wanglab/gogpt-training-data huggingface dataset:
Protein: SAR-endolysin (EC 3.2.1.17) (Endolysin) (Gene product 22) (gp22) (Lysis protein) (Lysozyme) (Muramidase) (Q9T1X2)
Organism: Escherichia phage Mu (Bacteriophage Mu)
Function: Signal-arrest-release (SAR) endolysin with lysozyme activity that degrades host peptidoglycans and participates with the releasin and spanin proteins in the sequential events which lead to programmed host cell lysis releasing the mature viral particles. The SAR-endolysin is released by the releasin protein into the periplasm, where it breaks down the peptidoglycan layer.
Subcellular location: Host cell inner membrane {ECO:0000255|HAMAP-Rule:MF_04136}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04136}; Periplasmic side {ECO:0000255|HAMAP-Rule:MF_04136}. Note=Secreted as a signal-anchored, membrane-tethered, inactive endolysin which is subsequently refolded, activated and released by membrane depolarization driven by the pinholin. {ECO:0000255|HAMAP-Rule:MF_04136}.
Interaction partners:
Sequence:
MAGIPKKLKAALLAVTIAGGGVGGYQEMTRQSLIHLENIAYMPYRDIAGVLTVCVGHTGPDIEMRRYSHAECMALLDSDLKPVYAAIDRLVRVPLTPYQKTALATFIFNTGVTAFSKSTLLKKLNAGDYAGARDQMARWVFAAGHKWKGLMNRREVEMAIWNIRGADDLRQ
Protein: Nodal homolog 2-A (Nodal-related protein 2-A) (Xnr-2-A) (Xnr2-A) (nr-2) (Q91620)
Organism: Xenopus laevis (African clawed frog)
Function: Cooperation and regulatory loops of multiple nodals are essential for mesendoderm patterning in early embryos. Essential for mesoderm formation and axial patterning during embryonic development. Activates the activin-like signaling pathway to induce dorsal and ventral mesoderm in animal cap ectoderm. In addition, also dorsalizes ventral marginal zone (VMZ) tissues during gastrulation. Induces muscle actin. Appears to act as both a short-range and long-range morphogen. The unprocessed protein inhibits bmp- and wnt-signaling.
Subcellular location: Secreted {ECO:0000269|PubMed:12070085, ECO:0000269|PubMed:15530392}.
Interaction partners:
Sequence:
MASLGVILFFVIASLIHGKPIHSERKAAKIPLEGSNLGYKKPNNIYGSRLSQGMRYPPSMMQLYQTLILGNDTDLSILEYPVLQESDAVLSLIAKSCVVVGNRWTLSFDMSSISSSNELKLAELRIRLPSFERSQDVTVEIYHTKEGQENLFMGSFKTNPSVAMGSSWKIFNLTRMLQYYLHQGEPFTNVEYIEVKNMHERAKPHVIKRGVRAEVEEGLQRNKDNTPASSFPTERVVLVVFTRDKPTASHFGSPSLIHTVESSKYVMSENTVRVTDTRRPRRNQKTKNTIVMNTIPSRSVGKTLCRRVDMIVDFEKIEWGDRIVYPKRFNAYRCEGACPIPLNETFKPTNHAYIKSLVKLYDQEKVECSSCVPVKMSPLSMLLYEDGEVVLKHHEDMIVDECGCN
Protein: Probable chromosome partitioning protein ParA (Q1LVD4)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable chromosome-partitioning protein ParB
- Ribosomal RNA small subunit methyltransferase G
- Probable DNA-3-methyladenine glycosylase I TagA
- Conserved protein similar to jag protein
- Membrane protein insertase YidC
- DNA topoisomerase 1
- Chromosomal replication initiator protein DnaA
Sequence:
MSAPWGPVAAGPSALVRSGQASTIEPFQREMTPPTPTPEAAHNPTMNVSRETSTEFDTPIGAAAERAMRVLHTTHEPLQRPGRRRVLTIANQKGGVGKTTTAVNIAAALAVQGLKTLVIDLDPQGNASTALGITDRQSGTPSSYEMLIGEVSLHTALRRSPHSERLFCIPATIDLAGAEIELVSMVARENRLRTALAALDNFDFDYVFVDCPPSLGLLTINALVAAPEVMIPIQCEYYALEGVSQLMRNIEMVKAHLNPQLEVTTVILTMYDGRTKLADQVADEVRQYFGSKVLRTVIPRSVKVSEAPGYSMTIIDYDPGSRGAMSYLDASRELAERDRPPSAKGRP
Protein: 40S ribosomal protein S24 (Q38AM9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribosomal protein L37
- 40S ribosomal protein S5, putative
- 60S ribosomal subunit protein L31, putative
- Ribosomal protein
- Large ribosomal subunit protein uL5
- 60S ribosomal protein L35A, putative
- 60S ribosomal protein L2, putative
- 40S ribosomal protein S15a, putative
- 40S ribosomal protein S4
- 40S ribosomal protein S27, putative
Sequence:
MVFQKKKAEVTVRTSQFKVNKLLNRKQFVVEVNHPGWCGTVPAKLIRNRLASLYKVADENQISVFGFKTKFGGGKTTGFGLIYDDLAAMKRIEPNYRKARLGMGKKKLPARKSVKERRNRNKKIRGKAKGKMQTKKK
Protein: Stathmin (Q4VBT7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAKTAIAYKEKMKELSLVSLICSCLYPEARKNIMGEFEDMEVKAINKRASGQAFEVILKPPSPTTEGGYSITSPPKKRDMSLEDIQKKLEAAEDRRRSQEAQVLKALAEKREHERDVLLKAMEENSNFSRMAEEKLILKMEQIKENRDAHLAAMMDRLHEKEKHAQLVRRNKELREELTA
Protein: Matrix metalloproteinase-28 (MMP-28) (EC 3.4.24.-) (Epilysin) (Q9H239)
Organism: Homo sapiens (Human)
Function: Can degrade casein. Could play a role in tissues homeostasis and repair.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Hemopexin
- Furin
Sequence:
MVARVGLLLRALQLLLWGHLDAQPAERGGQELRKEAEAFLEKYGYLNEQVPKAPTSTRFSDAIRAFQWVSQLPVSGVLDRATLRQMTRPRCGVTDTNSYAAWAERISDLFARHRTKMRRKKRFAKQGNKWYKQHLSYRLVNWPEHLPEPAVRGAVRAAFQLWSNVSALEFWEAPATGPADIRLTFFQGDHNDGLGNAFDGPGGALAHAFLPRRGEAHFDQDERWSLSRRRGRNLFVVLAHEIGHTLGLTHSPAPRALMAPYYKRLGRDALLSWDDVLAVQSLYGKPLGGSVAVQLPGKLFTDFETWDSYSPQGRRPETQGPKYCHSSFDAITVDRQQQLYIFKGSHFWEVAADGNVSEPRPLQERWVGLPPNIEAAAVSLNDGDFYFFKGGRCWRFRGPKPVWGLPQLCRAGGLPRHPDAALFFPPLRRLILFKGARYYVLARGGLQVEPYYPRSLQDWGGIPEEVSGALPRPDGSIIFFRDDRYWRLDQAKLQATTSGRWATELPWMGCWHANSGSALF
Protein: Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCH-L1) (EC 3.4.19.12) (Neuron cytoplasmic protein 9.5) (PGP 9.5) (PGP9.5) (Ubiquitin thioesterase L1) (P09936)
Organism: Homo sapiens (Human)
Function: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins (Probable). This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes (By similarity). The homodimer may have ATP-independent ubiquitin ligase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19261853}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19261853}; Lipid-anchor {ECO:0000269|PubMed:19261853}. Note=About 30% of total UCHL1 is associated with membranes in brain. Localizes near and/or within mitochondria to potentially interact with mitochondrial proteins. {ECO:0000250|UniProtKB:Q9R0P9}.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- E3 ubiquitin-protein ligase parkin
- Alpha-synuclein
- Heat shock cognate 71 kDa protein
- Heat shock protein HSP 90-alpha
- Parkinson disease protein 7
- Leucine-rich repeat serine/threonine-protein kinase 2
Sequence:
MQLKPMEINPEMLNKVLSRLGVAGQWRFVDVLGLEEESLGSVPAPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLGFEDGSVLKQFLSETEKMSPEDRAKCFEKNEAIQAAHDAVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAAKVCREFTEREQGEVRFSAVALCKAA
Protein: Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (Q53XC0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, Stress granule {ECO:0000256|ARBA:ARBA00004210}.
Interaction partners:
Sequence:
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEVDGDDDAEEMEAKAED
Protein: glutamine--fructose-6-phosphate transaminase (isomerizing) (EC 2.6.1.16) (Q3S344)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Glucosamine 6-phosphate N-acetyltransferase
- N-acetylglucosamine-6-phosphate deacetylase
- Glucose-6-phosphate isomerase
- Glucose-6-phosphate isomerase
- Phosphoribosylglycinamide formyltransferase.
- Glutamine synthetase
- Glutamine synthetase
- Glutamine synthetase
- Glucosamine-6-phosphate isomerase
- Glucosamine-6-phosphate isomerase.
Sequence:
MCGIFAYLNYHVPHTRREILEVLIKGLRRLEYRGYDSAGVGIDGGNSKDWESNSKCIHLIKQTGKVQALDEEIQRQQDIDLDVEFDVHLGIAHTRWATHGVPSPVNSHPQRSDKTNEFIVIHNGIITNYKDLKKFLESKNYEFESETDTETIAKLVKYMYDNRESNDITFATLVEQVTQQLEGAFALVFKSVHFPGQAVGSRRGGPLLIGVRSDHRLSTDHIPILYRSSGKDKKTCNTLPRMDEDTCLFPVDEKAVEYYFASDASAVIEHTNRVIFLEDDDIAAVSDGRLSIHRIKRTAGDHPARAIQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRGRVNFENNTVILGGLKDHIKEIQRCRRLIMIACGTSYHAGVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKERGALTVGITNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFVALVMFALLMCDDRISVQPRRKEIIQGLRILPDLIKEVLTLDEEIQKLAAELYPQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLALVDKLMPVIMIIMRDHTYTKCQNALQQVVARQGRPIVICDKEDNETINNSKRTIKVPHCVDCLQGILSVIPLQLLSFHLAVLRGYDVDCPRNLAKSVTVE
Protein: Tropomodulin, isoform D (Tropomodulin, isoform E) (Tropomodulin, isoform F) (Tropomodulin, isoform I) (Tropomodulin, isoform L) (Q9VA59)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSDIEDVFGGSAEETKPEPDAQSKTSVVTEHTEEVIPGETEKMVTETIDEDGDVVEETTEVTRKTVKRTMKITETSATTKTTTLTTPAKLYGKDLSEYDDVDVESLLAQLSPEEITILAKEVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQPEFEPFVQGKVRGKKWVPPPRDARDIEAEEQIAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQDQYHASLLNKGQPVGLGWDGITKSTQQKLFPMDPPNNTDVEESIKRVKDDDSKLIDLNLNNIKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFRASNQRSAVLGNKIEMEITDLVEKNSSLLRLGLHLEFNDARHRVAAHLQRNIDRIRVKRLNQRK
Protein: Actin-related protein 3 (Q59Z11)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 5
- Arp2/3 complex 34 kDa subunit
- Actin-related protein 2/3 complex subunit
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 4
- Actin-binding protein
- Actin
- SPIN90/Ldb17 leucine-rich domain-containing protein
- Centractin
Sequence:
MSMNTPAVVMDNGTGLTKLGFAGNDSPSFVFPTAIATSSASSKAGKGPRGSSLASKRGLEDLDFYIGDEALEAASGSQYGLHYPIKHGQIEDWDQMERFWESSIFKYLRCEPEDHYFLLTEPPLNPPENRESTAEIMFESFNCAGLYIAVQAVLALAASWTSPKVQDRSLSGTVIDSGDGVTHVIPVAEGYVIGAAIKNIPLAGRDITLFIQQLLRDRGEADTSLQTAEKIKQEFCYVCPDIVQEFSRFDQYPQEKFAQYMVEYTDKNKRNTVDVGYERFLAPEIFFNPEICSSDFLTPLPTVVDQVIQASPIDVRKKLYKNIVLSGGSTMFKDFGKRLQRDLKSIVSERIQLSERLSGSQSTGVDVQVISHKKQRNAVWFGGSLLAQTSEFKSYCYTKSDYDEYGPSIVRNFSLFSVP
Protein: GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC 2.4.1.131) (Asparagine-linked glycosylation protein 11 homolog) (Glycolipid 2-alpha-mannosyltransferase) (Q2TAA5)
Organism: Homo sapiens (Human)
Function: Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol-linked oligosaccharide chain.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20080937}; Single-pass membrane protein {ECO:0000250|UniProtKB:P53954}.
Interaction partners:
- Dol-P-Man:Man
- Alpha-1,3/1,6-mannosyltransferase ALG2
- Man
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Phosphomannomutase 2
- UDP-N-acetylglucosamine transferase subunit ALG13
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Man:Man
Sequence:
MAAGERSWCLCKLLRFFYSLFFPGLIVCGTLCVCLVIVLWGIRLLLQRKKKLVSTSKNGKNQMVIAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDVNVNGQQILEGAFRRFNIRLIHPVQFVFLRKRYLVEDSLYPHFTLLGQSLGSIFLGWEALMQCVPDVYIDSMGYAFTLPLFKYIGGCQVGSYVHYPTISTDMLSVVKNQNIGFNNAAFITRNPFLSKVKLIYYYLFAFIYGLVGSCSDVVMVNSSWTLNHILSLWKVGNCTNIVYPPCDVQTFLDIPLHEKKMTPGHLLVSVGQFRPEKNHPLQIRAFAKLLNKKMVESPPSLKLVLIGGCRNKDDELRVNQLRRLSEDLGVQEYVEFKINIPFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIVVPHEGDITGFLAESEEDYAETIAHILSMSAEKRLQIRKSARASVSRFSDQEFEVTFLSSVEKLFK
Protein: Protein lin-52 homolog (Q52LA3)
Organism: Homo sapiens (Human)
Interaction partners:
- Myb-related protein B
- Histone-binding protein RBBP4
- Protein lin-54 homolog
- Protein lin-9 homolog
- Protein lin-37 homolog
- Retinoblastoma-like protein 2
- Retinoblastoma-like protein 1
- Dual specificity tyrosine-phosphorylation-regulated kinase 1A
- Transcription factor E2F4
- Myb-related protein A
Sequence:
MGWKMASPTDGTDLEASLLSFEKLDRASPDLWPEQLPGVAEFAASFKSPITSSPPKWMAEIERDDIDMLKELGSLTTANLMEKVRGLQNLAYQLGLDESREMTRGKFLNILEKPKK
Protein: Slingshot protein phosphatase 2 (A0A8I6APG2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTLSTLADERKAPPASTCSLGGPDMIPYFSANAVISQNAINQLISESFLTVKGAALFLPRGNGSSTPRISHRRNKHAGDLQQHLQAMFILLRPEDNIRLAVRLESTYQNRTRYMVVVSTNGRQDTEESIVLGMDFSSNDSSTCTMGLVLPLWSDTLIHLDGDGGFSVSTDNRVHIFKPVSVQAMWSALQSLHKACEVARMHNYYPGSLFLTWVSYYESHINSDQSSVNEWNAMQDVQSHRPDSPALFTDIEFKTVLKTQRDLTEINSASSPFQIRTELEMQMVCNLREFKEFIDNEMIVILGQMDSPTQIFEHVFLGSEWNASNLEDLQNRGVRYILNVTREIDNFFPGVFEYHNIRVYDEEATDLLAYWNDTYKFISKAKKHGSKCLVHCKMGVSRSASTVIAYAMKEYGWNLDRAYEYVKERRTVTKPNPSFMRQLEEYQGILLASKQRHNKLWRSHSDSDLSDHHEPICKPGLELNKKEMTTSADQITEVKTVESLAAMPPVFMEHVVPQDVNQKGLRTKERVICLEFSSQEFHAGQIEDELNLNDINGCSSGCCLSESKFPLDNCHASKALLQPGQAPDIANKFPDLAVEDLETDALKADVRVHLLPMEELTSRLKDLPMSPDLESPSPQAGCQAAISDFSTDRIDFFSALEKFVELSQETRSRSFSHSRIEELGGGRSEGCRLSVMEMAPSEMVTDDQRSSSLSDTPHASEESSVDEDQPKAVSELVSPDIIMQSHSENAISVKEIVTEIESISQGVGQVQLKGDILSNPCHTPKKNIIHELPLERVQGPENKPGHLEQDESFCSVQLELARDSGKCAPEEGCLATLSSTGDLEEEEPVEGEHDWGPGTHPGAKWCPGSVRRATLEFEERLRQEQENHGTASPGPTLSNRKNSKNDSSVADLMPKWKSDETASEHSLSPKEAEPGKGKGKCSGSEAGPLSHCEHNPAAAAPQLLEHHPSPAPQDCLGSESRSEKQEEDLRKQRTVVSNQECETQAALLPLPKKIEIIEYTPTVTSLDHTEPGGETTPSKESEKQELRKVKMERSITMFCTLDENLNRTLDPSQVSLRPQVLPLPHSSSEYDRLTDPTPMLSSPQDKGDSPSTPFKTPARLVGCSTQGASVSLDCSHRHSVLHLEGCTEQSSTTDSRLSSEHMNWEDSQGDFLSSSTGMAHTSSPLTNEDLSLINKLGDSVGVLPKKLDPSPEACRIPHSSSSENIRDLSHGPGVVKEHAKEIEPRVIFQAAFSKTSQMRRSASLAKLGYLDLCKDYLPDRELGSSESPHLKLLQPFLRTDSGMHALMVHEPSESPGAHPNPQPTKYFVEQLKTTECVVQSKPVERPHVQYAKEFGFSQQCLLPKARPELTSSEGGLPLLQTQGLQYPGPSPGLAVAPRQQHGRTHPLRRLKRANDKKRTTNPFYNTM
Protein: Kinetochore-associated protein DSN1 (P40568)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as essential component of the kinetochore MIND complex, which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with the kinetochore.
Interaction partners:
- Kinetochore-associated protein MTW1
- Kinetochore-associated protein NSL1
- Kinetochore-associated protein NNF1
- Kinetochore protein SPC24
- Kinetochore protein SPC25
- Outer kinetochore KNL1 complex subunit SPC105
- Monopolin complex subunit CSM1
- Inner kinetochore subunit CTF19
- Kinetochore protein NUF2
- Outer kinetochore KNL1 complex subunit KRE28
Sequence:
MSLEPTQTVSGTPPMLHQRTHKQVYPLRMETIPILESDSKATLQSNEPTQKDEEETEYFENKQSVSNLSPDLKFKRHKNKHIQGFPTLGERLDNLQDIKKAKRVENFNSSAPIADDNHSGDATANATANATANATANVNASAMPAPYMPYYYYYHPMNAPTPAMIPYPGSPMHSIMPNSSLQPFYSQPTAAGGPDMTTPQNISSSQQLLPAPQLFPYGSFHQQQLQQPHYIQRTRERKKSIGSQRGRRLSMLASQANGGSTIISPHKDIPEEDFYTVVGNASFGKNLQIRQLFNWCLMRSLHKLELKAKNQEEEGELEHLTKKSKLESTKAETDYVDPKRLAMVIIKEFVDDLKKDHIAIDWEDEEKYEDEDEEKILDNTENYDDTELRQLFQENDDDDDDDDEVDYSEIQRSRRKFSERRKALPKEPKKLLPNSKNVENTKNLSILTSKVNAIKNEVKEWAVTLDTSRPDLEWQELTSFSSQPLEPLSDTEEPDLAIADVETKLETKVDELRYQSHILNSHSLALNEITNSKVNKLNIETMRKISSETDDDHSQVINPQQLLKGLSLSFSKKLDL
Protein: Nicotinate phosphoribosyltransferase pncB2 (NAPRTase pncB2) (EC 6.3.4.21) (P9WJI7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the Preiss-Handler pathway, which is a recycling route that permits the salvage of free nicotinamide (NM) and nicotinic acid (Na) involved in the NAD biosynthesis. Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. It is not able to use nicotinamide. PncB2 appears to be responsible for the increased salvage synthesis of NAD during infection of host tissues.
Interaction partners:
- Nicotinamidase/pyrazinamidase
- Probable polyglutamine synthesis accessory protein Rv0574c
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- CinA-like protein
- Probable nicotinate-nucleotide adenylyltransferase
- Possible transcriptional regulatory protein NadR
- NAD-capped RNA hydrolase NudC
- Nicotinate phosphoribosyltransferase pncB1
- Purine nucleoside phosphorylase
- Probable cation-transporting ATPase F
Sequence:
MAIRQHVGALFTDLYEVTMAQAYWAERMSGTAVFEIFFRKLPPGRSYIMAAGLADVVEFLEAFRFDEQDLRYLRGLGQFSDEFLRWLAGVRFTGDVWAAPEGTVIFPNEPAVQLIAPIIEAQLVETFVLNQIHLQSVLASKAARVVAAARGRPVVDFGARRAHGTDAACKVARTSYLAGAAGTSNLLAARQYGIPTFGTMAHSFVQAFDSEVAAFEAFARLYPATMLLVDTYDTLRGVDHVIELAKRLGNRFDVRAVRLDSGDLDELSKATRARLDTAGLEQVEIFASSGLDENRIAALLAARCPIDGFGVGTQLVVAQDAPALDMAYKLVAYDGSGRTKFSSGKVIYPGRKQVFRKLEHGVFCGDTLGEHGENLPGDPLLVPIMTNGRRIRQHAPTLDGARDWARQQIDALPPELRSLEDTGYSYPVAVSDRIVGELARLRHADTAEAHPGSNVVGAKAKRP
Protein: BBG-LP12 (Q15K23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
ATINDDYITVVEVDDPTSNPKDRLKKLVKRQSSVAEDSSFITVLTINEMELLQQRKQEKDVGSGSSPTMEEQIENVTVFRLPGERLGFGLKFQGGTRSTELVQKLYIQSCAADSPASKVSTSWGNLREGDEIVSIDGRDVRELTRIDCVRGLKDNVAIKLVVRNGHGQKPPSEEDPQQQEHLSITLNAQPPPPPPVPPRKLVRRQNSKENQAQLLIEKPLTPPPDAEYYLNLLTESIKAGSESDDTASTISTVIDKFSVGSNYSSDSSLNGHELAKVLQPFTLLEQEFLPLEQPLGHPKLLIPGNNYENVEFKTEKVNVYENVELRSPETTPTPKPRVQLATVEPKKRSIIPMPRKIPTPTKLPIEVTPPRVPILEEPKTPTNNKVDSPKTPTNELKESPISATKIPKAKFSRAKTEGEIKLHLPAPKQQSPQSKSRIPIVSTPAAQKTVPKPVSPTLNGTPLSSNIPRXLQKQKSETDLKLNLYRSKSKESSPRPPLQRANSAEAPERTFIPVLLNGNSKSSNSLESVSSIGSSSSGNSVRSPXXXXXXPPERVQSLQKTQIPKLQALPTTPPQQIPKLSMQTFKQSPPTPRSTPVGTPSPTSNREIRFKIQTYESKTQDEDKLPSLFDLVHSQENDKDKDRDSDSLKTHNSITALLAAAAAEAADLSRESPPPLVVGKCMKIVDDTNTTTCYSSSSSGEEDEDDLDASNREYICEDGEKLGPPELINGPGPSEAYFNMFWHSNMLPTIGEVEEEFSSLEPQSLTNGNLVKSEESKKLPKMEVNAGGLAQLTDDKIADHDASATRADTRDEVTTNQTQEISSSSSSSVKSQKTTTTTRVTTTKTSSSSSPSSCSSTVIPDVAFKLQPYEERDDILSEPITTIHEERRVLSEQKTLSESRTRDALTGEEQLVTSANSKSSSARFKKISSNDNLLDLGDEQDMQEQPLTATITQESSLRERLECPQDNQSIERGTLTLSERGKQLSEKEGLTTYTECETSEKESYLEGQQVLNGKGGFVSQDENSDQPTYEREVSETLTIVNDGEKQVTKKLEQNKEIAGKKGAKLLKKTDEERRLEQEAQKLIESYQKVKKEAEKLYKLELADDDQGFDLSAFQQAEEEDKPQVSEEIKEVKDSQPVKVDIQIEEKVKTPNQVIGEVKVEDVXXXIKETVQVSQQEIKKEVKVSHXETKETFESEEKDESNELKIVKEEVKVTHQDLREQIQEIEAVKVVHKEVKVIKESAKVTTTTSHKQATKEVIISKEGDHKNDSGALPAVSTTKVETISPPLEDDLGYVLHKHIILPQEKVKTAPTPLPKPKPKPPVPTNKPKMPVNLTKPKSAPPPVPSKRSELSGSGGKPTPTQRRGSLETAQPPKPLERIIVGVEQRDEPEKPQPIINLASVDLPNVAPNSKQATVETTPVVEMPPDELQFESHQLPDDGEKEKDLHQESNDLLSGSSSSSVTTPITTPILVSATSSMDSVQSVIEVVNGMPIISNQQTDDDDIDEVAAYDDGMHLEAEGTKDVR
Protein: UPF3 domain-containing protein (Q9CS15)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKEEKDHRPKEKRVTLFTPQGATGGCIGATAEGAKGDDRQDRNRDKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDILLFRDRFDGYVFLDNKGQEYHAIVEFAPFQKAAKKKIKKRDTKVGTIEDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKRTTPLLSFLKNKQRMREEKREERRRREIERKRQREEE
Protein: Tumor necrosis factor receptor superfamily member 6 (Apo-1 antigen) (Apoptosis-mediating surface antigen FAS) (FASLG receptor) (F1QG24)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}.
Interaction partners:
- FAS-associated death domain protein
- Tumor necrosis factor ligand superfamily member 6
- Death domain-associated protein 6
- FAS-associated factor 1
- Caspase 10, apoptosis-related cysteine peptidase
- Caspase 8, apoptosis-related cysteine peptidase
- Caspase-8
- Receptor
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Lymphotoxin-alpha
Sequence:
MFVCKFGVFIVFVMPTLTYSWRLRRDASCEFGTYQHERNTCCLCPAGFKVSTHCTNTDKTECKQCEDGYYLNNNNNENQCRPCKICDANAKMKEIEKCSKSSNTVCGCEEGRFCDKDKDCNVCYPCDPCPNGVKEQCTETHNTVCHDAKDLTGTIAAVLVPLILIAVLAFMIFIWKKKKFCFQVRPSTDKVQTEEALPLIDLSPHLPKIADVLCWKTVKEVARRSGMTAKDIEEQEMNHPKDVREQTFGLLEAWSQRQGLDKAYRALITTLQDIGEKATADKIRNIVEASSQP
Protein: Mast cell protease 1-like 3 (A0A0G2K5U4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
PPLPNLVTGDWVFLVPEEIVGGVESIPHSRPYMAHLKITTEKGYVTFCGGFLISRQFVLTAAHCNGREITVTLGAHDVSKRESTQQKLKVEKQIIHKNYNFFSNIHDIMLLKLEKQVELTPAVDVVPLPSPSDFIDPGTMCQAAGWGQTGVTDPTSYTYTLREVELRIMDVEACKIFSDYDYNFQMCVGSPGRMRSPYEGDSGGPLLCAGVAHGIVSHGREDAKPPAVFTRISPYVPWINIVLSASS
Protein: Chemokine-like protein TAFA-5 (Q7Z5A7)
Organism: Homo sapiens (Human)
Function: Acts as a chemokine-like protein by regulating cell proliferation and migration through activation of G protein-coupled receptors (GPCRs), such as S1PR2 and FPR2 (By similarity). Stimulates chemotactic migration of macrophages mediated by the MAPK3/ERK1 and AKT1 pathway (By similarity). Blocks TNFSF11/RANKL-induced osteoclast formation from macrophages by inhibiting up-regulation of osteoclast fusogenic and differentiation genes (By similarity). Stimulation of macrophage migration and inhibition of osteoclast formation is mediated via GPCR FPR2 (By similarity). Acts as an adipokine by negatively regulating vascular smooth muscle cell (VSMC) proliferation and migration in response to platelet-derived growth factor stimulation via GPCR S1PR2 and G protein GNA12/GNA13-transmitted RHOA signaling (By similarity). Inhibits injury-induced cell proliferation and neointima formation in the femoral arteries (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:15028294, ECO:0000269|PubMed:29453251}.
Interaction partners:
Sequence:
MAPSPRTGSRQDATALPSMSSTFWAFMILASLLIAYCSQLAAGTCEIVTLDRDSSQPRRTIARQTARCACRKGQIAGTTRARPACVDARIIKTKQWCDMLPCLEGEGCDLLINRSGWTCTQPGGRIKTTTVS
Protein: Beta-amyrin synthase (AtBAS) (EC 5.4.99.39) (Lupeol synthase 4) (AtLUP4) (B6EXY6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts oxidosqualene to beta-amyrin.
Interaction partners:
- Squalene epoxidase 2, mitochondrial
- Squalene epoxidase 3
- Squalene epoxidase 1
- Squalene epoxidase 4
- Squalene epoxidase 6
- Squalene epoxidase 5
- Hydroxymethylglutaryl-CoA synthase
- Tirucalladienol synthase
- Amyrin synthase LUP2
- Marneral synthase
Sequence:
MWRLKIGEGNGDDPYLFTTNNFAGRQTWEFDPDGGSPEERHSVVEARRIFYDNRFHVKASSDLLWRMQFLREKKFEQRIAPVKVEDSEKVTFETATSALRRGIHFFSALQASDGHWPAENAGPLFFLPPLVFCLYITGHLDEVFTSEHRKEILRYIYCHQKEDGGWGLHIEGHSTMFCTTLNYICMRILGESPDGGHDNACGRAREWILSHGGVTYIPSWGKTWLSILGVFDWSGSNPMPPEFWILPSFFPVHPAKMWSYCRMVYLPMSYLYGKRFVGPITSLILQLRKELYLQPYEEINWMKVRHLCAKEDTYYPRPLVQELVWDSLYIFAEPFLARWPFNKLLREKALQLAMKHIHYEDENSRYITIGCVEKVLCMLACWVEDPNGDYFKKHLSRISDYLWMAEDGMKMQSFGSQLWDTGFAMQALLASNLSSEISDVLRRGHEFIKNSQVGENPSGDYKSMYRHISKGAWTFSDRDHGWQVSDCTAHGLKCCLLFSMLAPDIVGPKQDPERLHDSVNILLSLQSKNGGMTAWEPAGAPKWLELLNPTEMFSDIVIEHEYSECTSSAIQALSLFKQLYPDHRTTEITAFIKKAAEYLENMQTRDGSWYGNWGICFTYGTWFALAGLAAAGKTFNDCEAIRKGVQFLLAAQKDNGGWGESYLSCSKKIYIAQVGEISNVVQTAWALMGLIHSGQAERDPIPLHRAAKLIINSQLESGDFPQQQATGVFLKNCTLHYAAYRNIHPLWALAEYRARVSLP
Protein: AT5G19950 protein (Tudor domain protein (DUF1767)) (Q8L502)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA topoisomerase 3-beta
- DNA topoisomerase 3-alpha
- DNA topoisomerase
- Crossover junction endonuclease MUS81
- Crossover junction endonuclease MUS81
- DNA repair endonuclease UVH1
- ATP-dependent DNA helicase Q-like 4A
- ATP-dependent DNA helicase Q-like 4B
- ATP-dependent DNA helicase Q-like 1
- ATP-dependent DNA helicase Q-like 5
Sequence:
MVGTSSSSAGDHTHTVVINALTSRGWCFRDVEYLKSLVTEISSLIGGGNKTGAIVESVEAELLNMDIKLIGGKSLPDPTELRRCSHLQGPKVLQISYVRDVTRSSAEEFVGSSTGKRVLKFALTDGKTEISALEYSHIPTINNDVTPGTKVRLENKAVIRDGLVCLTPKEVTVLGGYVQSLTEEWQMKKKYASLARSQESKAGDGPPPFEELKIRTGSHHRDYNKTTSRNNVPIAAESSVKHAGGEKGESSEVDGNKRGTNKNIQRNPADSDPKISVEVENQEKRSSSDTRPKQVVEAVPLQNQAAAQILLEKMKHSSSNDRQYQGRRGRGRGRGRGRGREEEDSAVFTLDEWEKRNTGGGALPTANHPSDTTRDEDLAWQLQNQFDLEDSYGQEMPGAGAADIRMNMFDYGRTEDNFGHGRGRGGGRGRGRGRGHRRGRGRV