wanglab/gogpt-training-data huggingface dataset:
Protein: Biodegradative arginine decarboxylase (ADC) (EC 4.1.1.19) (P28629)
Organism: Escherichia coli (strain K12)
Function: Component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach (Probable). ADC can be found in two forms: biodegradative (this enzyme) and biosynthetic (speA). The biodegradative form plays a role in regulating pH by consuming proteins. Converts arginine imported by AdiC to agmatine which is then exported by AdiC (Probable).
Subcellular location: Cytoplasm.
Interaction partners:
- Biosynthetic arginine decarboxylase
- Argininosuccinate lyase
- Agmatinase
- Arginine N-succinyltransferase
- Arginine/agmatine antiporter
- Chaperone protein DnaK
- Argininosuccinate synthase
- Carbamate kinase-like protein YahI
- Carbamate kinase-like protein YqeA
- Carbamate kinase
Sequence:
MKVLIVESEFLHQDTWVGNAVERLADALSQQNVTVIKSTSFDDGFAILSSNEAIDCLMFSYQMEHPDEHQNVRQLIGKLHERQQNVPVFLLGDREKALAAMDRDLLELVDEFAWILEDTADFIAGRAVAAMTRYRQQLLPPLFSALMKYSDIHEYSWAAPGHQGGVGFTKTPAGRFYHDYYGENLFRTDMGIERTSLGSLLDHTGAFGESEKYAARVFGADRSWSVVVGTSGSNRTIMQACMTDNDVVVVDRNCHKSIEQGLMLTGAKPVYMVPSRNRYGIIGPIYPQEMQPETLQKKISESPLTKDKAGQKPSYCVVTNCTYDGVCYNAKEAQDLLEKTSDRLHFDEAWYGYARFNPIYADHYAMRGEPGDHNGPTVFATHSTHKLLNALSQASYIHVREGRGAINFSRFNQAYMMHATTSPLYAICASNDVAVSMMDGNSGLSLTQEVIDEAVDFRQAMARLYKEFTADGSWFFKPWNKEVVTDPQTGKTYDFADAPTKLLTTVQDCWVMHPGESWHGFKDIPDNWSMLDPIKVSILAPGMGEDGELEETGVPAALVTAWLGRHGIVPTRTTDFQIMFLFSMGVTRGKWGTLVNTLCSFKRHYDANTPLAQVMPELVEQYPDTYANMGIHDLGDTMFAWLKENNPGARLNEAYSGLPVAEVTPREAYNAIVDNNVELVSIENLPGRIAANSVIPYPPGIPMLLSGENFGDKNSPQVSYLRSLQSWDHHFPGFEHETEGTEIIDGIYHVMCVKA
Protein: Far upstream element binding protein 3 (G3V829)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Poly
Sequence:
MAELVQGQSAPVGLKAEDFVDALHRVRQIAAKIDSIPHLNNSTPLVDPSVYGYGVQKRPLDDGVGNQLGALVHQRAVITEEFKVPDKMVGFIIGRGGEQISRIQAESGCKIQIASESSGIPERPCVLTGTPESIEQAKRLLGQIVDRCRNGPGFHNDIDGNSTIQELLIPASKVGLVIGKGGETIKQLQERTGVKMVMIQDGPLPTGADKPLRITGDPFKVQQAREMVLEIIREKDQADFRGVRSDFTSRAGGGSIEVSVPRFVVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGISPERAAQVMGPPDRCQHAARIINELILTAQEREILGGLTGTRGRGRGRGDWSVGTPGGIQEITYTVPADKCGLVIGKGGENIKSINQQSGAHVELQRNPPPNTDPNLRIFTIRGAPQQIEVARHLIDEKVGGASLGAPTAFGQSPFSQPPAAPHQNTFPPRAFPNIAAKVNGNPHSTPVSGPPAFLTQGWGSTYQAWQQPTQQVPSQQSQPQNSQPDYSKAWEDYYKKQGHTTSAAPQASSPPDYTMAWAEYYRQQAAFYGQTLGQAQAHSQEQ
Protein: 60S acidic ribosomal protein family (F4IGR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKVVAAFLLAVLSGKASPTTGDIKDILGSGIMVLVLDCVVIGDCFGAETEDSQIELLLKEVKGKDLAELIAAGREKLASVPSGGGGGVAVASATSGGGGGGGAPAAESKKEEKKEEKEESDDDMGFSLFE
Protein: Thiosulfate sulfurtransferase PspE (TST) (EC 2.8.1.1) (Phage shock protein E) (P23857)
Organism: Escherichia coli (strain K12)
Function: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspE catalyzes the sulfur-transfer reaction from thiosulfate to cyanide, to form sulfite and thiocyanate. Also able to use dithiol (dithiothreitol) as an alternate sulfur acceptor. Also possesses a very low mercaptopyruvate sulfurtransferase activity.
Subcellular location: Periplasm {ECO:0000269|PubMed:1712397}.
Interaction partners:
- Phage shock protein D
- Thiosulfate sulfurtransferase GlpE
- Phage shock protein A
- Phage shock protein C
- Phage shock protein B
- Psp operon transcriptional activator
Sequence:
MFKKGLLALALVFSLPVFAAEHWIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKVYCNAGRQSGQAKEILSEMGYTHVENAGGLKDIAMPKVKG
Protein: Elongator complex protein 1 (ELP1) (IkappaB kinase complex-associated protein) (IKK complex-associated protein) (Q7TT37)
Organism: Mus musculus (Mouse)
Function: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). The elongator complex catalyzes the formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. Regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation. ELP1 binds to tRNA, mediating interaction of the elongator complex with tRNA (By similarity). May act as a scaffold protein that assembles active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK) (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19185337, ECO:0000269|PubMed:23717213, ECO:0000269|PubMed:31827135}. Nucleus {ECO:0000250|UniProtKB:O95163}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 4
- Elongator complex protein 5
- Elongator complex protein 2
- Elongator complex protein 6
- Protein KTI12 homolog
- Diphthamide biosynthesis protein 3
- ESF1 homolog
- NF-kappa-B essential modulator
- Adenylyltransferase and sulfurtransferase MOCS3
Sequence:
MRNLKLHRTLEFRDIQAPGKPQCFCLRAEQGTVLIGSERGLTEVDPVRREVKTEISLVAEGFLPEDGSGCIVGIQDLLDQESVCVATASGDVIVCNLSTQQLECVGSVASGISVMSWSPDQELLLLATAQQTLIMMTKDFEVIAEEQIHQDDFGEGKFVTVGWGSKQTQFHGSEGRPTAFPVQLPENALPWDDRRPHITWRGDGQYFAVSVVCRQTEARKIRVWNREFALQSTSESVPGLGPALAWKPSGSLIASTQDKPNQQDVVFFEKNGLLHGHFTLPFLKDEVKVNDLLWNADSSVLAIWLEDLPKEDSSTLKSYVQLWTVGNYHWYLKQSLPFSTTGKNQIVSLLWDPVTPCRLHVLCTGWRYLCCDWHWTTDRSSGNSANDLANVAVIDGNRVLVTVFRQTVVPPPMCTYRLLIPHPVNQVIFSAHLGNDLAVLDASNQISVYKCGDKPNMDSTVKLGAVGGNGFKVPLTTPHLEKRYSIQFGNNEEEEEEEVNALQLSFLTWVEDDTFLAISYSHSSSQSIIHHLTVTHSEVDEEQGQLDVSSSVTVDGVVIGLCCCSKTKSLAVQLADGQVLKYLWESPSLAVEPWKNSEGIPVRFVHPCTQMEVATIGGEECVLGLTDRCRFFINDTEVASNITSFAVCDDFLLVTTHSHTCQVFSLSGASLKMLQAALSGSHEASGEILRKVERGSRIVTVVPQDTKLILQMPRGNLEVVHHRALVLAQIRKWLDKLMFKEAFECMRKLRINLNLIHDHNPKVFLENVETFVKQIDSVNHINLFFTELREEDVTKTMYPPPITKSVQVSTHPDGKKLDLICDAMRAAMEAINPRKFCLSILTSHVKKTTPELEIVLQKVQELQGNLPFDPESVSVEEALKYLLLLVDVNELFNHSLGTYDFNLVLMVAEKSQKDPKEYLPFLNTLKKMETNYQRFTIDKYLKRYEKALGHLSKCGPEYFTECLNLIKDKNLYKEALKLYRPDSPQYQAVSMAYGEHLMQEHLYEPAGLVFARCGAQEKALEAFLACGSWQQALCVAAQLQMSKDKVAGLARTLAGKLVEQRKHSEAATVLEQYAQDYEEAVLLLLEGSAWEEALRLVYKYDRVDIIETSVKPSILEAQKNYMDFLDSETATFIRHKNRLQVVRALRRQAPQVHVDHEVAHGPESDLFSETSSIMSGSEMSGRYSHSNSRISARSSKNRRKAERKKHSLKEGSPLEGLALLEALSEVVQSVEKLKDEVRAILKVLFLFEFEEQAKELQRAFESTLQLMERAVPEIWTPAGQQSSTTPVLGPSSTANSITASYQQQKTCVPALDAGVYMPPKMDPRSQWKLSLLE
Protein: Neurofibromin 1, isoform E (A0A0B4KI28)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTQKPGEWASALLARFEDQLPNRIGAYGTQARMSQDQLVACLIHISRYRFSLVISGLTKMLQRVNEAALQNRHEPERCYFESLVIILTTLERCLTNQTKDTARFEEAMNVKLLLREISQFVDVQSDSNPNAAQLKALASKVLFALSQNHFSAVFNRISARIQELTSCSEENPDYNDIELIQHIDMDMIKLTKLLQETITKFRSKRAPPLILLYSLEKAIWNWIEYHPQEFQDLQRGTNRDISTCWEPLMDFVEYFKTENKKSKTLVWPLQMLLLILNPSCLEAVVNELQQSEKEKEKDKEKVASKSAQSTSRDKDFSAKQFIESIKRGLGQHSPSKQVTESAAIACVKLCKASTYINNTDSNNVVFKLVQFFINDLKALLFNPAKPFSRGQGYNFADIELMIDCWVSCFRINPHNIEALKVCLNLSSPQAYHFVIVCSLLRLAHIYVDFRLQNKNPFRIVNQPRLSWWPQTDVVHYRSAELRALFTDTLNKATQGYIAHTPLRYITSLTLKSKDTQKGLTRAEEGPAHKMLLLLLVRLIHADPTLLLNTQGKVAHEVQSSTLELINGLVSLVHQTTMPDVAQEAMEALLALHAPEKIEVWNPEAPINTFWDVSSQVLFSISQKLIQHQIANYTDVLKWLREILICRNTFLQRHKDYAHVGSQIAICKQAHIKMEVVFFMYLWSVDLDAVLTSLSCFGLLCEEAEICCSSDELTVGFIMPNYHIYQELAQLSTSATDSRICFFDNTHGNVLSRLTLQKRIMTLLRKIEHCVHGVQPAWEETFRNWEVSSKVLQTYPKCKGEDGQAEVFHRGMGKRRASHQSSEHDLEEQINEWANMTWFLLALGGVCLHKRSSSRQMLLQQSQNNASLGSLAQNSLYSSSTSSGHGSLHPSTVSLSTLPPAPPQDVSYCPVTQFVGQLLRLLVCSNEKIGLNIQKNVKELVGEEMSTQLYPILFDQVRAIVEKFFDQQGQVNVNVTDINTQFIEHTIYIMKSILDPKANKDPNNDQPSPSEHLGVTSIEGMMLGIVRYVRHLDMTVYAIRIKTKLCQLVEVMMKRRDDLAFRQEMKFRNKLVEYLTDWVMGTSHQIAPPSSADAAILTNTSLIFRDLDQACMEAVAALLRGLPLQPEESDRGDLMDAKSALFLKYFTLFMNLLNDCIDSSEAEKEMNNTPLLPPRPRMAAGKLTALRNATILAMSNLLGANIDSGLMHSIDLGYNPDLQTRAAFMEVLTQILQQGTEFDTLAETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEETCFEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFSKEQHMLCFNDFLRDHFEAGRRFFIQIASDCETVDQTSHSMSFISDANVLALHRLLWTHQEKIGDYLSSSRDHKAVGRRPFDKMATLLAYLGPPEHKPVDSHMMFSSYARWSSIDMSSTNFEEIMVKHQMHEKEEFKTLKSMNIFYQAGTSKSGYPVFYYIARRYKIGETNGDLLIYHVILTLKPFCHSPFEVVIDFTHTCSDNRFRTEFLQKWFYVLPTVAYENVHAVYIYNCNSWVREYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQQKLPGATLSLDEDLKVFSNALKLSHKDTKVAIKVGPTALQITSAEKTKVLAHSVLLNDVYYASEIEEVCLVDDNQFTLSITNESGQLSFIHNDCDNIVQAIIHIRNRWELSQPDSVTVHQKIRPKDVPGTLLNMALLNLGSCDPNLRTAAYNLLCALTATFDLKIEGQLLETQGLCIPSNNTIFIKSVSEKLATNEPHLTLEFLEESIQGFQRSTIELKHLCLEYMTPWLKNLVKFCKSNDDSKKLKVSQILDKLINLTIDQKEMYPSVQAKIWGSIGQIPELIDMVLDNFLHKSITYGLGSPQVEIMADTAVALASANVQLVSKKVITRICRVMDKSCTNPTQYLEQHMMWDDIAILGRYLLMLSFNNCLDVATSVPYLFHTITFLVCSGSLSMRASTHGLVINIIHSLCTCTNPSFSEEAQRVLRLSLDEFSLPKFYLLFGISKVKSAAVTAFRSSCRHPTDKWLGNERVTQPLPADRERLSLPSLEVITDALLEIMEACMRDVPDCEWLNTWTSLARSFAFCYNPALQPRALIVYGCISKSVTDHEVKQLLRILVKALESFNDLILIEALVMCLTRIQPLLRPESPIHRALFWVAISVLQLDEITLYGAGLALLEQNLHTLKSQGCFDKKETIAEVMMKTREKLEWHFKQLDHAVGLSFRSNFHFALVGHLIKGFRHPTPTTVSRTSRVLTMLLGIIAKPLHRDKFEVTPDSVAYLTALVAVSEEVRSRCHVKHALPRWPADLSSSVENGEASGGVQAIGLPLSRRQKSWDILDQSALQFARQHKVPTLQNARVLFKTQRSFSVPTTKDPNNATGIEERQERGSRSSVSNESNVLLDPEVLPDLSIQALVLTVLATLVKYSSDEGETRVLYQYLAEGSVVFPKVFPVIHSLLDQKINNILSVSHDQVVLNSVQNIIQNMLASEDPSQQQLHFLQSCGFGGLWRFAGPFTKYNMMGESSELFVNCLEAMVETCLPGDESAPVPPSPRPYNLSSSLSSLTLGSPTDKAAXITTTNPRTRRTTLIAKVMRFLNLLKKCF
Protein: Protein ATP12, mitochondrial (P22135)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the assembly of the mitochondrial F1-F0 complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:1826907}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}. Note=Mitochondrial, either as a constituent of the matrix, or in tenous association with the internal side of the inner membrane.
Interaction partners:
- Protein ATP11
- ATP synthase subunit alpha
- ATP synthase assembly factor FMC1, mitochondrial
- Autophagy protein 5
- Autophagy-related protein 3
- Ubiquitin-like-conjugating enzyme ATG10
- Cysteine protease ATG4
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy protein 16
- Autophagy-related protein 8
Sequence:
MLPSLRKGCFIVNSIRLKLPRFYSLNAQPLGTDNTIENNTPTETNRLSKTSQKFWEKVSLNRDVEKGKIALQLDGRTIKTPLGNGIIVDNAKSLLAYLLKLEWSSLSSLSIKTHSLPLTSLVARCIDLQMTNEPGCDPQLVAKIGGNSDVIKNQLLRYLDTDTLLVFSPMNEFEGRLRNAQNELYIPIIKGMEEFLRNFSSESNIRLQILDADIHGLRGNQQSDIVKNAAKKYMSSLSPWDLAILEKTVLTTKSFICGVLLLENKKDTANLIPALKTDMDNIVRAATLETIFQVEKWGEVEDTHDVDKRDIRRKIHTAAIAAFKQ
Protein: Rab5 GDP/GTP exchange factor (Rabex-5) (O18973)
Organism: Bos taurus (Bovine)
Function: Rab effector protein acting as linker between gamma-adaptin and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9323142}. Early endosome {ECO:0000269|PubMed:9323142}. Recycling endosome {ECO:0000269|PubMed:9323142}.
Interaction partners:
- Rab GTPase-binding effector protein 1
- Rab GTPase-binding effector protein 2
- RAB21, member RAS oncogene family.
- Ras-related protein Rab-21
- Ras-related protein Rab-5A
- small monomeric GTPase
- Ras-related protein Rab-17
- RAB22A, member RAS onco family
- Ras-related protein Rab-5C
- RAB20, member RAS onco family
Sequence:
MSLKSERRGIHVDQSELLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDWELAERLQREEEEAFASSQSSQGAQSLTFSKFEEKKTNEKTRKVTTVKKFFSASSRVGAKKAEIQEAKAPSPSINRQTSIETDRVSKEFIEFLKTFHKTGQEIYKQTKLFLEAMHYKRDLSIEEQSECTQDFYQNVAERMQTRGKVPPERVEKIMDQIEKYIMTRLYKYVFCPETTDDEKKDLAIQKRIRALHWVTPQMLCVPVNEEIPEVSDMVVKAITDIIEMDSKRVPRDKLACITKCSKHIFNAIKITKNEPASADDFLPTLIYIVLKGNPPRLQSNIQYITRFCNPSRLMTGEDGYYFTNLCCAVAFIEKLDAQSLNLSQEDFDRYMSGQTSPRKQESENWSPDACLGVKQMYKNLDLLSQLNERQERIMNEAKKLEKDLIDWTDGIAKEVQDIVEKYPLEIRPPNQSVAAIDSENVENDKLPPPLQPQVYAG
Protein: UDP-glucuronosyltransferase (EC 2.4.1.17) (D3XD97)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein {ECO:0000256|RuleBase:RU362059}.
Interaction partners:
Sequence:
MPSLPATLLAFLSILSLVFGGKVLVFPLDGSHWVNMKVLIEELHTRGHNVTVLRASNSWYIKKESPFYTSITVYNSGGIEKELFEEFSRNILVIRRQKRSFWTKLKLVSEVGAVFEEMHRNQLNLMGNIFENKDLMDSLQTAKYDLLLTDPAVGGGFFLAYRLGLPLVLNVRWTMHGEAHFEIAPSPLSYIPVPGLELTDKMTFVQRVQNILVYMFSKFQKARTVSKHYRSFCEKYFGSEINYKAILQDADIWLMRNDFTFEFPRPTMPNIVYMGGFQCKPSKPLPDDLEEFVKSSGDHGLIVMSLGTLFTHLPEDITEEIAAAFAGLPQKIIWRHTGPRPVNIGDNTLLVDWLPQNDLLGHAKTKVFITHGGTNGIQEAIYHGVPILGLPLVFDQPDNLSRMKVRGTAKLLDIAELNRTMFLEALKEVLYNPSYKENIQRLSKVHHDQPMKPLDRAMFWIEFVMRNKGASHLRTQSFRMSWIEYHSIDVILTLLMILVLFCVLIYSIVKCICLKVVLKKKVKTQ
Protein: DNA mismatch repair protein PMS1 (Postmeiotic segregation protein 1) (P14242)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLalpha heterodimer that forms a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats and in the repair of heteroduplex sites present in meiotic recombination intermediates.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA mismatch repair protein MSH6
- DNA mismatch repair protein MSH2
- DNA mismatch repair protein MSH3
- DNA mismatch repair protein MLH1
- MutS protein homolog 5
- Exodeoxyribonuclease 1
- MutS protein homolog 4
- DNA mismatch repair protein MLH3
- DNA polymerase delta catalytic subunit
- DNA mismatch repair protein MLH2
Sequence:
MTQIHQINDIDVHRITSGQVITDLTTAVKELVDNSIDANANQIEIIFKDYGLESIECSDNGDGIDPSNYEFLALKHYTSKIAKFQDVAKVQTLGFRGEALSSLCGIAKLSVITTTSPPKADKLEYDMVGHITSKTTTSRNKGTTVLVSQLFHNLPVRQKEFSKTFKRQFTKCLTVIQGYAIINAAIKFSVWNITPKGKKNLILSTMRNSSMRKNISSVFGAGGMRGLEEVDLVLDLNPFKNRMLGKYTDDPDFLDLDYKIRVKGYISQNSFGCGRNSKDRQFIYVNKRPVEYSTLLKCCNEVYKTFNNVQFPAVFLNLELPMSLIDVNVTPDKRVILLHNERAVIDIFKTTLSDYYNRQELALPKRMCSQSEQQAQKRLKTEVFDDRSTTHESDNENYHTARSESNQSNHAHFNSTTGVIDKSNGTELTSVMDGNYTNVTDVIGSECEVSVDSSVVLDEGNSSTPTKKLPSIKTDSQNLSDLNLNNFSNPEFQNITSPDKARSLEKVVEEPVYFDIDGEKFQEKAVLSQADGLVFVDNECHEHTNDCCHQERRGSTDTEQDDEADSIYAEIEPVEINVRTPLKNSRKSISKDNYRSLSDGLTHRKFEDEILEYNLSTKNFKEISKNGKQMSSIISKRKSEAQENIIKNKDELEDFEQGEKYLTLTVSKNDFKKMEVVGQFNLGFIIVTRKVDNKYDLFIVDQHASDEKYNFETLQAVTVFKSQKLIIPQPVELSVIDELVVLDNLPVFEKNGFKLKIDEEEEFGSRVKLLSLPTSKQTLFDLGDFNELIHLIKEDGGLRRDNIRCSKIRSMFAMRACRSSIMIGKPLNKKTMTRVVHNLSELDKPWNCPHGRPTMRHLMELRDWSSFSKDYEI
Protein: Protein phosphatase regulator (A0A1D8PS15)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- AAA family ATPase
- Doa1p
- Ubiquitin thioesterase OTU
- Derlin
- RING-type E3 ubiquitin transferase
- UBX domain-containing protein
- UBX domain-containing protein
- AAA family ATPase
- UBX domain-containing protein
- TUG ubiquitin-like domain-containing protein
Sequence:
MSENTPDSQLIAEFVSITNSSTYLAEQYLSRNSNDLVEAVEDFYANNEPSQKSETKKSSSSNAKGSGVKTFRDLNDEDDDEEDDKTNTNFFTGGEKSGLQVEDPNKDKDNDRSIIDQIFQKAREQMQQPDDRPSASQDDQPSPIKFSGKGFKLGDGNEPSQVVEDPNASAKKFRPSKVTREITFWKQGFTVGDGPLHRYDDPRNASVLQELNQGRVPMSILDVEFGQDVDVSVYKKTDEDWTPPKRKIGGYHGAGHRLGSPVPGEVLVNNEASSQPDIKTETEISKPKDEGEGDSTVQIRFANGKRTSHKFNSSDSILKVYEFVKNHEYNSEPTRPFTLSHAFPVKPIEESSDITISDAKLKNAVIVQRWK
Protein: Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (A0A3B3ISZ0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
Sequence:
MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGK
Protein: Pantothenate kinase 1 (hPanK) (hPanK1) (EC 2.7.1.33) (Pantothenic acid kinase 1) (Q8TE04)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14523052}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23152917}. Nucleus, nucleolus {ECO:0000269|PubMed:23152917}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:23152917}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:23152917}. Recycling endosome {ECO:0000269|PubMed:23152917}.
Interaction partners:
- Phosphopantothenate--cysteine ligase
- Phosphopantothenoylcysteine decarboxylase
- Bifunctional coenzyme A synthase
- Pantetheine hydrolase VNN2
- Pantetheinase
- Pantothenate kinase 2, mitochondrial
- Pantothenate kinase 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ferritin light chain
Sequence:
MLKLVGGGGGQDWACSVAGTSLGGEEAAFEVARPGDQGKAGGGSPGWGCAGIPDSAPGAGVLQAGAVGPARGGQGAEEVGESAGGGEERRVRHPQAPALRLLNRKPQGGSGEIKTPENDLQRGRLSRGPRTAPPAPGMGDRSGQQERSVPHSPGAPVGTSAAAVNGLLHNGFHPPPVQPPHVCSRGPVGGSDAAPQRLPLLPELQPQPLLPQHDSPAKKCRLRRRMDSGRKNRPPFPWFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPSCAMHRFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALEMAAKGDSTNVDKLVKDIYGGDYERFGLQGSAVASSFGNMMSKEKRDSISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALLELFKMTDDK
Protein: Aminopeptidase (Q306T3)
Organism: Streptomyces sp. KK565
Interaction partners:
Sequence:
MSPSRYRSLSASALAVVALLATAAPAVQAAPASRTAAAAPDIPVANVKAHLTQLQSIATANGGNRAHGRAGYKASIDYVKAKLDAAGYTTALQQFTSGGATGYNLIADWPGGDPNQVLMAGSHLDSVTSGAGINDNGSGSAAVLETALAVSRAQLTPDKHLRFAWWGAEELGLIGSKYYVNNLGATERAKLDGYLNFDMIGSPNAGYFVYDDDPVIEQTFKSYFAGLSVPTEIETEGDGRSDHAPFKSAGVPVGGLFTGASNTKSSAQAQKWGGTAGQSFDRCYHSSCDNTANINDTALDRNSDAVAHAIWTLSADTEPPTGEGVFSSTTDVAVPDAGSAVTSSIAVTGRTGNAPAALQVGVDIKHTWRGDLVVDLLAPDGTAYRLKNASGGDSADNVIETYTVNASSETANGTWKLQVRDTASQDTGFIDSWKLTF
Protein: Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1) (O08769)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-A2
- Cyclin-dependent kinase 2
- G1/S-specific cyclin-E1
- cyclin-dependent kinase
- Cyclin-dependent kinase 4
- S-phase kinase-associated protein 2
- G1/S-specific cyclin-D1
- Cyclin-A1
- G1/S-specific cyclin-D3
- G1/S-specific cyclin-D2
Sequence:
MSNVRVSNGSPSLERMDARQTEHPKPSACRNLFGPVNHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGRYEWQEVERGSLPEFYYRPPRPPKSACKVPAQESLDVSGSRQAVPSIGSQANSEDRHLVDQMPDSSDSPAGLAEQCPGMRKRPAAEDSSSQNKRANRTEENVSDGSPNAGTVEQTPKKPGLRRQT
Protein: Oxysterols receptor LXR-alpha (Liver X receptor alpha) (Nuclear receptor subfamily 1 group H member 3) (RLD-1) (Q62685)
Organism: Rattus norvegicus (Rat)
Function: Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity. Interaction with retinoic acid receptor (RXR) shifts RXR from its role as a silent DNA-binding partner to an active ligand-binding subunit in mediating retinoid responses through target genes defined by LXRES. LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides. Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (By similarity). Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Z0Y9, ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z0Y9}.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Retinoic acid receptor RXR-beta
- Oxysterols receptor LXR-beta
- P-type phospholipid transporter
- Nuclear receptor corepressor 2
- Nuclear receptor coactivator
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Proteasome activator complex subunit 3
- Nuclear receptor subfamily 0 group B member 2
- Nuclear receptor corepressor 1
Sequence:
MSLWLEAAVPDVSPDSATELWKTEPQDAGDQGGNTCILREEARMPQSTGGALRIGLESSEPTALLPRAETLPEPTELRPQKRKKGPAPKMLGNELCSVCGDKASAFHYNVLSCEGCKGFFRRSVIKGARYICHSGGHCPMDTYMRRKCQECRLRKCRHAGMREECVLSEEQIRLKKLKRQEEEQAQATSVSPRVSSPPQVLPQLSPEQLGMIEKLVAAQQQCNRRSFSDRLRVTPWPIAPDPQSREARQQRFAHFTELAIVSVQEIVDFAKQLPGFLQLSREDQIALLKTSAIEVMLLETSRRYNPGSESITFLKDFSYNREDFAKAGLQVEFINPIFEFSRSMNELQLNDAEFALLIAISIFSADRPNVQDQLQVERLQHTYVEALHAYVSINHPHDRLMFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE
Protein: MoaA/nifB/pqqE family protein (Q9A8M3)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
Sequence:
MAEAAKLGPAARGRGAKSNRTGRFESLVRDVFDDGWGEDAEPAQILTQLQPMKSRTIIARNQSPDVGFDRSINPYRGCSHGCIYCYARPAHAYLGLSPGLDFESKIFFKPQAGELLAKELSKPGYKPATIHIGGDTDPYQPDEKHLRVTRQVIETLERYNHPFTIITKSALILRDLDVLSRMAARGLTRVAISITTLDRRLARSMEPRAATPGKRIEAVRRLTEAGVPVTVLFAPAIPGLNDHEVEAVLEAAAKAGARGAGYVALRLPREIAQLFEEWLQADYPDRARKVMSLARQIRSGEVYRAAWGDRMVGDGPVAEVLRQRFHLAVKRYGLDHPWTALDISQFQPPRPVSPQMDLFG
Protein: GRB2-related adapter protein (Q13588)
Organism: Homo sapiens (Human)
Function: Couples signals from receptor and cytoplasmic tyrosine kinases to the Ras signaling pathway. Plays a role in the inner ear and in hearing.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q08012}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q08012}. Synapse {ECO:0000250|UniProtKB:Q08012}. Note=Localizes at the presynaptic terminal. {ECO:0000250|UniProtKB:Q08012}.
Interaction partners:
- Lymphocyte cytosolic protein 2
- Son of sevenless homolog 1
- Growth factor receptor-bound protein 2
- Linker for activation of T-cells family member 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- SHC-transforming protein 1
- Son of sevenless homolog 2
- Mast/stem cell growth factor receptor Kit
- FYN-binding protein 1
- Lck-interacting transmembrane adapter 1
Sequence:
MESVALYSFQATESDELAFNKGDTLKILNMEDDQNWYKAELRGVEGFIPKNYIRVKPHPWYSGRISRQLAEEILMKRNHLGAFLIRESESSPGEFSVSVNYGDQVQHFKVLREASGKYFLWEEKFNSLNELVDFYRTTTIAKKRQIFLRDEEPLLKSPGACFAQAQFDFSAQDPSQLSFRRGDIIEVLERPDPHWWRGRSCGRVGFFPRSYVQPVHL
Protein: Crooked legs, isoform H (M9PFM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQHVSAASSVPSVVTPVVTTGGTTITLGGPPPLPKSEHKEDGKPPHGIEMYKVNIEDISQLFTYHEVFGKIHGDVVNHQLAAAHGGQLPPPPPLPPQVTSHAASAAAAAAAASTNNAAVAAVMASANAAAAAAAAASAGGGLPPATSGNGGQQVTVTTTSSSTSSGGSTTSGGTTTTAGQTPHQCDVCGKKYTRKEHLANHMRSHTNETPFRCEICGKSFSRKEHFTNHILWHTAGETPHRCDFCSKTFTRKEHLLNHVRQHTGESPHRCSYCMKTFTRKEHLVNHIRQHTGETPFKCTYCTKAFTRKDHMVNHVRQHTGESPHKCTYCTKTFTRKEHLTNHVRQHTGDSPHRCSYCKKTFTRKEHLTNHVRLHTGDSPHKCEYCQKTFTRKEHLNNHMRQHSSDNPHCCNVCNKPFTRKEHLINHMSRCHTGDRPFTCETCGKSFPLKGNLLFHQRSHTKGQEMERPFACEKCPKNFICKVPHHSATTTMHTIQQITAGAAGGAGAVQLTPGLVPLVTSTLISHNAAAQQQSQKQQAAAAAAAQQQAAAAAAAQQQAAQQQAAAAHQQHQQQVAAQHQQQAAVAAHQQQQQQLQQQQQLLQLSIQQAAHHHQQEQHRQQQQQQHQQQQQQQHHQQQQQGHPQAPPPQQQQQPPPIALISDPSALARAAIQLQHLPANVEQHPVVY