wanglab/gogpt-training-data huggingface dataset:
Protein: Fibrinogen gamma chain (Q8VCM7)
Organism: Mus musculus (Mouse)
Function: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix (By similarity). Fibrin has a major function in hemostasis as one of the primary components of blood clots (By similarity). In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (By similarity). Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (By similarity). Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy (By similarity). Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (By similarity). May also facilitate the immune response via both innate and T-cell mediated pathways (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02679}.
Interaction partners:
- Fibrinogen alpha chain
- Fibrinogen beta chain
- Prothrombin
- Alpha-2-antiplasmin
- Antithrombin-III
- Integrin beta-3
- Fibronectin
- Alpha-2-HS-glycoprotein
- Integrin alpha-IIb
- Coagulation factor XIII B chain
Sequence:
MSWSLQPPSFLLCCLLLLFSPTGLAYVATRDNCCILDERFGSFCPTTCGIADFLSSYQTDVDNDLRTLEDILFRAENRTTEAKELIKAIQVYYNPDQPPKPGMIDSATQKSKKMVEEIVKYEALLLTHETSIRYLQEIYNSNNQKITNLKQKVAQLEAQCQEPCKDSVQIHDTTGKDCQEIANKGAKESGLYFIRPLKAKQQFLVYCEIDGSGNGWTVLQKRIDGSLDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWNGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYHQGGTYSKSSTTNGFDDGIIWATWKSRWYSMKETTMKIIPFNRLSIGEGQQHHMGGSKQAGDV
Protein: Ras association domain family member 1 (Q5FAQ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Serine/threonine-protein kinase 4
- Serine/threonine-protein kinase 3
- Ras association domain-containing protein 5
- GTPase NRas
- GTPase HRas
- G1/S-specific cyclin-D1
- Ras-related protein R-Ras
- TIAM Rac1 associated GEF 1
- RAS related 2
- Ras-related protein M-Ras
Sequence:
MSAEPELIELRELAPSGRIGPGRTRLERANALRIAPGTTRNPSQQHVPGRGHRFQPAGPTTHTWCDLCGDFIWGVVRKGLQCAHCKFTCHYRCRALVCLDCCGPRDLGWDPALERDTNVDEAVERETPDLSQAETEQKIKDYNGQINSNLFMSLNKDGSYTGFIKVQLKLVRPVSVPSSKKPPSLQDARRGTGRSSAVKRRTSFYLPKDAVKHLHVLSRTRAREVIEALLRKFMVVDDPRKFALFERTERHGQIYFRKLSDEEQPLKLRLLAGPSEKALSFVLKENDSGEVNWDAFSMPELHNFLRILQREEEEHLRQILQKYSRCRQKIQEALHACPLG
Protein: NAD-capped RNA hydrolase NUDT12 (DeNADding enzyme NUDT12) (EC 3.6.1.-) (NADH pyrophosphatase NUDT12) (EC 3.6.1.22) (Nucleoside diphosphate-linked moiety X motif 12) (Nudix motif 12) (Q9BQG2)
Organism: Homo sapiens (Human)
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to nutrient stress. Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle. Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12790796}. Peroxisome {ECO:0000269|PubMed:12790796}. Cytoplasmic granule {ECO:0000269|PubMed:31875550}. Note=Localizes to cytoplasmic granules in the presence of BLMH. {ECO:0000269|PubMed:31875550}.
Interaction partners:
- Glutamine-dependent NAD
- 5'-nucleotidase
- 5'
- 5'
- NAD-dependent protein deacetylase sirtuin-2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinate phosphoribosyltransferase
- NAD kinase 2, mitochondrial
- Nicotinamide riboside kinase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
Sequence:
MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPEIVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENYFSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLNYTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKRLCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPGETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDARWFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL
Protein: NK2 homeobox 4b (Transcription factor Nkx2-4c) (Q58A09)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSLSPKHSTPFSVTDILSPIEETYRKFGGMDSTGNLASSLGAYRQTQVSQPGIQQHAMCHNTGVGSTYHMPHSVSQFSSAIGGYCNGSIGNMGDLPSYQDTMRNGAAATAWYSANTEPRYPTISRFMGATTGMNMTGMGTLAGMDATKSMVTLHSAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKANQQIQQENGSVCSQQQSPRRVAVPVLVKDGKPCQNGSSITTSGQQQVQQQQNASGGAMTASGSAVVNHHNQQVNNPLSSEELEEMSPSSPILHSQINMAQTDAALLEYTNNMVSSNLLYGRTW
Protein: Small toxic polypeptide LdrD (Q6BF25)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system. Overexpression causes rapid cell killing and nucleoid condensation of the host cell. Overexpression induces stress-response and a number of membrane protein genes. May inhibit ATP synthesis due to its insertion in the cell inner membrane (By similarity).
Subcellular location: Cell inner membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Small toxic protein ShoB
- Small toxic protein TisB
- Small toxic polypeptide LdrA
- Toxic protein SymE
- Uncharacterized protein DinQ
- Small toxic polypeptide LdrB
Sequence:
MTFAELGMAFWHDLAAPVIAGILASMIVNWLNKRK
Protein: tRNA-specific adenosine deaminase 1 (EC 3.5.4.34) (tRNA-specific adenosine-37 deaminase) (P53065)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Deaminates adenosine-37 to inosine in tRNA-Ala.
Interaction partners:
- tRNA-specific adenosine deaminase subunit TAD2
- tRNA-specific adenosine deaminase subunit TAD3
- Bifunctional protein RIB2
- SUMO-conjugating enzyme UBC9
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- Cytidine deaminase
- Cytosine deaminase
- Adenine deaminase
- tRNA
- tRNA
Sequence:
MVSCQGTRPCIVNLLTMPSEDKLGEEISTRVINEYSKLKSACRPIIRPSGIREWTILAGVAAINRDGGANKIEILSIATGVKALPDSELQRSEGKILHDCHAEILALRGANTVLLNRIQNYNPSSGDKFIQHNDEIPARFNLKENWELALYISRLPCGDASMSFLNDNCKNDDFIKIEDSDEFQYVDRSVKTILRGRLNFNRRNVVRTKPGRYDSNITLSKSCSDKLLMKQRSSVLNCLNYELFEKPVFLKYIVIPNLEDETKHHLEQSFHTRLPNLDNEIKFLNCLKPFYDDKLDEEDVPGLMCSVKLFMDDFSTEEAILNGVRNGFYTKSSKPLRKHCQSQVSRFAQWELFKKIRPEYEGISYLEFKSRQKKRSQLIIAIKNILSPDGWIPTRTDDVK
Protein: Forkhead box protein R2 (Forkhead box protein N6) (Q6PJQ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Myc proto-oncogene protein
- E1A-binding protein p400
- Histone acetyltransferase KAT5
- MRG/MORF4L-binding protein
- Transformation/transcription domain-associated protein
- Enhancer of polycomb homolog 2
- Vacuolar protein sorting-associated protein 72 homolog
- Enhancer of polycomb homolog 1
- Bromodomain-containing protein 8
- Inhibitor of growth protein 3
Sequence:
MDLKLKDCEFWYSLHGQVPGLLDWDMRNELFLPCTTDQCSLAEQILAKYRVGVMKPPEMPQKRRPSPDGDGPPCEPNLWMWVDPNILCPLGSQEAPKPSGKEDLTNISPFPQPPQKDEGSNCSEDKVVESLPSSSSEQSPLQKQGIHSPSDFELTEEEAEEPDDNSLQSPEMKCYQSQKLWQINNQEKSWQRPPLNCSHLIALALRNNPHCGLSVQEIYNFTRQHFPFFWTAPDGWKSTIHYNLCFLDSFEKVPDSLKDEDNARPRSCLWKLTKEGHRRFWEETRVLAFAQRERIQECMSQPELLTSLFDL
Protein: Ubiquitin-like domain-containing protein (Q583M0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSETIPVSVQCCEGRFELSVDSNHTLRDVLRQFKREVAALDPINLEEYVVNHEGKLLLDDSVTLQTVGVKKDSVFVLVRKACCPAASPEKDEDDM
Protein: AT10229p (Ahuizotl) (GEO08584p1) (Q7K049)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neither inactivation nor afterpotential protein C
- Inactivation-no-after-potential D protein
- Kinase
- Calcium/calmodulin-dependent protein kinase type II alpha chain
- Nuclear factor of activated T-cells 5
- Inositol 1,4,5-trisphosphate receptor
- Transient-receptor-potential-like protein
- Calcium/calmodulin-dependent protein kinase type 1
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1
- Peptidyl-prolyl cis-trans isomerase Fkbp12
Sequence:
MEDISHEERVLILDTFRILDKDNEGAITSKEMAVVIRALGRQPNDAEVQSMINEVDSEGNGSIVAPEFCNVILRKMRDTNHEDELREAFRIFDKDNNGYITTTELKNVFTALGVKLSDDELEEMIREYDLDQDNHLNYEEFVNMMTMR
Protein: Tropomyosin (PoTRO) (allergen Pso o 10.0101) (Q3BJY7)
Organism: Psoroptes ovis (Sheep scab mite)
Function: Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
Interaction partners:
Sequence:
MEAIKKKMQAMKLEKDNAIDRAEIAEQKARDANLRAEKSEEEVRGLQKKIQQIENELDQVQEQLSAANTKLEEKKKALQTAEGDVAALNRRIQLIEEDLERSEERLKIATAKLEEASQSADESERMRKMLEHRSITDEERMDGLENQLKEARMMAEDADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAQQREEAHEQQIRIMTAKLKEAEARAEFAERSVQKLQKEVDRLEDELVHEKEKYKSISDELDQTFAELTGY
Protein: EG:86E4.3 protein (O46092)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSPRCLLVGHSAPVLCLVRASLLPENNFLVSSSENGEMCTWDLTDGKCMEAVKLPQVHTQIQSYHTANSEDVRLFCIGYYAEIMVMDPFSLEVIYVLSSKVKPDWISAIHVLRPMRRKDDVVLAITTTGTVKVWTLTGNENKHAEPIYENESKEIRCLNAITMNCCAQNQRTVLLVCTKYWQIYDAGDFTVLCSVIAPARERWQGGDFITSDRVMLWTDEGKGYLYKLPANCIPDNKEFHSKSVVRDAPYLYYVLQHAGDKVLSCPPAMKLLQGAGGQHNLLRGDSEGYISVWNVPEVPLDNISILQAKQMPPRPLKPHVCTSLVEAWSIMDPPPVGILDQLSRITESPVKLTSSIYLPQQSRLVIGREDGSIVIVPATQTVMMQLLVGIKQNFSDWPSHQILYGHRGRVNCLLCPSMIHSRYEKSHLLSGGIDFAVCLWDLYSGSLLHRFCVHAGEITQLLVPPESCSPRILKCICSVASDHSVTLVSLQERKCVTLASRHLFPVVTIKWAPLDDFLIVGCSDGSVYVWQMETGHLDRVLHGMLAEEVLSACDEQAEDGGSGGGGGSNGASASEMGMANPAVHFFRGLKSRNMNAIRHATQRGITQLQQLQGHNQGNFDFLMKHRSNPLVIQGLRTNPKDAESHILFFDIEGLIFELHSEEYAQMTPATLESLGVHLQNPKDGKSMHLDASKKIGDFFNKVKNKAVDVEKILKDKDKHGLVQKFKEKTEIVEKKVQAKVESLQKAVEPHEEQQDLKSKIASKMEVTHVMEVAQLLLSLLHSWGLDPHLDKMCETRLGLLRPIVPISYGVLSKAGYMSLLLPTWQNNYAIPPGIQLPSSSKKRPLPEELQRLEHLTAVFTSRLHWELSTTLTTNHILALVAMSNTLLSMSAASFLPDSEKHKKLQRLAQRTDSTLSNEEEREELMAHHISQIKHAWSLLATHHCFLLPDKIEALEPKKFKRPQVEMMVKRWQHHCIEIREAAQQILLGELTRMGKKGRKQLVESWAQYLPLYTHTEPIVGAQQQLALISQPASGGAGSGSGGNGGVGVGVSGGGGAGSGSGPGGSVPGGDAHQDEDYEEEEEEIIRKPSSLSELKRKQTTAVILLGVIGAEFGQDISQESPNHRGSISMATGANLTSGVAGGERRKSSVVEGFGIANNLARLTSMALAHLLYAPPSPKLPQYTPLRRAAIDLLGRGFTVWEPYLDVSKVLLGLLEISCEGKAVPNLNYKLPLTPQADACRTARHALRLIATARPAAFITTMAREVARYNTMQQNAQSINTPLTQSVLHKAKGEILQCVEMLIDKMQSEIAGLLVEVMDIALHCVDGNELKNRGLAELCPAICKFNQISHCAQTRRIAVGANSGNLAIYELRQNKCQMIPAHTHPITSLAFSPDGKYLVSYSCAENRLSFWQTSTGMFGLGQSQTRCTKGYSTAPIPDVSRLNPMRLAKLVWINNRTVTLMLADGSETRFNV
Protein: Golgi complex-localized glycoprotein 1, isoform A (LD19434p) (Q9VP27)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLHVLFSVLLMATANTAADTLQRSRRVAIDVDNAKDMHSIIDLAECQDLKKLCAHHKSTDNLSMLECALTFSSSQLMDLPEGCQNALWMQQRQLQLPAWLESTFLPAYCPAERPKLESCLNAVHLWSCLEQQRLKLLQNNACHQHLRRAYESLGQDYSAVDEFYTACGPLVEENKCGRLNVDHLPSVLSQLTTVQCLQESATKTGIEPVCQAAINSIELFRVCQEDFSSFCSQEKSGTAAGYKCLVRHKNHPSMSSQCSARITLRDQQIGRDYRVSHGLAKACKDDIKLYHCRRGVSEDKHVRLAQILLCLESVSKNGTKLAPPCLTELTDHRRMLMTDYQLSPELLNDCADDIPKFCPDEHKAQLVNGMTSTGGEIIHCLLEHVKARRPQRRVTAQCQRGLETLIKASDAGEDWRVDPVLRRACKPVVDVVCRDVQGGEARVMGCLMEHIGTPVMLPDCEQALLIIEYFVARDFKLDPQLYKHCRDDAVKYCRAKKQWDDAQNIQMDPERGPMILPCLHRMAFSEDEHQTLRKDCFQEVKRVMRQRAISMDLIPEVEDYCLNDLSAFCADCTEKGSEMECLQKNMDQLQPECKTVVVKYTEEEAAHVELNPVIMNVCGEAMQQHCSAILKSGKDNGDMMDCLIAHKNDADLRKDLRCRAAIEHFQIISLKSFHFTTKFKEACRPYVQRFCSSSATKNEVVACLSEVMRNDTIKAQRHQIPKECRHQVKAQLYQQRESIQLDPKLANACKRELEQFCEEEKGPGQALECLIRKTHSLGKPCHHAIFMVKKSELGDSGTDYTLLTTCKEMIYKFCPSTDSSKLLDCLKTYKDDTQFDQRCHLVVVNRMIEQNTDFRFNPSLQSACGKNIDRYCSNIVASALPNEELNGKVIHCLKDKFRQSALDEPCAKEMIKILQEQALNYKLNPLLQVFCKSEIQELCKANVDSDEHGQLAECLKTAFLQKQIINRQCQMEVATLIAEAKADIHVDPILETACTVDLLRYCSKVAAGNGRKLNCLRTLLKDTPNSLEADCREKLQRRIEMFRNADDTLALPPEDVQQLVQQVVASPARKFFLVILMSATGLVFLTGIFLGRATKRAMGLKNK
Protein: GRCD4 protein (D2T2F8)
Organism: Gerbera hybrida (Daisy)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGRVELKRIENKINRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSNRGKLYEFCSSSSMVKTLEKYHSCSYGSLKASQPENESQYNYHEYLRLKARVEVLQRSQRNLLGEDLAPLNTKELEQLEHQLEMSLRKIRSTKTQSMLDQLADLQRKEQVLAETNKALRKKLEESAQEYPVRQMWEGGAQTIPYNPLPTHSDEFFQPLGLNSTMHNSFNGLRYNPIVSDEMNVAGANNNSPNGLFPGWML
Protein: Methionine synthase reductase (MSR) (EC 1.16.1.8) (Aquacobalamin reductase) (AqCbl reductase) (Q9UBK8)
Organism: Homo sapiens (Human)
Function: Key enzyme in methionine and folate homeostasis responsible for the reactivation of methionine synthase (MTR/MS) activity by catalyzing the reductive methylation of MTR-bound cob(II)alamin. Cobalamin (vitamin B12) forms a complex with MTR to serve as an intermediary in methyl transfer reactions that cycles between MTR-bound methylcob(III)alamin and MTR bound-cob(I)alamin forms, and occasional oxidative escape of the cob(I)alamin intermediate during the catalytic cycle leads to the inactive cob(II)alamin species (Probable). The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine. Also necessary for the utilization of methyl groups from the folate cycle, thereby affecting transgenerational epigenetic inheritance (By similarity). Also acts as a molecular chaperone for methionine synthase by stabilizing apoMTR and incorporating methylcob(III)alamin into apoMTR to form the holoenzyme. Also serves as an aquacob(III)alamin reductase by reducing aquacob(III)alamin to cob(II)alamin; this reduction leads to stimulation of the conversion of apoMTR and aquacob(III)alamin to MTR holoenzyme.
Subcellular location: [Isoform B]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm {ECO:0000269|PubMed:18221906}.
Interaction partners:
- Methionine synthase
- Methylenetetrahydrofolate reductase
- Cobalamin trafficking protein CblD
- Cystathionine beta-synthase
- Cystathionine beta-synthase-like protein
- Lysosomal cobalamin transport escort protein LMBD1
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, cytosolic
- Cytochrome P450 4F8
- Methylmalonic aciduria type A protein, mitochondrial
Sequence:
MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPVFQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSGKALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS
Protein: Bacteriocin carnobacteriocin B2 (Carnocin CP52) (P38580)
Organism: Carnobacterium maltaromaticum (Carnobacterium piscicola)
Function: Has antibacterial activity against Listeria and Enterococcus.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MNSVKELNVKEMKQLHGGVNYGNGVSCSKTKCSVNWGQAFQERYTAGINSFVSGVASGAGSIGRRP
Protein: Uncharacterized protein (Q584W1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSNDPQFATVTILIRNADEVTLRVPIKEDITVRRLAKEAMQRLLARLQGKQELTRETISVVEIYVNTASGKAEIFAQDLVSQVVAVKEEVIHMRLHVKENDNCVTAPDADSSLSNAAVATTSVVDSSEASSRVDEGASPKTAENLQSTRKKECNNETTGADRTPRISCRNLNTTIAGVKRHASFVEGENKDDNRKRKDRTKVGEAASEKGGSDVNGSGPLKLHTTPSTVVVKKIVGKEKHKKEKRTAGKVRKPAASAKVLPIEGCREALRGGRELRLQKRWQGHGTEVKIAVSDRLGWGREASKYFPENYTTSPDKIPRLIREAKRREQMRLKEERGRANQPVEVHNVSEAEGRRSGTTETQVAAKTPQDPSTSAAPFLGEKNSDAGRQSGEGCSATCPIVVERQLFNDGDDLLHTPVSQLAHNENRSDEVKTEGKELSNQSGGTPLPPGWGKSAIKYFDAKTYCDDPTKAKLSPDILAMPLRAGLRRSCL
Protein: SWR complex protein 2 (Q9P790)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Participates in the catalytic exchange of histone H2A for the H2A variant pht1, an euchromatin-specific factor, leading to chromatin remodeling and changes in transcription of targeted genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SWR1-complex protein 5
- SWR1 complex subunit vps71
- SWR1-complex protein 4
- Protein AF-9 homolog
- Helicase swr1
- Histone H2A.Z
- RuvB-like helicase 1
- RuvB-like helicase 2
- Actin-like protein arp6
- Actin-related protein 4
Sequence:
MSATESLVAGRTRRANAGNKMRELLEKEHLRMTQQNAEIEKEDEEYNIEEEEEAERDIEISSESSDEEAELKKLEEEGEEVEKILRDEERIKKRKIQKNRAANLQRTLQPPKRPTPSAASEVPKKKYKKIKVDPSARRTSSRMHTVLMAQSTETRLQEAKPRRKYTVSASANRQKGTMTQQQRFEEAAKTEAQNLSSLRNYVHLEEQRRLRLKRNAAKHRQLREPILKFISKTISTEDGREASNYYVAPLEHPLCHSAPPLQMPQHRAVECVITGKPAIYLDPVTQLPISNVQAFQQVREVYNQRYSWSAMLNLFH
Protein: Aminoacylase-1B (ACY-1B) (EC 3.5.1.14) (ACY IB) (N-acyl-L-amino-acid amidohydrolase) (Q6PTT0)
Organism: Rattus norvegicus (Rat)
Function: Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYTRGAQDMKCVSIQYLEAVKRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRHEFHALRAGFALDEGLANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEEQLQSWCQEAGEGVTFEFAQKFTEPRMTPTDDTDPWWAAFSGACKEMTLTLEPEIFPAATDSRYIRAVGIPALGFSPMNRTPVLLHDHNERLHEAVFLRGVDIYTRLVAALASVPALPGES
Protein: Intraflagellar transport protein 57 homolog (HIP1-interacting protein) (Q8BXG3)
Organism: Mus musculus (Mouse)
Function: Required for the formation of cilia. Plays an indirect role in sonic hedgehog signaling, cilia being required for all activity of the hedgehog pathway. Has pro-apoptotic function via its interaction with HIP1, leading to recruit caspase-8 (CASP8) and trigger apoptosis. Has the ability to bind DNA sequence motif 5'-AAAGACATG-3' present in the promoter of caspase genes such as CASP1, CASP8 and CASP10, suggesting that it may act as a transcription regulator; however the relevance of such function remains unclear.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:31637240}. Cytoplasm, cytoskeleton, cilium basal body. Golgi apparatus. Note=Concentrates within the inner segment of cilia.
Interaction partners:
- Intraflagellar transport protein 80 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 20 homolog
- Intraflagellar transport protein 27 homolog
- Intraflagellar transport protein 74 homolog
Sequence:
MAAAAAVIPPSGLDDGVSRARGEGAGEAVVERGPGAAYHMFVVMEDLVEKLKLLRYEEELLRKSNLKPPSRHYFALPTNPGEQFYMFCTLAAWLINKTGRAFEQPQEYDDPNATISNILSELRSFGRTADFPPSKLKSGYGEQVCYVLDCLAEEALKYIGFTWKRPSYPVEELEEETVPEDDAELTLSKVDEEFVEEETDNEENFIDLNVLKAQTYRLDTNESAKQEDILESTTDAAEWSLEVERVLPQLKVTIRTDNKDWRIHVDQMHQHKSGIESALKETKGFLDKLHNEISRTLEKIGSREKYINNQLEHLVQEYRGAQAQLSEARERYQQGNGGVTERTRLLSEVTEELEKVKQEMEEKGSSMTDGTPLVKIKQSLTKLKQETVQMDIRIGVVEHTLLQSKLKEKCNMTRDMHAAVTPESAIGFY
Protein: Antitoxin Rv0298 (P9WJ09)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin Rv0299.
Interaction partners:
- Toxin Rv0299
- Putative ribonuclease VapC50
- Putative antitoxin VapB50
- Putative ribonuclease VapC45
- Putative antitoxin VapB48
- Toxin RelK
Sequence:
MTKEKISVTVDAAVLAAIDADARAAGLNRSEMIEQALRNEHLRVALRDYTAKTVPALDIDAYAQRVYQANRAAGS
Protein: Argonaute protein (Argonaute-1, isoform B) (SD07515p) (Q7KY08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYPVGQQSQWTPSPTRPQSPSQAQTSFDTLTSPPAPGSSVNPTAVTSPSAQNVAAGGATVAGAAATAAQVASALGATTGSVTPAIATATPATQPDMPVFTCPRRPNLGREGRPIVLRANHFQVTMPRGYVHHYDINIQPDKCPRKVNREIIETMVHAYSKIFGVLKPVFDGRNNLYTRDPLPIGNERLELEVTLPGEGKDRIFRVTIKWQAQVSLFNLEEALEGRTRQIPYDAILALDVVMRHLPSMTYTPVGRSFFSSPEGYYHPLGGGREVWFGFHQSVRPSQWKMMLNIDVSATAFYKAQPVIDFMCEVLDIRDINEQRKPLTDSQRVKFTKEIKGLKIEITHCGQMRRKYRVCNVTRRPAQMQSFPLQLENGQTVECTVAKYFLDKYRMKLRYPHLPCLQVGQEHKHTYLPLEVCNIVAGQRCIKKLTDMQTSTMIKATARSAPDREREINNLVKRADFNNDSYVQEFGLTISNSMMEVRGRVLPPPKLQYGGRVSTGLTGQQLFPPQNKVSLASPNQGVWDMRGKQFFTGVEIRIWAIACFAPQRTVREDALRNFTQQLQKISNDAGMPIIGQPCFCKYATGPDQVEPMFRYLKITFPGLQLVVVVLPGKTPVYAEVKRVGDTVLGMATQCVQAKNVNKTSPQTLSNLCLKINVKLGGINSILVPSIRPKVFNEPVIFLGADVTHPPAGDNKKPSIAAVVGSMDAHPSRYAATVRVQQHRQEIIQELSSMVRELLIMFYKSTGGYKPHRIILYRDGVSEGQFPHVLQHELTAIREACIKLEPEYRPGITFIVVQKRHHTRLFCAEKKEQSGKSGNIPAGTTVDVGITHPTEFDFYLCSHQGIQGTSRPSHYHVLWDDNHFDSDELQCLTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVEKEHDSGEGSHQSGCSEDRTPGAMARAITVHADTKKVMYFA
Protein: Beta-amylase 5 (AtBeta-Amy) (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) (Protein REDUCED BETA AMYLASE 1) (P25853)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-amylase activity. Major cytosolic beta-amylase isoform in rosette leaves and inflorescences stems.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8552713}. Note=Present in the continuous phloem cytoplasm.
Interaction partners:
- 4-alpha-glucanotransferase DPE2
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Isoamylase 3, chloroplastic
- alpha-D-xyloside xylohydrolase
- Alpha-amylase 1
- Probable alpha-amylase 2
- Alpha-amylase 3, chloroplastic
- Isoamylase 2, chloroplastic
- Isoamylase 1, chloroplastic
- Alpha-glucan phosphorylase 2, cytosolic
Sequence:
MATNYNEKLLLNYVPVYVMLPLGVVNVENVFADPETLETQLKRLKEEAGVDGVMVDVWWGIIESKGPKQYDWTAYKTLFQLIARLGLKIQAIMSFHQCGGNVGDIVTIPIPQWVRDVGDNDPDIYYTNRKGTRDIEYLSIGVDNLPLFAGRTAVQLYSDYMSSFKENMADLIEAGVIVDIEVGLGPAGELRYPSYPQSQGWVFPGIGEFQCYDKYLKKDFKEAAAKAGHPEWDLPEDAGEYNDKPEETGFFKKDGTYVSEKGKFFMTWYSNKLIFHGDQILGEANKIFAGLKVNLAAKVSGIHWLYNHHSHAAELTAGYYNLFKRDGYRPIARMLSKHYGILNFTCLEMKDTDNTAEALSAPQELVQEVLSKAWKEGIEVAGENALETYGAKGYNQILLNARPNGVNPNGKPKLRMYGFTYLRLSDTVFQENNFELFKKLVRKMHADQDYCGDAAKYGHEIVPLKTSNSQLTLEDIADAAQPSGAFKWDSETDLKVDG
Protein: Uncharacterized GMC-type oxidoreductase Rv1279 (EC 1.1.-.-) (P9WMV5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1278
- Calcineurin-like phosphoesterase domain-containing protein
- Phosphatidylserine decarboxylase proenzyme
- Phospholipase C B
- Phospholipase C C
- Phospholipase C A
- Phospholipase C D
- Cytochrome bc1 complex cytochrome c subunit
- Omega-hydroxy-beta-dihydromenaquinone-9 sulfotransferase Stf3
- Tetratrico peptide repeat group 5 domain-containing protein
Sequence:
MDTQSDYVVVGTGSAGAVVASRLSTDPATTVVALEAGPRDKNRFIGVPAAFSKLFRSEIDWDYLTEPQPELDGREIYWPRGKVLGGSSSMNAMMWVRGFASDYDEWAARAGPRWSYADVLGYFRRIENVTAAWHFVSGDDSGVTGPLHISRQRSPRSVTAAWLAAARECGFAAARPNSPRPEGFCETVVTQRRGARFSTADAYLKPAMRRKNLRVLTGATATRVVIDGDRAVGVEYQSDGQTRIVYARREVVLCAGAVNSPQLLMLSGIGDRDHLAEHDIDTVYHAPEVGCNLLDHLVTVLGFDVEKDSLFAAEKPGQLISYLLRRRGMLTSNVGEAYGFVRSRPELKLPDLELIFAPAPFYDEALVPPAGHGVVFGPILVAPQSRGQITLRSADPHAKPVIEPRYLSDLGGVDRAAMMAGLRICARIAQARPLRDLLGSIARPRNSTELDEATLELALATCSHTLYHPMGTCRMGSDEASVVDPQLRVRGVDGLRVADASVMPSTVRGHTHAPSVLIGEKAADLIRS