wanglab/gogpt-training-data huggingface dataset:
Protein: Lysine-specific demethylase rbr-2 (Histone demethylase rbr-2) (EC 1.14.11.67) (Jumonji/ARID domain-containing protein rbr-2) ([histone H3]-trimethyl-L-lysine(4) demethylase rbr-2) (Q23541)
Organism: Caenorhabditis elegans
Function: Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. Required for normal longevity of the soma in a germline-dependent manner. Implicated in the epigenetic inheritance of lifespan over several generations. Involved in larval development and vulva formation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:20555324}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit delta, mitochondrial
- Oligomycin sensitivity conferral protein
- F-ATPase gamma subunit
- Set1/Ash2 histone methyltransferase complex subunit ash-2
- Histone-lysine N-methyltransferase set-2
- ATP synthase subunit d
- ATP synthase subunit alpha
- ATP synthase subunit alpha, mitochondrial
- Lysine-specific histone demethylase 1
Sequence:
MRARRQENSISTPSAPSTSTSPRKKASIGNSRSKNHGSKMEMYDQFYKKFVRPPMAPIYYPTEEEFSDPIEYVAKIRHEAEKFGVVKIVPPANFKPPFAIDKEAFTFRPRTQKLNEVEAIVKEKHTFIDRLINFNRYSGLTFEFPVDRDGNIVDLYRLHRIVQNFGGCEEVNEDEKWRDVAREYLPKEQMARGVPSAFINLIRSHYNLHIEPFNRNLKEKAMKNDDESDDEMEELKHKYQHHHGTMRTEIEVPNDKTTEGGEDECPVSMQSGRRRSKNKKASSSRKTLGTSSKKNSTRGRKNKKKAEGDDDDDEDPMDQVFCVACNEGKDEDLLLLCDIDGCNNGRHTYCCDPVLDEVPEGEWRCPKCIESEDAKIGLDWGFYDADTEYNLNSFTEFANKWKCDYFGVKDVSQVSCDAVERSFWKNVISHENPVSVKYGADLITSRVGSGFPRKEDKHTGPDLKLKQQYASHAWNLNNMPVLRESVLSHFNTGISGMMVPWVYVGMCFSTFCWHTEDHWTYSVNYNHFGERKIWYGVGGEDAEKFEDALKKIAPGLTGRQRDLFHHMTTAANPHLLRSLGVPIHSVHQNAGEFVITFPRAYHAGFNEGLNFAEAVNFAPIDWLSKGRECVESYSNVRRYLVFSHDELLFKMVEAMDKLGISMSLATHEELIRIYEKQKMLRELLARLGVSNRQMQQVMFEKIPDEQRSCRFCKTTLFMCALVCNKHKKMTCVEHHDHLCNSCTTKDYRYQYRFELDQLNNMCDELGKRTVNYNGWKEESDEMLEEEGKPKLERIEEFIDSAKQNKYPQTDQVHKLITIRHTAKSAIEKANQLLFKKVRTRTKTRCQRADTRTDTEGVRSLIEQMQAMDCNLTVIIDKLEKWMEQVEMWRNRAKDAIYREQEYSKEEIEKIIEEGDEYDIKLEEIDELRKVIQMKDWSDRARKVTTWKATPDMEKDIDFEYKLRYASSDILSLIRDSPRNPTDGTSKLVFELQQMLRDANTLEVIANNFCENPALDQLQSIWQSLRETDWFYEKYINMVRYEIIHVAKIKSMIDAAIPVLSEFDLKTQLQKIVNVEITLSKAAEISKAFETSKCLNGSEEHLGILDMISTMNAFTQRIAILFKPNNAYHNLFEILSERDDLTPLAEGQTIPLYFQGGAVHPSDEWHQMKEFESLDQIVHHQSSLREMQMRIFEKVKQANSARGLEACSCLGFNKSDDSESTLTCIMCDSEFHVRCCEWSPFLEKLPEGCFLCVRCLRGQRPVIDDVTTALNGTPSGCLETHLVRNLIQKTRGITQNLMEAANKRKSGESSDDICKIALFDWLSCEILNPNGLPKARELISEFYMEYLQKQSSAALELKNRPVRSKPSVSLFDPKITAKRKRPSVSHKETSKKSRKRQSQASPSEYYEDESEFKSCQARACLKPYGDSVNWVMCEAGCKNWFHVICLGFTLREINDMHEYRCSSCLDHADSPTSSVSTD
Protein: Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma (PI3K-C2-gamma) (PtdIns-3-kinase C2 subunit gamma) (EC 2.7.1.137) (EC 2.7.1.154) (Phosphoinositide 3-kinase-C2-gamma) (O70173)
Organism: Rattus norvegicus (Rat)
Function: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. May play a role in SDF1A-stimulated chemotaxis (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:9516481}; Peripheral membrane protein {ECO:0000269|PubMed:9516481}.
Interaction partners:
- Phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 beta
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Inositol polyphosphate-4-phosphatase type I A
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 4-kinase type 2-beta
- 1-phosphatidylinositol 3-phosphate 5-kinase
Sequence:
MAYNWQTEPNRAEPQEGGHDHQQCHHADQHLSSRQVRLGFDQLVEELSNKTPLPEDEKEGTCFVPDTPNLDSKWQSIYGPHPRHFNEFTSQSPHFSQLPFGKASAIGFNPAVLPAHQFIHEGASWRNPTRKYHGGEDPRFSALTPSSTGLDKCHQQGQSGTEHCNYYVEPENNVPHHYSPYSMDSIPDSEEKGSGDADLVEPSLVFSKDSFLPRASENMSVESTEPIGCPLEIVEAPQGSNKSLASFCNNVTKIRGLYHASDTNSNSGKIWAITTAYPSRLFADTQFRVKISTDNSAQLLLLKPPANYLVKDLIAEILLLCANEQLSPKEYLLSICGSEEFLQTDHCLGSHKIFQKSKSVIQLHLQRSRDTPGKLSRKRDDDRSRVHLNQLLEFTHIWKISRQCLSTVMKSYNLHVEHLLKTQEDVEEKPLSSMFSCGRHPPQPHGNDIIEDVRNICSVLGCIETKQVSDAVKELTLILQRPSQNFHQNSETSKKGFIENVTSELSRSLHQLVDVYCSSFCTDFRPARAPGGVSRDHAGLHSHLSFTVCSLHNVPETWAHSYKAFSFSCWLTYAGKKLCQVKSCRSLPVTKSFSFSVNWNEIINFPLEIKSLPRESMLVIKLFGIDSATHSANLLAWTCLPLFPKEKSPLGSRLLSMTLQSEPPIEMMAPGVWDGSQPTPLTLQIDFPAATWEYVKPETEENRTDHQEPPRECLKHIARLSQKQPPLLLSVEKRRYLWFYRFYCNNENSSLPLVLGSAPGWDEGTVSEMHAVLRRWTFSHPLEALGLLTSRFPDQDIREVAVQQLDNFLTDELLDCLPQLVQAVKFEWSLESPLVELLLHRSLQSIRVAHRLFWLLRDAQGEDYFKSWYQELLAALQFCAGEALIEELSKEQKLVKLLGDIGEKVKSAGDAQRKDVLKKEIGSLEEFFKDIKTCHLPLNPALCVKGIDRDACSYFTSNALPLKITFINANPMGKNISVIFKAGDDLRQDMLVLQIIQVMDNVWLQEGLDMQMIIYGCLATGKAQGFIEMVPDAVTLAKIHLHSGLIGPLKENTIKKWFSQHNHLKEDYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNTQHFQDFVELCCRAYNIVRKHSQLLLSLLEMMLHAGLPELRGIEDLKYVHDNLRPQDTDLEATSHFTTKIKQSLECFPVKLNNLIHTLAQMPAFSLARPAPQTPPQECCVLNKTRTIQRVTILGFSKTHSNLYLIEVTRSDNRKNLAKKSFEQFYRLHSQIQKQFPLLTLPEFPHWWHLPFTDSHHERIRDLSHYVEQVLHGSYEVANSDCVLSFFLSEHIQQTLEDSPFVDPGDHSPDKSPQVQLLMTYEDTKLTILVKHLKNIHLPDGSAPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDDVSGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYPLGNSII
Protein: Small ribosomal subunit protein eS1A (40S ribosomal protein S1-A) (RP10A) (P33442)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS7A
- Small ribosomal subunit protein uS17A
- Small ribosomal subunit protein uS8A
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS4A
- Small ribosomal subunit protein uS19
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein eS27B
- Protein LTV1
- Small ribosomal subunit protein eS30A
Sequence:
MAVGKNKRLSKGKKGQKKRVVDPFTRKEWFDIKAPSTFENRNVGKTLVNKSTGLKSASDALKGRVVEVCLADLQGSEDHSFRKIKLRVDEVQGKNLLTNFHGMDFTTDKLRSMVRKWQTLIEANVTVKTSDDYVLRIFAIAFTRKQANQVKRHSYAQSSHIRAIRKVISEILTKEVQGSTLAQLTSKLIPEVINKEIENATKDIFPLQNIHVRKVKLLKQPKFDVGALMALHGEGSGEEKGKKVTGFKDEVLETV
Protein: Receptor-type guanylate cyclase gcy-9 (EC 4.6.1.2) (E7EAU8)
Organism: Caenorhabditis elegans
Function: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Involved in the sensing of CO2 levels and acidity by the BAG neurons. May act as a direct receptor for CO2 and H+.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:21173231}. Note=Localizes in cilium of sensory neurons. {ECO:0000269|PubMed:21173231}.
Interaction partners:
- ETS domain-containing transcription factor ets-5
- FMRF-Like Peptide
- FMRFamide-like neuropeptides 19
- Cyclic nucleotide-gated channel
- Sialin
- Cyclic nucleotide-binding domain-containing protein
- Probable glutaryl-CoA dehydrogenase, mitochondrial
Sequence:
MRLYLFFISSLLLAESRRSISKISHDEINQHVKTTLSSEGIVRIGHLHPTNPIIAHEPDVLKMCADDLKMRNILPQNYTLTVFTMESCNKYSGVEHAAFLHYLKNASVYFGPGCNNEMLVIGRLAPRWNVPIIAHMSGDDALSDRVQFPTLGSVALTSASEMAKATVTYLNLNNWDQIGIVRPSVGYERLSVYSLQHQIKKRDINLNVILDIEPFSSPEEIISTGKLTTLKSMARIIVVELGMDIHSVTNFMLAIHRSEIKNEEFVFVIPWLAHQNDHYPWEAANVDKQEVKLAFENTIIITAHGYDKKFFDDFQMKFSAVTGVLANHYATLSYMSLYDALFLYGLALRDAFEDGGGYNVHMNGSLIWSRMTNRQFIGMTGQVLMNNKAIRVPSYATYHAINGTLKIVVELEAKNNDRGQCEKNEEMCSEHVAHETIQYYWPSDSGKLPPAVPKCGFTGAECDYRPYFIGASLLAFILTVGPLSYFIYLKQKERLLYDMTWRIPRESIKMLEGKSKSEHSLASKSQSSGSFSGSMNSKQNGLIAAKQAVSNGVKLAIKRYQQVRNITFPKSELRLLKELKICENDNLNKFYGISFNQQNEFIVMWVLCSRGSLEDILFNDELKLGRNFQVSFAKDVVKGLNFLHTSPLLHHGMLCLQNCLVDSNWTVKLTNFATEAVIFEKLDHNELRPFINTDSESADDVSDPTKDFARKKYLQQAPEIIREIVTTKTIPEGSQSADIYALGMVLYQILFRVEPFHERNKSINKLMETLAMANDDDQLIRPTFPSSNTGEGYNLQLLSCIEACWLEIPEMRPPIKKVRTMVNANLKSTGKGSLVDQMMKMMEEYTANLENMVRDRTALLEEAQKQADRLLNSMLPKSIAEDLKIGKPVLPQLYSCATVLFSDIRGFTRISSTSTPLQVVTFLNDMFSGFDAIIAKHDAYKVETIGDAYMIVSGVPTENGNSHAQNIADVALKMRAFICNFKLAHRPEELMMVRIGFHSGPVAAGVVGLAAPRYCLFGDTVNTASRMESTGVANKIQISEGAYNLLHCFFPQFQMVERGKIEVKGKGECLTYYLEGRTGKQ
Protein: Growth differentiation factor-9B (Q9WUW1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MALLTILRILLWGMVLFMEHKVQMAKVEWPSTTLLAENPTLPSSLDLAKEAPGKEMKQWPQGYPLRYMLKLYQRSADPHGHPRENRTIGAKMVRLIKPSASAMRLLRGPWHIQTLDFPLASNEVAYQLIRATVVYRHQLHLVHYHLSCHVEPWVPKCRTKHFPSKSGSAKPSSVSKAWREMNITHCIQQKLWNRKGRRVLRLRFMCQQQKGNETLELRWHGMTSLDVAFLLLYFDDTDESAQAKLLARGQEELTDRESPFLMRSVRQTCSIASDVPCPSQEQDRSVNNQCSLHPYKVSFHQLGWDHWIIAPRLYTPNYCKGICTGVLPYGLNSPNHAIIQSLVNELVNRSVPQLSCVPYKFLPMSILLIEANGSILYKEYEGMIAQSCTCR
Protein: UDP-glucuronosyltransferase 1A7 (UGT1A7) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-7) (UDPGT 1-7) (UGT1*7) (UGT1-07) (UGT1.7) (UDP-glucuronosyltransferase 1-G) (UGT-1G) (UGT1G) (Q9HAW7)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormone epiestradiol. Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist caderastan, a drug which can inhibit the effect of angiotensin II. Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan. Also metabolizes mycophenolate, an immunosuppressive agent.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17179145}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A4
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A3
- UDP-glucuronosyltransferase 1A9
- Cytochrome P450 3A4)
- UDP-galactose translocator
- Cytochrome P450 1A1
Sequence:
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLFFSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEGAQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVTAYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Protein: Inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 (Polypeptide GalNAc transferase 15) (GalNAc-T15) (pp-GaNTase 15) (Protein-UDP acetylgalactosaminyltransferase 15) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 15) (Q9D4M9)
Organism: Mus musculus (Mouse)
Function: Probable inactive glycosyltransferase required during spermatid development. May participate in protein loading into the acrosomes and accumulation of ubiquitin-proteasome systems around the head-tail coupling apparatus region.
Subcellular location: Late endosome membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Localizes to the juxtanuclear region, possibly the late endosome. Not localized in the Golgi apparatus in round spermatids (PubMed:24398516). {ECO:0000269|PubMed:24398516}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
Sequence:
MKSVIIQGLFCGFLAIGLWASMLLLFLHLEQEDMLENEKEELLKKRSLGKNAHQQTRHSEDVTHDEVNFSDPELIQGLRRYGLNAIMSRRLGIEREVPDSRDKICQQKHYPFNLPTASIIICFYNEEFNTLLRAVSSVVNLSPQHLLEEIILVDDMSEFDDLKDKLDYYLEIFRGKVKLIRNKKREGLIRSKMIGASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCPIIDVINELTLDYMAAPIVRGAFDWNLNLRWDNVFAYELDGPEGPSTPIRSPAMTGGIFAINRHYFNELGQYDNGMDICGGENVELSLRIWMCGGQLFILPCSRVGYNSKALSQHRRANQSALSRNLLRVVHVWLDEYKGNFFLQRPSLTYVSCGNISERVELRKRLGCKSFQWYLDNIFPELEPFNTERKRKKNRF
Protein: Exocyst complex component sec15 (O75006)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component sec8
- Exocyst complex component exo70
- Exocyst complex component sec10
- Exocyst complex component exo84
- Exocyst complex component sec6
- Exocyst complex component sec5
- Uncharacterized protein C17G8.12
- Rab guanine nucleotide exchange factor sec2
- Cell division control protein 42 homolog
- F-box protein pof6
Sequence:
MDIDVLEFVDKIASIESAGDTLDRLPQLISLACEKGQETQVYERLNELASKSAIRVEQLSAENNQDFSKSVNQLSVVRSELRSLQSLMADLNTDIQASGRDLQNMKQQLNSLSTSERFLTKYHNLVRSCMQVLHQVQYSQELLSKKQYLPTLRICSEISEVHLKRLDGLGMYSTIQQYIVTTKEAICSAVMEDLHEWLFSIRQKLPLVGKSCSQQIDEARRRWAREYKEDLVNLSSKTSISLELYLLEMMDFSPLDNEIVKISFEPLYICLQVHSYLGLLSSFRSSFERDRRRQQEFLAPKSLTTLDMAVVSEWLNSIAGFMIVEYYILQCIPNFRSYEEVQNIWTIICEKLVETILSVAFTEQSTTTIIKLKNQIVLLMHTMERFGFSVESLRNLCVELIDAFGGALILKHSVFFEEAFEKDVYAPMIVETQEEYDHYIAPYWNFPSEPFPRTMSFSKMCPLCCTTLSKFVRHFFMFLNDSVILATEVNEKAPRFYRRFILRSLVDRLKSLYPKLALSQMSQLVKNFYAFEDPLLQIEKSLVLNKPIHQIGAEASSSNNVKSTELLEGLANARKSALHEIFVKINLKIDDFLGLAEYDWTTTQVRKDVSGYLQEMVTYLQTMYLESLAGLPKHDKSYVYLETLDHLCTAMVDLLSDPSIRKVTTAAAEGFKLDVEYLESFAAQVPDQSIVNADSFIELRQCANLLLGDNMEEYLDTDKFMRDFNRLQPAVAIKFLERHINNYSANPLSNDRPKRRAIEILIATLKKR
Protein: Methylmalonyl-CoA epimerase, mitochondrial (EC 5.1.99.1) (DL-methylmalonyl-CoA racemase) (Q96PE7)
Organism: Homo sapiens (Human)
Function: Methylmalonyl-CoA epimerase involved in propionyl-CoA metabolism.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Methylmalonyl-CoA mutase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Ethylmalonyl-CoA decarboxylase
- Methylmalonic aciduria type A protein, mitochondrial
- Malonate--CoA ligase ACSF3, mitochondrial
- Sepiapterin reductase
- Carbonyl reductase 1])
- Cobalamin trafficking protein CblD
- Corrinoid adenosyltransferase MMAB
Sequence:
MARVLKAAAANAVGLFSRLQAPIPTVRASSTSQPLDQVTGSVWNLGRLNHVAIAVPDLEKAAAFYKNILGAQVSEAVPLPEHGVSVVFVNLGNTKMELLHPLGRDSPIAGFLQKNKAGGMHHICIEVDNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQA
Protein: V-type proton ATPase subunit B (V-ATPase subunit B) (Vacuolar proton pump subunit B) (Q59PT0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Non-catalytic subunit of the V1 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 translocates protons (By similarity). Plays an important role in resistance to several stresses, as well as in autophagy and virulence.
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P16140}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit a
- H
- V-type proton ATPase subunit a
- V-type proton ATPase subunit
- V-type proton ATPase subunit D
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit H
- V-type proton ATPase subunit F
- V-type proton ATPase subunit C
- H
Sequence:
MSLSDKELFELNKKAVTEGFKIKPRINYNTVGGVNGPLVILDNVKFPRYNEIVNLTLPDGSVRQGQVLEVRGTKAIVQVFEGTSGIDVKKTRVEFTGENLKIPVSEDMLGRIFDGSGRPIDKGPKIFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAGLVRPTKDVHDGHEENFSIVFAAMGVNLETSRFFKQDFEENGSLERTTLFLNLANDPTIERIITPRLALTTAEFLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQVPILTMPNDDITHPIPDLTGYITEGQIFIDRQLHNRGIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYAKYAIGKDAAAMKAVVGEEALSTEDKLSLEFLEKFEKNFISQGAYENRSIFESLDLAWSLLRIYPKELLNRISPKILEELYGRDREQDDDEDEDEEDPDKSGDKLIDA
Protein: Hematopoietically-expressed homeobox protein HHEX (Homeobox protein HEX) (Homeobox protein PRH) (Proline-rich homeodomain protein) (Q03014)
Organism: Homo sapiens (Human)
Function: Recognizes the DNA sequence 5'-ATTAA-3' (By similarity). Transcriptional repressor (By similarity). Activator of WNT-mediated transcription in conjunction with CTNNB1. Establishes anterior identity at two levels; acts early to enhance canonical WNT-signaling by repressing expression of TLE4, and acts later to inhibit NODAL-signaling by directly targeting NODAL (By similarity). May play a role in hematopoietic differentiation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P43120}. Nucleus, nuclear body {ECO:0000269|PubMed:12554669}. Cytoplasm {ECO:0000269|PubMed:12554669}.
Interaction partners:
- Proton-coupled zinc antiporter SLC30A8
- Threonylcarbamoyladenosine tRNA methylthiotransferase
- Insulin-like growth factor 2 mRNA-binding protein 2
- Transcription factor 7-like 2
- Alpha-ketoglutarate-dependent dioxygenase FTO-)-demethylase FTO)
- Kinesin-like protein KIF11
- Tetraspanin-8
- ATP-sensitive inward rectifier potassium channel 11
- Exostosin-2
- Potassium voltage-gated channel subfamily KQT member 1
Sequence:
MQYPHPGPAAGAVGVPLYAPTPLLQPAHPTPFYIEDILGRGPAAPTPAPTLPSPNSSFTSLVSPYRTPVYEPTPIHPAFSHHSAAALAAAYGPGGFGGPLYPFPRTVNDYTHALLRHDPLGKPLLWSPFLQRPLHKRKGGQVRFSNDQTIELEKKFETQKYLSPPERKRLAKMLQLSERQVKTWFQNRRAKWRRLKQENPQSNKKEELESLDSSCDQRQDLPSEQNKGASLDSSQCSPSPASQEDLESEISEDSDQEVDIEGDKSYFNAG
Protein: Kinesin-like protein KIF23 (Kinesin-like protein 5) (Mitotic kinesin-like protein 1) (Q02241)
Organism: Homo sapiens (Human)
Function: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Plus-end-directed motor enzyme that moves antiparallel microtubules in vitro.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, spindle. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Note=Localizes to the interzone of mitotic spindles. Detected at the midbody during later stages of mitotic cytokinesis.
Interaction partners:
- Rac GTPase-activating protein 1
- Protein ECT2
- Kinesin-like protein KIF11
- Protein regulator of cytokinesis 1
- Anillin
- Serine/threonine-protein kinase PLK1
- Abnormal spindle-like microcephaly-associated protein
- ADP-ribosylation factor 6
- Inner centromere protein
- Centrosomal protein of 55 kDa
Sequence:
MKSARAKTPRKPTVKKGSQTNLKDPVGVYCRVRPLGFPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQAKRYVFKSNDRNSMDIQCEVDALLERQKREAMPNPKTSSSKRQVDPEFADMITVQEFCKAEEVDEDSVYGVFVSYIEIYNNYIYDLLEEVPFDPIKPKPPQSKLLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNVLQEKEQITISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAEVTQEVEVARPVDKAICGLTPGRRYRNQPRGPVGNEPLVTDVVLQSFPPLPSCEILDINDEQTLPRLIEALEKRHNLRQMMIDEFNKQSNAFKALLQEFDNAVLSKENHMQGKLNEKEKMISGQKLEIERLEKKNKTLEYKIEILEKTTTIYEEDKRNLQQELETQNQKLQRQFSDKRRLEARLQGMVTETTMKWEKECERRVAAKQLEMQNKLWVKDEKLKQLKAIVTEPKTEKPERPSRERDREKVTQRSVSPSPVPLSSNYIAQISNGQQLMSQPQLHRRSNSCSSISVASCISEWEQKIPTYNTPLKVTSIARRRQQEPGQSKTCIVSDRRRGMYWTEGREVVPTFRNEIEIEEDHCGRLLFQPDQNAPPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVPHAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGDIYKTRGGGQSVQFTDIETLKQESPNGSRKRRSSTVAPAQPDGAESEWTDVETRCSVAVEMRAGSQLGPGYQHHAQPKRKKP
Protein: Uncharacterized protein (Q57X52)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MESPAKGDSRQGLKGTQKHLEFQLQREKAYTRELEEKVKLQQAQIATLEQDKAELRREKLMHTDDDKKRGKLEERCHTLQKDLSEKQSALVAEQKRAARAECEKEQIRRDAHASIAKWCDAEKQWITENETIQRQLEESRTAYSKLADEFKELNVTLKEVQKQLQREKDHTTKLESLSHEGEKKITLLHSRIEALQNDVHTRDETVFKLEEAKSKWEEVCHVKDNEIKSLEVQLGMQKSTIEKLQNTVSTLNQQIEAAKLINIEEKGRVEKANCDLRESEKGNKLLMMELETMRRDFEHASENSSKHQEVIVELRSKISALNDQVIEKCAESRKYELSVSQLKADVNRLEQERTDSSRRAAILESNLQELRSALERTRMDLESVVSAKSFLETEFQRVKSMQDTKDENLVLMRVDYEEKIDSLRREAKDLTSEIDARRGVIDKLTGQLGEANARNEDLYRKVMQSSEFSTQLRSATEEMQLNNFMLQVKVLELEEQAARWSLSKESADENLDIHGILVVNIDTAVTHFYEETNLLKKKVEELTHQKDTEILRLSEARLRLEAERSTLIRGKEELVEELRTKEAEILDLQEGARRDKEQLFLLGKEIERENINNEDRTANQKVLSDKLIETENLLREATLYSEDRMRLSQWMANWLEHFSRFFVDIVDQYSALTVEKTLAVAEEYRVLYTNKNDELLRRLSHLEKVRRNAEDMCSHLELKLREIESRVEGSEKLLVEQREGLTRKINVAENEKEKAEKNSENLMEKISDLSRQHAADIQKKDDQVRELSRLLDTEKRNVDELEQRTQKLRSKLDYEISRKGEYKKALEAVKAKREETECFRAKEKDWAMKAIHRANEEVNYWIKSFEQLKGMLEDMSRKSGAQITAVDKAKIQQMEVALCRVSVREPNLISNLCDEGNCGAKRQRSN
Protein: Retrograde regulation protein 3 (P38165)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor that regulates CIT2 gene expression. Binds to two identical sites oriented as inverted repeats 28 bp apart in a regulatory upstream activation sequence element (UASR) in the CIT2 promoter. The core binding site is 5'-GGTCAC-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Retrograde regulation protein 1
- Negative regulator of RAS-cAMP pathway
- Protein BMH1
- Retrograde regulation protein 2
- Protein BMH2
- Target of rapamycin complex subunit LST8
- Nitrogen regulatory protein GLN3
- Citrate synthase, peroxisomal
- Endoplasmic reticulum transmembrane helix translocase
- Ras-like protein 2
Sequence:
MMNNNESEAENQRLLDELMNQTKVLQETLDFSLVTPTPHHNDDYKIHGSAYPGGETPAQQHEKLSYINTHNSNDNNNLMGSQARSNSQTPTASTIYEEAESQSSYLDDMFRTSQGGRPVTQNSISSIGQGPLRSSYSMAYDSPVDRAMNTPLQQQEGLKAELPHDFLFQHGTDDTMYNLTDDLSSSLSSSINSDMMTPNTYSSSFSYNPQSLGPASVSSTYSPKVRSPSSSFRAGSFLSSSFRHGSINTPRTRHTSISSNMTENIGPGSVPKILGGLTSDEKLRRKREFHNAVERRRRELIKQKIKELGQLVPPSLLNYDDLGKQIKPNKGIILDRTVEYLQYLAEILEIQARKKKALLAKIKELEEKKSSVAALSPFTNNHHASSGQNNSENSEERIIDIRSVPNALMNEQNSKAELHNWEPPLYDSVGNHNHAGTMESHPHTNIHEELKEFLSGDLIEAEDNAKLMFGDDNSNPADYLLEFGSG
Protein: Receptor expression-enhancing protein 2 (Q9BRK0)
Organism: Homo sapiens (Human)
Function: Required for endoplasmic reticulum (ER) network formation, shaping and remodeling. May enhance the cell surface expression of odorant receptors (By similarity).
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Receptor expression-enhancing protein 1
- Reticulon-2
- Atlastin-1
- Receptor expression-enhancing protein 4
Sequence:
MVSWIISRLVVLIFGTLYPAYSSYKAVKTKNVKEYVKWMMYWIVFAFFTTAETLTDIVLSWFPFYFELKIAFVIWLLSPYTKGSSVLYRKFVHPTLSNKEKEIDEYITQARDKSYETMMRVGKRGLNLAANAAVTAAAKGVLSEKLRSFSMQDLTLIRDEDALPLQRPDGRLRPSPGSLLDTIEDLGDDPALSLRSSTNPADSRTEASEDDMGDKAPKRAKPIKKAPKAEPLASKTLKTRPKKKTSGGGDSA