG
Protein: Nucleophosmin (Q5BL09)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MEDSMDMNMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDEEDVKLLGMSGKRSAPGGGNKVPQKKVKLDEDDEDDDEDDEDDEDDDDDDFDEEETEEKVPVKKSVRDTPAKNAQKSNQNGKDLKPSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKAH
Protein: Tail sheath protein (TSP) (B6V2P4)
Organism: Bacillus phage SP01 (Bacteriophage SP01)
Function: Polymerizes as an extended structure around the baseplate-tail tube complex. During ejection, the sheath shifts to a contracted form, thereby making the inner tail tube protrude through the host cell envelope.
Subcellular location: Virion {ECO:0000250|UniProtKB:P79678}. Host cytoplasm {ECO:0000250|UniProtKB:P79678}. Note=Tail. {ECO:0000250|UniProtKB:P79678}.
Interaction partners:
Sequence:
MAINQYGVNFNGRRIVHPGAYGSIDDSAMVVTSDGSSNIPIVIGTADSGKSGEVLWYTGVEDARNELGGGDLPQALEMMFSPSPEGGGGASLVGVIVANKTVPATATIGGVKFTAAEYGEGGNKIQVKLEDGSIPGSKKFTAYKWDTQDLDTFDNIGSVMSVAYTGTAKVAVIDVVVTDGVATKIETKVGEDAENLTVDLQLDLTNERYSTIEAVAQYLNSVSDYSASYVTSMSLELESSKLDAITGQDIKTKSYLTALKGDLEFRISQYADLVDVEVTGEIVNFDNTYLSGGEKGTTPASWSDYLDLIKKQYSDILVVLTDSEAIHAEALAHVQQMENRKQRQMLFVGGGKGEAPERAIERASLLNSSRAVLAYPGIYHSSYYSGSRELPAYFTAAMIAGRVAGVSQSTPVTFNKFNLVSLGRDMLAGDPEIDQLITSGVCTLEKVKNGAIRLVQGITTYIGSNNTLLREISVRRTADLVATSVEQTLEDTFVGKKGVSTTVSSVETVVSDTLAEKVRTEDIIGYGDIKVTFKNTMIYVDYEVAVVEPMNYILVRSHFVPDTGQFTTEEV
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (A0A4D6K823)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein pangolin, isoform J
- Mitogen-activated protein kinase kinase kinase 7
- FI16976p1
- Armadillo segment polarity protein
- Forkhead box protein O
- Putative mitogen-activated protein kinase kinase kinase 7-like
- Protein prickle
- Axin
Sequence:
MSVSMSLVQGGAAGGAPQGASAILAAAAPYYQPPAVPQDVQPDRPIGYGAFGVVWAVTDPRDGRRVALKKLPNVFQSLVSSKRVFRELKMLCFFKHENVLSALDILQPPHLDFFQEIYVITELLQSDLHKIIVSPQHLSADHIKVFLYQILRGLKYLHSARILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDQAKHMTQEVVTQYYRAPEILMGARHYSSAVDVWSVGCIFGELLGRRILFQAQNPVQQLELITELLGTPTMEDMRHACEGARTHMLRRAPKPPSFSVLYTLSSHATHEAVHLLCQMLVFDPDKRISVTDALAHPYLDEGRLRYHSCMCKCCFTTSAGMRQYTADFEPSAGQPFDDLWERKLTSVQQVKEEMHKFIAEQLQTGRVPLCINPQSAAFKSFASSTVAHPSELPPSPHQWEXRQNEAIAA
Protein: SH3 and multiple ankyrin repeat domains protein 2 (Shank2) (Cortactin-binding protein 1) (CortBP1) (Proline-rich synapse-associated protein 1) (Q9UPX8)
Organism: Homo sapiens (Human)
Function: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. May play a role in the structural and functional organization of the dendritic spine and synaptic junction.
Subcellular location: Apical cell membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Postsynaptic density {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with cortactin in growth cones in differentiating hippocampal neurons. Colocalized with PDE4D to the apical membrane of colonic crypt cells (By similarity). {ECO:0000250}.
Interaction partners:
- Disks large homolog 4
- Disks large-associated protein 1
- SH3 and multiple ankyrin repeat domains protein 3
- Src substrate cortactin
- Disks large-associated protein 2
- SH3 and multiple ankyrin repeat domains protein 1
- Neuroligin-4, X-linked
- Neuroligin-3
- Homer protein homolog 1
- Disks large-associated protein 3
Sequence:
MPRSPTSSEDEMAQSFSDYSVGSESDSSKEETIYDTIRATAEKPGGARTEESQGNTLVIRVVIHDLQQTKCIRFNPDATVWVAKQRILCTLTQSLKDVLNYGLFQPASNGRDGKFLDEERLLREYPQPVGEGVPSLEFRYKKRVYKQASLDEKQLAKLHTKTNLKKCMDHIQHRLVEKITKMLDRGLDPNFHDPETGETPLTLAAQLDDSVEVIKALKNGGAHLDFRAKDGMTALHKAARARNQVALKTLLELGASPDYKDSYGLTPLYHTAIVGGDPYCCELLLHEHATVCCKDENGWHEIHQACRYGHVQHLEHLLFYGADMSAQNASGNTALHICALYNQDSCARVLLFRGGNKELKNYNSQTPFQVAIIAGNFELAEYIKNHKETDIVPFREAPAYSNRRRRPPNTLAAPRVLLRSNSDNNLNASAPDWAVCSTATSHRSLSPQLLQQMPSKPEGAAKTIGSYVPGPRSRSPSLNRLGGAGEDGKRPQPLWHVGSPFALGANKDSLSAFEYPGPKRKLYSAVPGRLFVAVKPYQPQVDGEIPLHRGDRVKVLSIGEGGFWEGSARGHIGWFPAECVEEVQCKPRDSQAETRADRSKKLFRHYTVGSYDSFDTSSDCIIEEKTVVLQKKDNEGFGFVLRGAKADTPIEEFTPTPAFPALQYLESVDEGGVAWQAGLRTGDFLIEVNNENVVKVGHRQVVNMIRQGGNHLVLKVVTVTRNLDPDDTARKKAPPPPKRAPTTALTLRSKSMTSELEELVDKASVRKKKDKPEEIVPASKPSRAAENMAVEPRVATIKQRPSSRCFPAGSDMNSVYERQGIAVMTPTVPGSPKAPFLGIPRGTMRRQKSIDSRIFLSGITEEERQFLAPPMLKFTRSLSMPDTSEDIPPPPQSVPPSPPPPSPTTYNCPKSPTPRVYGTIKPAFNQNSAAKVSPATRSDTVATMMREKGMYFRRELDRYSLDSEDLYSRNAGPQANFRNKRGQMPENPYSEVGKIASKAVYVPAKPARRKGMLVKQSNVEDSPEKTCSIPIPTIIVKEPSTSSSGKSSQGSSMEIDPQAPEPPSQLRPDESLTVSSPFAAAIAGAVRDREKRLEARRNSPAFLSTDLGDEDVGLGPPAPRTRPSMFPEEGDFADEDSAEQLSSPMPSATPREPENHFVGGAEASAPGEAGRPLNSTSKAQGPESSPAVPSASSGTAGPGNYVHPLTGRLLDPSSPLALALSARDRAMKESQQGPKGEAPKADLNKPLYIDTKMRPSLDAGFPTVTRQNTRGPLRRQETENKYETDLGRDRKGDDKKNMLIDIMDTSQQKSAGLLMVHTVDATKLDNALQEEDEKAEVEMKPDSSPSEVPEGVSETEGALQISAAPEPTTVPGRTIVAVGSMEEAVILPFRIPPPPLASVDLDEDFIFTEPLPPPLEFANSFDIPDDRAASVPALSDLVKQKKSDTPQSPSLNSSQPTNSADSKKPASLSNCLPASFLPPPESFDAVADSGIEEVDSRSSSDHHLETTSTISTVSSISTLSSEGGENVDTCTVYADGQAFMVDKPPVPPKPKMKPIIHKSNALYQDALVEEDVDSFVIPPPAPPPPPGSAQPGMAKVLQPRTSKLWGDVTEIKSPILSGPKANVISELNSILQQMNREKLAKPGEGLDSPMGAKSASLAPRSPEIMSTISGTRSTTVTFTVRPGTSQPITLQSRPPDYESRTSGTRRAPSPVVSPTEMNKETLPAPLSAATASPSPALSDVFSLPSQPPSGDLFGLNPAGRSRSPSPSILQQPISNKPFTTKPVHLWTKPDVADWLESLNLGEHKEAFMDNEIDGSHLPNLQKEDLIDLGVTRVGHRMNIERALKQLLDR