wanglab/gogpt-training-data huggingface dataset:
Protein: Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic (AtPPOX1) [Includes: Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase); Probable NAD(P)HX epimerase (EC 5.1.99.6)] (Q9LTX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). Involved in the PLP salvage pathway. Has a higher preference for PNP over PMP. May also catalyze the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21051239}.
Interaction partners:
- mRNA-decapping enzyme subunit 2
- mRNA-decapping enzyme-like protein
- Pyridoxal kinase
- Probable pyridoxal 5'-phosphate synthase subunit PDX2
- Pyridoxal 5'-phosphate synthase subunit PDX1.1
- Pyridoxal 5'-phosphate synthase-like subunit PDX1.2
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 2
- ATP-dependent
- Pyridoxal 5'-phosphate synthase subunit PDX1.3
- DEAD-box ATP-dependent RNA helicase 12
Sequence:
MRNVIRRVTTMTFTFLLQSPPLPISPSPPQFSLSSSPLSKTQRFITPSQGSRLRTLCTKVIIPNMQDSGSPPLSYLTQREAAEIDETLMGPLGFSIDQLMELAGLSVAASIAEVYKPEEYSRVLAICGPGNNGGDGLVAARHLHHFGYKPFICYPKRTAKPLYTGLVTQLDSLSVPFVSVEDLPDDLSKDFDVIVDAMFGFSFHGAPRPPFDDLIRRLVSLQNYEQTLQKHPVIVSVDIPSGWHVEEGDHEDGGIKPDMLVSLTAPKLCAKRFRGPHHFLGGRFVPPSVAEKYKLELPSYPGTSMCVRIGKPPKVDISAMRVNYVSPELLEEQVETDPTVQFRKWFDEAVAAGLRETNAMALSTANKDKKPSSRMVLLKGFDENGFVWFTNYESKKGSDLSENPSAALLFYWEILNRQVRIEGPVERIPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVLYDEYEELTKQYSDGSVIPKPKNWGGFRLKPNLFEFWQGQPSRLHDRLQYSLQDVNGNPAWKIHRLAP
Protein: Protein kinase, putative (EC 2.7.1.-) (Q384V5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin 9
- Transcription initiation protein, putative
- [RNA-polymerase]-subunit kinase
- Spt4/RpoE2 zinc finger domain-containing protein
- Plastid-encoded RNA polymerase subunit alpha
- DNA damage-binding protein 1
- Protein kinase, putative
Sequence:
MEQQGDSEAKEHGELTRNGITDNAYDNSVGAFNRTILDRYAHWMTQLDQGACGLRIWKAEELWKRYERVIRVGRGSFGSVFIVYDTERKAYLTVKCMELLGKPGPALRSLSQPTLREVILLSQIDHPNVVRLIDYYLTSDGMLHMCMPIVSHDLVSLIRIWKMRGPRGESSLGRMPLPTVKCVFRQLLRGLEYLHRRNIIHRDLKPSNVMLDDNGVVKIVDFGWARFVPRRWQGRLTGPPCVVTYRPPEILLGGQCSFKYDSSIDIWSAGCILYEMLTGGKAFSNARNEQQALAAITDMLGSPSSRSEVYYGAAGGSRLRPSKRQPRNFEERCRMVNMSNESIDFLGEMLQLEPNSRKSASQLLGHSWFSTSPLPCEPEEVSLPGSNTYRLLERKRTR
Protein: Adr-2-binding protein 1 (G5EDW1)
Organism: Caenorhabditis elegans
Function: Required for the A-I editing activity of the double-stranded RNA-specific adenosine deaminase adr-2 by facilitating adr-2 nuclear localization.
Subcellular location: Nucleus {ECO:0000269|PubMed:18780728}.
Interaction partners:
- Double-stranded RNA-specific adenosine deaminase adr-2
- A-to-I RNA editing regulator adr-1
- Protein kinase domain-containing protein
Sequence:
MSFASGCTPVSFDKLFEVSSGDKVSRENWGMIARPEPQHDSLKRRNTTSSIAKKKAKMTRGDEQITDETARKAATQLLDQIQDTPGRISLNFETPEAASVCPIPTSLNQIVNTKWTVNQLQEGQLTMLLAQDANKFKSLGVKNIKKGSVETQILPRQMDVKEIVEKLKKQDNDSDQFVGYAAAVANVLRRCDAETAQKITQAITATIEKEAPSIVNC
Protein: INO80 complex subunit D (Q66JY2)
Organism: Mus musculus (Mouse)
Function: Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- INO80 complex subunit E
- Chromatin-remodeling ATPase INO80
- INO80 complex subunit C
- INO80 complex subunit B
- RuvB-like 1
- TCF3 fusion partner homolog
- RuvB-like 2
- Nuclear factor related to kappa-B-binding protein
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
- Actin-related protein 8
Sequence:
MYEGKHIHFSEVDNKPLCSYSPKLCKQRRLNGYAFCIRHVLEDKTAPFKQCEYVAKYNSQRCTNPIPKSEDRRYCNSHLQVLGFIPKKERKKKTDPVDEVKARHQMDAMAFSLTVPTLALKMPNGLDSMSLSPPGARVPLHYLDTELEDPFAFNEEDDDLKKGVTVRKKLQSKLAQNRQRQRETEILKVRQEHFSTPPTPPQQHTHLSPLSTSLKPPAPPQGSVCKSPQPQNTSLPMQGVAPTTHSIAQIRQASHKRPLPLLPSSRAPISDAPRTDRILMKAAAFSPHLSCISRLQRLVKLCTQKRQLDADLFPHLGLDWSEESGEELEDADQASPYQVAWSIRETLRHERHTSDDDDMESRSSRVTQLCTYFQQKYKHLCRLERAESRQKKCRHTFRKALLQAASKEPECTGQLIQELRRAACSRASLRQTKLKEVEPAACSGTVKGEQCTKQALPFTRHCFQHILLNRSQQLFSSCTAKFADGQQCSVPVFDITHQTPLCEEHAKKMDNFLRGDNSRKVQHQQQRKPRKKTKPPALTKKHKKKRRRGPRRPQKPIPPAVPQGNLSMPTSVSLPVEASQMRSPSTPELSADELPDDIANEITDIPHDLELNQEDFADVLPRLPDDLQDFDFFEGKNGDLLPTTEEAEELERALQAVTSLECLSTIGVLSQSDGVPVQGLSDRGMGVFSTGTDASGIQSLSREVNTDLGELLNGRIVHDSFSSLELDENLLHSAPLSSPPTALAGQIQGQFSAPASAGLTSATLLSQSALGERAFPGQFHGLHDGSHASQRPHPAQLLSKADDLITSRQQYSSDHSHSSPHGSHYDSEHVPSPYSDHITSPHTSYSGDNMAATFSAEMPIMAQHLLPTQLEVPLGGVVNPRTHWGNLPVNLGDPSAFSNLLGADGHLLSTSLSTPPTTSNSETTQPAFATVTPSSSSVLPGLPQTSFSGMGPSAELMASTSPKQQLPQFSAAFGHQLSSHSGIPKDLQPSHSSIAPPTGFTATGATATSTNNASPPFPSPN
Protein: Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH5 (EC 3.6.4.13) (DEAH RNA helicase homolog PRP22) (Q38953)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:19245862}.
Interaction partners:
- AT3G18790 protein
- Zinc finger CCCH domain-containing protein 42
- At1g31870
- At2g32600/T26B15.16
- Trimethylguanosine synthase
- Pre-mRNA-processing-splicing factor 8A
- Zinc finger CCCH domain-containing protein 5
- Cell division cycle 5-like protein
- Zinc finger CCCH domain-containing protein 4
- DEAD-box ATP-dependent RNA helicase 36
Sequence:
MEKEELNKLNHLSLVSNVCNELETHLGSAEKVLAEFIIDLGRHSETVDEFDKNLKEAGAEMPDYFVRSLLTTIHGIYPPKPKSEKKKEEGDDQKFKGLAIKDTKDKVKELEKEIEREAEERRREEDRNRDRDRRESGRDRDRDRNRDRDDRRDRHRDRERNRGDEEGEDRRSDRRHRERGRGDGGEGEDRRRDRRAKDEYVEEDKGGANEPELYQVYKGRVTRVMDAGCFVQFDKFRGKEGLVHVSQMATRRVDKAKEFVKRDMEVYVKVISISSDKYSLSMRDVDQNTGRDLIPLRKPSDEDDSSRSNPSYRTKDGQVTKTGISGIRIVEENDVAPSRRPLKKMSSPERWEAKQLIASGVLRVDEFPMYDEDGDGMLYQEEGAEEELEIEMNEDEPAFLQGQTRYSVDMSPVKIFKNPEGSLSRAAALQSALTKERREMREQQQRTMLDSIPKDLNRPWEDPMPETGERHLAQELRGVGLSAYDMPEWKKDAFGKTPTFGQRSKLSIQEQRESLPIYKLKKELIQAVHDNQVLVVIGETGSGKTTQVTQYLAEAGYTTKGKIGCTQPRRVAAMSVAKRVAEEFGCRLGEEVGYAIRFEDCTGPDTVIKYMTDGMLLREILIDENLSQYSVIMLDEAHERTIHTDVLFGLLKKLMKRRLDLRLIVTSATLDAEKFSGYFFNCNIFTIPGRTFPVEILYTKQPETDYLDAALITVLQIHLTEPEGDILVFLTGQEEIDSACQSLYERMKGLGKNVPELIILPVYSALPSEMQSRIFDPPPPGKRKVVVATNIAEASLTIDGIYYVVDPGFAKQNVYNPKQGLESLVITPISQASAKQRAGRAGRTGPGKCYRLYTESAYRNEMPPTSIPEIQRINLGMTTLTMKAMGINDLLSFDFMDPPQPQALISAMEQLYSLGALDEEGLLTKLGRKMAEFPLEPPLSKMLLASVDLGCSDEILTMIAMIQTGNIFYRPREKQAQADQKRAKFFQPEGDHLTLLAVYEAWKAKNFSGPWCFENFIQSRSLRRAQDVRKQLLSIMDKYKLDVVTAGKNFTKIRKAITAGFFFHGARKDPQEGYRTLVENQPVYIHPSSALFQRQPDWVIYHDLVMTTKEYMREVTVIDPKWLVELAPRFFKVSDPTKMSKRKRQERIEPLYDRYHEPNSWRLSKRRA
Protein: Oligopeptide-binding protein OppA (P9WGU5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Periplasm {ECO:0000269|PubMed:38548954}. Note=Attached to the external side of the transmembrane subunits OppB and OppC. {ECO:0000269|PubMed:38548954}.
Interaction partners:
- Oligopeptide transport system permease protein OppB
- Oligopeptide transport system permease protein OppC
- Oligopeptide transport ATP-binding protein OppD
- Probable dipeptide-transport ATP-binding protein ABC transporter DppD
- Uncharacterized lipoprotein Rv2585c
- Probable dipeptide-transport integral membrane protein ABC transporter DppC
- Probable dipeptide-transport integral membrane protein ABC transporter DppB
- Beta-carbonic anhydrase 1
- Probable lipoprotein aminopeptidase LpqL
- Probable periplasmic dipeptide-binding lipoprotein DppA
Sequence:
MADRGQRRGCAPGIASALRASFQGKSRPWTQTRYWAFALLTPLVVAMVLTGCSASGTQLELAPTADRRAAVGTTSDINQQDPATLQDGGNLRLSLTDFPPNFNILHIDGNNAEVAAMMKATLPRAFIIGPDGSTTVDTNYFTSIELTRTAPQVVTYTINPEAVWSDGTPITWRDIASQIHAISGADKAFEIASSSGAERVASVTRGVDDRQAVVTFAKPYAEWRGMFAGNGMLLPASMTATPEAFNKGQLDGPGPSAGPFVVSALDRTAQRIVLTRNPRWWGARPRLDSITYLVLDDAARLPALQNNTIDATGVGTLDQLTIAARTKGISIRRAPGPSWYHFTLNGAPGSILADKALRLAIAKGIDRYTIARVAQYGLTSDPVPLNNHVFVAGQDGYQDNSGVVAYNPEQAKRELDALGWRRSGAFREKDGRQLVIRDLFYDAQSTRQFAQIAQHTLAQIGVKLELQAKSGSGFFSDYVNVGAFDIAQFGWVGDAFPLSSLTQIYASDGESNFGKIGSPQIDAAIERTLAELDPGKARALANQVDELIWAEGFSLPLTQSPGTVAVRSTLANFGATGLADLDYTAIGFMRR
Protein: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit I) (NDH subunit I) (NADH-plastoquinone oxidoreductase subunit I) (Q6ENA3)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01351}.
Interaction partners:
- NAD
- NAD
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Uncharacterized protein
- NAD
- NADH dehydrogenase iron-sulfur protein 4
- Ribosomal protein/NADH dehydrogenase domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MFPMVTGFMSYGQQTIRAARYIGQSFIITLSHTNRLPITIHYPYEKSITSERFRGRIHFEFDKCIACEVCVRVCPIDLPLVDWRFEKDIKRKQLLNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALSRLPISIMGDYTIQTIRNSTQSKIDEEKSWNSRTITDY
Protein: candidapepsin (EC 3.4.23.24) (G8B6Y8)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSSHQLSITPMTTIAIFTKNVLLAIAFALFAQGAAIPDPAKRDDNPGFVALDFEVTRKPLDVNATSELSKRSSPSSPLYFEGPSYGIRVSVGSNKQEQQVVLDTGSSDFWVVDSSASCQKGNCKQYGTFDPHSSTSFKSLGSSFSIGYGDKSSSIGTWGQDTIYLGGTSITNQRFADVTSTSVNQGILGVGRVETESANPPYDNVPITLKKQGKIKTNAYSLYLNSPGAATGTIIFGGVDNAKYSGKLIEEPLVSDRYLAVNLKSLNYNGDNSNAGFGVVVDSGTTISYLPDSIVDDLANKVGAYLEPVGLGNELYFIDCNANPQGSASFTFDNGAKITVPLSEFVLQSTANACVWGLQSSDRQNVPPILGDNFLRHAYVVFNLDKETVSLAQVKYTSASSVSAI
Protein: E3 ubiquitin-protein ligase APD1 (EC 2.3.2.27) (Protein ABERRANT POLLEN DEVELOPMENT 1) (Q0WS06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pollen mitosis II (PMII) regulation during male gametogenesis.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:22897245}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:22897245}; Multi-pass membrane protein {ECO:0000255}. Note=Associated with intracellular membranes and in the tonoplast and endosomes in the germinating pollen tubes. {ECO:0000269|PubMed:22897245}.
Interaction partners:
- Ethylene-responsive transcription factor-like protein At4g13040
- Protein VAC14 homolog
- Probable protein phosphatase 2C 38
- Probable protein phosphatase 2C 79
- Probable protein phosphatase 2C 63
- Probable protein phosphatase 2C 68
- LOB domain-containing protein 27
- Probable protein phosphatase 2C 64
- Probable protein phosphatase 2C 46
- Homeodomain-like superfamily protein
Sequence:
MDSAPSPSSLDFELSPPVLVTMTSTSSSASDNVEGADDDANTHGIFNWRDFSSCWRVSESNLYCFSLALLIWFFASFILIENLYGPKNVWLGPSSSILVEPSSIFVKSIKVKVLDYSEPGLQLYGFYRTPALDCFVNWSESRVLSISHESYKGWPYYLNSGSLLNITYTVKPQGSAVQLVVDEGHQGVPQSVLNDPAYRYNVWSWNLIEGSGMIQLEIRKSSSYYLAVANLKSKDVEVELNIDVKAVLYDTKQSFYNCNFSNGECTFNAMSLVGNSVVVTSPAASQGVSIEDEWYIRFSYQPREIAYVIGTGVVICFMLVAIQFCNRFQCSGGEGHLTEDDSARTRLLADKDDDGSSMGSCDDSYANDDADLEEFMGNDGEASNRSRRLCAICFDVPRDCFFLPCGHSVSCYECGTTMQEADGSCPICRRKMKKVKRIYTV
Protein: Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (MLC-2) (MLC-2v) (Myosin light chain 2, slow skeletal/ventricular muscle isoform) (MLC-2s/v) (P08733)
Organism: Rattus norvegicus (Rat)
Function: Contractile protein that plays a role in heart development and function (By similarity). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force. During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity).
Subcellular location: Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:17885681}.
Interaction partners:
- Myosin light chain 3
- Myosin-6
- Myosin-7
- Troponin T, cardiac muscle
- Troponin I, cardiac muscle
- Troponin C, slow skeletal and cardiac muscles
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin I, slow skeletal muscle
- Myosin-binding protein C, cardiac-type
- F-actin cross-linking protein
Sequence:
MSPKKAKKRLEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD
Protein: homocitrate synthase (EC 2.3.3.14) (Q4WPU2)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Putative aconitate hydratase, mitochondrial
- Acetyl-coenzyme A synthetase
- Acetyl-CoA acetyltransferase erg10B, cytosolic
- Acetyl-CoA acetyltransferase erg10A, mitochondrial
- Acetyl-CoA hydrolase
- Malate synthase
- Acetyl-CoA carboxylase
- Acetyltransferase component of pyruvate dehydrogenase complex
- 2-isopropylmalate synthase
- Succinyl-CoA synthetase beta subunit, putative
Sequence:
MCPGADNEPNGHTNGANGTVPHPGFTAVETRQNPHPSASRNPYGHNVGVTDFLSNVSRFKIIESTLREGEQFANAFFDTEKKIEIAKALDDFGVDYIELTSPCASEQSRKDCEAICKLGLKAKILTHIRCHMDDARVAVETGVDGVDVVIGTSSYLREHSHGKDMTYIKNTAIEVIEFVKSKGIEIRFSSEDSFRSDLVDLLSIYSAVDKVGVNRVGIADTVGCASPRQVYELVRVLRGVVSCDIETHFHNDTGCAIANAYCALEAGATHIDTSVLGIGERNGITPLGGLMARMMVADPEYVKSKYKLEKLKDIEDLVAAAVEVNIPFNNYITGFCAFTHKAGIHAKAILNNPSTYEIINPADFGMTRYVHFASRLTGWNAIKSRAQQLNIEMTDAQYKECTAKIKALADIRPIAVDDADSIIRAYYRNLKSGENKPLLDLTAEEQAQFAAKEKELAGSGVIA
Protein: At1g64700 (DUF4228 domain protein) (F13O11.2 protein) (F1N19.27) (Q9XIS1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- D-ribose-binding periplasmic protein
- DUF4228 domain protein
- 6,7-dimethyl-8-ribityllumazine synthase
- Basic-leucine zipper transcription factor K
- DUF4228 domain protein
- At2g01340
- At5g37840
- Uncharacterized protein At1g76660
- HTH-type transcriptional regulator
- At1g29190/F28N24_12
Sequence:
MGNCLFGGLGDEEEDLLIKVIKSDGGVLEFYSPVTAGFVSHGFSGHALFSAVDLLWKPLAHDHLLVPGQSYYLFPNIVSDELKTFVGSCHVRSNSESLSAITPYRMSLDYNHRVLKRSYTDVFSRNSHIRTRQKEKKTRRRRTSSKGAIWKVNLIINTEELLQILSEDGRTNELIESVRAVAKGETSSITSSSSENFLSVVQT
Protein: Carbazole 1,9a-dioxygenase, terminal oxygenase component CarAa (CARDO) (EC 1.14.12.22) (D5IGG0)
Organism: Sphingomonas sp
Function: Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Catalyzes the dioxygenation at the angular (C-9a) and adjacent (C-1) positions of carbazole to yield a highly unstable cis-hydrodiol intermediate which is spontaneously converted to 2-aminobiphenyl-2,3-diol.
Interaction partners:
Sequence:
MANQPSIAERRTKVWEPYIRAKLGFRNHWYPVRLASEIAEGTPVPVKLLGEKILLNRVGGKVYAIQDRCLHRGVTLSDRVECYSKNTISCWYHGWTYRWDDGRLVDILTNPGSVQIGRRALKTFPVEEAKGLIFVYVGDGEPTPLIEDVPPGFLDENRAIHGQHRLVASNWRLGAENGFDAGHVLIHKNSILVKGNDIILPLGFAPGDPDQLTRSEVAAGKPKGVYDLLGEHSVPVFEGMIEGKPAIHGNIGSKRVAISISIWLPGVLKVEPWPDPELTQFEWYVPVDETSHLYFQTLGKVVTSKEAADSFEREFHEKWVGLALNGFNDDDIMARESMEPFYTDDRGWSEEILFEPDRAIIEWRGLASQHNRGIQEAR
Protein: Vacuolar protein-sorting-associated protein 25 (hVps25) (Dermal papilla-derived protein 9) (ELL-associated protein of 20 kDa) (ESCRT-II complex subunit VPS25) (Q9BRG1)
Organism: Homo sapiens (Human)
Function: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. The ESCRT-II complex may be involved in facilitating the budding of certain RNA viruses.
Subcellular location: Cytoplasm. Endosome membrane. Nucleus, nucleoplasm. Note=Distributes diffusely throughout the cytoplasm and nucleoplasm, but exhibits a punctate distribution on coexpression with CHMP6.
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar-sorting protein SNF8
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 28 homolog
- Charged multivesicular body protein 2a
- Tumor susceptibility gene 101 protein
- Charged multivesicular body protein 3
- Charged multivesicular body protein 7
- Vacuolar protein sorting-associated protein 37B
- Hepatocyte growth factor-regulated tyrosine kinase substrate
Sequence:
MAMSFEWPWQYRFPPFFTLQPNVDTRQKQLAAWCSLVLSFCRLHKQSSMTVMEAQESPLFNNVKLQRKLPVESIQIVLEELRKKGNLEWLDKSKSSFLIMWRRPEEWGKLIYQWVSRSGQNNSVFTLYELTNGEDTEDEEFHGLDEATLLRALQALQQEHKAEIITVSDGRGVKFF
Protein: DHH family protein (Q72ER3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Phosphoadenosine phosphosulfate reductase, putative
- Adenylylsulphate reductase, beta subunit
- sulfate adenylyltransferase
- Adenylyl-sulphate reductase, alpha subunit
- tRNA pseudouridine synthase B
- YlxP-like protein
- Translation initiation factor IF-2
- Small ribosomal subunit protein uS15
Sequence:
MQEPQARIAALLRDADDILITTHANPDGDAIGSLGAMGHVLATLGKRFCLCNVSGVPSHLSWVPLPGQVYTSFDELPFQPRLAIVLDCGDEKRPGEALRAPLADLPSINIDHHQGNPLFGTVDNWVEPQRAATGEMVAEIALALGQPLAGALGECLYLALVSDTGSFSFGNTSARVLSLAAEIVGNGLDVAALTERHDNQWSFARMQLWGRLMQEMRLAFDGTVAISVIPDALIESCGARRADLEGWASQMRKVRGVRVSVMVRGNGPEGSKVSLRSTGSDDVRAVAARFGGGGHRNAAGVEMPLPPEEASRQVVAALGEQLGLDGDGASLYV
Protein: ADP-ribosylation factor guanine nucleotide-exchange factor sec71 (ARF-GEP sec71) (Q9UT02)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in protein transport.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11075}. Golgi apparatus {ECO:0000250|UniProtKB:P11075}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P11075}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:P11075}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P11075}.
Interaction partners:
- Uncharacterized protein C211.03
- ADP-ribosylation factor guanine nucleotide-exchange factor sec72
- Putative acetyltransferase C18B11.09c
- Signal peptidase complex catalytic subunit sec11
- U6 small nuclear RNA
- m7GpppX diphosphatase
- SVP1-like protein 2
- ADP-ribosylation factor 1
Sequence:
MTDLEIETVSRVSSNPDEVKGSSVVEEEPDSESTIKSRVSDEIDEHDSIPEQSNTEKSIEINDKNLEAEKDIESNLSLRPPEDDLDSRSIESEQTGTLSKQTTSTSEAPQDLKIWKNISNASNQNSGKLNPQLFVIEAFKHMSKAKATKRHKKLREAINNVQIELQKQPFLLPEVILEPLVMACQTNSTTLLTITLDCFAKLIDYNYFDSPTLNPSDITLMERVVNTIASCFCGESTPERVQLQIVKALLAAITSERTIIRHSFLLTAVRQTYNIFLLCKDSTTQAIAQVALLQMVDSVFQRLSTVLNHEREFSTINMNKSSSNGTPDRANSPIPSQLSENKLTLESFEHRKSFDQVREEAPLEEDSLEQQLLRDAFLLIRALCKLSIKNIPYEHEYDLKSQSMRSKLMSLHLIYHILRTYMNILSDINVKIRSPTSTPTPLIDAVKQYICLALAKNVVSHVLPVFEISCEIFWLILSELKNFFKSELEVFFTEIFFPILEMRTSSNQQKIVLLNIFHRMCEEPQTLIELYLNYDCISGNTENIYERAIVTLSRIASQSTSDPPPSFVFRDDQLVIDKPGFVYHTLNDIPQLNSSTIGSYVHSHNPPYFDYQIRLKSYRCLISTLSSLFTWCNQTFAPTVEITAKDDETESTSKGEEPQKSKSEPPSAGINSTSMDNLESSGQALATDDPSQFENLKHRKKQLQEAIQKFNYKPKEGIKILLSSHFIASKTPTDIAKFLISTEGLDKAVLGEYLGEGNDENIAIMHSFVDHMSFNDIPFVNALRSFLQKFRLPGEAQKIDRFMLKFAEKYIDDNLGVFKNADTAYILAYSIIMLNTDLHSPQVKNRMTCQDFIKNNRGVDDGANLSDSFLTEVYEEIQKNEIVLKDEQDPTSNFPEIPGTSNLSFAANISNALATVGRDLQREAYYMASNKMANKTEALFKDLIREQRERGKLSGNDIYYTARHFEHVCPMFEAVWMPILAAFSEPLQLSSDPALIQLSLDGFRLAMNVIFFFSMDLPRNAFMQTLTKFTHLNNTSELKWTNMHALKTLLEISLAHGDKLRDSWKDVLLCISQLERVQLISAGVDINSLPDVSTTKPLRKSLDKNIRQSRSGSISLKHSKSFQSASTHSTKSSSVEIVREYSSREVVMAVDMLFSNTRNLGSEGIYDFVKALIEVSWEEIECSLELSNPRLFSLQKLVEISYYNMRRIRMEWSSIWSLLGTYFTQVSCHENSIIASFALDSLRQFSMQFLEIEELSHFKFQKDFLQPFSHAMENSQDLKIKDLVLRCIDQMIKARYQNIRSGWRTIFHILAYASKIENLLVLQCAISVVSSLGHEHISCVLTQGAYIDLISCITKFAKLNGNQKFCLSCVDMLKNLEHELIKHLKHMKKESVYSKKLEEEYWLPFLLSFNEIICEASDLEVRSKALKVLFDCLYRHADDFDEEFWETVSNKALLSIFSILSITNSQRLYLAKNTEETEVWMLTTMVEALKAFIELIKNLFERLHFLLPKALNLLEKCICQENSMISKVGLSCFSQFVLKNKNQFKDVDWDEIINSINQLLQMTLPIELRDPSLYPQVNSDSSLEDVKENSFRPHEISRFNSQSVFKSKKHHLKSIVVKCTLQLLMLNCLWELFHSDNMLTNIPKRKMVKLLDILKQSWEFAESFNSDFEIRAKILSSGIVEHMPNLLSQEALCAKLYFYTAFECMSSLKSDSHDTEEYNDLMDVFQKKIYLASQLVLHGFQRVIGDNPVKGVAAFQPVIAALVSYINSLDEIQFSRGKSEFYQLLCAIVACGHIDQQLGTSLSNAFLRYAC
Protein: Uncharacterized protein, isoform I (A0A0B4KHX6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTEFSTNNDHSKPHFTASQQKPHQNSPIHQQAFTPSNPNTHPHLLQRLAQQQQQQQQQQHQRPHKFQQSLPFSQLNNGNNTAAHILPGSSPHSPLSYRNPLNSPSNSPFSNTAQTTIGKRYQQQQLTDRLLQQQHLQQCQQQQLQSLGSSDVEEDLAAEELSEESLKQNVAIVLSNLDRYNNALRSIILNEQVSSSIITPSDSLLFGEDSSGLLYCDNDNSRKHKGNNNFVLGKMAATPESDYNSNATTPGGRSSEQQLQQQQQQQQLGVGGMLCGGGGGGGVGMRETTNGGGNNLNCSLASSHDFTHDNSDYQWFLDYGYRDGCGGMQRSVLSSLSASYNAMGDLIYYEDLAKNLDANLAEVDMESFRAEDIHSLLSHLPAYCKSLGGTNSRLQQSLLLQQQQQQQQQLQQQQVLQHNSMLQHMSQTSTTSTNELIDNSFCKSELLFSPVRESHISVDSLDMDAYPDDGEIILTCNKDNYTIAFEGSVLYSDDSFYADPSDIAARNKQNCINLHSNLEDIVKRNKALEVSMSRSAQAFQPLCPMSPKGQAATTSAAKLQRYPSGNNNTETITITRHLPQCTVRKSSSLPNLQNEEAMAGSCHKEQGPEESGPQAVPLNVSQAISTSTMEAGKSRSRNLLPMCQMPISISVSISERLQQQADQQLPSEQITPTSQQPQQQHHHSHHHRHKHRCSCSQESHISGSASSGNSSNPPAFNLVKLFIKQKSSNSSGGQEDLGAQASAHTCMDVSSGCWPSSDAASSSSGSLEQRLRKKSMNDSGKGSAVSRHDEEEHYPDTETPRRQLRARSEAVFYDDVASSSSTGSLTATNSPAHRRRSMPLRNPQLYQLAAQVSTGSQMSSEASSEQLTQVPRRAEAGCGTSTRPLSCASSSEMITRSMQTSCGSLSTTRSSLSDRYRCVPPSFLEKLNNLGEERQAPIYVIYPNYALPDLGFVKTNASTDVIFSPFNYKMTMDGATGSTSSSGSLRKQRNSSQSVSEDEILKTLDYKHVADWQSLATLLPSEYRRRLQHIPEVKHLVRQLDAELSQRPLFCMSPPLRRNRTHICDCAKYFQGQQTQTDEASSSGSSQQPSSGYRGSSTLLTDSELDVDPLKQMYVYQYDQQRMDSGVETSPGSQLTQTPPQPMPRSILRKAHSAQSRSKRNSMIEAQQTQKLTKLEKRRSLQEPPNNYGLGSTDELADVFEEEEHSQPAPPVKQRLSRKDLDARARAESFLASLPRSELKYYAEIASILESSGEHVTYDAAALKKEVSRVLSQQKKVSFNDEGVAAGLQQHAKRFATPPNSPNISMGALKRDTVDVLEQRKIESNRFKRLQIQWELMSKDSSMLKELASEAATKSGGSTPTSGNSTGSNSAPRSRIPRPVSYPAGRSSTPTSSRTAPVLATPSPARPATPKTVTKSHNKPGLFTSPRPSRLTSAQEAAGGNKVSTRSPSRIVQPKRYSLAGATTPTSTTPTSARARTPTNRVAVTAPNTPKRQAVAQSPRPTSRVR
Protein: Derlin (Q386J4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363059}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363059}.
Interaction partners:
- Katanin p60 ATPase-containing subunit A-like 2
- Derlin
- Protein OS9-like domain-containing protein
- MRH domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Ubiquitin fusion degradation protein, putative
- UBX domain-containing protein
- MPN domain-containing protein
- Glucose-regulated protein 78, putative
Sequence:
MDFNFLWEIPPVTRLLLCLSVISVVLVSFGLVHPLQMIFSPTLAFQEKHYWRLVSTFFYFGPLNLSSIIELHWLYMVSSSIELQYFHRRRLDYCLTLFTGAGLLLFLRSTRAIETPYLSNQFSKTLVYLFGRLLPHQEASIFGLLTVQVRYLPLVFLLMSVMFGEVGIGTEVMADLVGHILWYLLEIFPRITKIHPLRVQRYFIR
Protein: Endophilin-A2 (Endophilin-2) (Q6FGM0)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, podosome {ECO:0000256|ARBA:ARBA00004188}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004220}.
Interaction partners:
Sequence:
MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKEMEKKVDVTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMIRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCEKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREASSRPKREYKPKPREPFDLGEPEQSNGGFPCTTAPKIAASSSFRSSDKPIRTPSRSMPPLDQPSCKALYDFEPENDGELGFHEGDVITLTNQIDENWYEGMLDGQSGFFPLSYVEVLVPLPQ