wanglab/gogpt-training-data huggingface dataset:
Protein: Pantothenate kinase (EC 2.7.1.33) (Pantothenic acid kinase) (O74962)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in the physiological regulation of the intracellular CoA concentration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C4B3.18
- Pantoate--beta-alanine ligase
- Probable thymidylate synthase
- Probable coatomer subunit gamma
- Probable acetyl-coenzyme A synthetase
Sequence:
MSETECGRFSTISRETISNVERQLSQPPSVWLNLTGARIIENEGQFDKDIALPNNKSHVTHIAVDIGGSLAKVMYYVCESSSPSSSSSSISEAENYTGGRLSFMIFETAKIEDCIQFMANLIDNHVKNCNKKKITLIATGGGAYKFYDRMSKQLDIKVIREDEMECLIMGLNYFVSCIPREVFVLDLDTCELTFQNHLNCYHYPHMLVNIGSGVSILKVTGPSQFERIGGSSLGGGTLWGLLSLLTPANSFDEMLELSKGGDNTSVDMLVGDIYGKDIGYERFGLKSTTIASSFGKVFRERKPLEEFAPQDISRSLLLAISNNIGQIAYLHAQKHNVQNIYFGGSFIRNHVQTMHTLTYAIQYWSNHTMNAYFLRHEGYLGVFGAFMKYATSQPSNVPVPSIS
Protein: tRNA (uracil-5-)-methyltransferase homolog B (EC 2.1.1.35) (TRM2 homolog B) (rRNA (uracil-5-)-methyltransferase TRMT2B) (EC 2.1.1.-) (Q8BQJ6)
Organism: Mus musculus (Mouse)
Function: Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine in tRNAs and 12S rRNA. Catalyzes the methylation of uridine at position 54 (m5U54) in all tRNAs. Specifically methylates the uridine in position 425 of 12S rRNA (m5U425). Does not affect RNA stability or mitochondrial translation (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q96GJ1}.
Interaction partners:
- 12S rRNA N
- tRNA
- 5-cytosine rRNA methyltransferase NSUN4
- rRNA methyltransferase 3, mitochondrial
- Pseudouridylate synthase RPUSD4, mitochondrial
Sequence:
MHNPRLFLSRAGFFSKPGLLPWDTGRPPDLSQSLLGRAYKGSFTSVIAKKHPSRQKYQKKQRHCRDDSWQERLADVVTPLWRLSYEAQLKVKFEAQKKLLQSLESHLKVLHGVSDTVAAHQSEGLRCLLHPIIPSPTTTGYRNKSTFSVYRSPDGNPKTVGYYLGTWKDGNVVCLPCNHLKNIPEKHSQVAQYYEVFLRQSSVEPCLLFHEGGHWRELVVRTNRQGHTMAIVTFHPQGLSEEEVCVQKVTLKDFFTKGPGAICELTSLYFQESTMTRCSHQQSPYQLLFGEPHIFEDLLGLKIRISPDAFFQINTAGAEMLYRIIGELSGVNSESLLLDICCGTGVIGLSVAQRASQVHGIELVEQAVEDARWTAAFNGVTNCEFHAGRAETILPQLLKSQKDEKLTVAVVNPARAGLHYRVVRAIRNCRTIHTLVFVSCKPHGESTRNFIELCCPPNSAKQLLGDPFVLREAVPVDLFPHTPHCELVLLFTR
Protein: Protein AF1q (Q13015)
Organism: Homo sapiens (Human)
Function: Cofactor for the transcription factor TCF7. Involved in regulation of lymphoid development by driving multipotent hematopoietic progenitor cells towards a T cell fate.
Subcellular location: Nucleus {ECO:0000269|PubMed:21715312, ECO:0000269|PubMed:26079538}. Cytoplasm {ECO:0000269|PubMed:21715312, ECO:0000269|PubMed:26079538}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21715312}. Note=Continuous nuclear export is followed by degradation. {ECO:0000269|PubMed:21715312}.
Interaction partners:
- Histone-lysine N-methyltransferase 2A
Sequence:
MRDPVSSQYSSFLFWRMPIPELDLSELEGLGLSDTATYKVKDSSVGKMIGQATAADQEKNPEGDGLLEYSTFNFWRAPIASIHSFELDLL
Protein: Chitinase-like protein 1 (AtCTL1) (Protein ANION ALTERED ROOT MORPHOLOGY) (Protein ECTOPIC DEPOSITION OF LIGNIN IN PITH 1) (Protein ECTOPIC ROOT HAIR 2) (Protein POM-POM1) (Protein SENSITIVE TO HOT TEMPERATURES 2) (Q9MA41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: No chitinase activity. Essential for normal plant growth and development. Regulates cell expansion extent and differentiation at least in roots and hypocotyls. Prevents lignin accumulation in the pith. May modulate ethylene-mediated regulation during development. Probably required to establish thermotolerance acclimation. Plays a role for controlled anisotropic cell expansion in the regulation of waving during root gravitropism and thigmotropism. Involved in the root system architecture adaptation to multiple environmental conditions such as nitrate. Contributes to salt tolerance and possibly to drought by preventing the overaccumulation of sodium ions.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Cellulose synthase A catalytic subunit 3
- Protein CELLULOSE SYNTHASE INTERACTIVE 1
- Protein COBRA
- Cellulose synthase A catalytic subunit 1
- Endoglucanase 25
- Cellulose synthase A catalytic subunit 6
- Chitinase family protein
- Chitinase-like protein
- COBRA-like protein 4
Sequence:
MVTIRSGSIVILVLLAVSFLALVANGEDKTIKVKKVRGNKVCTQGWECSWWSKYCCNQTISDYFQVYQFEQLFSKRNTPIAHAVGFWDYQSFITAAALFEPLGFGTTGGKLMGQKEMAAFLGHVASKTSCGYGVATGGPLAWGLCYNREMSPMQSYCDESWKFKYPCSPGAEYYGRGALPIYWNFNYGAAGEALKADLLNHPEYIEQNATLAFQAAIWRWMTPIKRAQPSAHDIFVGNWKPTKNDTLSKRGPTFGSTMNVLYGEYTCGQGSIDPMNNIISHYLYFLDLMGIGREDAGPNDELSCAEQKPFNPSTVPSSSSS
Protein: D-dopachrome decarboxylase (EC 4.1.1.84) (Q6IQL4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPFINIETNLPASKFPEDFLKRLCSTLAAALGKPEDRMNLVVKPDLPMFFAGSSSPCVLMTVSAIGVTDTAEKNKQHSAKIFQFLQGEFGLSDDRILVLFYPLEPSQIGKKGTVMSFL
Protein: DNA-binding protein REPIN1 (Zinc finger protein 464) (Zfp-464) (Q5U4E2)
Organism: Mus musculus (Mouse)
Function: Sequence-specific double-stranded DNA-binding protein required for initiation of chromosomal DNA replication. Binds on 5'-ATT-3' reiterated sequences downstream of the origin of bidirectional replication (OBR) and a second, homologous ATT sequence of opposite orientation situated within the OBR zone. Facilitates DNA bending (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:20727851}. Cytoplasm, cytosol {ECO:0000269|PubMed:20727851}.
Interaction partners:
Sequence:
MLEQRCRGPTAMGPAQPWLFSGPSQESSQPDRGLRYQGKSAQPRGQTPGKVHRCAHCRKRFPGWVALWLHARRCQARLPLPCHECNQRFRHAPFLALHLQVHASAVPDLGFICHLCGHSFRGWVALVLHLRAHSASKRPITCPECDRRFWRQKQLRAHLRRCQPPVPEARPFICGNCGRSFAQWDQLVVHKRVHVAEALEEAAAKALGPRPRGRPAAPRPGGDAVDRPFQCACCGKRFRHKPNLIAHRRVHTGERPHQCPECGKRFTNKPYLTSHRRIHTGEKPYPCTECGRRFRHKPNLLSHSKIHKRLEVSAQAAPHPESHQIAAEPMAQPALGVPLGSPRTPAEAPALLHSCSDCGRSFRLERFLRLHQRQHTGERPFACTECGKNFGKKTHLVAHSRVHSGERPFACEECGRRFSQGSHLAAHRRDHAPERPFVCPDCGKAFRHKPYLAAHRRIHTGEKPYVCPDCGKAFSQKSNLVSHRRIHTGERPYACPDCDRSFSQKSNLITHRKSHIRDGAFCCAICGQTFDDEDRLLMHQKKHDA
Protein: Protein phosphatase methylesterase 1 (PME-1) (EC 3.1.1.-) (Q95R98)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Serine/threonine-protein phosphatase PP2A
- Leucine carboxyl methyltransferase 1
- Well-rounded, isoform B
- Protein phosphatase PP2A 55 kDa regulatory subunit
- Serine/threonine protein phosphatase 2A regulatory subunit
- Uncharacterized protein, isoform B
Sequence:
MSSLQRTMLKGKLPPTIPGGRIGRADSFKKSRIRDYKPGMWNEFFAEKEDVTVDEQRTFRIYRTKQPEKPGPVLLLLHGGGYSALTWAHFCSEVTSMIHCQCLCIDMRGHGDSKVDDEDDLSADTLAKDIGDLILKLYPEEVPQLFVVGHSMGGAIAVHFAHMALVPNLIGITVIDVVEGTAMEALASMQSFLRSRPKYFQSIPNAIEWCIRSGQVRNVDSAKVSMPGQIINCTTNKLATNDLPLPDDVLEEAHHNSMFPNPFSISEDEESSPPGDDAADGSSESAAAGADFKKPNTTKSTTEAAKNYTWRIDLSKSEKYWVGWFSGLSDKFLNLRLPKQLLLASIDGLDRTLTVGQMQGRFQMQVLARCGHAVHEDRPHEVAEVISGYLIRNRFAEAASEFRCHMPSC
Protein: Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (P0A744)
Organism: Escherichia coli (strain K12)
Function: Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Interaction partners:
- Peptide methionine sulfoxide reductase MsrB
- Free methionine-R-sulfoxide reductase
- Thiol:disulfide interchange protein DsbE
- DNA polymerase I
- Protein-methionine-sulfoxide reductase catalytic subunit MsrP
- Thioredoxin reductase
- Tyrosine--tRNA ligase
- Peroxiredoxin Bcp
- Thiol:disulfide interchange protein DsbD
Sequence:
MSLFDKKHLVSPADALPGRNTPMPVATLHAVNGHSMTNVPDGMEIAIFAMGCFWGVERLFWQLPGVYSTAAGYTGGYTPNPTYREVCSGDTGHAEAVRIVYDPSVISYEQLLQVFWENHDPAQGMRQGNDHGTQYRSAIYPLTPEQDAAARASLERFQAAMLAADDDRHITTEIANATPFYYAEDDHQQYLHKNPYGYCGIGGIGVCLPPEA
Protein: Pleckstrin homology domain protein OPY1 (Overproduction-induced pheromone-resistant yeast protein 1) (P38271)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane {ECO:0000269|PubMed:22562153}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:22562153}.
Interaction partners:
- Protein transport protein TIP20
Sequence:
MIAGATAPSSQHEILIASNLIKKPSTSQNKTPTAQSSSGNNGAADGAPQGYHHHHHHHRHLWWPRTTDHQYWCVLRKNQFAYYKTRDEREAISVIPRFDILNFKISELDGILTVYTPSKDLIFKFPRGQNEKVGMELMHNWKIALEKFLSSPSGNESVTTGSDYDEEEDDDDLIVVDEKAGPSSSKHSCSLTMDEQLSREDKEFYRMFDPRNAEHQVCSGILYTKVKKKKLFNRAKWQKFNVELTNTSFNLYSFKTGKLKKSIKLDKIIDCIELDNNSKMKNDDTNFALITFDERLSFKAANDQDMVDWIINFKSGILIRKKLKAENI
Protein: Vesicle-associated protein 4-2 (Plant VAP homolog 4-2) (AtPVA42) (VAMP-associated protein 4-2) (Q8VYN2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in vesicle trafficking.
Interaction partners:
- Toll-Interleukin-Resistance
- Calcium-binding EF hand family protein
- At5g57460
- Transducin/WD40 repeat-like superfamily protein
- Transducin/WD40 repeat-like superfamily protein
- Calcium-binding EF hand family protein
- AP-2 complex subunit sigma
- Beta-adaptin-like protein B
- Actin-related protein 3
- AP-2 complex subunit alpha-1
Sequence:
MTMTEEKPTSDGKGGWGFFKIPFRNSSGHRNAASSAATSPFPSGASSSSTSSHLHNHHQHHHQHHHQHHHQLGYNGPHGDGSGQNQHPTPSPSVSSVAKSFLPTKRRLKLDPSEKLYFPYEPGKQVRSAIKIKNTSKSHVAFKFQTTAPKSCFMRPPGAILAPGETIIATVFKFVEPPENNEKPMDQRSRVKFKIMSLKVKGPMDYVPELFDEQKDDVSKEQILRVIFLDPERSNPALEKLKRQLAEADAAVEARKKPPEETGPKMIGEGLVIDEWKERRERYLAQQQGEGADSV
Protein: MFS transporter fmqE (Fumiquinazoline biosynthesis cluster protein E) (Q4WLW9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: MFS transporter; part of the gene cluster that mediates the biosynthesis of the antitumor cytotoxic peptidyl alkaloids fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts. Probably involved in fumiquinazolines metabolism and transport.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:24612080}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- FAD-dependent monooxygenase fmqB
- FAD-linked oxidoreductase fmqD
Sequence:
MPEDKVEAIEHVESSRHDATVNEKAIADFLNAEKEMTTWQAVRAHRRLLLFAAYRVTHLAILPFVCASNYGYDTVSNGSSIAMPAFIMSFGAMNHATGSMYLPSIWTSLWTSMTNLGQALGSLIAGFLAERIGRRWTAVSLAILSIVGTFILVFSSTRGMLLVGKTMNGAVVGGLMAIGTTYAADVAPIKLRGALLQAIVFFGVAMQGVSLGIVRAFILDMRPLAWKIVFGIQWAFATLVLIAAFLVPESPVFYVAHGKHDKAQSALRRLHGSSDQYLHIRYGAIVHALDEERKQQSESVSWAELFKGCNLKRTITIGFIMFSTSAIGVPFLTQNIYFLITVGLNVTSVFDIGIGGFFLGCLFVMLGWLSNEGIGRRRLWLWGLIGNFLCMVTIGALGFSTTKASQLAIAVIMNVLISYGVYATVGVAWTICPEISSHRLRQYSQSVAFIVGAVGGWLFNFITPYMYNVDSGNLGAKTGFVYAGLTVVVAVISWFLVPETAGLSVEDIDRAYEMGTAPRHFKSAKATVSAESGH
Protein: Pyruvate kinase PKLR (EC 2.7.1.40) (Pyruvate kinase 1) (Pyruvate kinase isozymes L/R) (R-type/L-type pyruvate kinase) (Red cell/liver pyruvate kinase) (P30613)
Organism: Homo sapiens (Human)
Function: Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis.
Interaction partners:
- L-lactate dehydrogenase A-like 6A
- L-lactate dehydrogenase C chain
- L-lactate dehydrogenase A-like 6B
- L-lactate dehydrogenase A chain
- Enolase 4
- Beta-enolase
- Alpha-enolase
- Glucose-6-phosphate isomerase
- Gamma-enolase
- Fructose-bisphosphate aldolase B
Sequence:
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Protein: Serpin family H member 1 (E9PMI5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSLLLLSAFCLLEAALAAEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENILVSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSLSNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRSALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKMVDNRGFMVTRSYTVGVMMMHRTGLYNYYDDE
Protein: Defective chorion protein, FC106 isoform [Cleaved into: Defective chorion protein, FC106 isoform; FC106 S80; FC106 S60] (P18170)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for proper assembly of the eggshell.
Subcellular location: Secreted {ECO:0000269|PubMed:3378704}.
Interaction partners:
Sequence:
MRLFSLLPLLALLVVQAAGQSEVTSDDPATDAGSTTNSTTDTKPRIPSQDEILGQMPSINPIRTGNPQMDAFYMMFPALGSLLKWGSLFPAYSILGAIPDNLQPTAAASKVVLVLADDATAKTRVARQNPPPNPLGQLMNWPALPQDFQLPSMDLGPQVGSFLAQLPAMPTVPGLLGAAAPVPAPAPAPAAAPPPAPAPAADPPAAPVPDAPQPAILGQAALQNAFTFFNPANFDASSLLGQSVPTFAPPNLDFVAQMQRQFFPGMTPAQPAAAGTDAQASDISEVRVRPEDPYSQEAQMKIKSALEMEQERQQQAQVKDQEQVPLLWFRMPTTQNQDATEEKTLEDLRVEAKLRAFERQVIAELRMLQKIELMAKQMRSSAAAQNGDSPYRISYPLSRTPIHKITRADIEQALRDDYVRRLVNKEAQRRARNSGINTQKANALKRQAKSQDQTLSKEDIVQIMAYAYRMANEQMESEKGKQDKVYAAYRTEQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQQNQQQIQQNPMMVQQRQWSEEQAKIQQNQQQIQQNPMMMQQRQWSEEQAKIQHDQQMAQQMAQQGLMMTEQRQRQWSEDQAKIQQAQQMAQQTPMMMPQMQQRQWTEDPQMVQQMQQRQWAEDQTRMQMAQQNPMMQQQRQMAENPQMMQQRQWSEEQTKIEQAQQMAQQNQMMMQQMQQRQWSEDQAQIQQQQRQMMQQTPMMMKERQWAEENPQSVQQQGPMMMQQQMPSMMQREVEDEDNKAEDDLVGEAGPQMPENEGTARHKVDALGVGGNKRKKSKSKSAPPTVINYYYAAPQRPVVQSYGTSYGGGGYGSNAYGVPRPVNSYQSQGYRAAVGNDEVDEMLRQHQTMARATHFRQ
Protein: Nuclear transcription factor Y subunit C-3 (AtNF-YC-3) (Q9ZVL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Nuclear transcription factor Y subunit B-2
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit B-6
- Nuclear transcription factor Y subunit A-2
- Nuclear transcription factor Y subunit B-1
- Nuclear transcription factor Y subunit A-4
- Nuclear transcription factor Y subunit A-1
- Nuclear transcription factor Y subunit B-9
- Nuclear transcription factor Y subunit A-6
- Nuclear transcription factor Y subunit A-3
Sequence:
MDQQGQSSAMNYGSNPYQTNAMTTTPTGSDHPAYHQIHQQQQQQLTQQLQSFWETQFKEIEKTTDFKNHSLPLARIKKIMKADEDVRMISAEAPVVFARACEMFILELTLRSWNHTEENKRRTLQKNDIAAAVTRTDIFDFLVDIVPREDLRDEVLGGVGAEAATAAGYPYGYLPPGTAPIGNPGMVMGNPGAYPPNPYMGQPMWQQPGPEQQDPDN
Protein: POU domain, class 2, transcription factor 2 (Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2) (Octamer-binding protein 2) (Oct-2) (Octamer-binding transcription factor 2) (OTF-2) (Q00196)
Organism: Mus musculus (Mouse)
Function: Transcription factor that specifically binds to the octamer motif (5'-ATTTGCAT-3'). Regulates IL6 expression in B cells with POU2AF1. Regulates transcription in a number of tissues in addition to activating immunoglobulin gene expression. Modulates transcription transactivation by NR3C1, AR and PGR.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17285328}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:17285328}. Note=In alveolus epithelial cells of mammary glands, present in the nucleus and cytoplasm. In HC11 mammary epithelial cells, present in the nucleus and preinuclear regions.
Interaction partners:
- POU domain, class 2, transcription factor 3
- POU domain class 2-associating factor 1
- POU domain, class 2, transcription factor 1
- Transcription factor Sp1
Sequence:
MVHSSMGAPEIRMSKPLEAEKQSLDSPSEHTDTERNGPDINHQNPQNKASPFSVSPTGPSTKIKAEDPSGDSAPAAPPPPQPAQPHLPQAQLMLTGSQLAGDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQPPKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPTSYSPHLVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGGGGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLSGLNPSAGPGLWWNPAPYQP
Protein: Venom nerve growth factor (v-NGF) (vNGF) [Cleaved into: Truncated venom nerve growth factor] (P25428)
Organism: Macrovipera lebetinus (Levantine viper) (Vipera lebetina)
Function: Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. It stimulates division and differentiation of sympathetic and embryonic sensory neurons as well as basal forebrain cholinergic neurons in the brain. Its relevance in the snake venom is not clear. However, it has been shown to inhibit metalloproteinase-dependent proteolysis of platelet glycoprotein Ib alpha, suggesting a metalloproteinase inhibition to prevent metalloprotease autodigestion and/or protection against prey proteases (By similarity). Binds a lipid between the two protein chains in the homodimer. The lipid-bound form promotes histamine relase from mouse mast cells, contrary to the lipid-free form (By similarity). It promotes neurite outgrowth in rat PC12 pheochromocytoma cells.
Subcellular location: Secreted {ECO:0000269|PubMed:19463841}.
Interaction partners:
Sequence:
MSMLCYTLIIAFLIGIWAAPKSEDNVSLGSPATPDLSDTSCAKTHEALKTSRNTDQHYPAPKKAEDQEFGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVEFLDNADSLNRNIRAKRATHPVHNRGEFSVCDSVSVWVANKTTATDIRGNVVTVMVDVKLNNNVYRQYFFETKCKNPSPVSSGCRGIDAKHWNSYCTTTDTFVRALTMEGNQASWRFIRIDTACVCVISRKNDNFG
Protein: 3beta-hydroxysteroid dehydrogenase/Delta(5)-Delta(4) isomerase 1 (HSD-1) (EC 1.1.1.145) (EC 5.3.3.1) (3beta_HSD domain-containing protein 1) (Q9XWF0)
Organism: Caenorhabditis elegans
Function: Hydroxysteroid dehydrogenase involved in the biosynthesis of dafrachonic acids. Catalyzes the dehydrogenation of cholesterol or its derivatives and the isomerization of the double carbon bond on the sterol ring. Modifies sterols into a Delta(4)-3-keto-sterols such as cholest-4-en-3-one, precursor of Delta(4)-dafachronic acid. Contributes to the production of Delta(7)-dafachronic acid in the XXX cells. Dafachronic acids act as ligands and bind directly to the nuclear hormone receptor (NHR) daf-12 suppressing dauer formation and inducing reproductive growth. Acts in parallel to AKT-1 to promote reproductive development via DAF-16/FoxO and DAF-12.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sterol 4-C-methyltransferase strm-1
- 3beta-hydroxysteroid dehydrogenase dhs-16
- Cholesterol 7-desaturase
- 3-ketosteroid oxygenase
- Ubiquitin-like domain-containing protein
- NADPH--cytochrome P450 reductase
- Alkylglycerol monooxygenase
- 7-dehydrocholesterol reductase
- Sigma non-opioid intracellular receptor 1
- Probable ergosterol biosynthetic protein 28 homolog
Sequence:
MSIKRLSMRLKKGIHRSWNRMTSLEAGLEEEKEIKIVEEPEPRPWKVLITGGAGHLAENLVAKLEEMTRDSIRPKIREMLEKEMPAVISTKVDKEVEKRLPMYIQIVLVDVLEPRGRVLKHHVAFVKCSFDDECTMKTALEQVDTVYHLAAVGMTGQYARDRKACMDINAVGTMNLLIWARNSGVQRFIYTSSVGVVFSGEPMYNATEEVGYPDDFYNYYCESKAHAERIVQKASGHRMRTTVLRFNGIYGPGEKRVTERVVKFMLTGMWIATCKPNGVEAQTQLSSVANCIQGLVKAELALRWSDTPHGQIYNIMDKTPVGTFSFWTPLNIALGFSSSMITVPATPIRLFAYLSQIIADRMRIDPIVSVLEVDLLLVNNTFNIEKAERDLGYEPSVSAIPEIIEHYLHRLPPDVVRPKGRSDFYVKVAVLVLGTILIFVAVFSFTFWMYLIFQRLSRWNPF
Protein: Ras-related protein Rab-5C (EC 3.6.5.2) (P35278)
Organism: Mus musculus (Mouse)
Function: Protein transport. Probably involved in vesicular traffic.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side {ECO:0000250|UniProtKB:P20339}. Early endosome membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}. Melanosome {ECO:0000250|UniProtKB:P51148}.
Interaction partners:
- Rab5 GDP/GTP exchange factor
- Early endosome antigen 1
- Rab GDP dissociation inhibitor alpha
- Rabenosyn-5
- Rab GDP dissociation inhibitor beta
- Ras and Rab interactor 1
- Rab GTPase-binding effector protein 1
- GTPase-activating protein and VPS9 domain-containing protein 1
- Alsin
- Clathrin heavy chain 1
Sequence:
MAGRGGAARPNGPAAGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNTDTFARAKNWVKELQRQASPNIVIALAGNKADLASKRAVEFQEAQAYADDNSLLFMETSAKTAMNVNEIFMAIAKKLPKNEPQNAAGAPGRTRGVDLQESNPASRSQCCSN
Protein: DNA-Binding protein G5P (G5P) (GPV) (Single-stranded DNA-binding protein) (P69543)
Organism: Enterobacteria phage f1 (Bacteriophage f1)
Function: Binds to DNA in a highly cooperative manner without pronounced sequence specificity. During synthesis of the single-stranded (progeny) viral DNA, prevents the conversion into the double-stranded replicative form. G5P is displaced by the capsid protein G8P during phage assembly on the inner bacterial membrane (By similarity).
Interaction partners:
Sequence:
MIKVEIKPSQAQFTTRSGVSRQGKPYSLNEQLCYVDLGNEYPVLVKITLDEGQPAYAPGLYTVHLSSFKVGQFGSLMIDRLRLVPAK
Protein: 5' exonuclease Apollo (EC 3.1.-.-) (Beta-lactamase MBLAC2) (EC 3.5.2.6) (DNA cross-link repair 1B protein) (SNM1 homolog B) (Q8C7W7)
Organism: Mus musculus (Mouse)
Function: 5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint. Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin (By similarity). Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem) (By similarity).
Subcellular location: Chromosome, telomere {ECO:0000269|PubMed:20551906, ECO:0000269|PubMed:20619712}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome.
Interaction partners:
- Telomeric repeat-binding factor 2
- Structure-specific endonuclease subunit SLX4
- Structure-specific endonuclease subunit MUS81
- Fanconi anemia group M protein homolog
- Structure-specific endonuclease subunit SLX1
- DNA excision repair protein ERCC-1
- Fanconi anemia group D2 protein homolog
- Fanconi anemia group I protein homolog
- Structure-specific endonuclease subunit EME1
- TERF1-interacting nuclear factor 2
Sequence:
MNGVVIPQTPIAVDFWSLRRAGSARLFFLTHMHCDHTVGLSSTWARPLYCSPITACLLHRRLQVSKHWIRALEVGESHVLPLDEIGQETMTVTLIDANHCPGSVMFLFEGYFGTILYTGDFRYTPSMLKEPALILGKQIHTLYLDNTNCNPALVLPSRQEATQQIVQLIRQFPQHNIKIGLYSLGKESLLEQLALEFRTWVVLSPQRLELVQLLGLADVFTVEEEAGRIHAVDHTEICHSAMLQWNQSHPTIAIFPTSRKVRSPHPSIYTVPYSDHSSYSELRAFVAALRPCQVVPIVHQKPCGEFFQDSLSPRLAMPLIPHSVQQYMSSSSRKTNVLWQLERRLKRPRTQGVVFESPEEKANQVKVDRDSKKHKKENLSPWAGHLERLCPHPLQARKQLFPDFCRKERDEPVLFCDSNKMATVLTAPLEFSVQLQPIDEFLFPETREKIGLESPLLSRGDSGSPARGNQSDCVGCGSPPAHISRAVPLTPESRGLALKYLLTPVHFLQAGFSSRNFDKQVEKHQRVQRSSPAVLSPVDVG