wanglab/gogpt-training-data huggingface dataset:
Protein: NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 5) (NADH-plastoquinone oxidoreductase subunit 5) (P56752)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- Photosystem I iron-sulfur center
Sequence:
MEHTYQYSWIIPFIPLPVPILLGVGLLLFPTATKNLRRMWTFLSIFLLSIVMIFSIYLSIQQIFLSCIHQNVWSWTINNEFSFEFGYFIDPLTSIMSILITTVGILVLIYSDNYMSHDQGYLRFFAYMGFFNTSMLGLVTSSNLIQVYFFWELVGMCSYLLIGFWFTRPIAANACQKAFVTNRVGDFGLLLGILGLYWITGSFEFQDLFEIFNNLILNNRVNLLFLTLCAFLLFVGPIAKSAQFPLHVWLPDAMEGPTPISALIHAATMVAAGIFLVARLLPLFIVIPSIMYIISLIGIITVLLGATLALAQKDIKRGLAYSTMSQLGYMMLALGMGSYRSALFHLITHAYSKALLFLGSGSIIHSMEAIVGYSPDKSQNMILMGGLTKHVPITKTAFLIGTLSLCGIPPLACFWSKDEILNDSLLFSPIFAIIACSTAGLTAFYMFRIYLLTFEGHLNTYFLNYSGKKSGSFYSLSLWGKEEEKKLNKNFGLVPLLTMNNTKRASFFCNKTYKISNNVRNQIFITVENFGLNTRTFYYPHESDNTILFPMLILVLFTLFIGAIGIPFNQEGIDFDILSKFFTPSINLLHKNSQNFVDWYEFLRNATFSVSIAFFGIFIAYCLYKPFYSSLLNLTLLNSFQKWNSKRIHWEKLINFVYNWSYNRGYIDSFFKTSLIESIRRLAKQTTFFDKRIIDGITNGVGITSFFVGEVTKYIGGSRISSYLFLYLSYVLIFLMILFFFYFEKF
Protein: RE37651p (Q8SYS5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00025701}; Lipid-anchor {ECO:0000256|ARBA:ARBA00025701}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00025701}.
Interaction partners:
Sequence:
MVEPIFEYQFRLILIGDSTVGKSSLLKFFTDGKFAELSDPTVGVDFFARLIEMKDGTQIKLQLWDTAGQERFRSITKSYYRNSVGVLLVYDISNHASFEHIPLWMMEAQRHIEPHRSVFALVGCKLDLINAGGHREVTTEEAQKFAKQHGLHFVETSARSGANVEEAFRMVTQEVYARIRSGEYKAEDGWDGIKSGFSRPNSLDFNLVVAEPEKSSCC
Protein: Chromosome segregation protein sudA (DA-box protein sudA) (Q00737)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in chromosome segregation in mitosis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Chromosome segregation protein sudA
- Double-strand-break repair protein rad21
- Nuclear cohesin complex subunit
- Sister chromatid cohesion acetyltransferase Eco1, putative
- Sister chromatid cohesion protein
- DNA polymerase eta
- BimD protein
- Rad21/Rec8 N terminal domain protein
- Separin
- Polo-like kinase
Sequence:
MYVKQIIIQGFKSYKDQTVIEPFSPKHNVIVGRNGSGKSNFFAAIRFVLSDAYTHLGREERQALLHEGSGSAVMSAYVEIIFDNSDERFPTGKPELVLRRTIGLKKDEYTLDRKNATKNDVMNLLESAGFSRSNPYYIVPQGRVTALTNMKDSERLNLLKEVAGTQVYEARRAESLKIMHETNSKREKIDELLDFINERLAELEEEKDELRNFQEKDKERRCLEYTIYSREQQEIASFLDSLEEQRQTGVEDTDINRDRFIQGEKEMAQVDAEIAECKQQIEFLKVDKAQLEDERREASKALAQVELQAKSLSDNQAAAQESKARHDESLKAVQSAIEERQTELKELVPRFISAKDAEDAARAKLTEAETARQRLYAKQGRNSRFKNKSERDKWLQAEIKNNNASISSVQSVLSQTQEDINDIENDIALLEPETERLRQQIDGRGDTIQSVEQQVQAAKDERDRLMDQRKYVDWPRTSCATLTIHRELWREEAKLDSILINASNEVDRAERNLSQMMDHNTSRGIAAVRRIKRQHNLEGVYGTLAELFEVNDRYRTAVEVTAGQSLFHYVVDTDDTATKVLEILQHEKAGRVTFMPLNRLRTKPLNMPKASDTIPMIEKLQYDRAYEKAFQHVFGKTIICPNLQVASQYARSHGVNATTPEGDRSDKRGALTGGFHDSRQSRLDAVKNLAKWRDEYETKKSRGSEIRKELEELDQLITRAVGELQKLEQQRHQVQNSSGPLRQELRSKRDLLQKQNDNLDAKRRALRNIEGNLAALKDQVDAFEAELSSPFHKALTDEEEARLESLNSNVQEYRREYQELSGKRSELETRKSVLEVELRENLNPRLDQLLAQDADIADEDGQGNIKETQREQKRLTKVLDKLAQRLAQVDESMEQANSRVTELTQRNAESRRELEELAKSIEKHQRRMEKSMQKKAALTKQAAECAANIRDLGVLPDEAFTKYKNTDSNTVVKKLHKVNEALKKYAHVNKKAFEQYNNFTKQRETLTSRREELDASQKSIDDLISVLDHRKDEAIERTFKQVSREFATIFEKLVPAGRGRLIIQRKTDRTQRAEDDLESEDEEAKHSVENYVGVGISVSFNSKHDDQQRIQQLSGGQKSLCALALVFAIQACDPAPFYLFDEIDANLDAQYRTAVAQMLKTISDSTNGQFICTTFRPEMLHVAEKCYGVSFRQKASTIDVVSREEALKFVEEQKS
Protein: At5g46230 (Q9FL37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3g07470/F21O3_18
Sequence:
MSSQETKSDQREGAEICNGESNCKQKAKEILSTMNLPKGLLPLDNMTEIGHNKSTGYVWIKIKNKVQHRFKAIGRNVSYDSEVTAILENRRMSQLTGIKSKEILIWVTISEIFVNHQDPTQITFANPTGLSRTFPVTAFEEDE
Protein: Potassium channel subfamily K member 18 (Two-pore-domain potassium channel TRESK) (Q6VV64)
Organism: Mus musculus (Mouse)
Function: Outward rectifying potassium channel. Produces rapidly activating outward rectifier K(+) currents. May function as background potassium channel that sets the resting membrane potential. Channel activity is directly activated by calcium signal. Activated by the G(q)-protein coupled receptor pathway. The calcium signal robustly activates the channel via calcineurin, whereas the anchoring of 14-3-3/YWHAH interferes with the return of the current to the resting state after activation. Inhibited also by arachidonic acid and other naturally occurring unsaturated free fatty acids. Channel activity is also enhanced by volatile anesthetics, such as isoflurane. Appears to be the primary target of hydroxy-alpha-sanshool, an ingredient of Schezuan pepper. May be involved in the somatosensory function with special respect to pain sensation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20006580}; Multi-pass membrane protein {ECO:0000269|PubMed:20006580}.
Interaction partners:
- Potassium channel subfamily K member 3 channel) channel 1)
- MNTK1
- Potassium channel subfamily K member 10
- Potassium channel subfamily K member 7
- Potassium channel subfamily K member 9 channel 3)
- Potassium channel subfamily K member 13
- Potassium channel TASK2
- Potassium channel subfamily K member 1
Sequence:
MEAEEPPEARRCCPEALGKARGCCPEALGKLLPGLCFLCCLVTYALVGAALFSAVEGRPDPEAEENPELKKFLDDLCNILKCNLTVVEGSRKNLCEHLQHLKPQWLKAPQDWSFLSALFFCCTVFSTVGYGHMYPVTRLGKFLCMLYALFGIPLMFLVLTDIGDILATILSRAYSRFQALLCLPHDIFKWRSLPLCRKQPDSKPVEEAIPQIVIDAGVDELLNPQPSKDPPSPSCNVELFERLVAREKKNKLQPPTRPVERSNSCPELVLGRLSCSILSNLDEVGQQVERLDIPLPVIALVVFAYISCAAAILPFWETELGFEDAFYFCFVTLTTIGFGDIVLVHPHFFLFFSIYIIVGMEILFIAFKLMQNRLLHTYKTLMLFVCQREVSLPW
Protein: Endopolygalacturonase A (EC 3.2.1.15) (Pectinase A) (Polygalacturonase A) (Q9P358)
Organism: Aspergillus awamori (Black koji mold)
Function: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MPSAKPLFCLATLAGAALAAPAPSRATDFNKRSTCTFTDAATASESKTSCSDIVLKDITVPAGETLNLKDLNDGTTVTFEGTTTWEYEEWDGPLLRISGKDITVTQSSDAVLNGNGAKWWDGEGTNGGKTKPKFFYAHDLDDSKISGLYIKNTPVQAISVESDNLVIEDVTIDNSDGDSEGGHNTDGFDISESTYITITGATVKNQGDCVAINSGENIYFSGGTCSGGHGLSIGSVGGRDDNTVKNVTFIDSTVSDSENGVRIKTVYDATGTVEDITYSNIQLSGISDYGIVIEQDYENGDPTGTPSNGVTISDVTLEDITGSVDSDAVEIYILCGDGSCTDWTMSGIDITGGETSSDCENVPSGASCSQ
Protein: Molybdopterin synthase sulfur carrier subunit (Molybdenum cofactor synthesis protein 2 small subunit) (Molybdenum cofactor synthesis protein 2A) (MOCS2A) (Sulfur carrier protein MOCS2A) (Q9Z224)
Organism: Mus musculus (Mouse)
Function: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03051}.
Interaction partners:
Sequence:
MVPRCQIDVLYFAKSAEIAGVRSETISVPQEIKASELWKELEMLHPGLADVRNQVIFAVRQEYVELGDQQLLLQPGDEVAIIPPISGG
Protein: SH3 domain-containing protein (F4IL68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein SGT1 homolog B
- Protein SGT1 homolog A
- Peptidyl-prolyl cis-trans isomerase CYP40
- Co-chaperone protein p23-2
- Co-chaperone protein p23-1
- Heat shock 70 kDa protein 17
- Ankyrin repeat family protein
- Aha1 domain-containing protein
- AT5g58110/k21l19_90
- DNAJ heat shock N-terminal domain-containing protein
Sequence:
MAESSGTTLMDLISADPTPVPAQSTSSSASSTASQPTSASASSSSHLHHPMSTKTTLGEKKSKRATLMQIQNDTISVAKAALNPVKANIMPQRQRQKKKPVSYSQLARSIHELAATLDQKSSQKQLVNHVFPKLAVYNSVDPSLAPSLLMLNQQCEDRNVLRYVYYYLARILSDTGMTPGGGIPTPNWDALADIDAGGGVTRADVVPRIVNQLTNEATNSEFEFHARRLQALKALTYSPSGNSELLSKLYEIVFGILEKVGDVPHKRKKGVFGTKGGDKESIMRSNLQYAAMSALRRLPLDPGNPLFLHRAAQGVFFADPVAVRHSLEILSELATRDPYTVAMTLEKLASPTGALQDILHMNDVLARVSLARLCHSISRARALDERPDIRSQFNSILYQLLLDPSERVCYEAILCILGKHDNTERHEMDERAAGWYRLTREILKLPEAPSLSSKDKSNKTKRPQPLIKLVMRRLESSFRSFSRPVLHAAARVVQEMGKSRAAAFAMGLQDIDESVHVNAFSDALDDAETNESSHPEGIRRTSSISAGPGRSDTIASLLAALMEVVRTTVACECVYVRAMVIKALIWMQSPDESLDELKSIIASELSDPGWPAALVNDVLLTLHARFKATPDMAVILLEIARIFATKVPGKIDADVLQLLWKTCLVGAGPDGKHTALEAVTIVLDLPPPQPGSMAGLTSIDRVSASDPKSALALQKLVQAAVWFLGENANYAASEYAWESATPPGTALMMLDADKMVAAASSRNPTLAGALTRLQRCAFSGSWEVRIVAIQALTTIAIRSGEPFRLQIYEFLYTLAEGGVQSQLSEMHLSNGEDQGASGTGLGVLITPMLKVLDEMYVGQDELIKDIRHHDNANKEWKDEELKKLYENHERLLDFVSMFCFIPRAKYLPLGPISAKLIDTYRTKHNITASTGSTDPAVVATGISDLIYESTQPAPAASNSSGLDDDLVNAWAANLGDDGLLGNNAPAMSRVNEFIAGVGTDAPDVEEENVFSRPSVGYDDMWAKTLLETSELEEEDARSGSSSPDSAGSVESSISSHFGGMNYPSLFSSKPSSQATAKSGGSKYQSTYEGYGSPIREEPPPPYSYSEPQSRESFENPVAGSGSRSYESDDEEPRKSTGTRFGTALYDFTAGGDDELNLTAEEELEIEYEVDGWFYVKKKRPGRDGKMAGLVPVLYVNQS
Protein: DNA polymerase subunit gamma-1 (EC 2.7.7.7) (Mitochondrial DNA polymerase catalytic subunit) (Q92076)
Organism: Gallus gallus (Chicken)
Function: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA (By similarity).
Subcellular location: Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}.
Interaction partners:
- DNA polymerase gamma 2, accessory subunit.
- Uncharacterized protein.
- Twinkle mtDNA helicase
- Single stranded DNA binding protein 1
- DNA-directed RNA polymerase
- DNA polymerase epsilon catalytic subunit
- Deoxycytidine kinase 2
- Mitochondrial inner membrane protein MPV17
- DNA primase
- Uncharacterized protein.
Sequence:
EEGWVPGPSLISLQMRVTPKLMRLAWDGFPLHYSEKHGWGYLVPGRQDNLPAASAEPEGPVCPHRAIERLYRQHCLQRGQEQPPEEAGVEDELMVLEGSSMWQKVEELSQLELDMERPGRAEQSQMQDEDGLPELVEESSQPSFHHGNGPYNDVNIPGCWFFKLPHKDGNENNVGSPFAKDFLPRMEDGTLRAAVGRTHGTRALEINKMVSFWRNAHKRVSSQVVVWLKKGELPRAVTRHPAYSEEEDYGAILPQVVTAGTITRRAVEPTWLTASNARADRVGSELKAMVQVPPGYSLVGADVDSQELWIAAVLGEAHFAGMHGCTAFGWMTLQGKKSDGTDLHSKTAATVGISREHAKVFNYGRIYGAGQPFAERLLMQFNHRLTQQQAREKAQQMYAVTKGIRRFHLSEEGEWLVKELELAVDKAEDGTVSAQDVQKIQREAMRKSRRKKKWDVVAHRMWAGGTESEMFNKLESIALSASPQTPVLGCHISRALEPAVAKGEFLTSRVNWVVQSSAVDYLHLMLVSMKWLFEEYDINGRFCISIHDEVRYLVQEQDRYRAALALQITNLLTRCMFAYKLGLQDLPQSVAFFSAVDIDRCLRKEVTMNCATPSNPTGMEKKYGIPRGEALDIYQIIEITKGSLEKK
Protein: Fibronectin-binding protein BBK32 (O50835)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
Sequence:
MKKVKSKYLALGLLFGFISCDLFIRYEMKEESPGLFDKGNSILETSEESIKKPMNKKGKGKIARKKGKSKVSRKEPYIHSLKRDSANKSNFLQKNVILEEESLKTELLKEQSETRKEKIQKQQDEYKGMTQGSLNSLSGESGELEEPIESNEIDLTIDSDLRPKSSLQGIAGSNSISYTDEIEEEDYDQYYLDEYDEEDEEEIRLSNRYQSYLEGVKYNVDSAIQTITKIYNTYTLFSTKLTQMYSTRLDNFAKAKAKEEAAKFTKEDLEKNFKTLLNYIQVSVKTAANFVYINDTHAKRKLENIEAEIKTLIAKIKEQSNLYEAYKAIVTSILLMRDSLKEVQGIIDKNGVWY
Protein: Rho family GTPase 2 (RhoN) (Q5HZE6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Plexin-B1
- Intersectin 2
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
- Intersectin-1
- Rho GTPase-activating protein 35
- Formin-binding protein 1
Sequence:
MEGQSGRCKIVVVGDAECGKTALLQVFAKDAYPGSYVPTVFENYTASFEIDKRRIELNMWDTSGSSYYDNVRPLAYPDSDAVLICFDISRPETLDSVLKKWQGETQEFCPNAKVVLVGCKLDMRTDLATLRELSKQRLIPVTHEQGTVLAKQVGAVSYVECSSRSSERSVRDVFHVATVASLGRGGHRQLRRTDSRRGLQRSTQLPGRPDRGNEGEIHKDRAKSCNLM
Protein: IPT/TIG domain-containing protein BACOVA_02650 (A7LXT4)
Organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
Function: Polysaccharide-binding protein present at the surface of the cell. Probably mediates xyloglucan-binding before xyloglucan transport in the periplasm for degradation.
Subcellular location: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. {ECO:0000269|PubMed:24463512}.
Interaction partners:
Sequence:
MKSIYKYLDTRLFLIGLLVLPFLAVVSCQNDDDDAIPVIHYIRVTDPAKADSTFTDVNPGTMIVVVGEHLGGTQKVYINDQEVSFNRNYVTSTSIILTVPNELELTGQNPELKGEIRIETEHGVAAYNMHVLSPAPYITRISATYPIKPGDQMTVIGGNFYEVQAVYLSTEQPAKDGTRPVDVQEITNYEVNNKYSQITLTAPANLLEEGYLVVECYTSSAVTEFKKNGPKPVVTAVSSTMPVVGSTVTITGQNFIEVSRVNINGEFDIPVGDITTSNTFDEISFVLPQAPTQSGHISVTAIGGTVESAEIFYPLENVILNYDGIGSHVWGDCSFVVADGSSAPYVSNGTCLGITGTVSASNYWWKQSYSNAQWVNTSIIPGNIPIDDLKLQFECFVKEVFTGPVFQIAMCENFDAALNGYVPVSSFTGKTETGKWMQCSVSLSSVVADATYQDFLNRNSTHIGVYATNPGSSQATIEVYFDNFRIVRK
Protein: Gamma-aminobutyric acid (GABA) B receptor, 1b (Gamma-aminobutyric acid type B receptor subunit 1 isoform X2) (F1QAJ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Gamma-aminobutyric acid
- T-complex protein 1 subunit theta
- Gamma-aminobutyric acid
- Pro-melanin concentrating hormone-like protein
Sequence:
MALSLVLLFLLGSFSLAMASRNITAGCAIIRPPRDGGIRYRGLTQEQIRSVQVLPVDYEIEYICRGSRVIVGPKVRKCLPDGTWTDLNQRSKCLLPCPRVWTSLENGRVTVHPPGPAVEGTILHYSCLEGFILVGRNSTQCNKLGKWDSPKPVCHYDRHYTGKKKLYIGALFPMSGGWPGGQACLPAAQMALDLVNKRTDILPDYELELIHYDSMCDPGEATKLLYDLLYTEPIKIVLMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVQLFQKWKWTKIATIQQTTEVFTSTLDDLEQRVKEAGIEISVRQSFLTDPAVAVKNLKRQDARIIVGLFYETEARKVFCEVYKEKLYGKKYVWFLIGWYADNWFKIKDPSINCTVEQMTEAVEGHVTTEIVMLNPETVRGASNLTSQEFLAQLMSKLGGKNPEETGGFQEAPLAYDAVWALALALNKTVGPLKAKGRRLEDFNYNNKDITAEIYRALNTSSFEGVSGHVVFDAQGSRMAWTLIEQLQGGSYKKIGYYDMTKGNLSWYGNDRWIGSGPPADQTVVIQKFRYLSQKLFVSVSVFAGLGILMGIVCLTFNIYNSNVRYIQNSQPYLNNMTAVGCMMALAAVFPLGIDGLHVRNSQFPVVCQFRLWLLGLGFSLAYGSMFTKIWWVHTVFTKKDEKKDKRKHLEPWKLYATVGVLLVIDILSLMIWQIVDPLHITVEKFTKEAPKGDVDELIEPLLQHCSSEKMNTWLGVVYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVSVLCMITAPVTMILSSKQDASFAFASLAIIFSVYITLVVLFVPKMRRLITRGEWQSDQQETMKTGSSTNNNDEEKSRQLERENKELQKIIQEKEERVSELRNQLSERQALRSRKRPTSNQNHSSPSIPTPQNDPKSLLPPPGYPLPSSDNHSFSNSSPLYQPDGKINRNNCHPGRLQLLYKCQH
Protein: Protection of telomeres 1B (A0A3B2WCG4)
Organism: Mus musculus (Mouse)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}.
Interaction partners:
Sequence:
MSSAPVAPSTYTPLNLLKEGTVVNVCGVVKFFKPPYLSKGTDYCSVVTIVDQTNVKLTCMLFSRDYDTLPSVYKVGDIVCFQGLKIQAYKNELQAISKFGFASLTFDGTLGAPIILRTLSKRFNFTAQDYSMV
Protein: C3H1-type domain-containing protein (H2KZI3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MADVYTPTKTMDGAFLPAVGSPNTSIDSPAVYVPTPLTAPSTSKTTPVKPEDQTTRQKYGGSVSYSPSNPGIRIVKRKPKPEAVAAAAAVPTAIYSGKRHATDDGEDAGLAALKLKPNRGILRGPAISNLNQRGTRRLIFADTRGLPLVHVKEIERIAAIHSNVADYRCSERNEAAAFGQEMEVFEDVEWSLVPVKRSKPARSEMSESGLREERRIEEEGIMRGAMFGMCQLEDNPALNEQAAVDRANYTPTIIPTVSVPSEPTTLATIRDLPLPGRPPRVRPQDLLLQVKPNQGFHTLPLYHSQRPENPRRPMYAQQQQQQSAHQTPTPHIQQVFQETEPVTNYYTATTSVPETPEPAPAAQPASRFELPSNLKEMLNQLKKKGFVSSDETPSPTTSAPPPVDPLAAAMQTAQQMMLQQGNTYASEEVPQDYPMDGYVATFATPEMMAQERRQDSRNSEGWTQSGWKIPEPCVYFISRPGGCNRGDQCRFIHDEEMRRQKMAELPPRGPNHHHDNFRGGRGRGFRGGYNNRNNYNNHHDRDFRDNAGGNRGRFGDTEGFRGARYARGGFAPRNNSRFDQKPAYNDDGGHLGSPNAHGSQYQDPVPTKRARVSRFDRQGEDDAPGQDMDQRPPRRNRFDEQPPRRTFRSRFDQQADHDEMSQA
Protein: Vomeronasal type-1 receptor (Q14C10)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MSSVENVLYFQAGFGVLPNVFLLLFYIFIILGHRPKPTDLISCQLTLVHIIMFLTGGNIWLADIFGFLNIENDIKCKATFYTSRVTRGLSICITCLLSVFQAVTISPSTSMLAKFKQKLKKYMNNALFYIWFFNLSVCSNMLFFVGGFTNVSETKQVKVTKSCSLFPMNYIIRELIVILSTSRDVFLVAVMLTTSAYMVNILHRHQRQYKHLHSIKSLRTSPEKKATQTILLLVVFFVVMYWVDFIISFTSLLLWMYDPVVLTVQKFLIYAYPTITPLVQISSDKRIINVLKNLQSKCH
Protein: Spastin (A0A2R8Y481)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPEAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
Protein: Cyclin-dependent kinase 2 (EC 2.7.11.22) (Cell division protein kinase 2) (O61847)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which, in association with cye-1, regulates proliferation, quiescent state and cell fate during the development of several cell lineages. In the embryo, initiates the establishment of cell polarity through the recruitment of the centrosomal proteins spd-2 and spd-5 during prophase. Phosphorylation and inhibition of the translational repressor gld-1 by the cdk-2/cye-1 complex regulates the pool of germline stem cells and the size of the mitotic zone in the gonads by preventing entry into meiosis.
Interaction partners:
- G2/mitotic-specific cyclin-A1
- Cyclin-like domain-containing protein
- G1/S-specific cyclin-E
- G2/mitotic-specific cyclin-B
- Cyclin N-terminal domain-containing protein
- Cell division control protein
- G1/S-specific cyclin-D
- Cyclin-dependent kinase inhibitor 1
- Cullin-1
- CDT1 Geminin-binding domain-containing protein
Sequence:
MSREIRSLESIISDARENTHEKMLIRKQRDMTTDIAPERDLQGRFCSLRRIGEGTYGVVFKAIHVRDNVKCALKMIRTDRDEEGIPSTCLREISCIKDLQHDNIVTLFDIIYANSKLYMVFEFIDRDLKNLLEMLEPTNSVLPPNYVKSFMWQLLSALSYCHLRRIVHRDLKPQNILVSDSGVIKIADFGLARNFSFPSRNYTHEVVTLWYRPPEILLGSQRYSTSLDMWSLGCIFSEIASNKPLFPGECEISQLFKIFEIVGTPNIKSWPGVDSFPHYKAVFPQWPVNLKKLEETSCLTGNGLDVLREILRYPPERRLTAKGALSHRYFLQNGFTQNRPSVTDLMKDIRAQNRTPPLLNNHQEKSIF
Protein: Uncharacterized membrane protein C663.14c (O74520)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized membrane protein C1322.03
- Uncharacterized protein C663.15c
- Stretch-activated cation channel yam8
- Calcium-channel protein cch1
Sequence:
MKLILLAYFAVLSNILSSVEGRVRYSKRPNHKLGTAEYAECMSNAPIVFNRFDASYYTRNLSVVFNILGYSSVDANVTFDIIVEAYGEQRARFTFDPCEINLNTVCPVARDTAITTQGILPVSPQDVQMIPKIAWGIPDFEGLVRFRMYRSEDIAASSIDNSTPLACMIATLNNGHTFKNKVVKALSGTALALSIAGVLGFYVIGMEHSTYLTRQVFINSVPSLQHMGELLQCIAFTGAIGITQPKVLVAWASNFAWILGFITNKEIENSLESFRKHSNGNLSSPKIGGVHRRDAVATNPQSPIPGFYHGFQGLATEVGTLTTNLFTLTLIWFLISLAIAGGIVIIFVLIIKFLRQTRIIAKSSCDYITRYWFRVLFNACMRWVLVCWPVLVTMIIYQFTLREAYGPVILAALLLALLFGLFLWLTIKVIRVITTSGLSNEDNPETLISDPKIYTWWGWLYLDLKERRWLYVYACFAHYFSFALVLALVQQFAKIQTILLFVIEIISFILLAVFRPFVGFKNSFCVFLVALTRVVSFALLIPIAFDLAIIPKVIIAIILIIIQGLVFSFMALWSLWNFITMLGTAWPAISYTVPWLRRLIDEYQRQLHIDFENPAVSASEKLSTEEIIPQESNFEEPSTTKKEGNVDTKEDGNDDVFSLVNASPMRPASTIPSHSCDNGINEMQRTV
Protein: Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) (P0A6Y8)
Organism: Escherichia coli (strain K12)
Function: Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}.
Interaction partners:
- Co-chaperonin GroES
- Chaperonin GroEL
- Protein GrpE
- Chaperone protein ClpB
- Chaperone protein HtpG
- Chaperone protein DnaJ
- Curved DNA-binding protein
- RNA polymerase sigma factor RpoH
- Small heat shock protein IbpB
- ATP-dependent protease ATPase subunit HslU
Sequence:
MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKGTGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHAQQQTAGADASANNAKDDDVVDAEFEEVKDKK
Protein: V-type proton ATPase 116 kDa subunit a 1 (V-ATPase 116 kDa subunit a 1) (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit) (Vacuolar adenosine triphosphatase subunit Ac116) (Vacuolar proton pump subunit 1) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1) (Q93050)
Organism: Homo sapiens (Human)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that transports protons across cellular membranes. V-ATPase is responsible for the acidification of various organelles, such as lysosomes, endosomes, the trans-Golgi network, and secretory granules, including synaptic vesicles. In certain cell types, can be exported to the plasma membrane, where it is involved in the acidification of the extracellular environment (By similarity). Required for assembly and activity of the vacuolar ATPase (By similarity). Through its action on compartment acidification, plays an essential role in neuronal development in terms of integrity and connectivity of neurons.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit E 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit d 2
Sequence:
MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEMADPDLLEESSSLLEPSEMGRGTPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLIAEVWCPVTDLDSIQFALRRGTEHSGSTVPSILNRMQTNQTPPTYNKTNKFTYGFQNIVDAYGIGTYREINPAPYTIITFPFLFAVMFGDFGHGILMTLFAVWMVLRESRILSQKNENEMFSTVFSGRYIILLMGVFSMYTGLIYNDCFSKSLNIFGSSWSVRPMFTYNWTEETLRGNPVLQLNPALPGVFGGPYPFGIDPIWNIATNKLTFLNSFKMKMSVILGIIHMLFGVSLSLFNHIYFKKPLNIYFGFIPEIIFMTSLFGYLVILIFYKWTAYDAHTSENAPSLLIHFINMFLFSYPESGYSMLYSGQKGIQCFLVVVALLCVPWMLLFKPLVLRRQYLRRKHLGTLNFGGIRVGNGPTEEDAEIIQHDQLSTHSEDADEPSEDEVFDFGDTMVHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVIHIGLSVKSLAGGLVLFFFFTAFATLTVAILLIMEGLSAFLHALRLHWVEFQNKFYSGTGFKFLPFSFEHIREGKFEE