wanglab/gogpt-training-data huggingface dataset:
Protein: Heterochromatin protein 1-binding protein 3 (Protein HP1-BP74) (Q5SSJ5)
Organism: Homo sapiens (Human)
Function: Component of heterochromatin that maintains heterochromatin integrity during G1/S progression and regulates the duration of G1 phase to critically influence cell proliferative capacity. Mediates chromatin condensation during hypoxia, leading to increased tumor cell viability, radio-resistance, chemo-resistance and self-renewal.
Subcellular location: Nucleus {ECO:0000269|PubMed:24830416}. Chromosome {ECO:0000269|PubMed:20042602, ECO:0000269|PubMed:24830416}. Note=localized in nuclei but not in nucleoli in interphase. Colocalized with chromosomes in mitosis, with a gradually increased during G1 progression and a maximum level during late G1 phase (G1/S). {ECO:0000269|PubMed:24830416}.
Interaction partners:
- Tetratricopeptide repeat protein 9B
Sequence:
MATDTSQGELVHPKALPLIVGAQLIHADKLGEKVEDSTMPIRRTVNSTRETPPKSKLAEGEEEKPEPDISSEESVSTVEEQENETPPATSSEAEQPKGEPENEEKEENKSSEETKKDEKDQSKEKEKKVKKTIPSWATLSASQLARAQKQTPMASSPRPKMDAILTEAIKACFQKSGASVVAIRKYIIHKYPSLELERRGYLLKQALKRELNRGVIKQVKGKGASGSFVVVQKSRKTPQKSRNRKNRSSAVDPEPQVKLEDVLPLAFTRLCEPKEASYSLIRKYVSQYYPKLRVDIRPQLLKNALQRAVERGQLEQITGKGASGTFQLKKSGEKPLLGGSLMEYAILSAIAAMNEPKTCSTTALKKYVLENHPGTNSNYQMHLLKKTLQKCEKNGWMEQISGKGFSGTFQLCFPYYPSPGVLFPKKEPDDSRDEDEDEDESSEEDSEDEEPPPKRRLQKKTPAKSPGKAASVKQRGSKPAPKVSAAQRGKARPLPKKAPPKAKTPAKKTRPSSTVIKKPSGGSSKKPATSARKEVKLPGKGKSTMKKSFRVKK
Protein: Probable apyrase 6 (AtAPY6) (EC 3.6.1.5) (ATP-diphosphatase) (ATP-diphosphohydrolase) (Adenosine diphosphatase) (ADPase) (NTPDase) (Nucleoside triphosphate diphosphohydrolase 6) (O80612)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates (By similarity). Involved in the regulation of pollen and anther development.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|Ref.1}; Multi-pass membrane protein {ECO:0000269|Ref.1}.
Interaction partners:
- Apyrase 1
- Apyrase 2
- Ribonucleoside-diphosphate reductase small chain A
- Ribonucleoside-diphosphate reductase small chain C
- AICARFT/IMPCHase bienzyme family protein
- Ribonucleoside-diphosphate reductase large subunit
- At1g72880
- Probable UMP-CMP kinase 2
- UMP-CMP kinase 3
- Probable UMP-CMP kinase 1
Sequence:
MRRSHARSRVKNSSSSKSDMDPIKFQIRSGNRAPSSSSTYTLTKPNSKHAKSNLLLTVGSISVVLGVLFLCYSILFSGGNLRGSLRYSVVIDGGSTGTRIHVFGYRIESGKPVFEFRGANYASLKLHPGLSAFADDPDGASVSLTELVEFAKGRVPKGMWIETEVRLMATAGMRLLELPVQEKILGVARRVLKSSGFLFRDEWASVISGSDEGVYAWVVANFALGSLGGDPLKTTGIVELGGASAQVTFVSSEPMPPEFSRTISFGNVTYNLYSHSFLHFGQNAAHDKLWGSLLSRDHNSAVEPTREKIFTDPCAPKGYNLDANTQKHLSGLLAEESRLSDSFQAGGNYSQCRSAALTILQDGNEKCSYQHCSIGSTFTPKLRGRFLATENFFYTSKFFGLGEKAWLSNMISAGERFCGEDWSKLRVKDPSLHEEDLLRYCFSSAYIVSLLHDTLGIPLDDERIGYANQAGDIPLDWALGAFIQQTATETSQHAASGNLHWFHALFSNHPKTLHYLIGIPILMTVLVYLVTKWRKPQLKTIYDLEKGRYIVTRIR
Protein: C-Jun-amino-terminal kinase-interacting protein 2 (JIP-2) (JNK-interacting protein 2) (Islet-brain-2) (IB-2) (JNK MAP kinase scaffold protein 2) (Mitogen-activated protein kinase 8-interacting protein 2) (Q13387)
Organism: Homo sapiens (Human)
Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10490659}. Note=Accumulates in cell surface projections. {ECO:0000269|PubMed:10490659}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- C-Jun-amino-terminal kinase-interacting protein 1
- Mitogen-activated protein kinase kinase kinase 11
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 8
- C-Jun-amino-terminal kinase-interacting protein 3
- Mitogen-activated protein kinase kinase kinase 10
- Dual specificity mitogen-activated protein kinase kinase 3
- Fibroblast growth factor 12
- Kinesin light chain 2
Sequence:
MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEDDEDEEEEEEEEEGDGEGQEGGDPGSEAPAPGPLIPSPSVEEPHKHRPTTLRLTTLGAQDSLNNNGGFDLVRPASWQETALCSPAPEALRELPGPLPATDTGPGGAQSPVRPGCDCEGNRPAEPPAPGGTSPSSDPGIEADLRSRSSGGRGGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSSGRSSHLTNSIEEASSPASEPEPPREPPRRPAFLPVGPDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPAPRPPGEPVSPAGGAAQDSQDPEAAAGPGGVELVDMETLCAPPPPAPAAPRPGPAQPGPCLFLSNPTRDTITPLWAAPGRAARPGRACSAACSEEEDEEDDEEEEDAEDSAGSPGGRGTGPSAPRDASLVYDAVKYTLVVDEHTQLELVSLRRCAGLGHDSEEDSGGEASEEEAGAALLGGGQVSGDTSPDSPDLTFSKKFLNVFVNSTSRSSSTESFGLFSCLVNGEEREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPGPAKDLLGSKRSPCWVERFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVAQSVGRAFLEYYQEHLAYACPTEDIYLE
Protein: Transcription factor Sox-3 (Q6EJB7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional activator.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Gonadal soma derived factor variant 1
- POU domain, class 5, transcription factor 1
- Transcription factor Sox-19a
- Transcription factor Sox-2
- Catenin beta-1
- Neurogenin-1
- Paired box protein Pax-6
- Forkhead box protein L2
- Paired box protein Pax-2a
- Forkhead box I1.
Sequence:
MYNMMETEIKSPIPQSNTGSVTGGKNNSANDQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGADWKLLTDAEKRPFIDEAKRLRAMHMKEHPDYKYRPRRKTKTLLKKDKYSLPGGLLAPGANAVNNAVSVGQRMDYTHMNGWTNSAYSLMQDQLAYPQHPSMNSPQIQQMHRYDMAGLQYPMMSTAQTYMNAASTYSSMSPAYTQQTSSAMGLGSMASVCKTEPSSPPPAITSHSQRACLGDLRDMISMYLPPGGDSADHSSLQTSRLHSVHPHYQSAGTGVNGTLPLTHI
Protein: FYVE-type domain-containing protein (Q19088)
Organism: Caenorhabditis elegans
Interaction partners:
- small monomeric GTPase
- Receptor-mediated endocytosis protein 6
- Rab5 GDP/GTP exchange factor
- ADP-ribosylation factor-binding protein GGA1
- Secreted protein
- FYVE-type domain-containing protein
- ANK_REP_REGION domain-containing protein
- PX domain-containing protein
- PX domain-containing protein
- AN1-type domain-containing protein
Sequence:
MTEPSASEEVSAGVNAEEPPIPSKKISQVSPNPTLQCEMCQNYEVNLTALQENERKLKEEVKAAMELNERYQLDLSNERDYRKELEKKMNELSTNCLNQVNEAAKANAKSEQRLDELSAKHDKSIEVFTDQLNLARDKLQQADDDFVTLGKKYKKLLGSTRKSAQELRSEKIDMPADLDQLQFICLKNREELIETRAAKEHTEQQLQDEITVLRAQILEERAHREDQEVTFTAEISRLQSELGKINTRMVVASETIADQDSNIRQIRDLQTTVGELETQVQQVQNERAAVEQTAQNYKQRCTSLQQELDTSEVVQRDFVKLSQSLQIQLEKIRQSEQEVRWQWDDDVDQCSNCDTSFARVKVKPHCLHCGRIFCMNCLKDTVPSGPNHRPANVCKVCHTLLNRDTKPFFATQDK
Protein: Opsin Rh3 (Inner R7 photoreceptor cells opsin) (P04950)
Organism: Drosophila melanogaster (Fruit fly)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Phosrestin-1
- Transient-receptor-potential-like protein
- Opsin Rh1
- Guanine nucleotide-binding protein subunit beta-2
- Neither inactivation nor afterpotential protein C
- Transient receptor potential protein
- Inactivation-no-after-potential D protein
- Protein kinase C, eye isozyme
- Calphotin
- Phosrestin-2
Sequence:
MESGNVSSSLFGNVSTALRPEARLSAETRLLGWNVPPEELRHIPEHWLTYPEPPESMNYLLGTLYIFFTLMSMLGNGLVIWVFSAAKSLRTPSNILVINLAFCDFMMMVKTPIFIYNSFHQGYALGHLGCQIFGIIGSYTGIAAGATNAFIAYDRFNVITRPMEGKMTHGKAIAMIIFIYMYATPWVVACYTETWGRFVPEGYLTSCTFDYLTDNFDTRLFVACIFFFSFVCPTTMITYYYSQIVGHVFSHEKALRDQAKKMNVESLRSNVDKNKETAEIRIAKAAITICFLFFCSWTPYGVMSLIGAFGDKTLLTPGATMIPACACKMVACIDPFVYAISHPRYRMELQKRCPWLALNEKAPESSAVASTSTTQEPQQTTAA
Protein: Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) [Cleaved into: Extracellular death factor (EDF)] (P0AC53)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- Glucose-6-phosphate isomerase
- Phosphogluconate dehydratase
- Glucokinase
- KHG/KDPG aldolase
- Phosphoglucomutase
- 6-phosphogluconolactonase
- Triosephosphate isomerase
- Pyruvate kinase II
- Pyruvate kinase I
Sequence:
MAVTQTAQACDLVIFGAKGDLARRKLLPSLYQLEKAGQLNPDTRIIGVGRADWDKAAYTKVVREALETFMKETIDEGLWDTLSARLDFCNLDVNDTAAFSRLGAMLDQKNRITINYFAMPPSTFGAICKGLGEAKLNAKPARVVMEKPLGTSLATSQEINDQVGEYFEECQVYRIDHYLGKETVLNLLALRFANSLFVNNWDNRTIDHVEITVAEEVGIEGRWGYFDKAGQMRDMIQNHLLQILCMIAMSPPSDLSADSIRDEKVKVLKSLRRIDRSNVREKTVRGQYTAGFAQGKKVPGYLEEEGANKSSNTETFVAIRVDIDNWRWAGVPFYLRTGKRLPTKCSEVVVYFKTPELNLFKESWQDLPQNKLTIRLQPDEGVDIQVLNKVPGLDHKHNLQITKLDLSYSETFNQTHLADAYERLLLETMRGIQALFVRRDEVEEAWKWVDSITEAWAMDNDAPKPYQAGTWGPVASVAMITRDGRSWNEFE
Protein: Flagellar brake protein YcgR (Cyclic di-GMP binding protein YcgR) (P76010)
Organism: Escherichia coli (strain K12)
Function: Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. When bound to c-di-GMP it binds to elements of the flagellar motor and/or FliG and FliM, binding to FliM also occurs in the absence of c-di-GMP), causing the motor to slow down. Thus, increasing levels of c-di-GMP lead to decreased motility. Probably binds 1 c-di-GMP dimer per subunit.
Subcellular location: Bacterial flagellum basal body {ECO:0000269|PubMed:20303158}.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeH
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliG
- Probable diguanylate cyclase DgcE
- Probable diguanylate cyclase DgcQ
- Motility protein B
- Flagellar hook-associated protein 2
- RNA polymerase sigma factor FliA
- Flagellar secretion chaperone FliS
- Negative regulator of flagellin synthesis
Sequence:
MSHYHEQFLKQNPLAVLGVLRDLHKAAIPLRLSWNGGQLISKLLAITPDKLVLDFGSQAEDNIAVLKAQHITITAETQGAKVEFTVEQLQQSEYLQLPAFITVPPPTLWFVQRRRYFRISAPLHPPYFCQTKLADNSTLRFRLYDLSLGGMGALLETAKPAELQEGMRFAQIEVNMGQWGVFHFDAQLISISERKVIDGKNETITTPRLSFRFLNVSPTVERQLQRIIFSLEREAREKADKVRD
Protein: Pcdh9 protein (B2RXR7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MDLRDFYLLAALIACLRLDSAIAQELIYTIREELPENVPIGNIPKDLNISHINAATGTSASLVYRLVSKAGDAPLVKVSSSTGEIFTTSNRIDREKLCAGASYAEENECFFELEVVILPNDFFRLIKIKIIVKDTNDNAPMFPSPVINISIPENTLINSRFPIPSATDPDTGFNGVQHYELLNGQSVFGLDIVETPEGEKWPQLIVQQNLDREQKDTYVMKIKVEDGGTPQKSSTAILQVTVSDVNDNRPVFKEGQIEVHIPENAPVGTSVIQLHATDADIGSNAEIRYIFGAQVAPATKRLFALNNTTGLITVQRSLDREETAIHKVTVLASDGSSTPARATVTINVTDVNDNPPNIDLRYIISPINGTVYLSEKDPVNTKIALITVSDKDTDVNGKVICFIEREVPFHLKAVYDNQYLLETSSLLDYEGTKEFSFKIVASDSGKPSLNQTALVRVKLEDENDNPPIFNQPVIELSVSENNRRGLYLTTISATDEDSGKNADIVYQLGPNASFFDLDRKTGVLTASRVFNREEQERFIFTVTARDNGTPPLQSQAAVIVTVLDENDNSPKFTHNHFQFFVSENLPKYSTVGVITVTDEDAGENKAVTLSILNDNENFVLDPYSGVIKSNVSFDREQQSSYTFDVKATDGGQPPRSSTAKVTINVMDVNDNSPVVISPPSNTSFKLVPLSAIPGSVVAEVFAVDIDTGMNAELKYTIVSGNNKGLFRIDPVTGNITLEEKPAPTDVGLHRLVVNISDLGYPKALHTLVLVFLYVNDTAGNTSYIYDLIRRTMETPLDRNIGDSGQPYQNEDYLTIMIAIVAGAMVVIVVIFVTVLVRCRHASRFKAAQRSKQGAEWMSPNQENKQNKKKKRKKRKSPKSSLLNFVTIEESKPDDAVHEPINGTISLPAELEEQGIGRFDWGPAPPTTFKPNSPDLAKHYKSASPQPAFHLKPDTPVSVKKHHVIQELPLDNTFVGGCDTLSKRSSTSSDHFSASECSSQGGFKTKGPLHTRQPQDEFYDQASPDKRTEADGNSDPNSDGPLGPRGLAEATEMCTQECLVLGHSDNCWMPPGLGPYQHPKSPLSTFAPQKEWIKKDKLVNGHTLTRAWKEDTNRNQFNDRKQYGSNEGHFNNGGHMADIPLANLKSYKQAGGTIESPKEHQL
Protein: E3 ubiquitin-protein ligase NHLRC1 (EC 2.3.2.27) (Malin) (NHL repeat-containing protein 1) (RING-type E3 ubiquitin transferase NHLRC1) (Q8BR37)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.
Subcellular location: Endoplasmic reticulum {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes at the endoplasmic reticulum and, to a lesser extent, in the nucleus. {ECO:0000250}.
Interaction partners:
- Laforin
- Glycogen [starch] synthase, muscle
- Glycogen debranching enzyme
- Protein phosphatase 1 regulatory subunit 3C
Sequence:
MGEEATAVAAAGVRPELVREAEVSLLECKVCFERFGHWQQRRPRNLPCGHVVCLACVAALAHPRTLGLECPFCRRACRACDTSDCLPVLHLLELLGSTLHASPAALSAAPFAPGTLTCYHAFGGWGTLVNPTGLALCPKTGRVVVVHDGKRRVKIFDSGGGGAHQFGEKGDAAHDVKYPLDVAVTNDCHVVVTDAGDCSLKVFDFFGQIKLVVGKQFSLPWGVEITPHNGVLVTDAEAGTLHLLEADFPEGVLRRIERLQAHLCSPRGLAVSWLTGAIAVLEHPCAFGRTGCNNTRVKVFNSTMQLIGQVDSFGLNLLFPSKVTASAVTFDHQGNVIVADTSGPAIVCLGKPEEFPALKPIITHGLSRPVALAFTKENSLLVLDTASHSIKVFKVMEGNGG
Protein: Protein LEAD-SENSITIVE 1 (Protein Pb-SENSITIVE 1) (Q93V51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Confers tolerance to lead ions (Pb) stress mediated by Pb(NO(3))(2) probably by promoting Pb accumulation leading to subsequent glutathione-dependent phytochelatin (PC) synthesis and related gene expression, including PDR12/ABCG40, GSH1, GSH2, GR1, GR2, PCS1 and PCS2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27335453}.
Interaction partners:
- TRAM, LAG1 and CLN8
- Proline-rich extensin-like family protein
- Heat shock 70 kDa protein 17
- Acyl-CoA-binding domain-containing protein 1
- Acyl-CoA-binding domain protein
- ABC transporter G family member 36
- Iron-sulfur cluster co-chaperone protein HscB homolog
- ABC transporter B family member 25, mitochondrial
- Glutathione reductase, cytosolic
- Ankyrin repeat family protein
Sequence:
MGLLSNRIDRSSLKPGDHIYSWRTAYIYAHHGIYVGDDRVIHFTRRGQEVGTGTVLDLILVSSGPSRNHTHCPTCVPPNEGHGVVSSCLNCFLAGGVLYRFEYSVNAAHFLVKARGGTCTLAVADPNEIVVHRAKHLLQNGFGCYDVFKNNCEDFAIYCKTALLVLEGRTMGQSGQAVSIIGGPIAAVLSTPMRLLTTNVYGMAATAIGVYCASRYATDIGMRADVAKVEAEDLTRRLSSGLFQVLDPPLAAIALPSTS
Protein: D-galactonate dehydratase family member SEN1436 (EC 4.2.1.-) (D-gluconate dehydratase) (EC 4.2.1.39) (B5R541)
Organism: Salmonella enteritidis PT4 (strain P125109)
Function: Has low D-gluconate dehydratase activity (in vitro), suggesting that it has no significant role in D-gluconate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
Sequence:
MKVSNLKITNVKTILTAPGGIDLAVVKIETNEPGLYGLGCATFTQRIFAVKSAIDEYMAPFLVGKDPTRIEDIWQSGVVSGYWRNGPIMNNALSGVDMALWDIKGKLAGMPVYDLLGGKCRDGIPLYCHTDGGDEVEVEDNIRARMEEGYQYVRCQMGMYGGAGTDDLKLIATQLARAKNIQPKRSPRSKTPGIYFDPDAYAKSVPRLFDHLRNKLGFGIEFIHDVHERVTPVTAINLAKTLEQYQLFYLEDPVAPENIDWLKMLRQQSSTPISMGELFVNVNEWKPLIDNRLIDYIRCHVSTIGGITPARKLAVYSELNGVRTAWHGPGDISPVGVCANMHLDLSSPNFGIQEYTPMNDALRDVFPGCPEIDHGYAYLNDKPGLGIDIDEAKAAKYPCEGGIPSWTMARTPDGTASRP
Protein: L-proline--[L-prolyl-carrier protein] ligase (EC 6.2.1.53) (L-prolyl-AMP ligase) (Q5W263)
Organism: Serratia sp. (strain ATCC 39006) (Prodigiosinella confusarubida)
Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the conversion of L-proline to L-prolyl-AMP and the transfer of the L-prolyl group to acyl carrier protein PigG.
Interaction partners:
- Non-ribosomal peptide synthetase
- Probable acyl carrier protein PigG
- Beta-ketoacyl synthase
- Non-ribosomal peptide synthetase
- Non-ribosomal peptide synthetase
- Type I polyketide synthase
- Non-ribosomal peptide synthetase
- Peptide synthetase
- Probable NAD
- Beta-ketoacyl synthase PigJ
Sequence:
MTISTPVIIDSLIRHAQRTPEQTALLCGDQHWNYRQLVTRAHVMASALRQAGLSGQAILLNLPKSLDAVAAIYATWLSGNHYIPIDYSQPSSRIERIIAAAAPALIIDTAWLATLDSQPSFDAEQPVGRMVYHNPIAAILYTSGSTGTPKGVQISHEMLGFFIQWAVRDTQLTARDVLSNHASFAFDLSTFDLFASAYVGAATWIIRESEQKDCAALAQGLQRHAVSVWYSVPSILAMLEKSTLLNPTLGQSLRQVIFAGEPYPVTALKRLLPCLPQPCRVSNWYGPTETNVCVAYAIDRARLAMLKQVPIGLPLEGLTAQLEDENGDRHPLTAQLRLSGELLISGPCVTPGYSNVVVPRQAALHPHQCHATGDWVEMTPEGLVFRGRIDDMVKINGYRVELGEIESVLHQHPAIDRAALCVELGDLRQTLIMVISLQTGAVPPGLLELKQFLQQKLPSYMIPNKLVITESLPVNANGKVDRKQLAGVVAV
Protein: Probable alcohol acetyltransferase (AAT) (EC 2.3.1.-) (Intermediate cleaved by mitochondrial octapeptidyl aminopeptidase protein 32) (P53219)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable alcohol acetyltransferase that uses acetyl-CoA to synthesize acetate esters from various alcohols (Probable). Not involved in the synthesis of ethyl acetate.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Mitochondrial intermediate peptidase
- Tryptophan--tRNA ligase, mitochondrial
- Protein NAG1
- Small ribosomal subunit protein uS10m
Sequence:
MMILGKAGILAQYGTIYVRQNTIRNNLSSCIFKQSLCAFHSLAKVLQQKQVPLDLSYDIIKRDAVKTGDEGKPRPPIIILHGLFGNKLNNRSIGRNLNKKLGRDVYLLDLRNHGSSPHSSVHNYEVMSEDVKHFITKHELNTNGGPIIIGHSMGGKVAMMLVLKNPQLCSMLVCIENAPVSLRPNAEFVEYIKALMEIVNDKGKTIRTLKQADEHLAERIGGNELVRRFLLTALKKVKMDNSSSVSSYTFEERIPLATLKDAIVKGEIAAWPLDPARERWTRPALFIRATQSHYVVDEYLPIIGAFFPRFETRDIDAGHWVNAEKPGECAESIVDFVERHED
Protein: Rabenosyn-5 (110 kDa protein) (FYVE finger-containing Rab5 effector protein rabenosyn-5) (RAB effector RBSN) (Zinc finger FYVE domain-containing protein 20) (Q9H1K0)
Organism: Homo sapiens (Human)
Function: Rab4/Rab5 effector protein acting in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Required for endosome fusion either homotypically or with clathrin coated vesicles. Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the recycling of transferrin directly from early endosomes to the plasma membrane. Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3). Plays a role in the recycling of transferrin receptor to the plasma membrane.
Subcellular location: Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome membrane {ECO:0000269|PubMed:22308388, ECO:0000269|PubMed:35652444}; Lipid-anchor. Note=Enriched in endosomes that are in close proximity to clathrin-enriched regions at the cell surface. {ECO:0000269|PubMed:22308388}.
Interaction partners:
- Ras-related protein Rab-4A
- Ras-related protein Rab-5A
- Vacuolar protein sorting-associated protein 45
- EH domain-containing protein 1
- EH domain-containing protein 3
- Ras-related protein Rab-22A
- Ras-related protein Rab-5C
- Rabankyrin-5
- EH domain-containing protein 4
- Rab GTPase-binding effector protein 1
Sequence:
MASLDDPGEVREGFLCPLCLKDLQSFYQLHSHYEEEHSGEDRDVKGQIKSLVQKAKKAKDRLLKREGDDRAESGTQGYESFSYGGVDPYMWEPQELGAVRSHLSDFKKHRAARIDHYVVEVNKLIIRLEKLTAFDRTNTESAKIRAIEKSVVPWVNDQDVPFCPDCGNKFSIRNRRHHCRLCGSIMCKKCMELISLPLANKLTSASKESLSTHTSPSQSPNSVHGSRRGSISSMSSVSSVLDEKDDDRIRCCTHCKDTLLKREQQIDEKEHTPDIVKLYEKLRLCMEKVDQKAPEYIRMAASLNAGETTYSLEHASDLRVEVQKVYELIDALSKKILTLGLNQDPPPHPSNLRLQRMIRYSATLFVQEKLLGLMSLPTKEQFEELKKKRKEEMERKRAVERQAALESQRRLEERQSGLASRAANGEVASLRRGPAPLRKAEGWLPLSGGQGQSEDSDPLLQQIHNITSFIRQAKAAGRMDEVRTLQENLRQLQDEYDQQQTEKAIELSRRQAEEEDLQREQLQMLRERELEREREQFRVASLHTRTRSLDFREIGPFQLEPSREPRTHLAYALDLGSSPVPSSTAPKTPSLSSTQPTRVWSGPPAVGQERLPQSSMPQQHEGPSLNPFDEEDLSSPMEEATTGPPAAGVSLDPSARILKEYNPFEEEDEEEEAVAGNPFIQPDSPAPNPFSEEDEHPQQRLSSPLVPGNPFEEPTCINPFEMDSDSGPEAEEPIEEELLLQQIDNIKAYIFDAKQCGRLDEVEVLTENLRELKHTLAKQKGGTD
Protein: Proteasome regulatory non-ATP-ase subunit 5 (Q8WRS9)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MTDVDQWKCASFKQEEDHSEATDALLERINATAIPVLLRSTNSSLDDLVNELLALEKMARLGGDALSAKRLVVEILRIYRVHGDHEKMLDTLETLMRKRGQTKQSQGAMIAECGVLLTEGNLSREQRRIVLERVVHLTDSRIHVELEHVRFAIDLAKLMEDDGEKRAACDLLSGLHVETVTNMPRVEKLDALNRLIRLCLELEDYELARLVSRRINHRALSRPGALQAKLKYFELMREYFAQRRSYFHVARCWYETFLSETDETACVSALSSMAVHYLIAEHSSPKELEDHAECAAFSPATKLADRTAAIQGITTTLRKRLEENPQLQYLLEKFTSIELIRERVADDVEALCINHPQLAGFPERQALLRSRCSEHDLLVISRFYRRLRLVRLAELVGLTPQHTEEFLMMMVASRTLYAKIDRVDGLVVFEANKNANDVVTAWDEAVGRSVALLDKVSHLIVKERMLHNITLAQLQQSGATAS
Protein: Pre-mRNA-processing factor 19 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase PRP19) (P32523)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable ubiquitin-protein ligase involved in pre-mRNA splicing. Acts as a central component of the NTC complex (or PRP19-associated complex) that associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. It is also probably involved in DNA repair.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor PRP21
- Pre-mRNA-splicing factor PRP11
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2
- Pre-mRNA-splicing factor 8
- U2 snRNP component HSH155
- Pre-mRNA-splicing factor CWC24
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor RSE1
Sequence:
MLCAISGKVPRRPVLSPKSRTIFEKSLLEQYVKDTGNDPITNEPLSIEEIVEIVPSAQQASLTESTNSATLKANYSIPNLLTSLQNEWDAIMLENFKLRSTLDSLTKKLSTVMYERDAAKLVAAQLLMEKNEDSKDLPKSSQQAVAITREEFLQGLLQSSRDFVARGKLKAPKWPILKNLELLQAQNYSRNIKTFPYKELNKSMYYDKWVCMCRCEDGALHFTQLKDSKTITTITTPNPRTGGEHPAIISRGPCNRLLLLYPGNQITILDSKTNKVLREIEVDSANEIIYMYGHNEVNTEYFIWADNRGTIGFQSYEDDSQYIVHSAKSDVEYSSGVLHKDSLLLALYSPDGILDVYNLSSPDQASSRFPVDEEAKIKEVKFADNGYWMVVECDQTVVCFDLRKDVGTLAYPTYTIPEFKTGTVTYDIDDSGKNMIAYSNESNSLTIYKFDKKTKNWTKDEESALCLQSDTADFTDMDVVCGDGGIAAILKTNDSFNIVALTP
Protein: Guided entry of tail-anchored proteins factor 1 (Tail-anchored protein insertion receptor WRB) (Tryptophan-rich basic protein) (Q6P6S5)
Organism: Rattus norvegicus (Rat)
Function: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Together with CAMLG/GET2, acts as a membrane receptor for soluble GET3/TRC40, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. Required to ensure correct topology and ER insertion of CAMLG (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00258}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATPase Get3
- Guided entry of tail-anchored proteins factor CAMLG
- Guided entry of tail-anchored proteins factor 4
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
Sequence:
MSASETDRWAWLLVLCFVFGCNVLRILLPTLSSFISRVLQKDAEQESQMRAEIQSMKQELSTVNMMDEFARYARLERKINKMTDKLKTHVKARTAQLAKIKWFISVAFYVLQAALMISLIWKYYSVPVAVVPSKWITPLDRLVAFPTRVAGGIGVTCWILVCNKVVAIILHPFS
Protein: Pyrrolysyl-tRNA synthetase (B0S4P3)
Organism: Desulfitobacterium hafniense (Desulfitobacterium frappieri)
Interaction partners:
Sequence:
MFLTRRDPPLSSFWTKVQYQRLKELNASGEQLEMGFSDALSRDRAFQGIEHQLMSQGKRHLEQLRTVKHRPALLELEEKLAKALHQQGFVQVVTPTIITKSALAKMTIGEDHPLFSQVFWLDGKKCLRPMLAPNLYTLWRELERLWDKPIRIFEIGTCYRKESQGAQHLNEFTMLNLTELGTPLEERHQRLEDMARWVLEAAGIREFELVTESSVVYGDTVDVMKGDLELASGAMGPHFLDEKWEIFDPWVGLGFGLERLLMIREGTQHVQSMARSLSYLDGVRLNIN
Protein: Vang-like protein 1 (Loop-tail protein 2 homolog) (LPP2) (Strabismus 2) (Van Gogh-like protein 1) (Q8TAA9)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
- Segment polarity protein dishevelled homolog DVL-2
- Prickle-like protein 2
- Prickle-like protein 1
- Segment polarity protein dishevelled homolog DVL-3
- Prickle planar cell polarity protein 3
- Prickle-like protein 4
- Vang-like protein 2
- Cadherin EGF LAG seven-pass G-type receptor 1
- Protein scribble homolog
Sequence:
MDTESTYSGYSYYSSHSKKSHRQGERTRERHKSPRNKDGRGSEKSVTIQPPTGEPLLGNDSTRTEEVQDDNWGETTTAITGTSEHSISQEDIARISKDMEDSVGLDCKRYLGLTVASFLGLLVFLTPIAFILLPPILWRDELEPCGTICEGLFISMAFKLLILLIGTWALFFRKRRADMPRVFVFRALLLVLIFLFVVSYWLFYGVRILDSRDRNYQGIVQYAVSLVDALLFIHYLAIVLLELRQLQPMFTLQVVRSTDGESRFYSLGHLSIQRAALVVLENYYKDFTIYNPNLLTASKFRAAKHMAGLKVYNVDGPSNNATGQSRAMIAAAARRRDSSHNELYYEEAEHERRVKKRKARLVVAVEEAFIHIQRLQAEEQQKAPGEVMDPREAAQAIFPSMARALQKYLRITRQQNYHSMESILQHLAFCITNGMTPKAFLERYLSAGPTLQYDKDRWLSTQWRLVSDEAVTNGLRDGIVFVLKCLDFSLVVNVKKIPFIILSEEFIDPKSHKFVLRLQSETSV