wanglab/gogpt-training-data huggingface dataset:
Protein: ERO1-like protein beta (ERO1-L-beta) (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase beta) (Endoplasmic reticulum oxidoreductin-1-like protein B) (Oxidoreductin-1-L-beta) (Q86YB8)
Organism: Homo sapiens (Human)
Function: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10818100}; Peripheral membrane protein {ECO:0000269|PubMed:10818100}; Lumenal side {ECO:0000269|PubMed:10818100}. Note=The association with ERP44 may be essential for its retention in the endoplasmic reticulum.
Interaction partners:
- Protein disulfide-isomerase
- Protein disulfide-isomerase A4
- Endoplasmic reticulum resident protein 44
- ERO1-like protein alpha
- Thioredoxin domain-containing protein 5
- Protein disulfide-isomerase A6
- Endoplasmic reticulum resident protein 29
- Protein disulfide-isomerase A2
- Immunoglobulin J chain
- Endoplasmic reticulum chaperone BiP
Sequence:
MSQGVRRAGAGQGVAAAVQLLVTLSFLRSVVEAQVTGVLDDCLCDIDSIDNFNTYKIFPKIKKLQERDYFRYYKVNLKRPCPFWAEDGHCSIKDCHVEPCPESKIPVGIKAGHSNKYLKMANNTKELEDCEQANKLGAINSTLSNQSKEAFIDWARYDDSRDHFCELDDERSPAAQYVDLLLNPERYTGYKGTSAWRVWNSIYEENCFKPRSVYRPLNPLAPSRGEDDGESFYTWLEGLCLEKRVFYKLISGLHASINLHLCANYLLEETWGKPSWGPNIKEFKHRFDPVETKGEGPRRLKNLYFLYLIELRALSKVAPYFERSIVDLYTGNAEEDADTKTLLLNIFQDTKSFPMHFDEKSMFAGDKKGAKSLKEEFRLHFKNISRIMDCVGCDKCRLWGKLQTQGLGTALKILFSEKEIQKLPENSPSKGFQLTRQEIVALLNAFGRLSTSIRDLQNFKVLLQHSR
Protein: Probable long-chain-fatty-acid--AMP ligase FadD30 (FAAL) (EC 6.2.1.-) (Acyl-AMP synthetase) (FAAL30) (P9WQ57)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to a multifunctional polyketide synthase (PKS) for further chain extension.
Interaction partners:
- Probable membrane bound polyketide synthase Pks6
- Peptide synthetase MbtE
- Peptide synthetase MbtF
- Isonitrile lipopeptide synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Mycocerosic acid synthase-like polyketide synthase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phthioceranic/hydroxyphthioceranic acid synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit B
- Polyketide synthase Pks13
Sequence:
MSVISTLRDRATTTPSDEAFVFMDYDTKTGDQIDRMTWSQLYSRVTAVSAYLISYGRHADRRRTAAISAPQGLDYVAGFLGALCAGWTPVPLPEPLGSLRDKRTGLAVLDCAADVVLTTSQAETRVRATIATHGASVTTPVIALDTLDEPSGDNCDLDSQLSDWSSYLQYTSGSTANPRGVVLSMRNVTENVDQIIRNYFRHEGGAPRLPSSVVSWLPLYHDMGLMVGLFIPLFVGCPVILTSPEAFIRKPARWMQLLAKHQAPFSAAPNFAFDLAVAKTSEEDMAGLDLGHVNTIINGAEQVQPNTITKFLRRFRPYNLMPAAVKPSYGMAEAVVYLATTKAGSPPTSTEFDADSLARGHAELSTFETERATRLIRYHSDDKEPLLRIVDPDSNIELGPGRIGEIWIHGKNVSTGYHNADDALNRDKFQASIREASAGTPRSPWLRTGDLGFIVGDEFYIVGRMKDLIIQDGVNHYPDDIETTVKEFTGGRVAAFSVSDDGVEHLVIAAEVRTEHGPDKVTIMDFSTIKRLVVSALSKLHGLHVTDFLLVPPGALPKTTSGKISRAACAKQYGANKLQRVATFP
Protein: Protein unc-45 homolog B (Unc-45B) (SMUNC45) (Q8IWX7)
Organism: Homo sapiens (Human)
Function: Acts as a co-chaperone for HSP90 and is required for proper folding of the myosin motor domain. Plays a role in sarcomere formation during muscle cell development. Is necessary for normal early lens development.
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:33217308}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6DGE9}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CGY6}. Note=Expressed at the Z line and in the perinuclear region of myofibrils. Translocates to the A band in response to stress conditions and fibril damage. {ECO:0000250|UniProtKB:Q6DGE9}.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Myosin-1
- Activator of 90 kDa heat shock protein ATPase homolog 1
- Ubiquitin conjugation factor E4 A
- Ubiquitin conjugation factor E4 B
- Histone-lysine N-methyltransferase SMYD1
Sequence:
MAEVEAVQLKEEGNRHFQLQDYKAATNSYSQALKLTKDKALLATLYRNRAACGLKTESYVQAASDASRAIDINSSDIKALYRRCQALEHLGKLDQAFKDVQRCATLEPRNQNFQEMLRRLNTSIQEKLRVQFSTDSRVQKMFEILLDENSEADKREKAANNLIVLGREEAGAEKIFQNNGVALLLQLLDTKKPELVLAAVRTLSGMCSGHQARATVILHAVRIDRICSLMAVENEEMSLAVCNLLQAIIDSLSGEDKREHRGKEEALVLDTKKDLKQITSHLLDMLVSKKVSGQGRDQALNLLNKNVPRKDLAIHDNSRTIYVVDNGLRKILKVVGQVPDLPSCLPLTDNTRMLASILINKLYDDLRCDPERDHFRKICEEYITGKFDPQDMDKNLNAIQTVSGILQGPFDLGNQLLGLKGVMEMMVALCGSERETDQLVAVEALIHASTKLSRATFIITNGVSLLKQIYKTTKNEKIKIRTLVGLCKLGSAGGTDYGLRQFAEGSTEKLAKQCRKWLCNMSIDTRTRRWAVEGLAYLTLDADVKDDFVQDVPALQAMFELAKAGTSDKTILYSVATTLVNCTNSYDVKEVIPELVQLAKFSKQHVPEEHPKDKKDFIDMRVKRLLKAGVISALACMVKADSAILTDQTKELLARVFLALCDNPKDRGTIVAQGGGKALIPLALEGTDVGKVKAAHALAKIAAVSNPDIAFPGERVYEVVRPLVRLLDTQRDGLQNYEALLGLTNLSGRSDKLRQKIFKERALPDIENYMFENHDQLRQAATECMCNMVLHKEVQERFLADGNDRLKLVVLLCGEDDDKVQNAAAGALAMLTAAHKKLCLKMTQVTTQWLEILQRLCLHDQLSVQHRGLVIAYNLLAADAELAKKLVESELLEILTVVGKQEPDEKKAEVVQTARECLIKCMDYGFIKPVS
Protein: Probable methyltransferase tdiE (EC 2.1.1.-) (Terrequinone biosynthesis protein D) (A7XRZ1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent. The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD. The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules. The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain. TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1. Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5.
Interaction partners:
- Aminotransferase tdiD
- Probable NADPH-dependent quinone reductase tdiC
- Indole prenyltransferase tdiB
Sequence:
MVNRPYANMNDLANAVAESVQKYLDNSGQARNGLFQKTNNGERDIETERLALQHQLFHLTLDGKLQLSPLPSPVQSVLDIATGDSTWVHAFAEQNPSAYIVANDPSPTSKIPLGLSVIPDASDANEPWTYTRQFDFVHCRQHHRRLDEPRLFKQAFSSLTPGGWLEMQELSNPVTSDDGTLSENNPLSQWGRLLIEASKKMNRPVDNPAKYETWMREAGFVNCHTVAYNWPTNPWPADEKGKTLGLWNLYNVLQRFEEFSVALLVKVLGWEMDDAKTFLGNVKEELMNEGVHGYWPVYVVYGQKPAAPGSDVITDSE
Protein: Inhibitory synaptic factor 2A (InSyn2) (Q3USH1)
Organism: Mus musculus (Mouse)
Function: Component of the protein machinery at the inhibitory synapses, probably acting as a scaffold. Inhibitory synapses dampen neuronal activity through postsynaptic hyperpolarization. This synaptic inhibition is fundamental for the functioning of the central nervous system, shaping and orchestrating the flow of information through neuronal networks to generate a precise neural code.
Subcellular location: Postsynaptic density {ECO:0000269|PubMed:27609886}.
Interaction partners:
Sequence:
MVSKDSGRCILTTPEREVEPAACLALEMRYALDPNRQIKKRNKALQVRFKDICEAQNEQRDTQLSSGPLGEKREAKAVSCRVAYRKYMTVPARRSIPNVTKSTGVQTSPDLRKCYQTFPLDRKKGSLKGLPAADAFKSQNNGFLADSKEKSEAGPMEEPRPCSAGRIHKTTALVFHSNEHVNALGQPSGVNCAELCKSPDVLGYPEAVLQNSRPPSEEPIHQLQGRAKLDRGTLDSEEPAPLTHGRVFKTEVATVYPPAISTRAPEPGLSNSAAASQWSLCPADEEQRRAAHLNGLQASTGSAVACSTPVQYLSPECSEQPLQNQPSPTAGIGDEEHQQIVPHTEVVDLKAQLQVMENLISSSQETIKVLLGVIQELEKGEAHREGLSYRTGQDTANCDTCRNSACIIYRYVNILFPLCYSE
Protein: Zinc finger protein HD1 (Protein CONSTANS-like) (Protein HEADING DATE 1) (OsHd1) (Protein PHOTOPERIOD SENSITIVITY 1) (Q9FDX8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor involved in the regulation of flower development. Required for the promotion of flowering under short day (SD) conditions and the suppression of flowering under long day (LD) conditions. Regulates positively the floral activator HEADING DATE 3a (HD3A) under SD and negatively under LD conditions.
Subcellular location: Nucleus {ECO:0000269|PubMed:26537047}.
Interaction partners:
- MADS-box transcription factor 50
Sequence:
MNYNFGGNVFDQEVGVGGEGGGGGEGSGCPWARPCDGCRAAPSVVYCRADAAYLCASCDARVHAANRVASRHERVRVCEACERAPAALACRADAAALCVACDVQVHSANPLPAITIPATSVLAEAVVATATVLGDKDEEVDSWLLLSKDSDNNNNNNNNNDNDNNDNNNSNSSNNGMYFGEVDEYFDLVGYNSYYDNRIENNQDRQYGMHEQQEQQQQQQEMQKEFAEKEGSECVVPSQITMLSEQQHSGYGVVGADQAASMTAGVSAYTDSISNSISFSSMEAGIVPDSTVIDMPNSRILTPAGAINLFSGPSLQMSLHFSSMDREARVLRYREKKKARKFEKTIRYETRKAYAEARPRIKGRFAKRSDVQIEVDQMFSTAALSDGSYGTVPWF
Protein: Regulator of nonsense transcripts 1 (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent helicase smg-2) (Nonsense mRNA reducing factor 1) (Up-frameshift suppressor 1 homolog) (O76512)
Organism: Caenorhabditis elegans
Function: RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. The formation of an smg-2-3-4 surveillance complex is believed to activate NMD (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- MIF4G domain-containing protein
- Serine/threonine-protein kinase smg-1
- UPF3 domain-containing protein
- PIN domain-containing protein
- RRM domain-containing protein
- Nonsense-mediated mRNA decay protein
- Protein CASC3
- RNA-binding protein rnp-4
- Eukaryotic peptide chain release factor GTP-binding subunit
- PWI domain-containing protein
Sequence:
MDDSDDEYSRSHGETLTFVDPEDDGVSIGNTQDSQFAYEQFSVPTQSSQATDLLPGGTDGTTNDLPFHDVEDDESDSEKSLTEEQHEQKLPEHACRYCGISDPLCVAKCTVCRKWFCNSNDGTSGGHIVHHMVRSQHKEAYTHKDSPCGDTQLECYRCGSKNVFNLGFIPGKKDQVVVIICRTPCASIAFQNDDNWSPEDWKSVIAEKQLLSWIVNVPSEEQVARARKITATQAVRMEELWRDHPEATVDDLNKPGLDREPDHVQLRYVDAHHYSKVFRPLVAIEAEYDRRVKESASQAVGTVRWEQGLRQSVLAFFHLPQFADGVMKLAKGDELRLKHSQTVDGSEWTKIGSVFKIPDNHGDEVGIEIRGAVDKSVMESRIMFTVDVVWNATTFERQYKALAALLNDSKAISPYLYQKLLGHPAEEMMLKFDLPRRLSVAGLPELNSSQMQAVKQVLTRPLSLIQGPPGTGKTVVSATIVYHLVQKTEGNVLVCSPSNIAVDHLAEKIHKTGLKVVRLCARSREHSETTVPYLTLQHQLKVMGGAELQKLIQLKDEAGELEFKDDLRYMQLKRVKEHELLAAADVICCTCSSAADARLSKIRTRTVLIDESTQATEPEILVSIMRGVRQLVLVGDHCQLGPVVICKKAAIAGLSQSLFERLVLLGIRPFRLQVQYRMHPVLSEFPSNVFYDGSLQNGVTENDRHMTGVDWHWPKPNKPAFFWHCSGSEELSASGTSFLNRTEAANVEKLVSKLIKAGVQPHQIGVITSYEGQRSFIVNYMHTQGTLNSKLYENVEIASVDAFQGREKDYIIVTCVRSNDILGIGFLSDPRRLNVAITRAKYGLVLVGNAKVLARHDLWHELINHYKSKEMLYEGPINALKPLNLALPKATIRTKNNIAGNANRFGIKRMQYTFNEYKSNDPSQPRLPPTYSNSQNLLSMSKLAQTFNKNVPIPAHMMDPNVYAAARNQKDRRRGDQRRPPPQAEAAMDLSQGMMSQQSQQYPPQGASSQSQYLLDGASSLSGWSQSQTTTTTTRHHHHRQNRNSQQQMSQDMDDIQQKMDDLLFSQDC
Protein: Serralysin (EC 3.4.24.40) (Extracellular metalloproteinase) (Serratiopeptidase) (Serrapeptase) (Serrapeptidase) (Zinc proteinase) (P07268)
Organism: Serratia marcescens (strain ATCC 21074 / E-15)
Function: Naturally present in the silkworm intestine and allows the emerging moth to dissolve its cocoon.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MQSTKKAIEITESNFAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYRDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANLSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEAQSSDFIHFVDHFSGAAGEALLSYNASNNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV
Protein: Solute carrier family 7 member 14 (Gamma-aminobutyric acid transporter SLC7A14) (Q8TBB6)
Organism: Homo sapiens (Human)
Function: May be involved in arginine transport.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:22787143, ECO:0000269|PubMed:24670872}; Multi-pass membrane protein {ECO:0000255}. Note=Exhibits a punctated pattern in the cytoplasm, which partially ovelaps with lysosomes. {ECO:0000250}.
Interaction partners:
- DOMON domain-containing protein FRRS1L
Sequence:
MSGFFTSLDPRRVQWGAAWYAMHSRILRTKPVESMLEGTGTTTAHGTKLAQVLTTVDLISLGVGSCVGTGMYVVSGLVAKEMAGPGVIVSFIIAAVASILSGVCYAEFGVRVPKTTGSAYTYSYVTVGEFVAFFIGWNLILEYLIGTAAGASALSSMFDSLANHTISRWMADSVGTLNGLGKGEESYPDLLALLIAVIVTIIVALGVKNSIGFNNVLNVLNLAVWVFIMIAGLFFINGKYWAEGQFLPHGWSGVLQGAATCFYAFIGFDIIATTGEEAKNPNTSIPYAITASLVICLTAYVSVSVILTLMVPYYTIDTESPLMEMFVAHGFYAAKFVVAIGSVAGLTVSLLGSLFPMPRVIYAMAGDGLLFRFLAHVSSYTETPVVACIVSGFLAALLALLVSLRDLIEMMSIGTLLAYTLVSVCVLLLRYQPESDIDGFVKFLSEEHTKKKEGILADCEKEACSPVSEGDEFSGPATNTCGAKNLPSLGDNEMLIGKSDKSTYNVNHPNYGTVDMTTGIEADESENIYLIKLKKLIGPHYYTMRIRLGLPGKMDRPTAATGHTVTICVLLLFILMFIFCSFIIFGSDYISEQSWWAILLVVLMVLLISTLVFVILQQPENPKKLPYMAPCLPFVPAFAMLVNIYLMLKLSTITWIRFAVWCFVGLLIYFGYGIWNSTLEISAREEALHQSTYQRYDVDDPFSVEEGFSYATEGESQEDWGGPTEDKGFYYQQMSDAKANGRTSSKAKSKSKHKQNSEALIANDELDYSPE
Protein: Putative gonadotropin-releasing hormone II receptor (GnRH II receptor) (GnRH-II-R) (Type II GnRH receptor) (Q96P88)
Organism: Homo sapiens (Human)
Function: Putative receptor for gonadotropin releasing hormone II (GnRH II) which is most probably non-functional.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MSAGNGTPWDATWNITVQWLAVDIACRTLMFLKLMATYSAAFLPVVIGLDRQAAVLNPLGSRSGVRKLLGAAWGLSFLLAFPQLFLFHTVHCAGPVPFTQCVTKGSFKAQWQETTYNLFTFCCLFLLPLTAMAICYSRIVLSVSRPQTRKGSHAPAGEFALPRSFDNCPRVRLRALRLALLILLTFILCWTPYYLLGMWYWFSPTMLTEVPPSLSHILFLLGLLNAPLDPLLYGAFTLGCRRGHQELSIDSSKEGSGRMLQEEIHAFRQLEVQKTVTSRRAGETKGISITSI
Protein: Albumin (B7WNR0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
Protein: Thiol protease aleurain-like (EC 3.4.22.16) (Q8RWQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in proteolysis leading to mobilization of nitrogen during senescence and starvation.
Subcellular location: Vacuole {ECO:0000250}.
Interaction partners:
- UPF0235 protein At5g63440
- Peptidase C13 family
- Large ribosomal subunit protein P2w
- Thiamine thiazole synthase, chloroplastic
- Vacuolar-processing enzyme gamma-isozyme
- Vacuolar-processing enzyme alpha-isozyme
- Vacuolar-processing enzyme beta-isozyme
- Reactive Intermediate Deaminase A, chloroplastic
- Serpin-ZX
- Vacuolar-processing enzyme delta-isozyme
Sequence:
MSVKLNLSSSILLILFAAAASKEIGFDESNPIKMVSDNLHELEDTVVQILGQSRHVLSFSRFTHRYGKKYQSVEEMKLRFSVFKENLDLIRSTNKKGLSYKLSLNQFADLTWQEFQRYKLGAAQNCSATLKGSHKITEATVPDTKDWREDGIVSPVKEQGHCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGTFNNFGCHGGLPSQAFEYIKYNGGLDTEEAYPYTGKDGGCKFSAKNIGVQVRDSVNITLGAEDELKHAVGLVRPVSVAFEVVHEFRFYKKGVFTSNTCGNTPMDVNHAVLAVGYGVEDDVPYWLIKNSWGGEWGDNGYFKMEMGKNMCGVATCSSYPVVA
Protein: Chlorophyllase-1, chloroplastic (EC 3.1.1.14) (Chlorophyll-chlorophyllido hydrolase 1) (Chlase 1) (Q9MV14)
Organism: Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis)
Function: Catalyzes the hydrolysis of ester bond in chlorophyll to yield chlorophyllide and phytol.
Subcellular location: Plastid, chloroplast {ECO:0000269|Ref.3}.
Interaction partners:
Sequence:
MAAMVDAKPAASVQGTPLLATATLPVFTRGIYSTKRITLETSSPSSPPPPKPLIIVTPAGKGTFNVILFLHGTSLSNKSYSKIFDHIASHGFIVVAPQLYTSIPPPSATNELNSAAEVAEWLPQGLQQNLPENTEANVSLVAVMGHSRGGQTAFALSLRYGFGAVIGLDPVAGTSKTTGLDPSILSFDSFDFSIPVTVIGTGLGGVARCITACAPEGANHEEFFNRCKNSSRAHFVATDYGHMDILDDNPSDVKSWALSKYFCKNGNESRDPMRRCVSGIVVAFLKDFFYGDAEDFRQILKDPSFAPIKLDSVEYIDASSMLTTTHVKV
Protein: WASH1 WAHD domain-containing protein (Q38EF1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Actin-like protein 2, putative
- BTB domain-containing protein
- ARP2/3 complex subunit, putative
- Actin-related protein 2/3 complex subunit 5
- Arp2/3 complex 34 kDa subunit
- Arp2/3 complex 41 kDa subunit
- Actin-like protein 3, putative
- Actin-related protein 2/3 complex subunit 4
Sequence:
MYKETTMTPIHGYTLPVPLTNGGYASMLSVIRALGRLDQTSERVFGNIEQAVERSRETLEQLQGRIAVCADQVEQLQGRREAMVVKSRVRFPKQKHYTLPIGRAPCEDRGCVPERAYVMPAIIQADDSGASPVVGSSGGDSGNGSDPWQLGGQEGEDAYPKPVRRLDCPGAEQRLMKPQHPLQEATVKSLMPLGATWRYHSGVDRGLGRLPAHLMSVSSLLLFNTRENLYKEYHEMDVLTQQRQERVVATKQRLGTSDVHRDYVTQASTDEYAFVPLMEEVANLMDDLPENLPLEGIAEVAWNAYSLEDQDNIAPSGQRRLGERGDSVGSGSGSTRNKKKGQEALAITAGPDAAGGPSSRALVPSGLPPPPPPPGGLRPPGKAPPPPPPPPPMFAGKMKAPPPPPIKAPPPMPSLPGAAATKGLPIGNAPPAPPPPPPPPPPGQAKAPAKPAAKSDVKPAPKPATKSNLDALSSLLANRRKGILGMHSDGEDEDDDHGRRPPASGPSKGMAINRNAPAPPQKGGVPPPPPPPPPPKAPPPKGPPPKVAPPPPPPPPPPPAPGKLPPKRKTDDDDDW
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (Q7ZTW5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGAYLSQPNMEKSTGNGGSKNLNYGFSAMQGWRVSMEDAHNCIPELDDETAMFAVYDGHGGEEVALYCSKYLPGIIKEQKTYKEGKLQKALEDAFLDIDARITTEEVIKELVQIAGRPQEETEKVADEDDVDNEEAALLHEEATMTIEELLTRYGQNQNKNAKKPCPEASKESEDGEKSHAEKGINGETECGPSVADSIGKKPAGAENAAEGSKMRACRRAAASGGSASEGSAEKSGDAGPSCSSSAAAPPGSAKSKFFEDSEESGEEEEEEEGSEEEDGSEEDGENSSENEEEDDTEEGEEEDTDEEEEMCLPGMDGKEEPGSDSGTTAVVALIRGKQLIVANAGDSRCVVSEKGKALDMSYDHKPEDELELARIKNAGGKVTMDGRVNGGLNLSRAIGDHFYKRNKALPAEEQMISALPDVKVLTLNDDHEFMVIACDGIWNVMSSQEVIDFVSERMKTESGKNNPLSAIIDELLDHCLAPDTSGDSKKPKTE
Protein: MADS-box domain-containing protein (A0MFC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVRSTKGRQKIEMKKMENESNLQVTFSKRRFGLFKKASELCTLSGAEILLIVFSPGGKVFSFGHPSVQELIHRFSNPNHNSAIVHHQNNNLQLVETRPDRNIQYLNNILTEVLANQEKEKQKRMVLDLLKESREQVGNWYEKDVKDLDMNETNQLISALQDVKKKLVREMSQYSQVNVSQNYFGQSSGVIGGGNVGIDLFDQRRNAFNYNPNMVFPNHTPPMFGYNNDGVLVPISNMNYMSSYNFNQSG
Protein: Ethylene-responsive transcription factor 15 (AtERF15) (Ethylene-responsive element-binding factor 15) (EREBP-15) (Q8VYM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a transcriptional activator. 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 (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Defensin-like protein 16
Sequence:
MEYSQSSMYSSPSSWSSSQESLLWNESCFLDQSSEPQAFFCPNYDYSDDFFSFESPEMMIKEEIQNGDVSNSEEEEKVGIDEERSYRGVRKRPWGKFAAEIRDSTRNGIRVWLGTFDKAEEAALAYDQAAFATKGSLATLNFPVEVVRESLKKMENVNLHDGGSPVMALKRKHSLRNRPRGKKRSSSSSSSSSNSSSCSSSSSTSSTSRSSSKQSVVKQESGTLVVFEDLGAEYLEQLLMSSC
Protein: Delta and Notch-like epidermal growth factor-related receptor (Brain EGF repeat-containing transmembrane protein) (Q8JZM4)
Organism: Mus musculus (Mouse)
Function: Mediates neuron-glia interaction during astrocytogenesis. May promote differentiation of Bergmann glia during cerebellar development by activating DELTEX-dependent NOTCH1 signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}; Single-pass type I membrane protein {ECO:0000269|PubMed:11950833, ECO:0000269|PubMed:11997712}. Note=Present on the membrane of dendrites and cell bodies but excluded from axonal membrane. Also found in early endosomes in the somatodendritic region.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Zinc finger protein ZIC 4
- Amphiphysin
- E3 ubiquitin-protein ligase DTX1
- A-type potassium channel modulatory protein DPP6
Sequence:
MPPRRAQAPGAPLLPVLALLPLLLGAGPQSGCLASPVSAAPLPAPGPCASQPCRNGGVCTPRSVTDQEHPAADAEPRYSCTCPAGVSGTYCQFVADPCASNPCHHGNCSSSSSSSSDSYLCICNDGYEGLNCEQPLPSIPTSGWTESTAPRQLQPVPATQEPDIILPRSQATVTLPTWQPKTGQKVVEMKWDQVEVVPDVACGNASSNNSAGGRLVSFEVPQNTSVKIRQDANSLLILLWKVTATGFQQCSLIDGRSVTPLQAPGGLVLLEEMLALGPNHFIGFVNDSVAKSIVALRLTLVVKASNCVPGDSHSNDLECSGKGKCATKPSEATFSCTCQDQYIGTFCEEFDACQRKPCQNEASCIDANEKQDGSNFTCLCLPGYTGELCQSKIDYCVLDPCRNGATCVSSLSGFTCQCLEGYFGSACEEKVDPCMSSPCQNNGTCYVDGVHFTCSCSPGFTGPTCAQLVDFCALSPCAHGMCRSVGTSYKCLCDPGYHGLYCEEEYNECLSAPCLNAATCRDLINGYECVCLAEYKGTHCELYKDPCANISCLNGGTCDSEGLNGTCICAPGFTGEECDIDINECDSNPCHHAGTCLDQPNGYTCHCPHGWVGANCEIHLQWKSGHMAESLTNMPRHSLYIIIGALCVAFILMLIILIVGICRISRIEYQGSSRPAYEEFYNCRSIDSEFSNAIASIRHARFGKKSRPAMYDVTPIAYEDYSPDDKPLVTLIKTKDL
Protein: Endosome-associated-trafficking regulator 1 (Antigen NY-CO-3) (Serologically defined colon cancer antigen 3) (Q96C92)
Organism: Homo sapiens (Human)
Function: Endosome-associated protein that plays a role in membrane receptor sorting, cytokinesis and ciliogenesis. Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis; the function may involve PTPN13 and GIT1. Plays a role in the formation of cilia. Involved in cargo protein localization, such as PKD2, at primary cilia. Involved in the presentation of the tumor necrosis factor (TNF) receptor TNFRSF1A on the cell surface, and hence in the modulation of the TNF-induced apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A2AIW0}. Early endosome {ECO:0000269|PubMed:23108400}. Endosome {ECO:0000269|PubMed:25278552}. Recycling endosome {ECO:0000269|PubMed:23108400}. Midbody {ECO:0000269|PubMed:23108400}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:27767179}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27767179}. Note=Colocalizes in a WASHC2-dependent manner with the retromer CSC complex at endosomes (PubMed:25278552). During cytokinesis colocalized with PTPN13 at the midbody (PubMed:23108400). Colocalizes with IFT88 and gamma-tubulin at the basal body of primary cilia (PubMed:27767179). Colocalizes with IFT88 and pericentrin at the centrosome (PubMed:27767179). {ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:25278552, ECO:0000269|PubMed:27767179}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 13
Sequence:
MSGYQRRPGATPLSRARSLAIPDAPAFYERRSCLPQLNCERPHGRDLDSPFFGIRPAFMCYVPSPVLASVGDTDFGYGKGKCSKQSPSGAHGTHFGDDRFEDLEEANPFSFREFLKTKNLGLSKEDPASRIYAKEASRHSLGLDHNSPPSQTGGYGLEYQQPFFEDPTGAGDLLDEEEDEDTGWSGAYLPSAIEQTHPERVPAGTSPCSTYLSFFSTPSELAGPESLPSWALSDTDSRVSPASPAGSPSADFAVHGESLGDRHLRTLQISYDALKDENSKLRRKLNEVQSFSEAQTEMVRTLERKLEAKMIKEESDYHDLESVVQQVEQNLELMTKRAVKAENHVVKLKQEISLLQAQVSNFQRENEALRCGQGASLTVVKQNADVALQNLRVVMNSAQASIKQLVSGAETLNLVAEILKSIDRISEVKDEEEDS