wanglab/gogpt-training-data huggingface dataset:
Protein: V-type proton ATPase 116 kDa subunit a 1 (V-ATPase 116 kDa isoform a 1) (Uncoordinated protein 32) (Vacuolar proton translocating ATPase 116 kDa subunit a 1) (P30628)
Organism: Caenorhabditis elegans
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 translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Required for assembly and activity of the vacuolar ATPase (By similarity). Regulates the size of gut granules during embryonic development. In neurons, required for necrotic cell death by promoting intracellular acidification. Required for cell death induced by hypoxia. Required for acidification of synaptic vesicles and the release of neurotransmitters from adult neurons.
Subcellular location: Membrane {ECO:0000269|PubMed:11441002}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit
- V-type proton ATPase subunit D
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- Probable V-type proton ATPase subunit F
- V-type proton ATPase subunit C
- V-type proton ATPase subunit B 2
- Probable V-type proton ATPase subunit G
- V-type proton ATPase 16 kDa proteolipid subunit c 2
Sequence:
MGDYVTPGEEPPQPGIYRSEQMCLAQLYLQSDASYQCVAELGELGLVQFRDLNPDVSSFQRKYVNEVRRCDEMERKLRYLEREIKKDQIPMLDTGENPDAPLPREMIDLEATFEKLENELREVNKNEETLKKNFSELTELKHILRKTQTFFEEVDHDRWRILEGGSGRRGRSTEREETRPLIDIGDMDDDSAARMSAQAAMLRLGFVAGVIQRERLPAFERLLWRACRGNVFLRTSEIDDVLNDTVTGDPVNKCVFIIFFQGDHLKTKVKKICEGFRATLYPCPDTPQERREMSIGVMTRIEDLKTVLGQTQDHRHRVLVAASKNVRMWLTKVRKIKSIYHTLNLFNIDVTQKCLIAEVWCPIAELDRIKMALKRGTDESGSQVPSILNRMETNEAPPTYNKTNKFTKGFQNIVDAYGIATYREINPAPYTMISFPFLFAVMFGDMGHGAIMLLAALFFILKEKQLEAARIKDEIFQTFFGGRYVIFLMGAFSIYTGFMYNDVFSKSINTFGSSWQNTIPESVIDYYLDDEKRSESQLILPPETAFDGNPYPIGVDPVWNLAEGNKLSFLNSMKMKMSVLFGIAQMTFGVLLSYQNFIYFKSDLDIKYMFIPQMIFLSSIFIYLCIQILSKWLFFGAVGGTVLGYKYPGSNCAPSLLIGLINMFMMKSRNAGFVDDSGETYPQCYLSTWYPGQATIEIILVVLALVQVPIMLFAKPYFLYRRDKQQSRYSTLTAESNQHQSVRADINQDDAEVVHAPEQTPKPSGHGHGHGDGPLEMGDVMVYQAIHTIEFVLGCVSHTASYLRLWALSLAHAQLSDVLWTMVFRNAFVLDGYTGAIATYILFFIFGSLSVFILVLMEGLSAFLHALRLHWVEFQSKFYGGLGYEFAPFSFEKILAEEREAEENL
Protein: Kelch-like protein 40 (Kelch repeat and BTB domain-containing protein 5) (Sarcosynapsin) (Q2TBA0)
Organism: Homo sapiens (Human)
Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. The BCR(KLHL40) complex acts by mediating ubiquitination and degradation of TFDP1, thereby regulating the activity of the E2F:DP transcription factor complex (By similarity). Promotes stabilization of LMOD3 by acting as a negative regulator of LMOD3 ubiquitination; the molecular process by which it negatively regulates ubiquitination of LMOD3 is however unclear (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:23746549}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:Q9D783}.
Interaction partners:
- Kelch repeat and BTB domain-containing protein 13
- Cullin-3
- Kelch-like protein 41
- Leiomodin-3
- Nebulin
- Kelch-like protein 9
- Kelch-like protein 13
- Kelch-like protein 42
- Kelch-like protein 3
- Kelch-like protein 20
Sequence:
MALGLEQAEEQRLYQQTLLQDGLKDMLDHGKFLDCVVRAGEREFPCHRLVLAACSPYFRARFLAEPERAGELHLEEVSPDVVAQVLHYLYTSEIALDEASVQDLFAAAHRFQIPSIFTICVSFLQKRLCLSNCLAVFRLGLLLDCARLAVAARDFICAHFTLVARDADFLGLSADELIAIISSDGLNVEKEEAVFEAVMRWAGSGDAEAQAERQRALPTVFESVRCRLLPRAFLESRVERHPLVRAQPELLRKVQMVKDAHEGRITTLRKKKKGKDGAGAKEADKGTSKAKAEEDEEAERILPGILNDTLRFGMFLQDLIFMISEEGAVAYDPAANECYCASLSNQVPKNHVSLVTKENQVFVAGGLFYNEDNKEDPMSAYFLQFDHLDSEWLGMPPLPSPRCLFGLGEALNSIYVVGGREIKDGERCLDSVMCYDRLSFKWGESDPLPYVVYGHTVLSHMDLVYVIGGKGSDRKCLNKMCVYDPKKFEWKELAPMQTARSLFGATVHDGRIIVAAGVTDTGLTSSAEVYSITDNKWAPFEAFPQERSSLSLVSLVGTLYAIGGFATLETESGELVPTELNDIWRYNEEEKKWEGVLREIAYAAGATFLPVRLNVLCLTKM
Protein: Lethal giant larvae homologue 2 domain-containing protein (A0A0K3AWL6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MDRAKKKFASAIDGLRSLHNRTEINVDEKIQSEHCRFTRVVRHGLPEDPRCFAYDPVQRLIAIGTGRGHIRIIGDAGVDYLLKHESGEPVLHMQFLVNEGGLITSCGTDSIHLWNYRQKTAEIVHTVQLSKESVSCIHLPVAGKWLFIGTDKGNVYFLCLNSFLLSPYVINWNKAIDLSCRVHPGPVRQLAVSPAENTKLLIVYDKGIVVQWNLGTREVDRYPLDPPIKSVNWHFDGRQILTGNVDGSISLYNHKKSTEAIQRTTPHGSGPCRPIQQVEWKHMSETESIIMFSGGMPTDDGLPMPALTILKGGKSATVLEMDWPIIQFIPLNQNIWNSIPQCPHSVAVLLKHDFMVLDLNQNGHPVIESPHAMNIHESPVTCMAYYSDCPLDLIGALTLVGTKQRNKEFSARSWPVTGGLGRECATGHQELVVTGHKDGSLKFWQETGEHLQILYKLKSSSHFERLEEMETSDKVSHAVKYIELCLESRQLLVAGISGQVTLFRFTKQEICGTIAVVNIPLLGNLSSNLPNNDFDKSPVPNGPGKEIRRQRKIVSRESTNSLDTSDSGDERIVPFKVRGAPVKRPPGFVPELACFVPWHSHAKVDQITTICLNSSYGIIAIGTSSGLALVDTTQCALIYSWTTNELYGSDPTPAIQLSMQLSDAASPLEIDEFENDDTLIYNTDTGNYTLRSTRNSLTPSSNGFLHPGEMPTRPKSAANSSNKSGGMMGLFRRNTAELAATIRERYQGNRSESATTDRPDVEHRGETPPPTPNEGNKVQKAGRSHSVKGSFIRRFAKSSSSKEKKEVKIEVDNQSNSGIERSRSFHSHISEEGDSQRESPSSGRQLNTSSPSTSSQSLERSMSTQPQESITSLSFIHSYSKKNDSKMSPCLWVGTSAGASLALNLILPEDRFTSTIVVAPSAVEECTVVRLKGQVISQSFMDNTFCIISPASESYKEAAKEQSATSPDRSLLNRVNTKASLAPQYSSSIDSNDEISQILIVAAENEVKVVALPTFSQLYVQKFDEIPLVKATPTHIRGYPCLMCLSAAGQIIMLSLPSLRILQTSTIFPHSVEIDDPLCQKTAFSDHGLGVYMASQTEMEKYTMCSEIAEQTGESLGELFVPCEMPEQPKNNSFLKGVSSIFGGTPRNDPNDIDAILSENMGVKNSSGVNPMRSVARTIPGPSVQMDRAQAGGVSAGQAAAMALQNLNERTEKLNATVDATENLKNNAMSLSSRTGKLVEKYEKKKWYNF
Protein: One cut domain family member 3 (One cut homeobox 3) (Transcription factor ONECUT-3) (OC-3) (Q8K557)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator. Binds the consensus DNA sequence 5'-DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374, ECO:0000269|PubMed:15381696}.
Interaction partners:
Sequence:
MELSLESLGGLHGVTHAQAGELLSPGHARSAAAQHRSLVASGRPGLVAGMASLLDGGGAGGGGAGGAGAAGAAGGGPDFRGELAGPLHPAMGMACEAPGLGGTYTTLTPLQHLPPLAAVADKFHQHAVAGAHGGHPHAHPHPATAPPPPPPQRLAASVSGSFTLMRDERAALASVGHLYGPYGKELPTMGSPLSPLPSALPPALHSAPQPPPPPPLAAYGAPGHLAGDKLLPPAAFEPHAALLGRAEDALARGLPGGGGGAGGGGAAGGAAAGLLAPLGGLAAAGAHGPHSGGGGPGGGGGAGGGSGGPGAGAAAEEINTKEVAQRITAELKRYSIPQAIFAQRILCRSQGTLSDLLRNPKPWSKLKSGRETFRRMWKWLQEPEFQRMSALRLAACKRKEQDQQKERALQPKKQRLVFTDLQRRTLIAIFKENKRPSKEMQATISQQLGLELNTVSNFFMNARRRCMNRWAEEPGATPGTGTATATFSKA
Protein: Calcium-dependent protein kinase 11 (EC 2.7.11.1) (Calcium-dependent protein kinase isoform CDPK2) (AtCDPK2) (Q39016)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger. Functions as regulator of the calcium-mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA-responsive transcription factors ABF1 and ABF4 in vitro.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16438971}. Nucleus {ECO:0000269|PubMed:16438971}.
Interaction partners:
- Protein DEHYDRATION-INDUCED 19
- Respiratory burst oxidase homolog protein D
- ABSCISIC ACID-INSENSITIVE 5-like protein 4
- ABSCISIC ACID-INSENSITIVE 5-like protein 7
- Respiratory burst oxidase homolog protein B
- 17.6 kDa class II heat shock protein
- Calcium-binding protein CP1
- Respiratory burst oxidase homolog protein F
- Protein phosphatase 2C 56
- Guard cell S-type anion channel SLAC1
Sequence:
METKPNPRRPSNTVLPYQTPRLRDHYLLGKKLGQGQFGTTYLCTEKSTSANYACKSIPKRKLVCREDYEDVWREIQIMHHLSEHPNVVRIKGTYEDSVFVHIVMEVCEGGELFDRIVSKGHFSEREAVKLIKTILGVVEACHSLGVMHRDLKPENFLFDSPKDDAKLKATDFGLSVFYKPGQYLYDVVGSPYYVAPEVLKKCYGPEIDVWSAGVILYILLSGVPPFWAETESGIFRQILQGKLDFKSDPWPTISEAAKDLIYKMLERSPKKRISAHEALCHPWIVDEQAAPDKPLDPAVLSRLKQFSQMNKIKKMALRVIAERLSEEEIGGLKELFKMIDTDNSGTITFEELKAGLKRVGSELMESEIKSLMDAADIDNSGTIDYGEFLAATLHMNKMEREENLVAAFSYFDKDGSGYITIDELQSACTEFGLCDTPLDDMIKEIDLDNDGKIDFSEFTAMMRKGDGVGRSRTMMKNLNFNIADAFGVDGEKSDD
Protein: Solute carrier family 38 member 10 (Amino acid transporter SLC38A10) (Q5I012)
Organism: Mus musculus (Mouse)
Function: Putative sodium-dependent amino acid/proton antiporter.
Subcellular location: Membrane {ECO:0000305|PubMed:28593130}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTAASTSKWGLITNVVNSIVGVSVLTMPFCFKQCGIVLGALLLVFCSWMTHQSCMFLVKSASLSKRRTYAGLAFHAYGKAGKMLVETSMIGLMLGSCITFYVVIGDLGSNFFAPLLGLQVTRTVRVFLLFAVSLFIVLPLSLQRNMMASIQSFSAMALLFYTVFMFVIVLSSLKHGLFSGQWLRQVSYIRWEGVFRCVPIFGMSFACQSQVLPTYDSLDEPSVKTMSSIFASSLNVVTAFYVMVGFFGYVSFTDATTGNVLIHFPSNPVTEMIRVGFVMSVAVGFPMMILPCRQALNTLLFEQQQKDGTFAAGGYMPPLRFKVLTLSVVFGTMVGGVMIPNVETILGFTGATMGSLICFICPALIYKKAHKNAPSAQVVLWVGLGILVVSTLTTLSVTEEAPLDLTQEARSGHRGDAEGAMKVEAARLSVQDPVVVVAEDSQEKLKPAEDKEVLEQAQIKGPVDVPGGEAPKEKQEAAQLDRPGQGIAVPMGEAHRHEPPIPHDKVVVDEGQDQEGPEEKKPPPRLPDEGDPAGRGQGAPPLPESEKEKQEPERGGEGKRPGQVLAVGETEHPQKVPEANGQPPVQPRKEDSRPGNRDPQPAAQARDSVELKALAADDGREPAQKAGGALWKPVESAAESDAGGKAGLPVQRPEAAEQREKKEAEQQGGDQAGSKLEAEIKKLVAEAGRAEMLDHAVLLQVIQEQQVQQKRLLDQQEKLLAVIEEQHKEIRQQRQEGEEDKPKPADVQPEPGVAVLRGQEEEAEHAGETLGDDPSQPLQPVLGAPRGRPAPSQDMGQHLPGEVKVLPGRDLADLPAGGSETEPQGAPIDLREDPKAAIKAAGAGKELVPGDLEAVHKAAPPEVPKSPEKQVAKAVAGQRQDVFGEGSEERKETGKEAMAPGADTQKEAVQPLVGAEAKDTKSRQSGPTKAPVQTQAKFHPEPQAIFDTGQGSHPEVRSEAPRAVHIPPEEQHKGKGGAAIQEAKQRPDPNSGPKLAVPAGQKPENAKPNRDLKVQAGSDLRRRRRDLASHPEQELAPKDGVIISFNSLPNVQVNDLRSALDTQLRQAAGAALQVVHSRQIKQLSGDLEEA
Protein: Syndecan-1 (SYND1) (CD antigen CD138) (P47951)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Cell surface proteoglycan that bears both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix. Regulates exosome biogenesis in concert with SDCBP and PDCD6IP.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:P18827}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P18827}. Note=Shedding of the ectodomain produces a soluble form. {ECO:0000250|UniProtKB:P18827}.
Interaction partners:
Sequence:
MRRAALWLWLCALALRLQPVLPQIMAVNVPPEDQDGSGDDSDNFSGSGTGALPDITLSRQTSSTLKDVWLLTATPTAPEPTSRDTEATFTSILPAGEKPGEGEPVLIAEVDTSSTTWDKELEVTTRPRETTQLLVTHRVSTARATTAQAPVTSHPHRDVQPGLHETLAPTAPGQPDHQPPSGGTSVIKEVAEDGATNQLPTGEGSGEQDFTFETSGENTAVAAIEPDQRNQPPVDEGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA
Protein: Methylenetetrahydrofolate reductase (EC 1.5.1.53) (D4A7E8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Methionine synthase
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Methylenetetrahydrofolate dehydrogenase
- Thymidylate synthase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Cystathionine gamma-lyase
- Betaine--homocysteine S-methyltransferase 1
- Uncharacterized protein.
Sequence:
MSRNPAMSNEARRSGSPSPRSEGSSSGSESSKDSSRCSTPSLDPDRHERLREKMRRRMDSGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLFVDVTWHPAGDPGSDKETSSMMIASTALNYCGLETILHMTCCQQRQEEISGHLHRAKQLGLKNIMALRGDPVGDHWEAEEGGFSYATDLVKHIRNEFGDYFDICVAGYPKGHPDAESFEDDLKHLKEKVSAGADFIITQLFFEASSFFSFVKACEDIGISCPILPGIFPIQGYTSLRQLVKLSKLEVPQTIKDVIEPIKDNDAAIRNYGIELAVNLCRELLDSGLVPGLHFYTLNREVATMEVLKQLGMWTEDPRRPLPWAVSAHPKRREEDVRPIFWASRPKSYIYRTQGWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPREELLKMWGEELTSEESVFEVFEHYLSGEPNRHGYRVTCLPWNDEPLAAETSLMKEELLRVNRLGILTINSQPNINGKPSSDPVVGWGPSGGYVFQKAYLEFFTSRETVEALLQVLKTYELRVNYHIVDVKGENITNAPELQPNAVTWGIFPGREIVQPTVVDPISFMFWKDEAFALWIEQWGKLYEEESPSRMIIQYIHDNYFLVNLVDNEFLLDNCLWQVVEDTFELLNRHTTKKEAQAP
Protein: Autophagy-related protein 13 (Q2ULT1)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Activates the atg1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, atg13 is also required for glycogen storage during stationary phase (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06628}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q06628}.
Interaction partners:
- Autophagy-related protein 17
- Serine/threonine-protein kinase atg1
- Autophagy-related protein 101
- Autophagy-related protein 11
- Autophagy-related protein 9
- Autophagy-related protein 29
- Vacuolar protein 8
- Serine/threonine-protein kinase TOR
- Raptor N-terminal CASPase-like domain-containing protein
- Uncharacterized protein
Sequence:
MHQHPRSPAPTAPTSSARPNSSRSRELDYRPNSPAADVRVHNSRGLGIETEPDSSGQTVQPAKEAIAKLNQIISNYHTKAALIILHSRIELPPSFNKGSDTPRVNRWFNVEIEDTDVLREQLRTWRTCDATENRPPPLIIETYLDTKGLTNNQTLVALDENGKRWDVLEALAASQQAHPVRPPSASSDDVILERWRVELGDTSNALPADLGSILPTVYKKSIVLFRSLFTYSKFLPAWKFAKRNGRLRANPALRIKYRIIIGSPNQVSSKPDHLTMPLYESSSKVVETYSFGVTDSPAGPFSAQVTYRTSCDFRVDDSEALLSSRFMGADDEIFRPSLPTRVVDSKVPPPEIGSLPQERRTIEDPDPGRAYGSLSTFHQVGPTTSASPISALRAKGKLGTSSPSSPGSSSRKALAVAKASPVGRAAALASEGSPGVVRRPSISFQPFKAPPLSASPSLVDPPLSSPRSVSGPRPHPPMAASARKSFPAVQDNSIASPSSASPRPSSISRYSSAFSHRRGRPSSGGINKLEDDTSSGKASATSSAQPGSGLLAEPTGTSADSIHADDENISEFLKMLDLRKDLLNTSGSAALDATARRTTVTSAALTRFQRMRDSNAALSDSMSSSLLLQRSSNSSSKQLSGVPPMVAGTSISTASSPGKPISPHTPHTPAIPSRLSSNSIVDYTHSEGNGTELSQGHGSPLDENTSDGTTMEHGPSAVNAIDIPTSPRLFPPVYRRSSSAAHRPRTVAVDDDEIFPFNRSVSLGAEERSNLSLGALHRQHEYESSDTATHRAQREPRPMSSNEDAVVPPSSITRGQGSHKGVTPGPTVASSSSSHHHVYQPRFSHSRGRGSSGGHHSLSSGSSSLARGAAITPGLAERESERDGNGSGSNSVTSAMEDRRGVGRRPSAGRGGPPQSAQLEEDEPLLFAMSDFGASRRSFEEGKHVNHAHDPTGNIAGSRRGGSSRRGGGFHAWS
Protein: Alpha-L-fucosidase 1 (EC 3.2.1.51) (Alpha-1,3/4-fucosidase) (AtFUC1) (Alpha-L-fucoside fucohydrolase) (Q8GW72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes both 3- and 4-linked fucoses in Lewis determinants. Not active on neither 2-linked fucose nor on fucose in alpha-1,3-linkage to the innermost GlcNAc.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:11788770}.
Interaction partners:
- Alpha-L-fucosidase 3
- Alpha-L-fucosidase 2
- Beta-hexosaminidase 3
- Bifunctional fucokinase/GDP-fucose pyrophosphorylase
- BNR/Asp-box repeat family protein
- At5g04750
- Pre-mRNA-splicing factor
- Uncharacterized protein At2g27730
- Glycoprotein 3-alpha-L-fucosyltransferase A
- SKU5 similar 3
Sequence:
MNSQITLFFFFFSILSLSQISNSSSLLKPHPCPILPLPSSQQLQWQLGSMAMFLHFGPNTFTDSEWGTGKANPSIFNPTHLNASQWVQIAKDSGFSRVILTAKHHDGFCLWPSEYTDYSVKSSQWRNGAGDVVAELASAAKEAGIGLGLYLSPWDRHEQCYGKTLEYNEFYLSQMTELLTKYGEIKEVWLDGAKGDGEKDMEYFFDTWFSLIHQLQPKAVIFSDAGPDVRWIGDEAGLAGSTCWSLFNRTNAKIGDTEPSYSQEGDGYGQDWVPAECDVSIRPGWFWHASESPKPAVQLLDIYYNSVGRNCLFLLNVPPNSSGLISEQDIKVLEEFSEMKNSIFSNNLARKAFVNSSSIRGDQSSQFGPKNVLEEGLDKYWAPEENQNEWVLYLEFKDLVSFNVLEIREPIHMGQRIASFHLETRKTGSGEWERVVSGTTVGNKRLLRFLNVVESRSLKLVVDKARTDPLISYLGLYMDKFSGSSRNTTKITITRTLKEEQQLHDL
Protein: ABC transporter G family member 18 (ABC transporter ABCG.18) (ABC transporter mdrA2) (Q8ST66)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for endocytosis and endosomal pH regulation.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Uncharacterized protein csb family protein DDB_G0271196
- RING zinc finger-containing protein
- Probable myosin light chain kinase DDB_G0282429
- Protein rtoA
Sequence:
MENEEKREYLAKSRSNSRNFLNDSIESKNIFGVDKKSEPNLKQSIDGGLNFSTTSSYNPSNLPRTSVFVSARNLSSTVGHGKNEKKILTDLNFFLKPGSMVLLLGSPGCGKTSLMNTLALLTSNEKITGNLLFNGKTGDPNTHHRHVSYVVQDDFHMAPLTVRDTFKFSADCQSGDKSEKERIEIVDNVLDFLDLKHVQNTVVGDEFLRGISGGQKKRVTIGVELVKESNLLLMDEPTNGLDSSISLEMLTKIKNKVQQEKMSCLISLLQPGLEITKLFDYLMIMNQGQMSYFGPMNQAIGYFEGLGFKFPKHHNPAEFFQEIVDEPELYCGIDDGSSDGGSGDSGSSSGGSNYNYNFKNKASSTMMMMNNNNKIIPPLKGSDEFAMAYRKSIIYKHILEYIDSHIPDEEERSKFIDYSTTLKPYSTGFGRQLSLNVKRGFKLFLGNKASIRLRLLKNVIIGFILGTLYWKLDTTQADGSNRSGLLFFSLLTFVFGGFGSISVFFDQRQVFYSERAWKYYNTITYFLSMIVTDLPMSIVEVLIFSNFVYWMTGLNKTWDRFIYFFLTCLVCDVMSLSIIRSVCSFTKTKYAASAISPAVVSPFILMCGYMKHSNEIPGWWIWLYWISPIHYGFEGLLLNEHSGLDYHCSPDELMPPSFLPTFNTSYPVGFEGNQVCPITKGEQILDSIGFHTEFYYRWVDLAIISAFTLLFWLITLVCMKFLVFRVYRKDPVGIKKSKPNKTTTLIKMNRNSTDSTTTNNSMNYFNNKHNKKQNDDSDSGEEMESVDVDVKSSGKANLRKDIPIGCYMQWKDLVYEVDVKKDGKNQRLRLLNGINGYVKPGMLVALMGPSGAGKSTLLDVLANRKTGGHTKGQILINGQERTKYFTRTSAYVEQMDILTPVSTVREVILFSAKNRLPNSVPIQEKEEFVDNILETLNLLKIQHSLIGDVESGLSLSQRKRVNMGIELASDPQLLFLDEPTSGLDSSAALKVMNLIKKIASSGRSVICTIHQPSTTIFKKFDHLLLLKRGGETVYFGPTGTNSKIVLNYFAERGLICDPFKNPADFILDVTEDIIEIIQPPQTLPTSTSNENNNNNNNNNNNNNNNNNNNNNNNNNNNNGNTSDTLNNNNKKNLESSLSSSSISFDPVESFKESKENQKLLSIVENSIMPVGTPVAVYHGKYSSTIKTQFIELLKRSWKGGIRRVDTIRTRVGRSFVLGLVIGTLFLRLDKEQNDVFNRISFLFFSLMFGGMAGLSIIPTVSTERGVFYREQASGMYRVWIYYLTFVLSDLPFVIITSYAYVIPVYFLTGLSLSNHGWDFFYHSFISVMLYLNFGLTSIAFATSLPVEEMAFLLNGVLLSVTSLFAGFMIPPPSMPAAWKWAFYLDFISYPLKAFLITEFKDMEFVCTDNKGAIPIPIPSQNTTKFFCPITHGTQVLDRIDYKISFQYWDILIMASFTFALLVGGYLSLKFIRYQNK
Protein: 2-hydroxyacyl-CoA lyase 1 (EC 4.1.2.63) (2-hydroxyphytanoyl-CoA lyase) (2-HPCL) (Phytanoyl-CoA 2-hydroxylase 2) (Q9UJ83)
Organism: Homo sapiens (Human)
Function: Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids. Plays a significant role in the biosynthesis of heptadecanal in the liver (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:10468558, ECO:0000269|PubMed:21708296, ECO:0000269|PubMed:28289220}.
Interaction partners:
- Peroxisomal targeting signal 1 receptor
- PEX5-related protein
- Alanine--glyoxylate aminotransferase
- Citrate synthase, mitochondrial
- Myocardin-related transcription factor A
- Guanosine-3',5'-bis
- Sterol carrier protein 2
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2
- 2-iminobutanoate/2-iminopropanoate deaminase
Sequence:
MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVTLLGNIHAVTKQLLEELDKTPWQYPPESKWWKTLREKMKSNEAASKELASKKSLPMNYYTVFYHVQEQLPRDCFVVSEGANTMDIGRTVLQNYLPRHRLDAGTFGTMGVGLGFAIAAAVVAKDRSPGQWIICVEGDSAFGFSGMEVETICRYNLPIILLVVNNNGIYQGFDTDTWKEMLKFQDATAVVPPMCLLPNSHYEQVMTAFGGKGYFVQTPEELQKSLRQSLADTTKPSLINIMIEPQATRKAQDFHWLTRSNM
Protein: Cyclin-dependent kinase 2-associated protein 2 (CDK2-associated protein 2) (DOC-1-related protein) (DOC-1R) (Q9CPY4)
Organism: Mus musculus (Mouse)
Function: Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (By similarity). Inhibits cell cycle G1/S phase transition by repressing CDK2 expression and activation; represses CDK2 activation by inhibiting its interaction with cyclin E and A (By similarity). Plays a role in regulating the self-renewal of embryonic stem cells (ESCs) and in maintaining cell survival during terminal differentiation of ESCs. Regulates microtubule organization of metaphase II oocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12944431}. Nucleus {ECO:0000269|PubMed:12944431}. Note=Accumulates in immature oocytes in the nucleus. During the first meiotic division, accumulates in the cytoplasm and localizes in dots in the vicinity of the chromosomes in a region enriched in microtubules. {ECO:0000269|PubMed:12944431}.
Interaction partners:
Sequence:
MSYKPIAPAPSSTPGSSTPGPGTPVPTAGSVPSPSGSVPGAAAPFRPLFNDFGPPSMGYVQAMKPPGSQGSQSTYTDLLSVIEEMGKEIRPTYAGSKSAMERLKRGIIHARALVRECLAETERNART
Protein: Angiopoietin-like 2 (Angiopoietin-related protein 2b isoform X1) (Q5KQT9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDVPSLVCLVLLLASGWFPETEGSPQEFDSSDEGPEVEFLSTTRTRRAPEPPPQDKCSYTFIVPQQKVTGAICVNSKEPEAVLENRVNKQELELLNSELHKQKRQIETLQQLVEVDGGIVNEVKLLRKESRNMNSRVTQLYMQLLHEIIRKRDNALELSQLENKILNQTSEMLQLTNRYKDLEHKYQHLASLANNQSALIALLEAQCQRGPPVPRVPVQPQPQPQPQPQPHPQPRPSPPLNKPYQPPTFNRNNQITNEIQSDQNLKVPPAPPPTMPGGTHSPSTTNKPSGPWKDCLEALEDGHTNSGMHLVKPDNTNKLMQVWCDQRQDPGGWTVIQRRMDGSVNFFRNWETYKQGFGNIDGEYWLGLENIYWITNQGNYKLLVTLEDWSGRKTFAEYASFRLEPEADFYRLRVGRYHGNAGDSLTWHNGKQFTTLDRDHDVYTGNCAHYQKGGWWYNACAHSNLNGVWYRGGHYRSRYQDGVYWAEFRGGAYSLKKVVMMIRPNPNTFH
Protein: Transmembrane protein 132A (HSPA5-binding protein 1) (Q922P8)
Organism: Mus musculus (Mouse)
Function: May play a role in embryonic and postnatal development of the brain. Increased resistance to cell death induced by serum starvation in cultured cells. Regulates cAMP-induced GFAP gene expression via STAT3 phosphorylation (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MTERKAAAPRGPYGAWFCLLVALALEVVRVSSNHDTLDPIYLPVALELLDAPEHFRVQQVGHYPPANSSLASRSETFLLMQPWPRAQPLLRASYPPFATQQVVPPRVTEPHRRPVPWDVRAVSVEAAVTPAEPYARVLFHLKGQDWPPGPGSLPCARLHATHPAGTAHRACRFQPSLGACVVELQFPSHWFSQSATTRAELAYTLEPAGEGPGGCGLGTEEEPREQALPVGGVELHPEDPPQYQEVPLDEAVTLRAPDVPMRPGQLFTATLLLRHNFTASLLTLRIKVKKGLQVIAARPAQPTLWTAKLDRFKGSKHHTSLITCHRAGPAGPDSSPLELSEFLWVDFAVENSTGGGVAVTRPVTWQLEYPGQAPEAEKDKMVWEILVSERDIRALIPLAKAEELVNTAPLTGVPQRIPVRLVTVDSGGALEEVTEHIGCESANTQVLQVSEACDAVFVAGQESRGAKGVRVDFWWRRLRASLKLTVWAPLLPLRIELTDTTLEQIRGWRVPGSAEGQLEPETAAEEVERRSRGCRLQYQRAGVRFLVPFAAHPLDGGRRLTHLLGPDWLLDVSHLVAAHAHVQDPRIASLEGGRILVGREPGVTSIEVRSPLSDAILGEQALAVTDDKVSVLDLRVQPVMGISLSLSRGMSHPGEVTATCWAQSALPAPKQEVALSLWLSFSDHTLAPAELYDRNDLGLSVSAEEPSAVLPAEEQGAQLGVVVSGVGAEGLPLHVALHPPEPCRRGRHRVPLASGTAWLGLPPLPTPVPALPSSPVRTSPFTEATVEGKRQIAGDMGGHVGIRGKFERAEEEAGKEENEAKEEEEDEEEMVPAPQRVTDLELGMYALLGIFCLAILIFLVNGVVFVLRYQRKEPPDSATDPASPQPHNWVWLGTNQEELSRQLDRCSSSGPPKGEGGCPCESGAGGDASTVAPSASESPAGSSSTLARKEAGGRRKRVEFVTFAPAPPTQPPEEPVGAPAVQSILVAGEEDIRWVCEDMGLKDPEELRNYMERIRGSS
Protein: Kinase D-interacting substrate 220 (A0A1Y7VME9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSVLISQSVINYVEEENIPALKALLEKCKDVDERNECGQTPLMIAAEQGNVEIVKELIKNGANCNLEDLDNWTALISASKEGHIHIVEELLKCGANLEHRDMGGWTALMWACYKGRTDVVELLLSHGANPSVTGLYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGQQIEPLFQFSWLIVFLILLLCGGLGLVFAFTVDTNLAIAVSLSFLALLYIFFIVIYFGGRQEGESWNWAWALSTRLARHIGYLELLFKLMFVNPPELPEQTTKALPVRFLFTDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDSQGKKKWKKTCCLPSFIIFLFIVGCIIAGITLLAIFRVDPKHLTVNAILISIASIVGLAFVLNCRTWWQVLDSLLNSQRKRLHSAASKLHKLKSEGFMKVLKCEVELMARMAKTIDSFTQNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLRDSNINGHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDISCSEATGVQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQMQRTITRQMSFDLTKLLVTEDWFSDISPQTMRRLLNIVSVTGRLLRANQITFNWDRLASWINLTEQWPYRTSWLILYLGETEGIPDQMTLKTIYERISKNIPTTKDVEPLLEIDGDIRNFEVFLSSRTPVLVARDVKTFLPCTVNLDPKLREIIADVRAAREQINIGGLAYPPLPLHEAPPRPPSGYSQPASVCSSSASFNGPFPGGVVSPQPHSSYYSGLSGPQHPFYNRPFFAPYLYTPRYYPGGSQHLISRSSVKTSLPRDQNNGLLCDSGFNKQRQASVPATGTSLLLSSMTVDIVCEKLRQIEGLDQGMLPQYCTTIKKANINGRVLAQCNIDELKKEMAMNFGDWHLFRSMVLEMRSVENQVVPEDPRFLNENSSAPVAHGESARRTSHSELPHTELSSQTPYTLNFSFEELNTLGLDEGAPRHSNLSWQSQTRRTPSLSSLNSQDSSIEISKLTDKVQAEYRDAYREYIAQMSQLEGGTGSSTISGRSSPHSTYYIGQSSSGGSIHSNLEQERGKENELKQEEGRKSFLMKRGDVLDYSSSGVSTNEASPLDPITEEDEKSDQSGSKLLPGKKSSERPSLFQTDLKLKGSGLRYQKLPSDEDESGTEESDNTPLLKDDKDKKAEGKAERVAKSPEHSVEPIRTFIKAKEYLSDALLDKKDSSDSGVRSNESSPNHSLHNEAADDSQLEKANLIELEDEGHSGKRGMPHSLSGLQDPVIARMSICSEDKKSPSECSLIASSPEESWPSCQKAYNLNRTPSTVTLNNNTAPTNRANQNFDEIEGVRETSQVILRPGPSPNPTAVQNENLKSMAHKRSQRSSYTRLSKDASELHAASSDSTGFGEERESIL