wanglab/gogpt-training-data huggingface dataset:
Protein: Rab5 GDP/GTP exchange factor (RAP1) (Rabaptin-5-associated exchange factor for Rab5) (Rabex-5) (Q9UJ41)
Organism: Homo sapiens (Human)
Function: Rab effector protein acting as linker between gamma-adaptin, RAB4A or RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12505986}. Early endosome {ECO:0000269|PubMed:12505986}. Recycling endosome {ECO:0000269|PubMed:12505986}.
Interaction partners:
- Rab GTPase-binding effector protein 1
- Ras-related protein Rab-5A
- Ras-related protein Rab-21
- Polyubiquitin-C
- Early endosome antigen 1
- Rab GTPase-binding effector protein 2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ras-related protein Rab-22A
- ADP-ribosylation factor-binding protein GGA1
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MSLKSERRGIHVDQSDLLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDWELAERLQREEEEAFASSQSSQGAQSLTFSKFEEKKTNEKTRKVTTVKKFFSASSRVGSKKEIQEAKAPSPSINRQTSIETDRVSKEFIEFLKTFHKTGQEIYKQTKLFLEGMHYKRDLSIEEQSECAQDFYHNVAERMQTRGKVPPERVEKIMDQIEKYIMTRLYKYVFCPETTDDEKKDLAIQKRIRALRWVTPQMLCVPVNEDIPEVSDMVVKAITDIIEMDSKRVPRDKLACITKCSKHIFNAIKITKNEPASADDFLPTLIYIVLKGNPPRLQSNIQYITRFCNPSRLMTGEDGYYFTNLCCAVAFIEKLDAQSLNLSQEDFDRYMSGQTSPRKQEAESWSPDACLGVKQMYKNLDLLSQLNERQERIMNEAKKLEKDLIDWTDGIAREVQDIVEKYPLEIKPPNQPLAAIDSENVENDKLPPPLQPQVYAG
Protein: Bone morphogenetic protein 2 (Bone morphogenetic protein 2b precursor) (O93369)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Chordin
- Serine/threonine-protein kinase receptor
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- Receptor protein serine/threonine kinase
- Receptor protein serine/threonine kinase
- Receptor protein serine/threonine kinase
- Noggin-3
- Noggin-1
- Serine/threonine-protein kinase receptor
Sequence:
MVAVVRALTVLLLGQVLLGGAVGLIPEIDRRKYSDSGRHTPERTDTNFLNEFELRLLNMFGLKRKPTPSKSAVVPQYMLDLYYMHSENDDPNIRRPRSTMGKHVERAASRANTIRSFHHEEAFEALSSLKGKTTQQFFFNLTSIPGEELISAAELRIFRDQVLGDASTSGFHRINIYEVFRPALAPSKEPLTRLLDTRLVQDSHTRWESFDVGSAVARWARESQHNHGLLVEVLHPKESEVSEEAESNRRKHVRVSRSLHADEDSWAQARPLLVTYSHDGQGTAVLHSNREKRQARRGQKPRRKHHQRSNCRRHALYVDFSDVGWNEWIVAPPGYHAFYCHGECPFPLPDHLNSTNHAIVQTLVNSVNSNIPKACCIPTELSPISLLYLDEYEKVILKNYQDMVVEGCGCR
Protein: Eukaryotic translation initiation factor 4E1 (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) (P48598)
Organism: Drosophila melanogaster (Fruit fly)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. In 0-1 hour embryos, forms a complex with me31B, cup, tral and pAbp which binds to various mRNAs including maternal mRNAs, and down-regulates their expression during the maternal-to-zygotic transition.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:17178403}. Cytoplasm {ECO:0000269|PubMed:11500381}. Nucleus, nuclear body {ECO:0000269|PubMed:11500381}.
Interaction partners:
- Eukaryotic initiation factor 4A
- Eukaryotic translation initiation factor 4G1, isoform B
- Protein cup
- Polyadenylate-binding protein
- Eukaryotic translation initiation factor 4E-binding protein
- Eukaryotic initiation factor 4B
- Eukaryotic translation initiation factor 4E transporter
- ATP-dependent RNA helicase me31b
- ATP-dependent RNA helicase
- Eukaryotic translation initiation factor 4E-binding protein Mextli
Sequence:
MQSDFHRMKNFANPKSMFKTSAPSTEQGRPEPPTSAAAPAEAKDVKPKEDPQETGEPAGNTATTTAPAGDDAVRTEHLYKHPLMNVWTLWYLENDRSKSWEDMQNEITSFDTVEDFWSLYNHIKPPSEIKLGSDYSLFKKNIRPMWEDAANKQGGRWVITLNKSSKTDLDNLWLDVLLCLIGEAFDHSDQICGAVINIRGKSNKISIWTADGNNEEAALEIGHKLRDALRLGRNNSLQYQLHKDTMVKQGSNVKSIYTL
Protein: Pre-rRNA-processing protein PNO1 (Partner of NOB1) (Ribosomal RNA-processing protein 20) (Q99216)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for small ribosomal subunit (SSU) synthesis. Has a role in the processing of early nucleolar and late cytoplasmic pre-RNA species. Recruits DIM1 to nucleolar pre-RNAs. Indirectly required for cleavage at the A2 site of the 20S pre-rRNA, forming 18S rRNA, and at A1 and A2 sites of other pre-rRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12628929, ECO:0000269|PubMed:15037774}. Nucleus, nucleolus {ECO:0000269|PubMed:10923024, ECO:0000269|PubMed:15037774}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 10
- U3 small nucleolar RNA-associated protein 14
- Exosome complex component RRP45
- U3 small nucleolar ribonucleoprotein protein IMP4
- Serine/threonine-protein kinase RIO2
- Ribosome biogenesis protein TSR1
- Ribosome biogenesis protein BMS1
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 22
- Nucleolar complex protein 4
Sequence:
MVAPTALKKATVTPVSGQDGGSSRIIGINNTESIDEDDDDDVLLDDSDNNTAKEEVEGEEGSRKTHESKTVVVDDQGKPRFTSASKTQGNKIKFESRKIMVPPHRMTPLRNSWTKIYPPLVEHLKLQVRMNLKTKSVELRTNPKFTTDPGALQKGADFIKAFTLGFDLDDSIALLRLDDLYIETFEVKDVKTLTGDHLSRAIGRIAGKDGKTKFAIENATRTRIVLADSKIHILGGFTHIRMARESVVSLILGSPPGKVYGNLRTVASRLKERY
Protein: Glucosidase 2 subunit beta (Alpha-glucosidase 2 subunit beta) (Alpha-glucosidase II subunit beta) (Glucosidase II subunit beta) (Q04924)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. Specifically required for the cleavage of the final glucose.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16373354}.
Interaction partners:
- Glucosidase 2 subunit alpha
Sequence:
MVSMFSLFLLLIEQSPLVASLQQSQRHIVGVPWEKQHLYDSNEPDLTKWHCLNHEDIVLDISQINDGVCDCPDGSDEPGSAACVEDIFKSVAEGGGKVNKYFYCDNKGFIPRYIRKSEVADGICDCCDCSDELLSGYELFDAGSNCSQLKNEFDIMASKELSSYREGKEALEELERKYGTKEEAITRGNCLEEDKEKASAEIKVLSNRLSENRAKLEQLRGEYFNQLSHDPILYQFEQLNSTRLGSDILTSFTMVSRVSKGYQDIFKILSDLSEAYTPSLNDKVVNDNIKKFRKVRRRAEKAKINADSKIDDEQADNLYLYFTEEVPQIFLKRESENTLRYVIGKSNFVQALVEGKINYTNDILEYIREFRLIMDDISQNYNVNFQDAGVKSAVDSYKNYLGEYGELAELEPAHPSESLLRSLSEVTSFVNENAPKVLPPDAVESEQDTNSDHIGTSGDLRNKLKEILSKLNIFSSRKDLVSLEKRFRSCESQVSLLENELKQKMDYKKLLDETEDEGTNSTAGNLTELLELMGSQSYCLDDILDNYVYTICFQRPMTEGVIYQAEDKVDGKKVLIGRFKTSGFNVDLNMEKYAEHLKATYDEKSDLISNLAAIQDDDGNMQHYVFGNLNELNNGLVLEYENGDQCWNGPRRSATVFVRCSDKFKIRSVHEATKCNYIFDVVGPLGCNKTFEYEPPKFNLSE
Protein: p-hydroxybenzoate hydroxylase (PHBH) (PHBHase) (EC 1.14.13.2) (4-hydroxybenzoate 3-monooxygenase) (P00438)
Organism: Pseudomonas fluorescens
Function: Catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The reaction occurs in two parts: reduction of the flavin adenine dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate to the enzyme and oxidation of reduced FAD with oxygen to form a hydroperoxide, which then oxygenates p-hydroxybenzoate.
Interaction partners:
Sequence:
MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE
Protein: Glycerophosphocholine phosphodiesterase GDE1 (EC 3.1.4.2) (Glycerophosphodiester phosphodiesterase GDE1) (A0A1D8PNZ7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Glycerophosphocholine glycerophosphodiesterase responsible for the hydrolysis of intracellular glycerophosphocholine into glycerol-phosphate and choline. The choline is used for phosphatidyl-choline synthesis. Required for utilization of glycerophosphocholine as phosphate source. C.albicans can utilize GroPCho through transport and intracellular hydrolysis or through extracellular hydrolysis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:24114876}.
Interaction partners:
- Lysophospholipase NTE1
- Negative regulator of the PHO system
- Pho81p
- Bifunctional choline kinase/ethanolamine kinase
- Cyclin-dependent kinase 1
- ethanolamine kinase
- Cyclin-dependent protein kinase-activating kinase
- Lysophospholipase 1
- Lysophospholipase
- Lysophospholipase
Sequence:
MKFGKTYVTHQIPEWSIYYMNYKQLKKIIKSIDSAANTNVDESKYPEVISDTLGSFFYDLDRDIEKVDSFYNTKFKEYNRRLNKIFQVLGYQDGQITHNIESSEELDEIINILIELKSLFRNLKWFAELNHKGFIKILKKLDKKLTSILSQHSGVSVGGVSNHNQEAYMGSRINALPFANGTEASNCLDSIHHILSRIETRNDVVQETIPVENNETSISALIKNDDFEGLKKHITIKSSQKFLISTLNKAALANSTKCIDVIWNQLDMLYDDSDFNGRNFFHQHIISLGKAQFIREEQIVPGEVTNRLIGGDNGPDNSNKNDNPIGLLYILNKLKHKRLILAEDHYHRTPLHYASQYGLVEVTRYLVEFGVKWGLINTSISIDDVSIWGDQEGLTPLHLSIIGKHPKTTETLLGFNKAQTLTCPNLLLLAVRLNSPQILNSLIVEGNIDVNYTDIDHRNETALYIASKLNHPDLVEFLLESNANTEIGENVFGWTPIFIAASEGFMTIVKLLKEYGASYDIVDDSGWLPMEHACLRGHLDVTDLLLPKNEKLLLYDMYHPENNLPRIPSLAASPVLTGSDDGTVSTSSIDKLPEPQKNTVNQFYKQLKNNSSNNVSRSTSPKRNKRYKPVKSFGHRYLNEDESLILLTLGTTDLRDTNVPVELNKVSLAKSFATELDTALSLSITCRHKLTNNPVEPPVVVDLPLEDFHGSATDPISFKLSNDLTVNDVIITFDIIPTYQVNKKVIGRAIALLKDAYTKVGPNLRSLNNSIAIPIIESTNLDILGTIRFEYLQVLPFKHKAMSIARSDTYWKQLVSTRVIGHRGLGKNLSGKKSLQLGENTVESFIAAASLGASYVEFDVQLTKDHVPVVYHDFTVAESGVDIPMHLLTLEQFMGFNTPTEKPTHTVDDEVLTRGKQRAQSSYQLSNNHNDDIEKEFANQRDERMKFTKTWKNQGYKGNLRGSSVASNFVTLRELFRKLPNNVGFNIEVKYPMLDEAQLEDMGEIGVDLNFFVDTILKVIYDENTTGRDIVFSSFHPDICLLLSLKQPTMPVLFLTEAGTAPMYDIRASSLQNAVRFSKKWNLLGIVSNALALIKTPRLAQVVKSMGLVCVTYGTENNEPELAKIQMRAGVDAVIVDSVLAVREGLREHNETMNEFEDSPTE
Protein: General regulatory factor 1 (F4JJ94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATPGASSARDEFVYMAKLAEQAERYEEMVEFMEKVAKAVDKDELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNDDHVSLIRDYRSKIETELSDICDGILKLLDTILVPAAASGDSKVFYLKMKGDYHRYLAEFKSGQERKDAAEHTLTAYKAAQDIANSELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQIWISSLFDAFFWSNSDFGDCQLFYILIHSSILLSCGLILIMMILSNVFFNQDDVADDIKEAAPAAAKPADEQQS
Protein: Large ribosomal subunit protein uL14A (60S ribosomal protein L23-A) (P0CT60)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0CX41}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL39
- Elongation factor 3
- Large ribosomal subunit protein eL22
Sequence:
MSRGRGAASGTKYRMTLGLPVQAIMNCADNSGAKNLYIVSVFGTGARLNRLPAASCGDMVLATVKKGKPDLRKKIMPAIVVRQRKAWRRKDGVYLYFEDNAGVIVNPKGEMKGSAITGPVAKECADLWPRIASNAGTVV
Protein: Glycogen [starch] synthase, liver (EC 2.4.1.11) (Glycogen synthase 2) (P17625)
Organism: Rattus norvegicus (Rat)
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Interaction partners:
- 1,4-alpha-glucan branching enzyme
- UTP--glucose-1-phosphate uridylyltransferase
- Protein phosphatase 1 regulatory subunit 3C
- Protein phosphatase 1 regulatory subunit 3B
- Protein phosphatase 1, regulatory subunit 3D
- Protein phosphatase 1 regulatory subunit 3E
- Protein phosphatase 1 regulatory subunit 3A
- Glycogen synthase kinase-3 beta
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Sequence:
MLRGRSLSVTSLGGLPAWEAERLPVEDLLLFEVSWEVTNKVGGICTVIQSKAKTTANEWGENYFLIGPYFEHNVKTQVEPCEPANDAVRKAVDAMNKHGCQVHFGRWLIEGSPYVVLFDISSSVWNLDRWKGDFWEACGVGIPHDDREANDMLIFGSLTAWFLKEVTDHADGKHVIAQFHEWQAGTGLILSRARKLPIATIFTTHATLLGRYLCAANIDFYNQLDKFNIDKEAGERQIYHRYCMERASVHCAHVFTTVSEITAIEADHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHATYKARIQDFVRGHFYGHLDFDLEKTLFLFIAGRYEFSNKGADIFLESLSRLNFLLRMHKSNVTVVVFFIMPAKTNNFNVETLKGQAVRKQLWDTVHCMKEKFGKKLYDGLLRGEIPDMNSILDRDDLTIMKRAIFSTQRHSLPPVTTHNMIDDSTDPILSTIRRIGLFNNRTDRVKVILHPEFLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMQEHVADPTAYGIYIVDRRFRSPDDSCNQLTQFLYGFCKQSRRQRIIQRNRTERLSDLLDWRYLGRYYQHARHLTLSRAFPDKFHLEPTSPPTTDGFKYPRPSSVPPSPSGSQTSSPQSSDVENEGDEDERYDEEEEAERDRLNIKSPFSLNHIPKGKKKLHGEYKN
Protein: Small ribosomal subunit protein bS21m (28S ribosomal protein S21, mitochondrial) (MRP-S21) (S21mt) (P82920)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279123, ECO:0000269|PubMed:24799711}.
Interaction partners:
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS34
- Small ribosomal subunit protein uS5m
Sequence:
MAKHLKFIARTVMVQEGNVEGAYRTLNRILTMDGLIEDIKRRRYYEKPCRRRQRESYETCRRIYNMEMARKINFLMRKNRADPWQGC
Protein: Fe(2+)/Mn(2+) transporter pcl1 (Pombe ccc1-like protein 1) (Q9P6J2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in both calcium and manganese homeostasis. Involved in the transfer of iron and Mn(2+) from the cytosol to the vacuole for storage of these metals (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000250|UniProtKB:P47818, ECO:0000255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47818, ECO:0000255}.
Interaction partners:
- Iron-sulfur assembly protein 1
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Glutamate synthase
- CCAAT-binding factor complex subunit php4
Sequence:
MWSIFEARPKEAHSVNKIGWLRASVLGANDGILSLSGLLVGVVAANADIKVILITGVAGLMSGALSMAVGEYVSVSSQADLEDADLQLERREMDADWDAEVDELAAIYRGRGLDEELSRTVAVQLMEYNALEAHARDELGINIHTTAKPTLAALSSAASFSVGGIFPLLTSLITPLEYLSLVLPIATMFFLGMLGFVGAHIGGAKRVRAILRAVVLGLLAMAATALVGRLLEIHALSLQYAI
Protein: Centromere protein T (CENP-T) (Interphase centromere complex protein 22) (Q96BT3)
Organism: Homo sapiens (Human)
Function: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.
Subcellular location: Nucleus. Chromosome, centromere {ECO:0000269|PubMed:16716197, ECO:0000269|PubMed:19070575, ECO:0000269|PubMed:19412974}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19412974}. Note=Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore, and may connect it to the outer kinetochore via its N-terminus. {ECO:0000269|PubMed:19412974}.
Interaction partners:
- Centromere protein I
- Centromere protein C
- Centromere protein N
- Centromere protein S
- Centromere protein X
- Centromere protein H
- Centromere protein W
- Centromere protein O
- Centromere protein M
- Centromere protein U
Sequence:
MADHNPDSDSTPRTLLRRVLDTADPRTPRRPRSARAGARRALLETASPRKLSGQTRTIARGRSHGARSVGRSAHIQASGHLEEQTPRTLLKNILLTAPESSILMPESVVKPVPAPQAVQPSRQESSCGSLELQLPELEPPTTLAPGLLAPGRRKQRLRLSVFQQGVDQGLSLSQEPQGNADASSLTRSLNLTFATPLQPQSVQRPGLARRPPARRAVDVGAFLRDLRDTSLAPPNIVLEDTQPFSQPMVGSPNVYHSLPCTPHTGAEDAEQAAGRKTQSSGPGLQKNSPGKPAQFLAGEAEEVNAFALGFLSTSSGVSGEDEVEPLHDGVEEAEKKMEEEGVSVSEMEATGAQGPSRVEEAEGHTEVTEAEGSQGTAEADGPGASSGDEDASGRAASPESASSTPESLQARRHHQFLEPAPAPGAAVLSSEPAEPLLVRHPPRPRTTGPRPRQDPHKAGLSHYVKLFSFYAKMPMERKALEMVEKCLDKYFQHLCDDLEVFAAHAGRKTVKPEDLELLMRRQGLVTDQVSLHVLVERHLPLEYRQLLIPCAYSGNSVFPAQ
Protein: Kynurenine--oxoglutarate transaminase 1 (EC 2.6.1.7) (Cysteine-S-conjugate beta-lyase) (EC 4.4.1.13) (Glutamine transaminase K) (GTK) (Glutamine--phenylpyruvate transaminase) (EC 2.6.1.64) (Kynurenine aminotransferase 1) (Kynurenine aminotransferase I) (KATI) (Kynurenine--oxoglutarate transaminase I) (Q16773)
Organism: Homo sapiens (Human)
Function: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others. Also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:7883047}.
Interaction partners:
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Kynureninase
- Kynurenine 3-monooxygenase
- Aspartate aminotransferase, mitochondrial
- Kynurenine formamidase
- Cystathionine gamma-lyase
- Aspartate aminotransferase, cytoplasmic
- Cystathionine beta-synthase-like protein
- Putative aspartate aminotransferase, cytoplasmic 2
- 28S rRNA
Sequence:
MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFMLNQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVIIIEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVLNTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTLTIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFRQPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDEPYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKVEL
Protein: GTPase IMAP family member 6 (Immunity-associated nucleotide 2 protein) (IAN-2) (hIAN2) (Immunity-associated nucleotide 6 protein) (IAN-6) (hIAN6) (Q6P9H5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23454188}.
Interaction partners:
- GTPase IMAP family member 8
- GTPase IMAP family member 4
- GTPase IMAP family member 7
- GTPase IMAP family member 5
- GTPase IMAP family member 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- GIMAP1-GIMAP5 readthrough
Sequence:
MEEEEYEQIPQENPPEELSQDPVLELSGGLREKEQKTPRRLRLILMGKTGSGKSATGNSILGRDVFESKLSTRPVTKTSQRRSREWAGKELEVIDTPNILSPQVSPEVADAICQAIVLSAPGPHAVLLVTQLGRFTDEDQQVVRRLQEVFGVGVLGHTILVFTRKEDLAGGSLEDYVRETNNQALAWLDVTLARRHCGFNNRAQGEEQEAQLRELMEKVEAIMWENEGDYYSNKAYQYTQQNFRLKELQERQVSQGQGSEDVPGEESWLEGLSQIQKESEEAHRCLLGKADL
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (Immunosuppresant and temperature-sensitive protein 8) (Q8WZK2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:11297516}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:11297516}.
Interaction partners:
- GPI mannosyltransferase 2
- GPI mannosyltransferase 3
- Adenosine 5'-monophosphoramidase hnt1
Sequence:
MFGRLLLLGILFHVVFLKSIFDIYFVTPLIHGMKQYSAGEAPAKRLFLIVGDGLRPDKLLQPHSEKVIGEEQTYAAPFLRSIIQNNGTFGVSHTRVPTESRPGHVALIAGFYEDVSAVTKGWKKNPVNFDSVFNQSRHTYSFGSEDILPMFSEGASDPSRVDTFMYSSELEDFSSNGIVLDEWVFDRLDELLAQSLEDKELWDMLHRDKIVFFLHLLGIDTIGHNKHPDSVEYVENIQYIDGKIQELVDKMNNYYNNDGASSWVFTADHGMSDFGSHGDGNLDNTRTPIIAWGAGIQSPTHEKNYGHDEYSLPWNLTEIKRIDIQQADIAALMSYLVGLNFPVNSVGQIPLDYLDCSSRRKAEVALMNALEIGEQYNLKSASKDQTSIFFRPYSPLRNYTEVQASFYNSVIADIESGEYEIAIEHCFHFSQTVLSGLRYLQRYDWLLLRSIVFFGYLSWIGYVICFVFSLNIEPSSKIVKPVSVVKRVAFNIPFLLICIFFYIQSSPPFYYGYALFPTIFLQLIHSIFPNTKLGFKNFLTVAKQKHGFSLLKILFISLCILCLLQFIVYSYFHREGFSVILMGLAAWPWLLHADYAFSHKTISVSWSVLTSLLCFFTILPVNKKESLLFIFAGGFAMSVAGVFYILYRRNQAFQYSSTVTNKQLVLQVLIIMATVPVTLKIADSLQRNIAIPPILRLVAFGLFITSYIIPSHHIRSCKHYFLDRLAILFLTFSPTMCMLSISFEALFYVVLFITLGLWMELETELQKYTEQLHPEYSRKKDAKFHLSLSHIRISLFFYIFINVAFFGTGNVASLSTFALDSVKRFIPVFNPVTQGALLMYTILVPFIALSAAFGIMNKRLGGIQQVTFFLAVGMADIVTINFFYLVKDEGSWKDIGVSISHFCISNFLILFITALEHASAILCKNITYTIHEKVN
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (C9JEA7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASLLQDQLTTDQDLLLMQEGMPMRKVRSKSWKKLRYFRLQNDGMTVWHARQARGSAKPSFSISDVETIRNGHDSELLRSLAEELPLEQGFTIVFHGRRSNLDLMANSVEEAQIWMRGLQLLVDLVTSMDHQERLDQWLSDWFQRGDKNQDGKMSFQEVQRLLHLMNVEMDQEYAFSLFQAADTSQSGTLEGEEFVQFYKALTKRAEVQELFESFSADGQKLTLLEFLDFLQEEQKERDCTSELALELIDRYEPSDSGKLRHVLSMDGFLSYLCSKDGDIFNPACLPIYQDMTQPLNHYFICSSHNTYLVGDQLCGQSSVEGYIRALKRGCRCVEVDVWDGPSGEPVVYHGHTLTSRILFKDVVATVAQYAFQTSDYPVILSLETHCSWEQQQTMARHLTEILGEQLLSTTLDGVLPTQLPSPEELRRKILVKGKKLTLEEDLEYEEEEAEPELEESELALESQFETEPEPQEQNLQNKDKKKVVTCPLFCPSICCQIVAQAPISKPESLLLSRQKSKPILCPALSSLVIYLKSVSFRSFTHSKEHYHFYEISSFSETKAKRLIKEAGNEFVQHNTWQLSRVYPSGLRTDSSNYNPQELWNAGCQMVAMNMQTAGLEMDICDGHFRQNGGCGYVLKPDFLRDIQSSFHPEKPISPFKAQTLLIQVISGQQLPKVDKTKEGSIVDPLVKVQIFGVRLDTARQETNYVENNGFNPYWGQTLCFRVLVPELAMLRFVVMDYDWKSRNDFIGQYTLPWTCMQQGYRHIHLLSKDGISLRPASIFVYICIQEGLEGDES
Protein: Gamma-aminobutyric acid receptor-associated protein-like 1 (Early estrogen-regulated protein) (GABA(A) receptor-associated protein-like 1) (Glandular epithelial cell protein 1) (GEC-1) (Q9H0R8)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like modifier that increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles. While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover.
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20404487, ECO:0000269|PubMed:30661429, ECO:0000305|PubMed:23690988}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:20404487}; Lipid-anchor {ECO:0000269|PubMed:20404487}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0VGK0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q0VGK0}. Golgi apparatus {ECO:0000250|UniProtKB:Q0VGK0}.
Interaction partners:
Sequence:
MKFQYKEDHPFEYRKKEGEKIRKKYPDRVPVIVEKAPKARVPDLDKRKYLVPSDLTVGQFYFLIRKRIHLRPEDALFFFVNNTIPPTSATMGQLYEDNHEEDYFLYVAYSDESVYGK
Protein: RE18856p (Q6NR13)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSLPTDGLNMEITPSPTLAATSRGDLEKVLAMVVLGLGSLLFGLLPAFISERNRRRFPLTASLLLCFGAGILLATALVHILPEVREQMDSKFAEVAMCGGFFIIYFIDEFIHYFFGEAIQHTHAHDAETPATEPPRRPTNDNGYGAVDERGPFYQRNPIRQMGIRTIIATIMTTITRPAHLAVMMPV