wanglab/gogpt-training-data huggingface dataset:
Protein: Exocyst complex component SEC5A (AtSec5a) (Exocyst complex component 2) (Q8S3U9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. Probable component of an exocyst subcomplex specifically involved in autophagy-related, Golgi-independent membrane traffic to the vacuole. Regulates autophagosome formation and autophagy-related Golgi-independent import into the vacuole.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:24307681}. Secreted, extracellular exosome {ECO:0000269|PubMed:24307681}. Note=Localized to globular structures in the perinuclear region (PubMed:19895414). Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2 (PubMed:24307681). {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:24307681}.
Interaction partners:
- Exocyst complex component SEC6
- Exocyst complex component SEC3A
- Exocyst complex component SEC8
- Exocyst complex component EXO84B
- Exocyst complex component SEC3B
- Exocyst complex component SEC15B
- Exocyst complex component SEC10a
- Exocyst complex component EXO84A
- Exocyst complex component EXO84C
- Exocyst complex component SEC10b
Sequence:
MSSDSNDLDEDELLQMALKEQAKRDLTYQKPPSSSARKPVANLVQQPRQQKPVAAAAAPPKKSAAAVRKPSMDEDEESEVELLSISSGDDDLEREREIGGSSGGAGRGRGSDVREKGRARKEDDGAWDGGEPDCWKRVNEAELARRVRDMRESRTAPVVQKVEGKAPAPGKKVALTSLQSLPRGMECIDPLKLGIIDNKTLRLITESSGSPSKAEKVDNTLREKLVYFSDHFDPKLFLSRIHQDTTAADLEAGALGLKSDLKGRNLQRKQLVKDNFDCFVSCKTTIDDIESKLKRIEEDPEGSGTTHLFNCMKSVTSRANLAFEPLFERQAQAEKIRSVQGMLQRFRTLFNLPSIIRSSISKGEYDLAVREYKKAKSIALPSHVNILKRVLEEVEKVMLEFKGTLYKSMEDPKIDFTSLENTVRLLLELEPESDPVWHYLNVQNHRIHGLLEKCTYDHEARVEILRNDTHEKAISDAKWQQIQQNGVSYSDTASSNENNAVQVDLQSVEFPSEEIDILKGRYIKRLTAVLVHHIPVFWKTAISIFSGKFAKSSQVTDTSANKAEEKVTEARYSTHSLEEVAGMIRKTISVYEAKVNSTFCDFDESCILRPFMSDAINEVSKACQAFEAKESTPHSAVVALRKIQAEITKIYIQRLCSWMRASTEGISKEETWIPVSILERNRSPYAISYLPLAFRSVIVSGMEQVNLMILSVKSEAAKSEDMFAQIEEIIISVRLAFLNCFLDFAAHLEQIGADLSQSTSRQDNWKNGYSDEHQEEPSANTYGSVIDPHRRLLMVLSNIGYCKDELASELYNKFKYTWLQSRDKNEDSSDLQDLIMSFSGLGEKVLEHYTFAKANLIRTAATNYLLDSGIQWGSAPQVKGIRDAAVELLHTLVAVHAEVFAGAKPLLDKILGVLIEGLIDTFLSVVEENRSSDLRSIDANGFCQLMFELEYFETVLYSYFTSAATESLKSLQGTVLEIAIESISEAVETPGHNRRPTRGSEDTVSDDKQSVSADDLLALTKQCSNELLQQELERTRVNTACFAESAPLESTPPLPKATYSSFRGSMDSPSRNYRGSQSSGSPINARPRRR
Protein: 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS) (Q72EV5)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210}.
Interaction partners:
- Chorismate synthase
- Shikimate kinase
- Shikimate dehydrogenase
- Bifunctional chorismate mutase/prephenate dehydratase
- Shikimate kinase
- Prephenate dehydrogenase
- Cytidylate kinase
- AMP-binding enzyme family protein
- Predicted 3-dehydroquinate synthase
- Anthranilate synthase, glutamine amidotransferase component
Sequence:
MEPVVVTAPPSKSLSHRALIGAALAAGESTVEHVLESRDLTCTADILRAAGAHIERRAPGSYLVRGVAGTPAGGFEAPVSCDVHESGTTCRLLTAVLAAGMGRFRIHGAPRMHERPIGELTDALASLGVQIAFEARAGFPPLVIDAAGMRGGEVSIGMDESSQYLSGLLLAAPLTQGMTVNVAGKSVVSWPYVGLTLQTLEDFGIDFTVETRDAVDAPWGAVDWRSLHEAVPGLVRFRVRPGMYRAGSYRVEGDWSGASYFLAAGAVGPRPVRVEGLRVDSLQGDRALLDILTAMGADIRPGEGHVVVHPAPLHGVEVDMGHCPDLVPTVAAVAAFATGRTVVRNVAHLRIKESDRIAAPVGELRRAGVNAEERADGLVVQGGALATEPGTLFSAHGDHRMAMSLALLGLGGVDVRLDDPSCVSKSFPHFWELWEKVRA
Protein: Small ribosomal subunit protein mS38 (28S ribosomal protein S38, mitochondrial) (MRP-S38) (Aurora kinase A-interacting protein) (AURKA-interacting protein) (Q9DCJ7)
Organism: Mus musculus (Mouse)
Function: May act as a negative regulator of Aurora-A kinase, by down-regulation through proteasome-dependent degradation.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9NWT8}. Nucleus {ECO:0000250|UniProtKB:Q9NWT8}.
Interaction partners:
- Small ribosomal subunit protein mS37
- Small ribosomal subunit protein bS21m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein mS34
Sequence:
MFLARLTSRLARTVVPWAGFSRSCPGSGVIGSYAFRPLYSLQPASPSRAASLPGKRTQSELEEFLVPRKMAISPLESWLTAQYLLPRRNVEVPVTLAPSQFYECPPRQGEEEAQQGVREAWDATPVQCKNVLKIRRRKMNHHKYRKLVKRTRFLRRKVREGRLKKKQIKFEKDLKRIWLKAGLKEAPENWQTPKIYLKNK
Protein: Capsid scaffolding protein (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease) (Pr); Assembly protein (AP) (Capsid assembly protein)] (P09286)
Organism: Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3)
Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging.
Subcellular location: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.
Interaction partners:
Sequence:
MAAEADEENCEALYVAGYLALYSKDEGELNITPEIVRSALPPTSKIPINIDHRKDCVVGEVIAIIEDIRGPFFLGIVRCPQLHAVLFEAAHSNFFGNRDSVLSPLERALYLVTNYLPSVSLSSKRLSPNEIPDGNFFTHVALCVVGRRVGTVVNYDCTPESSIEPFRVLSMESKARLLSLVKDYAGLNKVWKVSEDKLAKVLLSTAVNNMLLRDRWDVVAKRRREAGIMGHVYLQASTGYGLARITNVNGVESKLPNAGVINATFHPGGPIYDLALGVGESNEDCEKTVPHLKVTQLCRNDSDMASVAGNASNISPQPPSGVPTGGEFVLIPTAYYSQLLTGQTKNPQVSIGAPNNGQYIVGPYGSPHPPAFPPNTGGYGCPPGHFGGPYGFPGYPPPNRLEMQMSAFMNALAAERGIDLQTPCVNFPDKTDVRRPGKRDFKSMDQRELDSFYSGESQMDGEFPSNIYFPGEPTYITHRRRRVSPSYWQRRHRVSNGQHEELAGVVAKLQQEVTELKSQNGTQMPLSHHTNIPEGTRDPRISILLKQLQSVSGLCSSQNTTSTPHTDTVGQDVNAVEASSKAPLIQGSTADDADMFANQMMVGRC
Protein: Transcription factor bHLH113 (Basic helix-loop-helix protein 113) (AtbHLH113) (bHLH 113) (Transcription factor EN 61) (bHLH transcription factor bHLH113) (Q9LT67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor bHLH143
Sequence:
MGDTAEDQDDRAMMEAEGVTSFSELLMFSDGVLSSSSDHQPEGNVGDGGEDSLGFVFSGKTGSRMLCFSGGYQNDDESLFLEPSVPTSGVSDLDPSCIKIDCRNSNDACTVDKSTKSSTKKRTGTGNGQESDQNRKPGKKGKRNQEKSSVGIAKVRKERLGERIAALQQLVSPYGKTDAASVLHEAMGYIKFLQDQIQVLCSPYLINHSLDGGVVTGDVMAAMKAKDLRSRGLCLVPVSSTVHVENSNGADFWSPATMGHTTSPSLPQGF
Protein: Inner centromere protein pic1 (INCENP-related protein pic1) (Q1MTN3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for chromosome segregation and cytokinesis. Has a role in sister chromatid cohesion and condensation.
Subcellular location: Nucleus {ECO:0000269|PubMed:16199877}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16199877}. Note=Associates with the elongating spindle during anaphase. {ECO:0000269|PubMed:16199877}.
Interaction partners:
- Aurora kinase
- Chromosomal passenger complex protein bir1
- Meiotically up-regulated gene 118 protein
- Kinetochore protein mis14
- Inner kinetochore subunit fta2
Sequence:
MGSNGSELWFNKELEYSQQLTNGKMKEFFFLVSETMDWLNEHMLEVSKLQLESDIYELVRTPTKIKEKYSTPRLSPVHRCALPTPRMRLTSIQHQLEEAAVEGYKSGESNTVKEPKELHTATNTETQFDDDRDSTKLSSEYVKDDIVNKSTKGGVSPIKETRLPTNLPAFSPTSVERRFTEWNVPLRETSPSPSETADSPNKLPKQKHPAYSFVTLPKREEILKRPASLHSRVESTNSFINQLNRRRTKDNLTNNPEISLDEPIKALPSTTSDAPSSLLNTNVSSSPSKFRKFLSSVIPAKTDLSAKESLTSSTRLSTSYKTRKRSSGVAFSSETVTSSSKERKRSVENEMLKPHPTIFESPPEITSFDKSNAVEAEALTAKLKSNEERLPVSSQPGSDAKSQEFDFFEAKIPDSIAKLNELTASNENHYELKTYDRAERLRQKIQEVSSNKRLIPSTPPTKKPINAVLDAAKNSAAKDLHLAKMKLNNKNDESSLSPAKSHAVITQAPKIPLISTFTRLSTRKSSNDFNSSNSRPSSNALKSDANENTDSSLPPSKKEFIEKSLHKLSEPLHDDSRQNSDHNFAPHSRPIAIRVATASQRELEQTEKRKAKNGAANASNMESRSSENETHRFKKFYGKERELSNNEFPSRQTKTVTSANSSNIRDMEHTISDKPRSEPDAIPSSKSMHSNKPFEEKSEKPTTKRLVTNPSNVNASWHSNMLKRQEDLRKKKPLTDNGATSRHMLKSGLTRVTSKPTQRFANELAEDMSLAFHSTIPKKMEPDSVTSVTQPSVGSLRNNFDIGTTNSQNEDRKKKIAAQKNKNPVHGNVGLTNQHGFKTMHHNVNPFTKQNGIMKGKLPSSSTSQSNKPFIEKASMHAPAKGRNSSMQEPSSKSPLLKTPKSNYFPGYGSLSPNTSVELPEINSDYSDDSDDEGNKKKVNLPSWAESPELREQLKRQQKWDPDKIFGMIKPLQMDEYFRSKDRSKIRFRPRSSSADWSSQDRLTQAEIDNYKKNMGFL
Protein: Protein PSP1 (Growth inhibitory protein 5) (Polymerase suppressor protein 1) (P50896)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA polymerase alpha mutation suppressor.
Subcellular location: Cytoplasm. Mitochondrion.
Interaction partners:
- Protein PSP2
- Checkpoint protein RAD24
- Protein virilizer
Sequence:
MDLPTVNSTTSISDNVDLKNYYEDLLFKNNSGKSLSDLPRKLNDNSNNSGSDTVDPLAGLNNLRNSIKSAGNGMENRRTFDDIDFMGRFPYLPPVPNQQQQPFSHQNGFIQEHPSSNLTSFQMSSSNSEPMSAPPISSNNNNLNSTQMGNYQAQQRSFPQFNGNSFHSNGNDLMGNRMDSDYMRLMNKTNIGFTSNSGSNFAAPSHSAGNPSSMNNQQVPSFNWQQPSHPESTIRRSSYISDTLINHQMPDARQKQTSQVQQQHAQGFNLFNSRFNYDNLNSTHLTAKGVPEFGNGVQPPYPYDNEPNNASISNSNNNNNSHNMVPMQQFRRNTQPVASFNPSLPTFQQQQQQPQQPQQPRNVNVPTSFNGERVDDVQLVQLQRSSSVPSSTNSHNLQNENSNEGNVSLDNGLVLIQGKHLTSSKTLHDLYSDCGSGYFASSAVFEFTDNIKKMLKLHDSNESYDAKNMGLIDEEGNTYQSLLNFLDILRSCNMNYVNDPESNNGIVSNNGGNKNRRKGSFTTELSCRNANNSFLPYTPLVLVALKNGKLELLSTPQATNLLLKRGDLVIIDGDRGRDLVLVVEPSVDLNLALFINFLKKKIHFDSLITSESQHYRNDEFIQMLIDSKNGQKKKLNPKLYDVVELTELIIPSKQVLRFATPWEVTTNLHNKFEDELKALHIAQSKLQALNDNSKSQNTNDSSSNNFTNAATYSKPKLNIKILNAEFQFDRKKLTFYYVCEERNDFRDLIKELFKYYKTRIWLCAIPNNLSIDSKYYDKQQKELKLYQNIVKNYNAEDLMNVNEFSQNRGNNRVNFAPPLNEIELDNFQIAVYEELVHELFH
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 3 (A4D1N4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00034476}; Lipid-anchor {ECO:0000256|ARBA:ARBA00034476}.
Interaction partners:
Sequence:
MGGTTSTRRVTFEADENENITVVKGIRLSENVIDRMKESSPSGSKSQRYSGAYGASVSDEELKRRVAEELALEQAKKESEDQKRLKQAKELDRERAAANEQLTRAILRERICSEEERAKAKHLARQLEEKDRVLKKQDAFYKEQLARLEERSSEFYRVTTEQYQKAAEEVEAKFKRYESHPVCADLQAKILQCYRENTHQTLKCSALATQYMHCVNHAKQSMLEKGG
Protein: Aspartic protease (EC 3.4.23.-) (O60020)
Organism: Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous)
Function: Possesses acidic protease activity. Hydrolyzes casein and azoalbumin in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:10091328}.
Interaction partners:
Sequence:
MISDTVIAILAVALVGSTVQAAPVDATATSTSGIIAVPISKSAAQLAREADPVVSLDWLKKTKAQAQYKHKQANARLHSKRATGASVLTDQGSESLWTGPITIGGQSFTVDWDTGSSDLWVPSSACSSAACNAHHKYTLTSTGKKQSGTFSISYGDGSSASGPVYKDNVVASGLQATSQVFGAVTSESSSFSSDPSDGISGLGWPALAQLSGTSYFWSLINQGTVTSPVFSFRLATTNSELYLGGINSAHYTGAITYTPVTQKAYWTIALGGVSVNGAAINPSVSSAIIDTGTTLVYGPTAGVAALYAKIPGSASMADTYGSDYQGYYTFPCSAVPTVALTFGGSSFSVPTSAFNLGTVSSGSKQCVGGIVGQGDGSWLVGDVFLQGVYSIYDVGNARVGFAKTV
Protein: Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic (ZmpTAC12) (B4FZ81)
Organism: Zea mays (Maize)
Function: Required for the activity of the plastid-encoded RNA polymerase (PEP) and full expression of genes transcribed by PEP. Required for the proper build-up and formation of the PEP-complex. Binds single-stranded (ss) DNA and RNA, but not double-stranded (ds) DNA.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:25599833}. Nucleus {ECO:0000269|PubMed:25599833}.
Interaction partners:
- Plastid transcriptionally active14
- Fructokinase-like 2
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE homolog, chloroplastic
- Protein PLASTID REDOX INSENSITIVE 2, chloroplastic
- Plastid transcriptionally active 3
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10
- Single-stranded DNA-binding protein WHY1, chloroplastic
- Plastid transcriptionally active 6
- mTERF family protein
- mTERF family protein
Sequence:
MASCYNPWRLFPGMSTAVPAGPVTAPAHSRTCKSSKVFSALPHRRGLLFLGTRRARIKCVKDDSLHFDPSKIEPPPYSSYFDSTSGQLEPASGARASIPGKEYWPEGTAARVRAARAPAPVGESAGMPSFGTKPGSRRRGYKEQVTSASGTEGAQTDDRKDGDEPDVAIIGSGDDALEEIKDSVDEYVIYETPEEEELSEYDMDKMMGRPHPFIDPAKAMSLGEPKTSEELWWHWRRKSQEEEMWSRWQRRRPDVDTVFAKAMAETGQIKIFGDHPSRTEAALAKTRRHLYKEERLEAEQRRLEEIGPIAYYSEWVEAYKNKDTSREAIQKHFEETGEDENVQLIKMFQHQTAGEYRIMMGTDVRIQRDPLAMRMREDQIKQIWGGDPVYPTINYVQDPDEVIDYRGPEFHEPTPEVVPYLMEHGIMITKEELYARLNEEREDVNQDITYIPEAKDPMATAIDIGEHSYNEDSDDEDEDVDKAAAQPQSLEDEEDDRDDVAEVEEKVNQNWSALKSTGQAEKPKEKSKKDEMTLKEAIDDSENLTDFLMDFEETE
Protein: Ethylene-responsive transcription factor 3 (AtERF3) (Ethylene-responsive element-binding factor 3) (EREBP-3) (O80339)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a transcriptional repressor. Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways and could also regulate other AtERFs.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- WUSCHEL-related homeobox 11
- Ras-related protein RABA4c
- Regulator of nonsense transcripts 1 homolog
- Regulator of nonsense transcripts UPF2
- Regulator of nonsense transcripts UPF3
- Nonsense-mediated mRNA decay factor SMG7
- Histone deacetylase complex subunit SAP18
- Histone deacetylase 19
- Eukaryotic translation initiation factor 4G
- Eukaryotic peptide chain release factor subunit 1-1
Sequence:
MRRGRGSSAVAGPTVVAAINGSVKEIRFRGVRKRPWGRFAAEIRDPWKKARVWLGTFDSAEEAARAYDSAARNLRGPKAKTNFPIDSSSPPPPNLRFNQIRNQNQNQVDPFMDHRLFTDHQQQFPIVNRPTSSSMSSTVESFSGPRPTTMKPATTKRYPRTPPVVPEDCHSDCDSSSSVIDDDDDIASSSRRRNPPFQFDLNFPPLDCVDLFNGADDLHCTDLRL
Protein: 2-oxoglutarate-dependent dioxygenase-like protein (T16N11.5 protein) (Q9M9D9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGGNETRELPIINLSDKNLKQNTELWSFTRDSVREAMEHHGWFVAEYNNFPTGLHQSILEAAKELLDLPVEIKLKNENHKAGHGYITMMSDGQPVHEGLGIDQVNDVQQCRGFSRLMWPDDHDDNDRFCETVHAYAKMQAELEQLVIRMLFESYNVEKYTEKYIGGTRYLLRLLKYRRLPNGEPNRKFISHTDKSFISILHQNHITGLMLKSEKEDVWYHFTPSPTRFVVIAGDAIMAWSNDRIKACYHKVEMESVEMRYSLGFFSFQEGMISTPEEMVDKDHPLAYNPFHHDGLLEYYETLEVHLKAHRTMTKAYCGIP
Protein: Cyk3p (A0A1D8PDV9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Formin-binding protein
- Inn1p
- CYK3 C-terminal Ig-like domain-containing protein
- Ras GTPase-activating-like protein IQG1
Sequence:
MTSTALPPLPFKVKTIVSWAGEEEGDLGFMENEIVQVFSIVDESWWSGKLRRNGAEGIFPKDYVTILEDKLNHSMSSLSLQDGRTTPTKQMDDHSRRSAGTTPLGNFSKLKTSQSFANDSIEYDQDHSFNQSFDDRYSKPFTPTKGNVRSSKYMSSAMNHPKNKLTYQQQEELLRKKEKEIEYFRSMQQQQNYQVKPKVNDSKRLSFQHTHHSSPDVASRLHQMDYTSPTSIKSPSYGDVPHSQNGKYQHLLNNYVATSDSTPTKTSKRATMASYEPEFLDEFDEIAKKKAQLEIELERLKQLEKLSK
Protein: Kinesin-like protein KIF26B (Q7TNC6)
Organism: Mus musculus (Mouse)
Function: Essential for embryonic kidney development. Plays an important role in the compact adhesion between mesenchymal cells adjacent to the ureteric buds, possibly by interacting with MYH10. This could lead to the establishment of the basolateral integrity of the mesenchyme and the polarized expression of ITGA8, which maintains the GDNF expression required for further ureteric bud attraction. Although it seems to lack ATPase activity it is constitutively associated with microtubules.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20439720}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20439720}.
Interaction partners:
- Kinesin-associated protein 3
- Myosin-10
Sequence:
MNSVAGNKERLAVSTRGKKYGVNEMCSPTKPSAPCSPESWYRKAYEESRAGSRPTPEGAGSALGSSGTPSPGSGTSSPSSFTGSPGPASPGIGTSSPGSLGGSPGFGTGSPGSGSGGGSSPGSDRGVWCENCNARLVELKRQALKLLLPGPLPGKDPAFSAVIHDKLQVPNTIRKSWNDRDNRCDICATHLNQLKQEAIQMVLTLEQAAGSEHYDTSLGSPPPISSIPTLVGSRHMGGLQQPREWAFVPAPYATSTYTGLVNKHSGKPNSLGVSNGAEKKSGSPTHQAKVSLQMATSPSNGNILNSVAIQAHQYLDGTWSLSRTNGVTLYPYQISQLMTETGREGLTESALNRYNADKPAASSVPAPQGSCVASETSTGTSVAASFFARAAQKLNLSSKKKKHRPSTPSVAEAPLFATSFSGILQTSPPPAPPCLLRAVNKVKDTPGMGKVKVMLRICSTSARDTSESSSFLKVDPRKKQITLYDPLTCGGQNAFQKRSSQVPPKMFAFDAVFPQDASQAEVCAGTVAEVIQSVVNGADGCVFCFGHAKLGKSYTMIGRDDSMQNLGIIPCAISWLFKLINERKEKTGARFSVRISAVEVWGKEENLRDLLSEVATGSLQDGQSPGVYLCEDPICGTQLQNQSELRAPTAEKAAFFLDAAIASRRSNQQDCDEDDHRNSHMLFTLHIYQYRMEKSGKGGMSGGRSRLHLIDLGSCVKALSKNREGGSGLCLSLSALGNVILALVNGSKHIPYKESKLTMLLRESLGNVNCRTTMIAHISAAASSYAETLSTIQIASRVLRMKKKKTKYTSSSSGGESSCEEGRMRRPTQLRPFHARAPVDPEFPLAPLSSDPDYSSSSEQSCDTVIYIGPNGTALSDKELTDNEGPPDFVPIVPALQKTRGDSRPGEAAEAAASKSERDCLKCNTFAELQERLDCIDGSEEPSKFPFEELPIQFGPEQAGRCAPLSQAVGPDTPSESEKEDNGSDNGQLTEREGTELPASKAQRNRSPAPTVTRSSSPSPASPRSIPGSSSQHSTSQLTQSPSLQSSRESLNSCGFVEGKPRPMGSPRLGIASLSKTSEYKPPSSPSQRCKVYTQKGVLPSSAPPPSLSKDSGMVSSESLLQPDVRTPPVGMSPQVLKKSMSAGSEGFPGTLVDGEDQEGPPADSKKEILSTTMVTVQQPLELNGEDELVFTLVEELTISGVLDSGRPTSIISFNSDCSVQALASGSRPVSIISSISEDLECYSSMAPVSEVSITQFLPLPKLGLDEKARDAGSRRSSISSWLSEMSAGSDGEQSCHSFIAQTCFGHGEAMAEPPASEFVSSIQNTAVVCREKPEVGPDNLLILSEMGEESGNKAAPIKGCKISTVGKAMVTISNTASLSSCEGYIPMKTNITVYPCIAMSPRNVQEPESSTATPKVSPKASQAQESKEPSTRREMKFEDPWLKREEEVKRENAYSSEEGVKCEPLPSSLKTEGKSEQELDGRPSSGNRLSSSSSEAAAFQGTDNVRRVVDGCEMALPGLVAQSPLHVNRNLKSSSLPRAFQKADRHEELDSFYHCLADSNGFSAASGIPSSKTTLERKVASPKHCVLARPKGTPPLPPVRKSSLDQKNRASPQHGGGSSNTSSPLNQPATFLACFPDESNGKTKDVSSSSKLFSAKLEQLASRSNSLGRTTVSHYECLSLERAESLSSVSSRMHAGKDSTMPRTGRSLGRSTGASPPSCGITQSTGASPKASQSKISAVSKLLLASPKSRSSLSTSTTKTLSFSTKSLPQSVGQSSNLPPSGKHMSWSTQSLSRNRGSGLASKLPLRAVNGRISELLQGSAGPRSAQLRAEAEERSGAPSEDKPAAAHLLPSPYSKITPPRKPHRCSSGHGSDNSSVLSGELPPAMGKTALFYHSGGSSGYESMMRDSEATGSASSAQDSMSENSSSVGGRCRSLKNQKKRSNSGSQRRRLIPALSLDTPSPVRKTASSTGVRWVDGPLRSTQRSLGEPFEIKVYEIDDVERLQRRRGATSKEVMCFNAKLKILEHRQQRIAEVRAKYEWLMKELEATKQYLMLDPNKWLREFDLEQVLQLDSLEYLEALEGVTERLESRVNFCKAHLMMITCFDITSRRR
Protein: Probable aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Q54XS2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- isocitrate lyase
- Isocitrate dehydrogenase regulatory subunit B, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Citrate synthase, peroxisomal
- Isocitrate dehydrogenase, mitochondrial
- Citrate synthase, mitochondrial
- Citrate synthase
- Isocitrate dehydrogenase regulatory subunit A, mitochondrial
- Probable ATP-citrate synthase
- ATP citrate synthase
Sequence:
MNSLVKGISKVRSTRSFSTVSMSPLEPNKKLNYEGIDAKLKQFRLHHNKPLTLAEKIIYGHLEDPSTKVERGITYLKLHPDRVAMQDATAQMAVLQFMSAGLPETAVPTTIHCDHLIEAYKGGEKDLEVAKDINKEVYDFLSTSAKKFGMGFWKPGSGIIHQIVLENYAFPGGLMIGTDSHTPNAGGLGMVAVGVGGADAVDVMAGIPWELKAPKIIGVKLTGSLKGWSSPKDVILRVADILTVKGGTGAIVEYFGSGVESLSCTGMATICNMGAEIGATTSLFPFNKRMVDYLNSTGRSNIANAANSFKHNLVADPNAHYDQLIELNLDTLEPYINGPFTPDLGHPLSKFAESVKTNNWPAELKVGLIGSCTNSSYEDMSRSASVAQQALDKGITAKAKFTITPGSEQIRATIERDGQMKVLEKVGGVVLANACGPCIGQWKREDVPKGEKNSIITSYNRNFTGRNDSNVNTHAFVASPEIVTALTIAGDITFNPMTDFLTDKDGNKFKLTPPTGDELPSRGFDAGENTYQPPSPNGQNINVIVDSESSRLQLLQPFAPWDKKDLVDMQVLIKVQGKCTTDHISMAGPWLKYRGHLDNISNNMLIGAINSENGKANAVLNQFTGEIGPVPTVARDYKKRGVNWIVVGDENYGEGSSREHAALEPRHLGGKAILVKSFARIHETNLKKQGILPLTFANPSDYDKISGDDRISIIGLKDLAPGKQLTLIVKSAKQGSEFEIKANHTMNAGQIEWFKAGSALNYIKSEKAKKN
Protein: DDRGK domain-containing protein 1 (Q9VDD1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96HY6}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- CDK5RAP3 protein homolog
- E3 UFM1-protein ligase 1 homolog
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ubiquitin-fold modifier 1
- Ubiquitin-like modifier-activating enzyme 5
Sequence:
MDLIILVGIAVALLVVIVTLYLLQKKNAAPETKVAAAPQRGVPQRAQEGVPRRAQIARNQRNRLRQNVPAAPVAAAAGALPAAGDSDHEDEGQVDGDEARVPQGAVLDEKMGAKKRAKMEAKEQKRLQREQELHDREQRKVKEAKEEAERKQQEDLEAEAERKRVDAERLAKEERERKEHEEYLKMKAAFSVEEEGFEEGDADDQDNLLADFIQYIRDNKVVVLEDLAVAFKLKTQQVIDRIQNLQADGTLTGVIDDRGKFIYVSEKELLAVAKFIKQRGRVSIAELAESSNNLINLTPISAGGGEASS
Protein: tRNA pseudouridine(27/28) synthase (EC 5.4.99.44) (tRNA pseudouridine synthase 2) (tRNA pseudouridylate synthase 2) (tRNA-uridine isomerase 2) (P53167)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial-specific pseudouridine synthase catalyzing the formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of mitochondrial transfer RNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17684231}.
Interaction partners:
- 21S rRNA pseudouridine
- tRNA pseudouridine synthase 4
- tRNA pseudouridine
- tRNA pseudouridine
- Bifunctional protein RIB2
- Multisubstrate pseudouridine synthase 7
- tRNA pseudouridine
- tRNA pseudouridine synthase 1
- H/ACA ribonucleoprotein complex subunit CBF5
- Tryptophan synthase
Sequence:
MLLGYCGSGYYGMQYNPPHKTIEGEILTKLFDVGAISEENSLAPKKNSFMAAARTDKGVHAMLNLLSLKITLREDTVAKLNAALPPEIRVWGIQPVNKKFNARSACDSRWYQYLIPEFILIGPPRSSLLHRNVGGCYREDGSQEVWDTFLEQTRGRFSGDELCRLQDTAQKLSESDPLVQDYVGLLSGTLSGYCLSPSKLDAFEAAMQEYVGTHNFHNFTTGKLWGDPSAQRHIKKVVVSQASPGWICVRIHGQSFMLHQIRRMVALAVLAARCQLPPNIVRNYFNAGPRKYIPRAPAQGLLLEGPVFDGYNTKLRNLLYCEIRPDDITLERMCRFRERQICTAIAHEETQRHVFCHFVRQMNRLATPLI
Protein: Protein tyrosine phosphatase type IVA 1 (EC 3.1.3.48) (Protein-tyrosine phosphatase 4a1) (Protein-tyrosine phosphatase of regenerating liver 1) (PRL-1) (Q78EG7)
Organism: Rattus norvegicus (Rat)
Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q93096}. Early endosome {ECO:0000250|UniProtKB:Q93096}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q93096}. Cytoplasm {ECO:0000250|UniProtKB:Q93096}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q93096}. Nucleus {ECO:0000269|PubMed:8196618}. Note=And mitotic spindle. {ECO:0000250|UniProtKB:Q93096}.
Interaction partners:
- Metal transporter
Sequence:
MARMNRPAPVEVTYKNMRFLITHNPTNATLNKFIEELKKYGVTTIVRVCEATYDTTLVEKEGIHVLDWPFDDGAPPSNQIVDDWLSLVKIKFREEPGCCIAVHCVAGLGRAPVLVALALIEGGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFKDSNGHRNNCCIQ
Protein: IP04187p (Q9VLP0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
Interaction partners:
- GEO08076p1
- UPAR/Ly6 domain-containing protein twit
Sequence:
MPGILLPLALLALVSNGAAIRCYVCDSSDNPSCADLGSNSSIVAEECTLDKMKSLDTWLFDLNKFSYFDNGANKSPLMNCQKVVAKDPDTRKVVTARFCQLDTGDSDACEILRTKLRIPSPEEREQRNRNQNKRRKGHGQDAEEDDEISAEDAFFCGICKSHRCNGAAAVTLSLATILAMIALQLGC
Protein: Nitrilase 3 (EC 3.5.5.1) (P46010)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Can convert indole-3-acetonitrile to the plant hormone indole-3-acetic acid.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Tightly associated with the plasma membrane.
Interaction partners:
- Amidase 1
- Indoleacetaldoxime dehydratase
- Myrosinase 5
- Indole-3-acetaldehyde oxidase
- Probable amidase At4g34880
- Indole-3-acetaldehyde oxidase
- Aldehyde oxidase 4
- Myrosinase 4
- Glutamate dehydrogenase 2
- Myrosinase 2
Sequence:
MSSTEEMSSVKNTTQVIGVDPSSTVRVTIVQSSTVYNDTPATLDKAEKFIVEAASKGAKLVLFPEAFIGGYPRGFRFGLAVGVHNEEGRDEFRNYHASAIKVPGPEVERLAELAGKNNVHLVMGAIEKDGYTLYCTALFFSPQGQFLGKHRKVMPTSLERCIWGQGDGSTIPVYDTPIGKIGAAICWENRMPLYRTALYAKGIEIYCAPTADYSLEWQASMIHIAVEGGCFVLSAHQFCKRREFPEHPDYLFNDIVDTKEHDPTVSGGGSVIISPLGKVLAGPNYESEGLVTADLDLGDIARAKLYFDVVGHYSKPDIFNLTVNEHPKKPVTFMTKVEKAEDESNK