wanglab/gogpt-training-data huggingface dataset:
Protein: NAD(P)H-quinone oxidoreductase chain 4 1 (EC 7.1.1.-) (NAD(P)H dehydrogenase I, chain 4 1) (NDH-1, chain 4 1) (Q8DKY0)
Organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Function: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00491}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00491}.
Interaction partners:
- NAD
- NAD
- NADH dehydrogenase subunit 5
- NAD
- NAD
- NAD
- NAD
- NADH-quinone oxidoreductase subunit J
- NAD
- NAD
Sequence:
MSTFPWLTTIILFPIVAALAIPFIPDPTGKGRPIRWYALAVGLIDFALIVYAFTNFYDLNTPGMQLWESYDWIPEIGLRWSVGADGLSMPLILLTGFITTLAILAAWPVTLKPRLFYFLMLAMYGGQIAVFAVQDMLVFFLAWELELIPVYLLLAIWGGHKRQYAATKFILYTAGSSLFILVAGLAMAFYGDTVSFDMQTLAAKDYALGFQLLVYAGFLVAYGVKLPIVPLHTWLPDAHGEATAPVHMLLAGILLKMGGYALIRMNVDMLPAAHAKFAPVLVILGVVNIIYAALTSYAQRNLKRKIAYSSISHIGFVLIGIASFTNLGMSGAVLQMVSHGLIGASLFFLVGATYDRTHTLILEEMGGVGQKMKKIFAMFTACSLASLALPGMSGFVAELMVFIGFATSDAYSLPFRVIVVFLAAVGVILTPIYLLSMLREIFYGPENKELVEHEALVDAEPREVFIIACLLVPIIGIGLYPKLLTQIYDATTGQVIARAREVLPTLAQQTEQPLGILPMVAPQLKANAQ
Protein: Spliceosome associated factor 3, U4/U6 recycling protein (A0A499FI31)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATAAETSASEPEAESKAGPKADGEEDEVKAARTRRKVLSRAVAAATYKTMGPAWDQQEEGVSESDGDEYAMASSAESSPGEYEWEYDEEEEKNQLEIERLEEQLSINVYDYNCHVDLIRLLRLEGELTKVRMARQKMSEIFPLTEELWLEWLHDEISMAQDGLDREHVYDLFEKAVKDYICPNIWLEYGQYSVGGIGQKGGLEKVRSVFERALSSVGLHMTKGLALWEAYREFESAIVEAARPVAGFLSPFDREQTFDSQLEKVHSLFRRQLAIPLYDMEATFAEYEEWSEDPIPESVIQNYNKALQQLEKYKPYEEALLQAEAPRLAEYQAYIDFEMKIGDPARIQLIFERALVENCLVPDLWIRYSQYLDRQLKVKDLVLSVHNRAIRNCPWTVALWSRYLLAMERHGVDHQVISVTFEKALNAGFIQATDYVEIWQAYLDYLRRRVDFKQDSSKELEELRAAFTRALEYLKQEVEERFNESGDPSCVIMQNWARIEARLCNNMQKARELWDSIMTRGNAKYANMWLEYYNLERAHGDTQHCRKALHRAVQCTSDYPEHVCEVLLTMERTEGSLEDWDIAVQKTETRLARVNEQRMKAAEKEAALVQQEEEKAEQRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKCAAVDVEPPSKQKEKAASLKRDMPKVLHDSSKDSITVFVSNLPYSMQEPDTKLRPLFEACGEVVQIRPIFSNRGDFRGYCYVEFKEEKSALQALEMDRKSVEGRPMFVSPCVDKSKNPDFKVFRYSTSLEKHKLFISGLPFSCTKEELEEICKAHGTVKDLRLVTNRAGKPKGLAYVEYENESQASQAVMKMDGMTIKENIIKVAISNPPQRKVPEKPETRKAPGGPMLLPQTYGARGKGRTQLSLLPRALQRPSAAAPQAENGPAAAPAVAAPAATEAPKMSNADFAKLFLRK
Protein: Protein fuzzy (O16868)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in the organization of cell polarity via a planar cell polarity (PCP) cascade. Involved in the development of the hairs on the wings. Specify the correct orientation of the hair by limiting the site of prehair initiation to the distal vertex of the wing cells. Controls wing cell hair number by maintaining the integrity of the cytoskeletal components that direct hair development.
Subcellular location: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- WD repeat-containing and planar cell polarity effector protein fritz
- Protein inturned
Sequence:
MSIYLLCLTTNGGLPVFTRKKGECENLPFSTVASLNGFHMFFKSLGIQLEATTTSKQQPIQNQAPADAEEWTYIWRDRESITLIVCGCGVGSEQLLQTLADLVFGAIGMFITRAAEMAHATLLDRLKKDAKKYVPIVDAILEAACAGTQLLGYTDCLLAAENAQLLQCLNEFSGHCGSLFCCLVVGHRIAVATEGWWDLDTRDRELLLFLLNSSSTMQHDVPVYLPVKSPHIAYRFVSIPVASNSALCVLCGAENASFRELHAHAMSAYRNEGNLLAAAERCVPRSLPEHLEIDGNVLAIILINRHTRKSLFTRNLNQSASVKRIIVGDLQRLDILKKFFDQTMDAVHQFETQSSSNKTTLVDQYSCSDYHKCYAHMDELGNVIFLLFVAAVPSHAMRFLAQRIHANILQEKSVCW
Protein: DUF724 domain-containing protein 4 (AtDUF4) (O81039)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the polar growth of plant cells via transportation of RNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:19795213}.
Interaction partners:
- Proteasome subunit beta type-2-A
Sequence:
MFLTNGSRAGPVKERGLLIIDADHPNYDASGRGKRRRVEQEHHSDLNNETAAPTGGSAGEEIVLPFTKTLASWKEFESDEVYKRTPQRPHFPSLAYTHPSFGEPTAAYLTAAFIDCVKTVDGMCEDTPKSELDVYRETFKMFEEQGFDVAEPLSQVLTLLVLRKMRRESLRQQKGMEKEMADDYSKLKKSLVRCKSSFEDKETAK
Protein: Gamma-secretase subunit aph-1 (Anterior-pharynx-defective protein 1) (Presenilin enhancer protein 1) (O45876)
Organism: Caenorhabditis elegans
Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral proteins such as Notch receptors (lin-12 or glp-1). It may represent a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex. Required for the localization of aph-2.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nicastrin
- Gamma-secretase subunit pen-2
- Presenilin hop-1
- Presenilin sel-12
- Presenilin spe-4
- Protein lin-12
- Peptidase A1 domain-containing protein
- Peptidase A1 domain-containing protein
- Peptidase A1 domain-containing protein
- Peptidase A1 domain-containing protein
Sequence:
MGYLLTIACYIASFSPSIALFCSFIAHDPVRIILFFLGSFFWLVSLLFSSLAWLGLSTVLPDTFLLSLTVCIIAQELSRVAYFMLLKKAQRGLNKITRQGQISVAPGVSDLHNARHMLALVCGLGMGVISALFYTMNAFAIFSGPGTIGLPNALKTGEIDTNRAGKYLPLCYTLSAILLTLFHVTWTIMVWDSCHKIGRIPSAFVPGAAAVVSHLLVTFLSSLNSRGFHVLVFAVQFLILLICIAYCNVIMGGTISSFVNGIGQSITDAVTLKQVRTLIEERKLRTQRQSVPDEPMTERAGTSNTVNA
Protein: Phaiodotoxin (Q5MJP5)
Organism: Anuroctonus phaiodactylus (Mafia scorpion)
Function: Sodium channel (Nav) specific neurotoxin. Causes impairment of movement and mild paralysis in crickets at a dose of 0.5 ug per animal. A dose of 0.8 ug per cricket causes clear flaccid paralysis. A dose of 1.0 ug per cricket causes death within 2 hours.
Subcellular location: Secreted {ECO:0000269|PubMed:15606762}.
Interaction partners:
Sequence:
MKTIPLLFLLFIYFECDGKFIRHKDESFYECGQLIGYQQYCVDACQAHGSKEKGYCKGMAPFGLPGGCYCPKLPSNRVKMCFGALESKCA
Protein: DNA repair-scaffolding protein (Scaffolding protein involved in DNA repair) (Q14159)
Organism: Homo sapiens (Human)
Function: Plays a role in DNA double-strand break (DBS) repair via homologous recombination (HR). Serves as a scaffolding protein that helps to promote the recruitment of DNA-processing enzymes like the helicase BLM and recombinase RAD51 to site of DNA damage, and hence contributes to maintain genomic integrity.
Subcellular location: Nucleus {ECO:0000269|PubMed:23509288}. Note=Together with BLM, is redistributed in discrete nuclear DNA damage-induced foci following hydroxyurea (HU) or camptothecin (CPT) treatment.
Interaction partners:
- ATPase SWSAP1
- DNA repair protein RAD51 homolog 1
- Fidgetin-like protein 1
Sequence:
MPRGSRARGSKRKRSWNTECPSFPGERPLQVRRAGLRTAGAAASLSEAWLRCGEGFQNTSGNPSLTAEEKTITEKHLELCPRPKQETTTSKSTSGLTDITWSSSGSDLSDEDKTLSQLQRDELQFIDWEIDSDRAEASDCDEFEDDEGAVEISDCASCASNQSLTSDEKLSELPKPSSIEILEYSSDSEKEDDLENVLLIDSESPHKYHVQFASDARQIMERLIDPRTKSTETILHTPQKPTAKFPRTPENSAKKKLLRGGLAERLNGLQNRERSAISLWRHQCISYQKTLSGRKSGVLTVKILELHEECAMQVAMCEQLLGSPATSSSQSVAPRPGAGLKVLFTKETAGYLRGRPQDTVRIFPPWQKLIIPSGSCPVILNTYFCEKVVAKEDSEKTCEVYCPDIPLPRRSISLAQMFVIKGLTNNSPEIQVVCSGVATTGTAWTHGHKEAKQRIPTSTPLRDSLLDVVESQGAASWPGAGVRVVVQRVYSLPSRDSTRGQQGASSGHTDPAGTRACLLVQDACGMFGEVHLEFTMSKARQLEGKSCSLVGMKVLQKVTRGRTAGIFSLIDTLWPPAIPLKTPGRDQPCEEIKTHLPPPALCYILTAHPNLGQIDIIDEDPIYKLYQPPVTRCLRDILQMNDLGTRCSFYATVIYQKPQLKSLLLLEQREIWLLVTDVTLQTKEERDPRLPKTLLVYVAPLCVLGSEVLEALAGAAPHSLFFKDALRDQGRIVCAERTVLLLQKPLLSVVSGASSCELPGPVMLDSLDSATPVNSICSVQGTVVGVDESTAFSWPVCDMCGNGRLEQRPEDRGAFSCGDCSRVVTSPVLKRHLQVFLDCRSRPQCRVKVKLLQRSISSLLRFAAGEDGSYEVKSVLGKEVGLLNCFVQSVTAHPTSCIGLEEIELLSAGGASAEH
Protein: Alkaline phosphatase, germ cell type (EC 3.1.3.1) (ALP-1) (Alkaline phosphatase Nagao isozyme) (Alkaline phosphatase, placental-like) (Germ cell alkaline phosphatase) (GCAP) (Placental alkaline phosphatase-like) (PLAP-like) (P10696)
Organism: Homo sapiens (Human)
Function: Alkaline phosphatase that can hydrolyze various phosphate compounds.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Cancer-related nucleoside-triphosphatase
- GTP cyclohydrolase 1
- 6-pyruvoyl tetrahydrobiopterin synthase
- Thiamine pyrophosphokinase 1
- Alkaline phosphatase, placental type
- Glutathione hydrolase 6
- Intestinal-type alkaline phosphatase
- Glutathione hydrolase 7
- Putative aspartate aminotransferase, cytoplasmic 2
- Inactive glutathione hydrolase 2
Sequence:
MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP
Protein: Aconitate hydratase B (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (Iron-responsive protein-like) (IRP-like) (RNA-binding protein) (Q8ZRS8)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein which regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of FtsH protease activity then influence sigma-32, DnaK and ultimately FliC production.
Interaction partners:
- Citrate synthase
- Isocitrate dehydrogenase
- Aconitate hydratase A
- 2-methylcitrate dehydratase
- 2-oxoglutarate dehydrogenase E1 component
- Fumarate hydratase class I, aerobic
- Isocitrate lyase
- Succinate--CoA ligase subunit beta
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Succinate dehydrogenase flavoprotein subunit
Sequence:
MLEEYRKHVAERAAQGIVPKPLDATQMAALVELLKTPPVGEEEFLLDLLINRVPPGVDEAAYVKAGFLAAVAKGDTTSPLVSPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALSHTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLSRPPLAEKITVTVFKVTGETNTDDLSPAPDAWSRPDIPLHAQAMLKNAREGIEPDQPGVVGPIKQIEALQKKGYPLAYVGDVVGTGSSRKSATNSVLWFMGDDIPNVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSNLNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREALGLPHSDVFRQAKDVAESSRGFSLAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPMTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVTTHHTLPDFIMNRGGVSLRPGDGVIHSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKMQPGITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASAERSAAGCTIKLNKEPIVEYLTSNIVLLKWMIAEGYGDRRTLERRIQGMEKWLADPQLLEADADAEYAAVIDIDLADIKEPILCAPNDPDDARLLSDVQGEKIDEVFIGSCMTNIGHFRAAGKLLDNHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVADGATVVSTSTRNFPNRLGTGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDTYRYLNFDQLSQYTEKADGVIFQTAV
Protein: C-type lectin domain-containing protein (Q8BJS9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MMSEQEVTYSTVRFHKSSGLQNQVRPEDNQGSREAGHKECSIPWHLIVIAFGILCVLLLVIVAVLVTNILQYKQEKHELQETLNCHHNCSTMQNDINAKEEMLRNMPLECSTGDDLLKSLNREQKRWYSETKSVLNSSKHPGGSLEIHWFCYGIKCYYFIMNKKGWRKCKQICEHYSLSLLKIDAEDELKFLQLQVTPDSYWIGFSFDKKSEKWTWIENGTSKYALNMSTYNVKSGECVFLSKTRLENNKCEHVYPCICEKRLDKFPDSLPNNS
Protein: Gastrotropin (GT) (Fatty acid-binding protein 6) (Ileal lipid-binding protein) (ILBP) (Intestinal 15 kDa protein) (I-15P) (Intestinal bile acid-binding protein) (I-BABP) (P51161)
Organism: Homo sapiens (Human)
Function: Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (By similarity). In vitro binds to bile acids in the order: deoxycholic acid > cholic acid > chenodeoxycholic acid and respective BA conjugation modifies affinities in the order taurine-conjugated > glycine-conjugated > unconjugated bile acids. Stimulates gastric acid and pepsinogen secretion (By similarity).
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000250|UniProtKB:P80020}. Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P50119}; Cytoplasmic side {ECO:0000250|UniProtKB:P50119}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17909007}. Note=Localized close to nucleus on the apical side of both normal and neoplastic cells. {ECO:0000269|PubMed:17909007}.
Interaction partners:
- Bile acid receptor
- Ileal sodium/bile acid cotransporter
- Bile salt export pump
- Hepatic sodium/bile acid cotransporter
- Nuclear receptor subfamily 0 group B member 2
- Cytochrome P450 7A1
- Aspartate aminotransferase, mitochondrial
- Fatty acid-binding protein, adipocyte
- Organic solute transporter subunit alpha
- Fatty acid-binding protein, intestinal
Sequence:
MAFTGKFEMESEKNYDEFMKLLGISSDVIEKARNFKIVTEVQQDGQDFTWSQHYSGGHTMTNKFTVGKESNIQTMGGKTFKATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKRLA
Protein: DNA polymerase eta (EC 2.7.7.7) (RAD30 homolog A) (Xeroderma pigmentosum variant type protein) (Q9Y253)
Organism: Homo sapiens (Human)
Function: DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS). Due to low processivity on both damaged and normal DNA, cooperates with the heterotetrameric (REV3L, REV7, POLD2 and POLD3) POLZ complex for complete bypass of DNA lesions. Inserts one or 2 nucleotide(s) opposite the lesion, the primer is further extended by the tetrameric POLZ complex. In the case of 1,2-intrastrand d(GpG)-cisplatin cross-link, inserts dCTP opposite the 3' guanine. Particularly important for the repair of UV-induced pyrimidine dimers. Although inserts the correct base, may cause base transitions and transversions depending upon the context. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have any lyase activity, preventing the release of the 5'-deoxyribose phosphate (5'-dRP) residue. This covalent trapping of the enzyme by the 5'-dRP residue inhibits its DNA synthetic activity during base excision repair, thereby avoiding high incidence of mutagenesis. Targets POLI to replication foci.
Subcellular location: Nucleus {ECO:0000269|PubMed:12606586, ECO:0000269|PubMed:16357261, ECO:0000269|PubMed:22801543, ECO:0000269|PubMed:24553286}. Note=Binding to ubiquitinated PCNA mediates colocalization to replication foci during DNA replication and persists at sites of stalled replication forks following UV irradiation (PubMed:12606586, PubMed:16357261, PubMed:24553286). After UV irradiation, recruited to DNA damage sites within 1 hour, to a maximum of about 80%; this recruitment may not be not restricted to cells active in DNA replication (PubMed:22801543). Colocalizes with TRAIP to nuclear foci (PubMed:24553286). {ECO:0000269|PubMed:12606586, ECO:0000269|PubMed:16357261, ECO:0000269|PubMed:22801543, ECO:0000269|PubMed:24553286}.
Interaction partners:
- Proliferating cell nuclear antigen
- DNA repair protein REV1
- DNA polymerase zeta catalytic subunit
- E3 ubiquitin-protein ligase RAD18
- RING finger and CHY zinc finger domain-containing protein 1
- Mitotic spindle assembly checkpoint protein MAD2B
- DNA-directed DNA/RNA polymerase mu
- Polyubiquitin-C
- DNA repair protein RAD51 homolog 1
- N-glycosylase/DNA lyase
Sequence:
MATGQDRVVALVDMDCFFVQVEQRQNPHLRNKPCAVVQYKSWKGGGIIAVSYEARAFGVTRSMWADDAKKLCPDLLLAQVRESRGKANLTKYREASVEVMEIMSRFAVIERASIDEAYVDLTSAVQERLQKLQGQPISADLLPSTYIEGLPQGPTTAEETVQKEGMRKQGLFQWLDSLQIDNLTSPDLQLTVGAVIVEEMRAAIERETGFQCSAGISHNKVLAKLACGLNKPNRQTLVSHGSVPQLFSQMPIRKIRSLGGKLGASVIEILGIEYMGELTQFTESQLQSHFGEKNGSWLYAMCRGIEHDPVKPRQLPKTIGCSKNFPGKTALATREQVQWWLLQLAQELEERLTKDRNDNDRVATQLVVSIRVQGDKRLSSLRRCCALTRYDAHKMSHDAFTVIKNCNTSGIQTEWSPPLTMLFLCATKFSASAPSSSTDITSFLSSDPSSLPKVPVTSSEAKTQGSGPAVTATKKATTSLESFFQKAAERQKVKEASLSSLTAPTQAPMSNSPSKPSLPFQTSQSTGTEPFFKQKSLLLKQKQLNNSSVSSPQQNPWSNCKALPNSLPTEYPGCVPVCEGVSKLEESSKATPAEMDLAHNSQSMHASSASKSVLEVTQKATPNPSLLAAEDQVPCEKCGSLVPVWDMPEHMDYHFALELQKSFLQPHSSNPQVVSAVSHQGKRNPKSPLACTNKRPRPEGMQTLESFFKPLTH
Protein: Dusky (LP20007p) (Q9VYU7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- IP18436p
Sequence:
MQHQQQQQQQQQQQQQQHKQVRYRNLRRNVEIGAKKIWLPLIIFLSLQVALVCADDVEVVKAIAGGPDDELTIALGDHENELDQMAQESEQEQQAQAQQQQQQQQQQQQQQQQQQHQQLPQIQMQLPQSVPKVQVHYQHNMPQPPPNVALTMRNNHQNIPLSFGQPFGPPPPPGAQFYKGPPPPQLQQRPQPPPQLQLQVQPQQQQQQQQQHTQQQGQQQQVQVPDLSVGGSSNNEIWAAPVQDMPKIVSLDVKCEKNGMKVFVQFDKPFNGIVFSKGHYSNMNCVHLPSGLGRSSASFDIGLHECGTAGNTDNYGQGYGHEAGSTGAGTYFENIIVIQYDPQVQEVWDQARKLRCTWHDQYEKSVTFRPFPVDMLDVVRADFAGDNVGCWMQIQVGKGPWASEVSGLVKIGQTMTMVLAIKDDDSKFDMLVRNCVAHDGKRAPIQLVDQRGCVTRPKLMSRFTKIKNFGASASVLSYAHFQAFKFPDSMEVHFQCTIQICRYHCPEQCSAETNLQDVHHLQVGPESQYGPPPQLHVDAYHVASAIGKRRDERRVQRRARAVAEPQVGLNRIIKVVSSGDLTFAIDDQAGGNGSSTNGANSGVDRSPQTMVFPLREEGLICMTTPGFAITLIVLLGILVTSCLTSAVLYVRLRPFSSFAGSAKERAVAFTNPQLAPLPVIQLPSPADLQGTLSKKRAMS
Protein: SD07967p (Q960C2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSEFPPSSRPYATLQSELKQVAEQLSSAGGEIVVSYSSPALLAESSQNFAANYRDLLSVSMEMAGQTQEEEVRSHMIESLRHVSTQSCSLLSTAKSIAADPGQPNAKNLLHAAARGVTESINQLVDASIQSAPGQKECDNAMRNIEALRLMLDYPHEPINELGYFDCVEQATGKSRNLGYAISEMINNAKQSQHVEFSQSVNNVNDSIQGLIESSSQAAYLIGVSHPSSVAGRPGIIDQAQLTWAYQGIRQHCDIVSSQQSTKPQMISALTVIAKHTSYLCSICRQASMNTSNPVAKNEFIVLAKQVATATSDLVQDIKAIEEQSAGGSRERLVDPLLEAVKAVRQYASSSEFSSVPAKISAEGRKAQEPVIQAGRGVIDGVVEMVKAAKSLALTPDNPPVWQQLSMHSTPVSESVKRLVDNIRDKAPGQAQCEQVLHTLGTCTRELDSCALAVNAQGLSQRRDNNLHGFSGQTMNSASELIDKLEPIRMAGKNNAEQLGHAVGEISRYVVPMVNGAIGACTHIVHSQQQMSLIQQTRSVVESAITLVQSAKDSAGNPRATHAHPRLDDAIDGTREAIQELQQTVEKINAETGIVTGLMEQVNRSITRLTDKRQSLLNASYSDTFVDYQTRMVARAKEIASLANEMNAKSSVEPSALPQLAVDMTQNYQQLTQDSVGASTTTSSPDVAMRIRTTVIDLGRSVSSMIQSSAGGARPNDAGAQKEIARSAREVSEKVAQVLAALQAGSRGTQACINAAHTVSGIIGDLDTTIMFATAGTLHSDGDGSFADHREHILQTAKALVEDTKVLVTGAAGTQDQLANAAQNAVSTITQLAEAVKRGACSLGSTQPDSQVMVINAVKDVASALGDLINCTKLASGKSINDPSMQDLKESARVMVLNVSSLLKTVKAVEDEHTRGTRAMEATVEAISQEIRAMHSPPPVGNTQVGPEDLIRVTMNVTAATAKAVAAGTSNLQADIVSAANLGRRAISEMLIVCRSVAWNCAETEELRSRTLEAGTAVGESYRDLLSGILHNCSADDRMHLSRRVAKCVTDLVAMARLLKGSDWIDPEDPTVIAENELLGAAASIDAAAKKLASLRPRRQADVKIELDENMKFDEMILEAAKGIMGASAALVRAANAAQRELIDTGKVARRPLTSSDDGQWSEGLISAARLVAAATHSLVEAAQNLVRGVGTEEMLISTAKQVAASTAQLLIACKVKSNPNSEAGRRLQAAGNAVIKSTDNLVHSAQQGLEAEEEHSLKINTSMVDGMAQEINARSAVLRKEKELEEARQLLKNVRHAQRYAKNAQGFTTDESDTEYAYRSQNNTLGRSGYYGSSEMPSSPSYLSGGQQQKHHYNHASPQPQHFHHPGAVSPPPSNYPPMDDPNGDFPPPPPPLSTTISNMQTATSGHSFRPNPKLTANAVPRPYPGSPGGSNGLISAPTTTGTPTNTNYQQSYESSSIKTLNSSPPAVPKKPTVNRNLAACVQDLHDKTFGQGGVVQLTGGNGYPGQNYEGYTSRYETRYFDKSANNTTSSSSELGAVKPLESSFSQMTLNTDGGKISIVDQGSERLTSMTQRVMERKSFTTTTESRSETKTEKHSFRLD
Protein: CCAAT/enhancer-binding protein (C/EBP) (Slow border cell protein) (Q02637)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the expression of gene products mediating border cell migration. Among the DNA sequences that this protein binds with high affinity is a conserved site within the promoter of its gene.
Subcellular location: Nucleus {ECO:0000269|PubMed:1459454}.
Interaction partners:
- Tribbles
- Cyclin-dependent kinase 2
- Transcription factor Jra
- Mitogen-activated protein kinase ERK-A
- Nuclear factor of activated T-cells 5
- Cryptocephal, isoform A
- FI24210p1
Sequence:
MLNMESPQMYADAVQTLAQLDLKKEPPLQQATIGQITLTAMSTAQQQQQQQQQQQQQQQQQQQQQQQQPQQQTTDANNNTSQDAALLVKQHAMHQMQQVAALGSNNNLLQKQMLQQYSTQTDLDELTTQEITLDLQHLIDDQFRDTETLGIFSDMVTSPGGLSATLPPSGMVSAAAKVLQQQTLRNQHGYGGRGGGGGAGGALAYMPQPVHATYNNSSDENSSVGSDSSTIKEEPIDPEYRRHLQEAASQQAAFMGNGAGLYNGYGSGANGLTGGGNPLNGGNTTPSSNGSNGSTGSSNGSQFTNLTTANVLAHHNLPHLAAAAGAHNLLKQHSKLHAQQQHQQHQQQQQHRKHSNKHVDKGTDEYRRRRERNNIAVRKSREKAKVRSREVEERVKSLLKEKDALIRQLGEMTNELQLHKQIYMQLMNHANPEVSRVCRSFLNTNEHSL
Protein: Transcription factor 7-like 1-B (HMG box transcription factor 3-B) (TCF-3-B) (xTcf-3) (Q90ZB6)
Organism: Xenopus laevis (African clawed frog)
Function: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of ctnnb1-A and possibly ctnnb1-B, and as an activator in the presence of these proteins. Required early in development for the establishment of the dorsal body axis in response to maternal Wnt signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:11821382}.
Interaction partners:
Sequence:
MPQLNSGGGDELGANDELIRFKDEGEQEEKSPGEGSAEGDLADVKSSLVNESENHSSDSDSEVERRPPPRETFEKPRDYLSEAFRRQQDAAFFKGPPYAGYPFLMIPDLGGHYLPNGALSPSARAYLQMKWPLLDSPSTAGLKDARSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNEHFSPGTPPGHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPQQGQPMYSIPPGGFRHPYPALAMNASMSSLVSSRFSPHMVPPPHHSLHTSGIPHPAIVSPIVKQEPSSGNISPNLSTKSNVVVKKEEEKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHSLSREEQAKYYELARKERQLHSQLYPSWSARDNYGKKKKRKREKQSPEMENYTKTKKMCVQHFPSDKSCDSPASSHGSMLDSPATPSAALASPAAPAATHSEQAQPLSLTTKPEARALSHSAAFLASKSPSSSSLSGHLPSPVGSPLLSRPIPLTSSILSPPGVFPSALQALPLLQAQPLSLVTRSSD
Protein: Vesicle-associated membrane protein 7 (VAMP-7) (Synaptobrevin-like protein 1) (P70280)
Organism: Mus musculus (Mouse)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane; Single-pass type IV membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane; Single-pass type IV membrane protein. Synapse, synaptosome. Note=In immature neurons expression is localized in vesicular structures in axons and dendrites while in mature neurons it is localized to the somatodendritic region. Colocalizes with LAMP1 in kidney cells. Localization to the endoplasmic reticulum membrane was observed in the intestine but not in liver or kidney (By similarity). {ECO:0000250}.
Interaction partners:
- Synaptosomal-associated protein 23
- Syntaxin-4
- Syntaxin-7
- Synaptosomal-associated protein 29
- Syntaxin-17
- Syntaxin-8
- Vesicle transport through interaction with t-SNAREs homolog 1B
- Ankyrin repeat domain-containing protein 27
- Vesicle transport through interaction with t-SNAREs homolog 1A
- BET1 homolog
Sequence:
MAILFAVVARGTTILAKHAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFSFLNEVKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKHHSENKSLDKVMETQAQVDELKGIMVRNIDLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCMKNIKLTIIIIIVSIVFIYIIVSLLCGGFTWPNCVKK