wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent chromatin assembly factor large subunit (Q9Y0W1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00475}.
Interaction partners:
Sequence:
MPICKREGFDLNQKEGKNETFHDNDQVFCCYITKRIFRDYEHYFRHVMVINSTVWQCEATGKENLTYEEAVKSERAARKKMEQFKQSLRAPVLLVVEHAQQSAVNTLNMIVAKFLRKRYFIGEEVSVQAKKNATYTVLGVKLDKNMPEPLNGIYEDTDNLVYRLRPNKGDPSAELDLPFRQLRRSRMEFNLENLSMFIKSNVSRVDGLLRPKPEAYKQYVTNPGVNFSTIFIGKMPRYSPAKIKKPDGKKQSTLNKYIVAGEATAAKSKAKAKSDAKSLAEELERVKREKEAKLIELEKQKAEKKAQLIERVENECNLLLQKTDDLERTDQKVLPRYRQIVTLLPEHLLGDAFMMREFMHTYTGLLSGIEVFRQNLSFYEMTRALTAREIAGPLSDILLVLLGTVFDLQKEEEEECAVTYLDRAAQTQEPYWSMAQAAKSHLYAKRHFSFKVNELPLDALTLSEVLRLHLLGSGAFVNEKAERWRVMYRNGYSSKEDPGLELRLEHSHILRILKNHSVYQLKFKDIMLLIRCLMSQIMTYSGTINLIEERMEQTAKARQDLRALVVGENKRLAAVEINRKKLTQMHHLEVNGVEPEKREALVEKLKKSIAELHAQSDQQHRKHELQMLKLHSQLFNFLVYLGMDRCYRKYYVLESMPGIFVEHSPDSLDTCLEQPITNKSQIEIRQQSALPKNRKDLRVYLLKLYGDDEKKTKKKAKHSLENKENQEHRLNGSAEPMDVESNSPEAPTHFELLMCSGDKRSCIVHDSRNGQRQRWAYIYKAEEIDELIKALNPNGLREYELLQELSVLRSLIEQHAKTCPVDLLSLENETMRKKFMAAMESETNRKYGEANFGLPNGTDLNEVMRLHLVDRIIQFENDIYTGDLGRLKVKDMEKWRSDLLGGNYDAQCKLQWGPGGKLEDEAGSDNESHETHEEDDGALLGKYARKPYRDPGMYLAASADTKPLPDSDDEEDQHTNAVLIPIAVHNMASALLQVEQAIGKRFLKEPYGMKKWDPKQEALKLACDSRLHQWEVSLMESTSFAQVFLHLNILHDCIQWRRSTNKSLCKVCRRGSDPEKMLLCDECNAGTHMFCLKPKLRSVPPGNWYCNDCVKSLGLSHGQNEKDKKQATKKKRKFIVEEEDDEATDEEEEEKKDDDMTDEDAEHENEKHDEDVEDDESVTSTPSSSRVNGRILRRPRTRPTSRRLTSKEIEEHAQEDVDSGDVSDDASLTAGEDTIEDESDEEKVCQKCFYDGGEIKCVQCRLFFHLECVHLKRPPRTDFVCKTCKPMPQRPRRRHSNMNGDHDRDEEEPKAKRPRNSLRLSIDKTARPSNGNNNNNNNNSSVNNNNHRRSGRRTNEHMPLNSAALYDLLEQIMKHKAAWPFLRPVLTSEVPDYHQIIKTPMDLAKIKSKLNMGAYQLNEELLSDIQLVFRNCDLYNVEGNEIYDAGCQLERFVIDRCRDMQLPFRPSDMNGEVKAC
Protein: Perforin-1 (P1) (Cytolysin) (Lymphocyte pore-forming protein) (P10820)
Organism: Mus musculus (Mouse)
Function: Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes. Perforin pores allow the release of mature caspase-7 (CASP7) into the extracellular milieu.
Subcellular location: Cytolytic granule {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:8164737}. Secreted {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:3261391}. Cell membrane {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:35148176}; Multi-pass membrane protein {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:35148176}. Endosome lumen {ECO:0000250|UniProtKB:P14222}. Note=Released from cytotoxic lymphocytes, together with proapoptotic granzymes: stored in cytolytic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell (PubMed:2040805, PubMed:8164737). May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes (By similarity). Inserts into the cell membrane of target cells and forms pores (PubMed:19446473, PubMed:21037563). Membrane insertion and pore formation requires a major conformation change (PubMed:19446473, PubMed:21037563). {ECO:0000250|UniProtKB:P14222, ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:8164737}.
Interaction partners:
- Granzyme B
- Granzyme A
- Tumor necrosis factor ligand superfamily member 6
- NKG2-D type II integral membrane protein
- Interferon gamma
- Serglycin
- Natural killer cells antigen CD94
- T-cell surface glycoprotein CD4
- Neural cell adhesion molecule 1
- Interleukin-2 receptor subunit beta
Sequence:
MATCLFLLGLFLLLPRPVPAPCYTATRSECKQKHKFVPGVWMAGEGMDVTTLRRSGSFPVNTQRFLRPDRTCTLCKNSLMRDATQRLPVAITHWRPHSSHCQRNVAAAKVHSTEGVAREAAANINNDWRVGLDVNPRPEANMRASVAGSHSKVANFAAEKTYQDQYNFNSDTVECRMYSFRLVQKPPLHLDFKKALRALPRNFNSSTEHAYHRLISSYGTHFITAVDLGGRISVLTALRTCQLTLNGLTADEVGDCLNVEAQVSIGAQASVSSEYKACEEKKKQHKMATSFHQTYRERHVEVLGGPLDSTHDLLFGNQATPEQFSTWTASLPSNPGLVDYSLEPLHTLLEEQNPKREALRQAISHYIMSRARWQNCSRPCRSGQHKSSHDSCQCECQDSKVTNQDCCPRQRGLAHLVVSNFRAEHLWGDYTTATDAYLKVFFGGQEFRTGVVWNNNNPRWTDKMDFENVLLSTGGPLRVQVWDADYGWDDDLLGSCDRSPHSGFHEVTCELNHGRVKFSYHAKCLPHLTGGTCLEYAPQGLLGDPPGNRSGAVW
Protein: Peroxidase 62 (Atperox P62) (EC 1.11.1.7) (ATP24a) (Q9FKA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- En/Spm-like transposon protein-like
- Berberine bridge enzyme-like 11
- Berberine bridge enzyme-like 10
- F13F21.11 protein
- Berberine bridge enzyme-like 8
- Probable ADP-ribosylation factor GTPase-activating protein AGD6
- Putative germin-like protein subfamily 1 member 9
- Berberine bridge enzyme-like 3
- Xanthotoxin 5-hydroxylase CYP82C2
- Cysteine-rich receptor-like protein kinase 26
Sequence:
MGLVRSFALVIVFLSCLIAVYGQGTRIGFYSTTCPNAETIVRTTVASHFGSDPKVAPGLLRMHNHDCFVQGCDGSVLLSGPNSERTAGANVNLHGFEVIDDAKRQLEAACPGVVSCADILALAARDSVSLTNGQSWQVPTGRRDGRVSLASNVNNLPSPSDSLAIQQRKFSAFRLNTRDLVTLVGGGHTIGTAACGFITNRIFNSSGNTADPTMDQTFVPQLQRLCPQNGDGSARVDLDTGSGNTFDTSYFINLSRNRGILQSDHVLWTSPATRSIVQEFMAPRGNFNVQFARSMVKMSNIGVKTGTNGEIRRVCSAVN
Protein: F-actin-uncapping protein LRRC16A (CARMIL homolog) (Capping protein regulator and myosin 1 linker protein 1) (Capping protein, Arp2/3 and myosin-I linker homolog 1) (Capping protein, Arp2/3 and myosin-I linker protein 1) (CARML1) (Leucine-rich repeat-containing protein 16A) (Q6EDY6)
Organism: Mus musculus (Mouse)
Function: Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments. Plays a role in lamellipodial protrusion formations and cell migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16054028}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16054028}. Cell membrane {ECO:0000250|UniProtKB:Q5VZK9}. Cell projection, lamellipodium {ECO:0000269|PubMed:16054028}. Note=Found on macropinosomes (By similarity). Colocalized with heterodimeric capping protein (CP) and F-actin in lamellipodia but not with F-actin in stress fibers (PubMed:16054028). {ECO:0000250|UniProtKB:Q5VZK9, ECO:0000269|PubMed:16054028}.
Interaction partners:
- Unconventional myosin-If
- Actin, cytoplasmic 2
- Myosin XVIIIb
- Mitogen-activated protein kinase kinase kinase 1
- Cytospin-A
- Thymosin beta 15b like
- F-actin-capping protein subunit beta
- Unconventional myosin-Ic
- CD2-associated protein
- Tropomodulin-3
Sequence:
MTDESSDVPRELMESIKDVIGRKIKISVKKKVKLEVKGDRVENKVLVLTSCRAFLLSARIPSKLELTFSYLEIHGVICHKPAQMVVETEKCNMSMKMVSPEDVSEVLAHIGTCLRRIFPGLSPLRIMKKVSMEPSERLASLQALWDSQTLAEPGPCGGFSQMYACVCDWLGFSYKEEVQWDVDTIYLTQDTRELNLQDFSHLEHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRIDFAQKLAGALAHNPNSGLHTINLAGNSLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLCQSLSANPLTASTLTHLDLSGNALRGDDLSHMYNFLAQPNTIVHLDLSNTECSLEMVCSALLRGCLQCLAVLNLSRSVFSHRKGKEVPPSFKQFFSSSLALIQINLSGTKLSPEPLKALLLGLACNHSLKGVSLDLSNCELGHCLRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNLVQMIQDEDSPLQSLSLADSKLKAEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDAAQALKTNPEKTEEALQKIENYLLRNHETRKYLQEQAYRLQQGIVTSTTQQMIDRICVKVQDHLNSLRACGGDAIQEDLKAAERLMRDAKNSKTLLPNLYHVGGASWAGASGLSSSPIQETLESMAGEVTRVVDEQLKDLLESMVDAAETLCPNVMRKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDSLSSSHRKLANHFSRLNKSLPQREDLEVELVEEKPVKRAILTVEDLTEVERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEMEFDLDKALEEVPIHIEDPPFPSVRQEKRSSGLISELPSEEGRRLEHFTKLRPKRNKKQQPTQAAVCTISILPQDGEQNGLMGRVDEGVDEFFTKKVTKMDCKRSSSRSSDAHELGEGDEKKKRDSRRSGFLNLIKSRSRSERPPTVLMTEELSSPKGAMRSPPVDTTRKEIKAAEHNGAPDRTEEIKTPEPLEEGPAEEAGRAERSDSRGSPQGGRRYVQVMGSGLLAEMKAKQERRAACAQKKLGNDVISQDPSSPVSCNTERLEGGATVPKLQPGLPEARFGSGTPEKNAKAEPRVDGGCRSRSSSSMPTSPKPLLQSPKPSPSARPSIPQKPRTASRPEDTPDSPSGPSSPKVALLPPILKKVSSDKERDGQNSSQSSPRSFSQEASRRSWGPAQEYQEQKQRSSGKDGHQGSKCSDSGEEAEKEFIFV
Protein: Riboflavin biosynthesis protein PYRD, chloroplastic [Includes: Diaminohydroxyphosphoribosylaminopyrimidine deaminase (DRAP deaminase) (EC 3.5.4.26) (Riboflavin-specific deaminase); Inactive 5-amino-6-(5-phosphoribosylamino)uracil reductase (HTP reductase)] (Q8GWP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Monofunctional pyrimidine deaminase involved in the riboflavin biosynthesis pathway. Has also a reductase domain that lacks catalytically essential substrate-binding residues.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23150645}.
Interaction partners:
- Monofunctional riboflavin biosynthesis protein RIBA 3
- Monofunctional riboflavin biosynthesis protein RIBA 2
- Bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic
- Riboflavin biosynthesis protein PYRR
- Riboflavin synthase
- 6,7-dimethyl-8-ribityllumazine synthase, chloroplastic
- Flavin mononucleotide hydrolase 1, chloroplatic
- tRNA-specific adenosine deaminase TAD3
- 5-amino-6-
- Cysteine-rich repeat secretory protein 42
Sequence:
MQISCLPISIPSITPRTSIPLLPSLSSNPRRIFNLTSLQSPNHCFFKRLHKSQTGFSNPVLAAMRREEDVEVDDSFYMRKCVELAKRAIGCTSPNPMVGCVIVKDGDIVGQGFHPKAGQPHAEVFALRDAGELAENATAYVSLEPCNHYGRTPPCTEALIKAKVRRVVIGMVDPNPIVFSSGISRLKDAGIDVTVSVEEELCKKMNEGFIHRMLTGKPFLALRYSMSVNGCLLDKIGQGASDSGGYYSKLLQEYDAIILSSSLSDELSSISSQEAINVSIQPIQIIVASNAQQSHILASSHTVEESGPKVVVFTAKESVAESGISSSGVETVVLEKINLDSILDYCYNRGLCSVLLDLRGNVKDLEVLLRDGFEQKLLQKVIIEVLPEWSTKDERQIASMKWLESKHVKDLQSKQLGGSVLLEGYF
Protein: Growth/differentiation factor 11 (GDF-11) (Bone morphogenetic protein 11) (BMP-11) (O95390)
Organism: Homo sapiens (Human)
Function: Secreted signal that acts globally to regulate anterior/posterior axial patterning during development. May play critical roles in patterning both mesodermal and neural tissues (By similarity). It is required for proper vertebral patterning and orofacial development. Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Activin receptor type-2B
- TGF-beta receptor type-1
- Activin receptor type-2A
- Follistatin
- Activin receptor type-1B
- WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 2
- Activin receptor type-1C
- Transcription factor ATOH7
- Follistatin-related protein 3
- Activin receptor type-1
Sequence:
MVLAAPLLLGFLLLALELRPRGEAAEGPAAAAAAAAAAAAAGVGGERSSRPAPSVAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
Protein: Transient receptor potential cation channel subfamily C member 3 (G1U2U3)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Stromal interaction molecule 1
- Protein kinase C beta type
- Bone morphogenetic protein receptor type-2
- Transient receptor potential cation channel subfamily C member 4
- RAR related orphan receptor A
- Histone acetyltransferase KAT5
- Stromal interaction molecule 2
- Transient receptor potential cation channel subfamily V member 4
- Transient receptor potential cation channel subfamily A member 1
- Short transient receptor potential channel 1
Sequence:
MVGGGGSASSLASNCSISGRAAPRLLPSRPALPAAAEGGEGALPGDRASPMWRKARGRQSPRLEPQPAAIVHPSSGKCKEAAKVTFPAPEEEEEEGEDEGAEPQRRRRGWRGVNGGLEPRSAPLRREPHGFCPPPFSPGPDLSMEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLEESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEAILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLLLKGARIERPHDYFCKCGDCTEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALELSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVHRHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTVAIKCLVVLVVALGLPFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVIDYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIFIAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFLAFMIGMFILYSYYLGAKVNPAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVVVLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFIMRIINFSKCRRRRLQKDLEMGIGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMKRLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKLNPSMLRCE
Protein: Pleckstrin homology-like domain family A member 2 (Beckwith-Wiedemann syndrome chromosomal region 1 candidate gene C protein) (Imprinted in placenta and liver protein) (Tumor-suppressing STF cDNA 3 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 3 protein) (p17-Beckwith-Wiedemann region 1 C) (p17-BWR1C) (Q53GA4)
Organism: Homo sapiens (Human)
Function: Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Solute carrier family 67 member A1
- Cyclin-dependent kinase inhibitor 1C
- Potassium voltage-gated channel subfamily KQT member 1
- Achaete-scute homolog 2
- U5 small nuclear ribonucleoprotein TSSC4
- Insulin-like growth factor 2
- Uncharacterized protein SLC67A1-AS
- Nucleosome assembly protein 1-like 4
- Tetraspanin-32
- Oxysterol-binding protein-related protein 5
Sequence:
MKSPDEVLREGELEKRSDSLFQLWKKKRGVLTSDRLSLFPASPRARPKELRFHSILKVDCVERTGKYVYFTIVTTDHKEIDFRCAGESCWNAAIALALIDFQNRRALQDFRSRQERTAPAAPAEDAVAAAAAAPSEPSEPSRPSPQPKPRTP
Protein: B-cell CLL/lymphoma 9-like protein (B-cell lymphoma 9-like protein) (BCL9-like protein) (Protein BCL9-2) (Q86UU0)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17129358, ECO:0000269|PubMed:17309600}.
Interaction partners:
- Pygopus homolog 2
- Catenin beta-1
- B-cell CLL/lymphoma 9 protein
- Transcription factor 4
- LIM domain-binding protein 1
- Pygopus homolog 1
- Transducin-like enhancer protein 1
- Transducin-like enhancer protein 3
- Transducin-like enhancer protein 4
- Hepatocyte nuclear factor 4-alpha
Sequence:
MRILANKTRLPHPRRREAPGSPPLSPRGHCPPAPAKPMHPENKLTNHGKTGNGGAQSQHQNVNQGPTCNVGSKGVGAGNHGAKANQISPSNSSLKNPQAGVPPFSSLKGKVKRDRSVSVDSGEQREAGTPSLDSEAKEVAPRSKRRCVLERKQPYSGDEWCSGPDSEEDDKPIGATHNCNVADPAMAAPQLGPGQTTQLPLSESSVPGAPHGPPPGLRPDAPGGGGGGGGVPGKPPSQFVYVFTTHLANTAAEAVLQGRADSILAYHQQNVPRAKLDQAPKVPPTPEPLPLSTPSAGTPQSQPPPLPPPPPPAPGSAPPALPPEGPPEDSSQDLAPNSVGAASTGGGTGGTHPNTPTATTANNPLPPGGDPSSAPGPALLGEAAAPGNGQRSLVGSEGLSKEQLEHRERSLQTLRDIERLLLRSGETEPFLKGPPGGAGEGGPPAQAPPPPQQPPTAPPSGLKKYEEPLQSMISQTQSLGGPPLEHEVPGHPPGGDMGQQMNMMIQRLGQDSLTPEQVAWRKLQEEYYEEKRRKEEQIGLHGSRPLQDMMGMGGMMVRGPPPPYHSKPGDQWPPGMGAQLRGPMDVQDPMQLRGGPPFPGPRFPGNQIQRVPGFGGMQSMPMEVPMNAMQRPVRPGMGWTEDLPPMGGPSNFAQNTMPYPGGQGEAERFMTPRVREELLRHQLLEKRSMGMQRPLGMAGSGMGQSMEMERMMQAHRQMDPAMFPGQMAGGEGLAGTPMGMEFGGGRGLLSPPMGQSGLREVDPPMGPGNLNMNMNVNMNMNMNLNVQMTPQQQMLMSQKMRGPGDLMGPQGLSPEEMARVRAQNSSGVMGGPQKMLMPSQFPNQGQQGFSGGQGPYQAMSQDMGNTQDMFSPDQSSMPMSNVGTTRLSHMPLPPASNPPGTVHSAPNRGLGRRPSDLTISINQMGSPGMGHLKSPTLSQVHSPLVTSPSANLKSPQTPSQMVPLPSANPPGPLKSPQVLGSSLSVRSPTGSPSRLKSPSMAVPSPGWVASPKTAMPSPGVSQNKQPPLNMNSSTTLSNMEQGTLPPSGPRSSSSAPPANPPSGLMNPSLPFTSSPDPTPSQNPLSLMMTQMSKYAMPSSTPLYHNAIKTIATSDDELLPDRPLLPPPPPPQGSGPGISNSQPSQMHLNSAAAQSPMGMNLPGQQPLSHEPPPAMLPSPTPLGSNIPLHPNAQGTGGPPQNSMMMAPGGPDSLNAPCGPVPSSSQMMPFPPRLQQPHGAMAPTGGGGGGPGLQQHYPSGMALPPEDLPNQPPGPMPPQQHLMGKAMAGRMGDAYPPGVLPGVASVLNDPELSEVIRPTPTGIPEFDLSRIIPSEKPSSTLQYFPKSENQPPKAQPPNLHLMNLQNMMAEQTPSRPPNLPGQQGVQRGLNMSMCHPGQMSLLGRTGVPPQQGMVPHGLHQGVMSPPQGLMTQQNFMLMKQRGVGGEVYSQPPHMLSPQGSLMGPPPQQNLMVSHPLRQRSVSLDSQMGYLPAPGGMANLPF
Protein: Large ribosomal subunit protein bL17c (50S ribosomal protein L17, chloroplastic) (CL17) (Q9M385)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein binds directly to 23S ribosomal RNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein bL9c
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein bL27c
- Large ribosomal subunit protein bL28c
- Small ribosomal subunit protein uS9c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- 50S ribosomal protein L33
- Large ribosomal subunit protein uL11c
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein uL22c
Sequence:
MAIPMSMAMATPTDSVSRVWSMSSLKSALPSTASLRLPSSSSRRPVTLRLPISSPSLPSFSGLSPVNPLLSIGLPDWQSFENGFKIVDGGGRIYAMRHGRRVPKLNRPPDQRKALLRGLTTQLLKHGRIKTTRARASAMRKFVDKMITLAKDGSLHKRRQALGYIYEKQIVHALFAEVPDRYGERNGGYTRIIRTLPRRGDNAPMAYIELV
Protein: NAD(+) kinase (EC 2.7.1.23) (Q6IDH2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- NAD kinase 2, mitochondrial
Sequence:
MTCLSDIDLATLHQHRLEEIFSYKLAWSGTGHQQTQYNDLLVRHNASLKRQRIIQHTANRASTRAKDQASTDDCVATSPGNIQAKSEQDPDDGYFDSTTRRTRSGTWPRTRSLNAPSPFQHFGPCGRIMKNSAMVMQIQDPASQRLTWYKPPLTVLVIKKKDSQVLPPFVQLVEWLVQEKHMVVWVESAVLEDKLLRDDVKLEQESSKFQKVHQQYAGVRARFLDLREKLVTFKDGRDDLTDRIDFIVCLGGDGTLLYASQLFQQSVPPVMAFYLGSLGFLTPFQCDNFQEQVTNVLEGHAALTLRSRLRCSIHRKGERRKESLLHSVGGNLLIPSFQRQLNYVELNNGQTGKAGSNNNNGHNNSILVLNEVVINRGPSPYLSNIDIFLEGKYITSVQGDGLIVSTPTGSTAYAAAAGASMIHPSVPAILVTPICPHSLSFRPIVVPAGVELKISISPDSRNTSRVSFDGRNDQELNHGDSLRVTTSIYPVPSICSQDQISDWFDSLAEGLHWNVRKRQKCLDELSDLTTSGSEDTLDDFDNLQIYDA
Protein: Accessory protein 9b (ORF-9b) (Q6S8E0)
Organism: Severe acute respiratory syndrome coronavirus (SARS-CoV)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
Interaction partners:
Sequence:
MDPNQTNVVPPALHLVDPQIQLTITRMEDAMGQGQNSADPKVYPIILRLGSQLSLSMARRNLDSLEARAFQSTPIVVQMTKLATTEELPDEFVVVTAK
Protein: Proline-rich protein 23D1 (E9PI22)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYGYRRLRSPRDSQTEPQNDNEGETSLATTQMNPPKRRQVEQGPSTGAKKPSISGAPHLNSYQSLELPQNQQDSGTEELMIVLEQGTEVRLSLEEVILILAPETVLQLTLENTVLVIVPEHVLRSEDGLQSPVQIQYIIPSVDDFSLEFHAQDGDISDMRRENVPFSPAEEGKAAPLYQQPLMIPQANHMAGISPSFLVTPLCIPRCRAAFPQCYPLPPTPSPVGRPRPADSSFSLHGMELLCTSSLRPMPPSPSPGPQVYHRVHHRPPSRARRCLFRK
Protein: Biglycan (Bone/cartilage proteoglycan I) (PG-S1) (P28653)
Organism: Mus musculus (Mouse)
Function: May be involved in collagen fiber assembly.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Fibronectin
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Toll-like receptor 2
- Toll-like receptor 4
- Decorin
- Elastin
- CCN family member 4
- Syndecan-1
- Collagen alpha-1
- Tumor necrosis factor
Sequence:
MCPLWLLTLLLALSQALPFEQKGFWDFTLDDGLLMMNDEEASGSDTTSGVPDLDSVTPTFSAMCPFGCHCHLRVVQCSDLGLKTVPKEISPDTTLLDLQNNDISELRKDDFKGLQHLYALVLVNNKISKIHEKAFSPLRKLQKLYISKNHLVEIPPNLPSSLVELRIHDNRIRKVPKGVFSGLRNMNCIEMGGNPLENSGFEPGAFDGLKLNYLRISEAKLTGIPKDLPETLNELHLDHNKIQAIELEDLLRYSKLYRLGLGHNQIRMIENGSLSFLPTLRELHLDNNKLSRVPAGLPDLKLLQVVYLHSNNITKVGINDFCPMGFGVKRAYYNGISLFNNPVPYWEVQPATFRCVTDRLAIQFGNYKK
Protein: Nucleolar complex protein 2 (Q389A0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- CCAAT-binding factor domain-containing protein
- CCAAT-binding factor domain-containing protein
- Pescadillo homolog
- Ribosome assembly factor mrt4
- Nucleolar protein, putative
- rRNA processing protein, putative
- Ribosome biogenesis protein BOP1 homolog
- RNA-binding protein, putative
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein NSA2 homolog
Sequence:
MAKEKKSFKKYAKKHLATVIENRRKGAKAKKEKLERVERKKVREEKEAEREEREHQEQLERLKDTDPEFYSYLEEEDPTLLQFGDKDMDIVDENEGSDAETEPDEEEDGNDIDDGDDNISGIADEGNGEQSIQESRVTSGELDRLIKEKNVEACVNIFVSALRELGYRVKESPRASTRRKFEDPSLVKESMLRVAQFIGSNLSTVITGKGAFKTPKTRHLVRRILSSLVVSLDESNTDAALAAGLLHALVAFVPILHFLKGMTKSVLKASLLLCCATEESVRVAAYVVVRSIATRATGTRSMYQSTAFKGVFLTLIRTAHSYNIRNAPLLAFLTNCVVDLYGTDMEAAYQHAFVYLRQLAIYLRGALQQQSQSNVRAVVNWQYLNALRAWGAVVSNYSEASQLGPLIHPVVQLATGLMDLFSSPRMFPMHLQVIEVLNHIALRADGVFIPVAPYLLRILTSPSIALGHHSNGSGRGETGDPVDLRFTIRVKKSQARNFSYHRSVWSECLYLLSEHLATHSHTVGFPEAFWSVEVTLKRLRTEVKVPKVHAQLSALLRHIQTTNQKIVSKREQSGPGPCDLAAVKQMEDELKASGNPLITYYQSLRQQRIEAFAAKQKDANGEERVTLEATVEREKSKKNRKRQRSDHNS
Protein: Retinol dehydrogenase 8 (EC 1.1.1.300) (Photoreceptor outer segment all-trans retinol dehydrogenase) (Short chain dehydrogenase/reductase family 28C member 2) (Q9NYR8)
Organism: Homo sapiens (Human)
Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity (By similarity).
Subcellular location: Membrane {ECO:0000305|PubMed:10753906}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lecithin retinol acyltransferase
- Retinal dehydrogenase 2
- Cytochrome P450 26A1
- Retinaldehyde dehydrogenase 3
- Beta,beta-carotene 15,15'-dioxygenase
- Aldehyde dehydrogenase 1A1
- All-trans-retinol 13,14-reductase
- Cytochrome P450 27C1
- Diacylglycerol O-acyltransferase 1
- Aldehyde oxidase
Sequence:
MAAAPRTVLISGCSSGIGLELAVQLAHDPKKRYQVVATMRDLGKKETLEAAAGEALGQTLTVAQLDVCSDESVAQCLSCIQGEVDVLVNNAGMGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPGMKRRRQGHIVVISSVMGLQGVIFNDVYAASKFALEGFFESLAIQLLQFNIFISLVEPGPVVTEFEGKLLAQVSMAEFPGTDPETLHYFRDLYLPASRKLFCSVGQNPQDVVQAIVNVISSTRPPLRRQTNIRYSPLTTLKTVDSSGSLYVRTTHRLLFRCPRLLNLGLQCLSCGCLPTRVRPR
Protein: B1 bradykinin receptor (B1R) (BK-1 receptor) (Q8HZN9)
Organism: Sus scrofa (Pig)
Function: This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P46663}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASQTLVVFQASNQSQLPPPNATLCDGAQEAWHLLHKVLPTCVVAICSGGLLGNLFVLSVFLVPRRRLNAAEIYLAHLAASDLVFALGLPFWAETIRNGFHWPFGAPLCRVVNGVIKANLFISIFLVVAISRDRYRALVHPVASWRRRRRRHWAQATCVLIWTAGGLLSIPTFLLRSVQVVPELNVSACVLPFPHEAWAFVRTVELNVLGFLLPLAAILFFNYHILAALRGREQLSRTRCGGPRDGKTTALILTLVAVFLLCWTPYHVCAFLEFLLHVRAIRGCFWEDFTDLGLQYTNFFAFINSCLNPVIYVFWGQLFRTKIWELYHRCLPRKLTAVSSSRRKEIFQIFWRN
Protein: Cytoplasmic polyadenylation element binding protein 4 (A0A8I6A633)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPNPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKAEENPGDNSSENSNGKEKIRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPGASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRNAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGASQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPDRPRTFDMHSLESSLIDIMRAENDSIKGKLRNNDSILVIAKSQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFTHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN