wanglab/gogpt-training-data huggingface dataset:
Protein: C-X-C motif chemokine 9 (Gamma-interferon-induced monokine) (Monokine induced by interferon-gamma) (MIG) (MuMIG) (Protein m119) (Small-inducible cytokine B9) (P18340)
Organism: Mus musculus (Mouse)
Function: May be a cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response.
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 3
- C-X-C motif chemokine 10
- C-C motif chemokine 5
- C-C chemokine receptor type 5
- Stromal cell-derived factor 1
- C-C motif chemokine 2
- Platelet factor 4
- C-C chemokine receptor type 2
- C-X-C chemokine receptor type 4
- C-X-C motif chemokine 13
Sequence:
MKSAVLFLLGIIFLEQCGVRGTLVIRNARCSCISTSRGTIHYKSLKDLKQFAPSPNCNKTEIIATLKNGDQTCLDPDSANVKKLMKEWEKKISQKKKQKRGKKHQKNMKNRKPKTPQSRRRSRKTT
Protein: ATP synthase F(0) complex subunit k, mitochondrial (ATP synthase membrane subunit DAPIT, mitochondrial) (Diabetes-associated protein in insulin-sensitive tissues) (Up-regulated during skeletal muscle growth protein 5) (Q3ZBI7)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. ATP5MK is a minor subunit of the mitochondrial membrane ATP synthase required for dimerization of the ATP synthase complex and as such regulates ATP synthesis in the mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:17060615}; Single-pass membrane protein {ECO:0000269|PubMed:17060615}.
Interaction partners:
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
Sequence:
MAGPEADAQFHFTGIKKYFNSYTLTGRMNCVLATYGSIALIVLYFKLRSKKTPAVKAT
Protein: Potassium channel Ftrac_2467 (Transmembrane protein 175) (MtTMEM175) (E4TN31)
Organism: Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus)
Function: Potassium channel; forms a potassium-permeable leak-like channel with weak selectivity for potassium. The channel is permeable for K(+), Rb(+) and Cs(+).
Subcellular location: Cell membrane {ECO:0000269|PubMed:32267231}; Multi-pass membrane protein {ECO:0000269|PubMed:32267231}.
Interaction partners:
Sequence:
MRKVFETVVGLNPNFSFRGKQQTRIETFSDAVFALAITLLVLSSTIPETFEDLWASMRDVIPFAICVALIIVIWYQHYIFFLKYGLQDKVTILLNTILLFVLLVYVYPLKFLARFLSEIYGGIFGIIETDLSRFGEYSHQNLKLLMVNYGLGAFAIFLVFSLMYWRAYKMKSLLDLNSYEIFDTKSSIIANLLMCSVPLLSLIITLIDPWGNFRTTILSGFLYFLYVPIMIVFGRITSKKSRRLLQD
Protein: Sodium/potassium exporting P-type ATPase 2 (EC 7.2.2.3) (Q01896)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of sodium or lithiums ions to allow salt tolerance.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7664728}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7664728}.
Interaction partners:
Sequence:
MSEGTVKENNNEEFNAYHTLTTEEAAEFIGTSLTEGLTQDESLRRLKAVGENTLGDDTKIDYKAMVLHQVCNAMIMVLVISMAISFAVRDWITGGVISFVIAVNVLIGLVQEYKATKTMNSLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLTGESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSLQGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAIIVMASQKFDVDKRVAIYAICVALSMIPSSLVVVLTITMSVGAAVMVSRNVIVRKLDSLEALGAVNDICSDKTGTLTQGKMLARQIWIPRFGTITISNSDDPFNPNEGNVSLIPRFSPYEYSHNEDGDVGILQNFKDRLYEKDLPEDIDMDLFQKWLETATLANIATVFKDDATDCWKAHGDPTEIAIQVFATKMDLPHNALTGEKSTNQSNENDQSSLSQHNEKPGSAQFEHIAEFPFDSTVKRMSSVYYNNHNETYNIYGKGAFESIISCCSSWYGKDGVKITPLTDCDVETIRKNVYSLSNEGLRVLGFASKSFTKDQVNDDQLKNITSNRATAESDLVFLGLIGIYDPPRNETAGAVKKFHQAGINVHMLTGDFVGTAKAIAQEVGILPTNLYHYSQEIVDSMVMTGSQFDGLSEEEVDDLPVLPLVIARCSPQTKVRMIEALHRRKKFCAMTGDGVNDSPSLKMANVGIAMGINGSDVSKEASDIVLSDDNFASILNAVEEGRRMTDNIQKFVLQLLAENVAQALYLIIGLVFRDENGKSVFPLSPVEVLWIIVVTSCFPAMGLGLEKAAPDLMDRPPHDSEVGIFTWEVIIDTFAYGIIMTGSCMASFTGSLYGINSGRLGHDCDGTYNSSCRDVYRSRSAAFATMTWCALILAWEVVDMRRSFFRMHPDTDSPVKEFFRSIWGNQFLFWSIIFGFVSAFPVVYIPVINDKVFLHKPIGAEWGLAIAFTIAFWIGAELYKCGKRRYFKTQRAHNPENDLESNNKRDPFEAYSTSTTIHTEVNIGIKQ
Protein: Big bang, isoform F (Big bang, isoform G) (Big bang, isoform H) (PDZ domain-containing protein BBG-LP15 transcript variant bbg-LP13) (PDZ domain-containing protein BBG-LP15 transcript variant bbg-LP15) (PDZ domain-containing protein BBG-LP15 transcript variant bbg-LP18) (Q17Q80)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MELLSSNTGTTTTTTTATHHLHQATTTKQLLVQDYLSYASPPTYSRLPPDGHEFPPNFSEPLIMHSHPLKVTTELSYEIQKGGKDESSAPPLPKTGPPATVPRKVYRQDLVINVEPAPSLTRDYQRSLSGGTPRKPSDWRKDEKSEKSVRDKIAMFSSNNELDAIPPAPATAPISSSFTRKPLNRSSENLLDSCSSSSAPSLKTRAMSVENLNDVQRQYQLAKQLPQLHVADSMYSLNTATPTPSYASLPRRSHGGSYSSGVERRISFSGEGGDAANRKAAITNILEQRRRSLSKLRGLVIPERPQLLEPILDLPEIKSQVKAASGEDSTDSGLGESHRSTVNRNCQLGAGGAANNYRSILNTNQRRPLEQQLSQPPAKPPRTSLTPLQPRSMMIPPPPPPLDQESDTDSVFSHTARVATPPEKFALTRTLSSETNTSIASSNTSTLTSGSSAGSQASCSSLGSTPAVDLTRRVLKSQVINGEAVALSSRKSILASAKCRSAKSRGQEEDNDSTDGEACSLANRRMKPISSYKLQQQQIQLGKQLVVDKLINVAAYVELTSDTDDSSRRSDTPAKISAMFIDEERKASFKGDPNQQAKVKVEQVKPMVLPMLLPSAKREPLKQQTTAELREKFERSAAAQAQTQNHSPVIHKVTQKPHHERFSSLDSLASSSSGVSSTTQNVSTTQETATEFGSFSSLGSNQSLITAQDVQQIVEEADPPLKTPEAFIIVLQRENPESSIGITLAGGSDYEAKEITIHKILSNTPAAKDGRLKKGDRILAVNGMSMRGLTHRESISVLKTPRPEVVLVVTRSESLVVKALTKKRSSLGSLSSLNEKPTELDYERKRNYHKASRSLDLDLDLVSNEAGESPVATTPSTGSVSPPQPASLHDEDAEATIAGIRARRQLSRGDAAKLSTSELLERAAEARNAIAAEIRAQAEDAAASGGGARCVEIVKDSCGLGFSIEGGFDSPLGNRPLIVKKVFMGGAAQKTNQVRNGDEILSINGASTSRMTRVDAWNYMKQLPLGPVKICFA
Protein: Voltage-dependent calcium channel gamma-4 subunit (Neuronal voltage-gated calcium channel gamma-4 subunit) (Transmembrane AMPAR regulatory protein gamma-4) (TARP gamma-4) (Q9UBN1)
Organism: Homo sapiens (Human)
Function: Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit. Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs), including GRIA1 and GRIA4. Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization and by mediating their resensitization.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21127204}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent calcium channel gamma-7 subunit
- Voltage-dependent calcium channel subunit alpha-2/delta-4
- Voltage-dependent L-type calcium channel subunit beta-4
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent L-type calcium channel subunit alpha-1F
Sequence:
MVRCDRGLQMLLTTAGAFAAFSLMAIAIGTDYWLYSSAHICNGTNLTMDDGPPPRRARGDLTHSGLWRVCCIEGIYKGHCFRINHFPEDNDYDHDSSEYLLRIVRASSVFPILSTILLLLGGLCIGAGRIYSRKNNIVLSAGILFVAAGLSNIIGIIVYISSNTGDPSDKRDEDKKNHYNYGWSFYFGALSFIVAETVGVLAVNIYIEKNKELRFKTKREFLKASSSSPYARMPSYRYRRRRSRSSSRSTEASPSRDVSPMGLKITGAIPMGELSMYTLSREPLKVTTAASYSPDQEASFLQVHDFFQQDLKEGFHVSMLNRRTTPV
Protein: Small ribosomal subunit protein uS17 (40S ribosomal protein S11) (P62280)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein eS10
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL36
- Elongation factor Tu, mitochondrial
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL30
Sequence:
MADIQTERAYQKQPTIFQNKKRVLLGETGKEKLPRYYKNIGLGFKTPKEAIEGTYIDKKCPFTGNVSIRGRILSGVVTKMKMQRTIVIRRDYLHYIRKYNRFEKRHKNMSVHLSPCFRDVQIGDIVTVGECRPLSKTVRFNVLKVTKAAGTKKQFQKF
Protein: Cytochrome P450 4F11 (CYPIVF11) (EC 1.14.14.1) (3-hydroxy fatty acids omega-hydroxylase CYP4F11) (Docosahexaenoic acid omega-hydroxylase) (EC 1.14.14.79) (Long-chain fatty acid omega-monooxygenase) (EC 1.14.14.80) (Phylloquinone omega-hydroxylase CYP4F11) (EC 1.14.14.78) (Q9HBI6)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives (oxylipins). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes with high efficiency the oxidation of the terminal carbon (omega-oxidation) of 3-hydroxy fatty acids, such as 3-hydroxyhexadecanoic and 3-hydroxyoctadecanoic acids, likely participating in the biosynthesis of long-chain 3-hydroxydicarboxylic acids. Omega-hydroxylates and inactivates phylloquinone (vitamin K1), and menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in blood coagulation. Metabolizes with low efficiciency fatty acids, including (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) and its oxygenated metabolite 8-hydroxyeicosatetraenoic acid (8-HETE). Catalyzes N- and O-demethylation of drugs such as erythromycin, benzphetamine, ethylmorphine, chlorpromazine, imipramine and verapamil.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18065749}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000269|PubMed:18065749}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- NADPH--cytochrome P450 reductase
- NADPH-dependent diflavin oxidoreductase 1
- Methionine synthase reductase
Sequence:
MPQLSLSWLGLGPVAASPWLLLLLVGGSWLLARVLAWTYTFYDNCRRLQCFPQPPKQNWFWGHQGLVTPTEEGMKTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVEKRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRRKPELILRAEGGLWLRVEPLGANSQ
Protein: SH3 and PX domain-containing protein 2B (Adapter protein HOFI) (Factor for adipocyte differentiation 49) (Tyrosine kinase substrate with four SH3 domains) (A1X283)
Organism: Homo sapiens (Human)
Function: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell projection, podosome {ECO:0000250}. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. {ECO:0000250}.
Interaction partners:
- Src substrate cortactin
- Hematopoietic lineage cell-specific protein
- Disintegrin and metalloproteinase domain-containing protein 15
- NADPH oxidase 1
- Matrix metalloproteinase-14
- Proto-oncogene tyrosine-protein kinase Src
- Actin nucleation-promoting factor WAS
- NADPH oxidase activator 1
- NADPH oxidase 3
Sequence:
MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGSTEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGGDQTSVDPMVLEQYVVVANYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVIQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKPGPGSPSHPGALDLDGVSRQQNAVGREKELLSSQRDGRFEGRPVPDGDAKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKNLSGWWYIQIEDKEGWAPATFIDKYKKTSNASRPNFLAPLPHEVTQLRLGEAAALENNTGSEATGPSRPLPDAPHGVMDSGLPWSKDWKGSKDVLRKASSDMSASAGYEEISDPDMEEKPSLPPRKESIIKSEGELLERERERQRTEQLRGPTPKPPGVILPMMPAKHIPPARDSRRPEPKPDKSRLFQLKNDMGLECGHKVLAKEVKKPNLRPISKSKTDLPEEKPDATPQNPFLKSRPQVRPKPAPSPKTEPPQGEDQVDICNLRSKLRPAKSQDKSLLDGEGPQAVGGQDVAFSRSFLPGEGPGRAQDRTGKQDGLSPKEISCRAPPRPAKTTDPVSKSVPVPLQEAPQQRPVVPPRRPPPPKKTSSSSRPLPEVRGPQCEGHESRAAPTPGRALLVPPKAKPFLSNSLGGQDDTRGKGSLGPWGTGKIGENREKAAAASVPNADGLKDSLYVAVADFEGDKDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP
Protein: FERM and PDZ domain-containing protein 2 (PDZ domain-containing protein 4) (PDZ domain-containing protein 5C) (Q68DX3)
Organism: Homo sapiens (Human)
Function: May play a role in the regulation of tight junction formation. Binds phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2).
Subcellular location: Cytoplasm {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:19706687, ECO:0000269|PubMed:23213202}. Cell junction, tight junction {ECO:0000269|PubMed:19706687}. Postsynaptic density {ECO:0000250|UniProtKB:A0A140LI67}. Note=Colocalizes with CTNNB1, CDH1 and PKP4 at the basolateral membrane. Colocalizes with TJP1 at tight junctions. Its recruitment to cell-cell contacts requires CDH1. Colocalizes with NOD2 to the basolacteral membrane in intestinal epithelial cells (PubMed:23213202). {ECO:0000269|PubMed:23213202}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 20
- Plakophilin-4
- Armadillo repeat protein deleted in velo-cardio-facial syndrome
- Catenin delta-2
Sequence:
MQPLTKDAGMSLSSVTLASALQVRGEALSEEEIWSLLFLAAEQLLEDLRNDSSDYVVCPWSALLSAAGSLSFQGRVSHIEAAPFKAPELLQGQSEDEQPDASQMHVYSLGMTLYWSAGFHVPPHQPLQLCEPLHSILLTMCEDQPHRRCTLQSVLEACRVHEKEVSVYPAPAGLHIRRLVGLVLGTISEVEKRVVEESSSVQQNRSYLLRKRLRGTSSESPAAQAPECLHPCRVSERSTETQSSPEPHWSTLTHSHCSLLVNRALPGADPQDQQAGRRLSSGSVHSAADSSWPTTPSQRGFLQRRSKFSRPEFILLAGEAPMTLHLPGSVVTKKGKSYLALRDLCVVLLNGQHLEVKCDVESTVGAVFNAVTSFANLEELTYFGLAYMKSKEFFFLDSETRLCKIAPEGWREQPQKTSMNTFTLFLRIKFFVSHYGLLQHSLTRHQFYLQLRKDILEERLYCNEEILLQLGVLALQAEFGNYPKEQVESKPYFHVEDYIPASLIERMTALRVQVEVSEMHRLSSALWGEDAELKFLRVTQQLPEYGVLVHQVFSEKRRPEEEMALGICAKGVIVYEVKNNSRIAMLRFQWRETGKISTYQKKFTITSSVTGKKHTFVTDSAKTSKYLLDLCSAQHGFNAQMGSGQPSHVLFDHDKFVQMANLSPAHQARSKPLIWIQRLSCSENELFVSRLQGAAGGLLSTSMDNFNVDGSKEAGAEGIGRSPCTGREQLKSACVIQKPMTWDSLSGPPVQSMHAGSKNNRRKSFIAEPGREIVRVTLKRDPHRGFGFVINEGEYSGQADPGIFISSIIPGGPAEKAKTIKPGGQILALNHISLEGFTFNMAVRMIQNSPDNIELIISQSKGVGGNNPDEEKNSTANSGVSSTDILSFGYQGSLLSHTQDQDRNTEELDMAGVQSLVPRLRHQLSFLPLKGAGSSCPPSPPEISAGEIYFVELVKEDGTLGFSVTGGINTSVPYGGIYVKSIVPGGPAAKEGQILQGDRLLQVDGVILCGLTHKQAVQCLTGPGQVARLVLERRVPRSTQQCPSANDSMGDERTAVSLVTALPGRPSSCVSVTDGPKFEVKLKKNANGLGFSFVQMEKESCSHLKSDLVRIKRLFPGQPAEENGAIAAGDIILAVNGRSTEGLIFQEVLHLLRGAPQEVTLLLCRPPPGALPELEQEWQTPELSADKEFTRATCTDSCTSPILDQEDSWRDSASPDAGEGLGLRPESSQKAIREAQWGQNRERPWASSLTHSPESHPHLCKLHQERDESTLATSLEKDVRQNCYSVCDIMRLGRYSFSSPLTRLSTDIF
Protein: Endolysin LysGH15 (D-alanyl-glycyl endopeptidase) (EC 3.4.22.-) (N-acetylmuramoyl-L-alanine amidase) (EC 3.5.1.28) (D6QY02)
Organism: Staphylococcus phage G15
Interaction partners:
Sequence:
MAKTQAEINKRLDAYAKGTVDSPYRIKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYQQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASKTPAPKKKATLKVSKNHINYTMDKRGKKPEGMVIHNDAGRSSGQQYENSLANAGYARYANGIAHYYGSEGYVWEAIDAKNQIAWHTGDGTGANSGNFRFAGIEVCQSMSASDAQFLKNEQAVFQFTAEKFKEWGLTPNRKTVRLHMEFVPTACPHRSMVLHTGFNPVTQGRPSQAIMNKLKDYFIKQIKNYMDKGTSSSTVVKDGKTSSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGDRVYCPVRTCQGVPPNHIPGVAWGVFK
Protein: Squalene synthase 11 (PgSS11) (SQS 11) (EC 2.5.1.21) (FPP:FPP farnesyltransferase SS11) (Farnesyl-diphosphate farnesyltransferase SS11) (A0A1P7Y0D4)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Catalyzes the biosynthesis of squalene (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGSLGAILKHPEDFYPLLKLKIAARHAEKQIPSEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSISTEVKVPILMAFHRHIYDNDWHFSCGTKEYKVLMDEFHHVSNAFLDLGSGYKEAIEDITMRMGAGMAKFICKEVETIDDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAKVIDQTKTMSDVYGAFFDFSCLLKSKVDNNDPNATKTLSRLEAIQKICKNSGALTTKRKSYIIENESGYNSTLIIILFIILAILYAYLSSNLPNSL
Protein: DNA-binding response regulator (A0A0H2UNK2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MGKRILLLEKERNLAHFLSLELQKEQYRVDLVEEGQKALSMALQTDYDLMLLNVNLGDMMAQDFAEKLSRTKPASVIMILDHWEDLQEELEVVQRFAVSYIYKPVLIENLVARISAIFRGRDFIDQHCSLMKVPRTYRNLRIDVEHHTVYRGEEMIALTRREYDLLATLMGSKKVLTREQLLESVWKYESATETNIVDVYIRYLRSKLDVKGQKSYIKTVRGVGYTMQE
Protein: Uncharacterized protein At5g24710 (Q0WLS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLRARAFRQTNGKIVKIQVHPTHPWLVTADDSDHVSVWNWEHRQVIYELKAGGVDERRLVGAKLEKLAEGESDYKAKPTEAIRGGSVKQVKFYDDDVRYWQLWRNRSAAAESPSAVNHLTSAFTSPAPSTKGRHFLVICCENKAIFLDLVTMRGRDVPKQELDNKSLLCMEFLSRSSGGDGPLVAFDSTDGVIRVLSMITWKLARRYTGGHKGSIYCLMNFMASSGEALLVSGGSDGLLVLWSADHGADSRELVPKLSLKAHDGGVVAVELSRVSGSAPQLITIGADKTLAIWDTMTFKELRRIKPVPKLACHSVASWCHPRAPNLDILTCVKDSHIWSIEHPTYSALTRPLCELSSLVPPQVLATHRKLRVYCMVAHPLQPHLVATGTNVGIIVSEFDPRAIPSAAPLPALPGSRENSAIYILGRELKLLNFQLSNTANPSLGNNSALSESGLSKGDPGEQLTVKQTKKQIVAPVPHDSYSVLSVSSSGKYVAVVWPDILYFSIYKVSDWSIVDSGSARLLAWDTCRDRFAILESVLPHRMPIIPKGGSSRKAKEAAAAAAQAAAAASAASSASVQVRILLDDGTSNILMRSVGGRSEPVIGLHGGALLGIGYRTSRRISPVAATAISTIQSMPLSGFGNSNVSSFSSYDDGFSSQKSAESAPLNYQLYSWENFEPVGGMLPQPEWTAWDQTVEYCAFAYQQYMVISSLRPQYRYLGDVAIAHATGAVWHRRQLFVATPTTIECVFVDAGVSEIDIETRKMKEEMKLKEAQARAVAEHGELALITVEGSQAAKQERISLRPPMLQVVRLASFQNAPSVPPFLSLPRQSRGDSDDIMDERRVNEVAVGGGGVSVAVTRFPVEQKRPVGPLVVAGVRDGVLWLIDRYMCAHAISLNHPGIRCRCLAAYGDAVSAVKWASRLGREHHDDLAQFMLGMGYATEALHLPGISKRLEFDLAMQSNDLKRALHCLLTMSNSKDIGQDGVGLDLSDILSLTATKKEDVVEAVEGIVKFAKEFLDLIDAADATGHADIAREALKRLATAGSVKGALQGHELRGLSLRLANHGELTRLSGLVNNLISIGLGRESAFSAAVLGDNALMEKAWQDTGMLAEAVLHAHAHGRPTLKNLVQAWNKTLQKEVEKAPSSKTDAASAFLASLEDPKLTSLSDASRKPPIEILPPGMSSIFASITAPKKPLLTQKTAQPEVAKPLALEEPTKPLAIEAPPSSEAPQTESAPETAAAAESPAPETAAVAESPAPGTAAVAEAPASETAAAPVDGPVTETVSEPPPVEKEETSLEEKSDPSSTPNTETATSTENTSQTTTTPESVTTAPPEPITTAPPETVTTTAVRPTENAATERRVTNYPPIRSQPIDFDFLNG
Protein: Transcription factor NIGT1 (MYB-domain transcription factor NIGT1) (Protein NITRATE-INDUCIBLE GARP-TYPE TRANSCRIPTIONAL REPRESSOR 1) (Q6Z869)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcriptional repressor that may play a role in response to nitrogen. May be involved in a time-dependent signaling for transcriptional regulation of nitrate-responsive genes. Binds specifically to the DNA sequence motif 5'-GAATC-3' or 5'-GAATATTC-3'. Represses the activity of its own promoter trough binding to these motifs.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:23324170}.
Interaction partners:
Sequence:
MEVDHADRDGARRRCREYLLALEEERRKIQVFQRELPLCFDLVTQTIEGMRSQMDAAGSEETVSDQGPPPVLEEFIPLKPSLSLSSSEEESTHADAAKSGKKEEAETSERHSSPPPPPPEAKKVTPDWLQSVQLWSQEEPQQPSSPSPTPTKDLPCKPVALNARKAGGAFQPFEKEKRAELPASSTTAAASSTVVGDSGDKPTDDDTEKHMETDKDNDKDAKDKDKEGQSQPHRKPRRCWAPELHRRFLQALQQLGGSHVATPKQIRELMKVDGLTNDEVKSHLQKYRLHTRRPSSTGQSSAAAGVPAPPAPQFVVVGSIWVPPPEYAAAAAAQQHVQLAAAGNNASGSANPVYAPVAMLPAGLQPHSHRKQHQQQQQGQRHSGSEGRRSGDAGDGSSSSPAVSSSSQTTSA
Protein: UBA domain-containing protein (P90879)
Organism: Caenorhabditis elegans
Interaction partners:
- Ubiquitin conjugation factor E4 ufd-2
- Ubiquitin-ribosomal protein eL40 fusion protein
- 26S proteasome non-ATPase regulatory subunit 4
- Proteasomal ubiquitin receptor ADRM1 homolog
- Ubiquitin-like domain-containing protein
- 26S proteasome regulatory subunit 7
- Uncharacterized protein ZK688.5
- 26S proteasome non-ATPase regulatory subunit 13
- Ubiquilin
- Uncharacterized protein B0303.4
Sequence:
MVKLHLKTTCREVPIEEIISTGQIQFFKHLSESTSEFKDQKNVERFRLIYNGRALNEESLKKITDADSIRVVLLPPLKTNNHIEEEQKNRISIALKECTAPYTRPNDRRLHGFNHDFALPDHMTTLLEKHPQLVHDNQFLSVLSDWSLFRAYCVQNDFKDDPIRGQFMYTNPDFLKVVENILSTVGSRYGYENLDYANVERNRPGMLAAQRPIGGAQPVTHALLQNALQAALANIAVPPANRVPAPANVQPAQQQQEEPMQQGYEQQAATLREFGFENDELIQLALEQANGDVQAAMEFLIDLQN
Protein: Maestro heat-like repeat family member 4 (E9PZ22)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MILRECPSVEKVQCHLASLLDLSHQHSRQREGIALAVGLASTKHLEEVWALLEHLGRTKFLQSVAATEDSQDEILKSSFLSATILLTRSLQAEYSSQRYKFTQTPELIQCLLGILQKEPNSLTNFLRQKIILVIIGLSNLRPRFKPLLKSQILKTCLQTVYMLPPAKDSRNDLFSVEQASDTTVLYKKTVRALDLLLQNFISENPSMDEVCFLLQHIEYWLMSDKIHERSRAVQSIYLLLQYVVDSLKLAKEAVPSLLGHQIGILILLWRDKDKITQQHSHFCVYLLMELVFQQKGKLVESAQWSKMKHFESNVFREWEMKLYHLVKVFKEDLTVAQHTQLILTLVHSLGSYNHLHSDLAAKLLLLICVEPGFRKEQIAELLQGLFQELPNIQSKSVQQAISQATLALGTQHIQEVVEVILSLCQPSERWILPLWKALAANYQVARDVITLLYIKLKLRPPRRLLQSTYRARLVSLMALGTIYELLYTKEYRNTVCWAFSGILLGLLTELYYLLEVGLVQGLFDYQEDDLGSKPLGPCRICLEALKGLFWTTEYWEVFADVKLIQGWELFGQLETFPKGVTLLARAMAHYNCEIKAVLGQALISLKSSEERDNIVGICIITEFLNSPDVSQHMSWKTMYNSLNLGLSSRNQMVRAMSLKGLGSTLMHPKKATLLRSKLMELLDNFLQPEFKDPAGLMKIMGHLLHCLSAQGIGIVSLKIAQHLLSLFTDERAAVREGAIFLFGDVIHYGGKKLRQSLKDVASQATVPLLFNMADPCQEVAMKARFTFLRCAILLKWEFRKELFGKLAWGQGLGAANDIFIYMLESNVGNYQQFLSQALTYLDSSHMTVKLAAMKFIGALLQDYFNDLCIYLRKKDVIFLKNCLEALRHDTDSRTRRFYLNYWNDAVELSYYVQD
Protein: Exonuclease domain-containing protein (Q580W2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGACEASFPPEFLHFPPVSILICICFLFSLFFLRKLQIHLVMFLSMFFFKSVINNNNNNYYYYYCVTYSAYRNMSPHNKRSMEQKKRNKDRIAAYHGQRVNSHGGHRNSHSHSGHRHRGGHTVRRNRIYDPGNPFDRQLFDYLIVVDVEATCEYKNDNYPHEIIELPGVLVDVRRGVVDKERSFRSYVRPQRNPLLTPFCKALTGITQEDVDSAPTLQEVVKLFEQWYTETIPRGAKVALATDGPWDLKNFVHEHSILRDHISFPTIFYEYLDIRTTFAHFFNRGTPLKLVPMLERLQLTFEGREHCGFDDAVNIARLAVSMMRAGCVFNYLVAIPLTDEFHYDMPNTALYRRKEGSGYLDPDVVDDIAKKCFGVDYFTFGERHMAEVMEHRRRYPQNFNQRNQLWKQTKMKNRGRRLYGVRFRMVAVAVLALLGLVLFLLLIYRKVMTLL
Protein: Chorion class B protein ERB4 (Chorion class B protein 6A2) (Q17217)
Organism: Bombyx mori (Silk moth)
Function: This protein is one of many from the eggshell of the silk moth.
Interaction partners:
Sequence:
MSSNVIVLCVSALFIQCAVSQCVGRIGSLRGGPFDGWGYDGLGYDGFGIGGWNGRGCGGLGDDIAAAAALGASHGGTLAVVSTSAAPTGLGIASENVYEGSVGVCGNLPFLGTADVAGEFPTAGLGGIDYTCGDGAVGITVENAINGISNVGYGLAPGIVGPAVAAPALGYGPGISSLGYNTAGRGCGCGANYY
Protein: PWWP domain containing 3A, DNA repair factor (J3KNX4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMADAKYVLCRWEKRLWPAKVLARTATSTKNKRRKEYFLAVQILSLEEKIKVKSTEVEILEKSQIEAIASSLASQNEVPAAPLEELAYRRSLRVALDVLSEGSIWSQESSAGTGRADRSLRGKPMEHVSSPCDSNSSSLPRGDVLGSSRPHRRRPCVQQSLSSSFTCEKDPECKVDHKKGLRKSENPRGPLVLPAGGGAQDESGSRIHHKNWTLASKRGGNSAQKASLCLNGSSLSEDDTERDMGSKGGSWAAPSLPSGVREDDPCANAEGHDPGLPLGSLTAPPAPEPSACSEPGECPAKKRPRLDGSQRPPAVQLEPMAAGAAPSPGPGPGPRESVTPRSTARLGPPPSHASADATRCLPCPDSQKLEKECQSSEESMGSNSMRSILEEDEEDEEPPRVLLYHEPRSFEVGMLVWHKHKKYPFWPAVVKSVRQRDKKASVLYIEGHMNPKMKGFTVSLKSLKHFDCKEKQTLLNQAREDFNQDIGWCVSLITDYRVRLGCGSFAGSFLEYYAADISYPVRKSIQQDVLGTKLPQLSKGSPEEPVVGCPLGQRQPCRKMLPDRSRAARDRANQKLVEYIVKAKGAESHLRAILKSRKPSRWLQTFLSSSQYVTCVETYLEDEGQLDLVVKYLQGVYQEVGAKVLQRTNGDRIRFILDVLLPEAIICAISAVDEVDYKTAEEKYIKGPSLSYREKEIFDNQLLEERNRRRR