wanglab/gogpt-training-data huggingface dataset:
Protein: GTP pyrophosphokinase ((p)ppGpp synthase) (ATP:GTP 3'-pyrophosphotransferase) (ppGpp synthase I) (Q9I524)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Nucleoside triphosphate pyrophosphohydrolase
- Exopolyphosphatase
- Nucleoside diphosphate kinase
- guanosine-3',5'-bis
- RNA polymerase sigma factor RpoS
- Adenylate cyclase
- Pyruvate kinase
- Pyruvate kinase
- CyaB
- Class III
Sequence:
MVQVRAHQPVNTDGSINLEAWLDHVQNLVPGLDRQGLLEACEFARESEQRAIAAQNSWAEGTSSFQTGLEIAEILADLKLDQESLVAAVIYRGVREGKITLEAVNKHFGPVVAKLIEGVLRMAAISASLNPRHSMVLGTQAQVENLRKMLVAMVDDVRVALIKLAERTCAIRAVKNADEEKRHRVAREVFDIYAPLAHRLGIGHIKWELEDLSFRYLEPDQYKQIAKLLHERRLDREQYIANVMSQLKEALAATGVQADLSGRAKHIYSIWRKMQRKGLDFSQIYDVRAVRVLVPEMRDCYTALGIVHTLWRHIPKEFDDYIANPKENGYRSLHTAVIGPEGKVLEVQIRTHSMHEEAELGVCAHWRYKGTDVKASSNHYEEKISWLRQVLEWHEELGDIGGLAEQLRVDIEPDRVYVFTPDGHAIDLPKGATPLDFAYRVHTEVGHNCRGAKINGRIVPLNYSLQTGEQVEIITGKHSGPSRDWLNSNLGYVTTSRARAKIVHWFKLQARDQNVAAGKALIERELSRLALPPVDFDRLAEKANVRTAEDMFAALGAGDLRLAHLVNYAQQLVEPDRDSEQLELIPRKPSKIGHGKRGDVQIQGVGNLLTQMAGCCQPLPGDPIVGYITLGRGVTIHRQDCATALQLAGREPERMIQVSWGPEPVRTYPVDIAIRAYDRSGLLRDVSQVLLNERINVLAVNTRSNKEDNTATMQLTIEIPGLDALGRLLARVSQLPNIIEARRNRTP
Protein: Monoacylglycerol lipase ABHD6 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 6) (Q9BV23)
Organism: Homo sapiens (Human)
Function: Lipase that preferentially hydrolysis medium-chain saturated monoacylglycerols including 2-arachidonoylglycerol. Through 2-arachidonoylglycerol degradation may regulate endocannabinoid signaling pathways (By similarity). Also has a lysophosphatidyl lipase activity with a preference for lysophosphatidylglycerol among other lysophospholipids (By similarity). Also able to degrade bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme for BMP catabolism. BMP, also known as lysobisphosphatidic acid, is enriched in late endosomes and lysosomes and plays a key role in the formation of intraluminal vesicles and in lipid sorting.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Lysophosphatidylserine lipase ABHD12
- Monoglyceride lipase
- Fatty-acid amide hydrolase 1
- Diacylglycerol lipase-alpha
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Diacylglycerol lipase-beta
- 
- G-protein coupled receptor 55
Sequence:
MDLDVVNMFVIAGGTLAIPILAFVASFLLWPSALIRIYYWYWRRTLGMQVRYVHHEDYQFCYSFRGRPGHKPSILMLHGFSAHKDMWLSVVKFLPKNLHLVCVDMPGHEGTTRSSLDDLSIDGQVKRIHQFVECLKLNKKPFHLVGTSMGGQVAGVYAAYYPSDVSSLCLVCPAGLQYSTDNQFVQRLKELQGSAAVEKIPLIPSTPEEMSEMLQLCSYVRFKVPQQILQGLVDVRIPHNNFYRKLFLEIVSEKSRYSLHQNMDKIKVPTQIIWGKQDQVLDVSGADMLAKSIANCQVELLENCGHSVVMERPRKTAKLIIDFLASVHNTDNNKKLD
Protein: 5-keto-4-deoxy-D-glucarate aldolase (KDGluc aldolase) (KDGlucA) (EC 4.1.2.20) (2-dehydro-3-deoxy-D-glucarate aldolase) (2-keto-3-deoxy-D-glucarate aldolase) (5-dehydro-4-deoxy-D-glucarate aldolase) (Alpha-keto-beta-deoxy-D-glucarate aldolase) (P23522)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde.
Interaction partners:
- 2-hydroxy-3-oxopropionate reductase
- Galactarate dehydratase
- Probable galactarate/D-glucarate transporter GarP
- Glucarate dehydratase
- 2-hydroxy-3-oxopropionate reductase
- Probable galactarate/D-glucarate transporter GudP
- Glyoxylate carboligase
- Hydroxypyruvate isomerase
- Glycerate 2-kinase
- Glucarate dehydratase-related protein
Sequence:
MNNDVFPNKFKAALAAKQVQIGCWSALSNPISTEVLGLAGFDWLVLDGEHAPNDISTFIPQLMALKGSASAPVVRVPTNEPVIIKRLLDIGFYNFLIPFVETKEEAELAVASTRYPPEGIRGVSVSHRANMFGTVADYFAQSNKNITILVQIESQQGVDNVDAIAATEGVDGIFVGPSDLAAALGHLGNASHPDVQKAIQHIFNRASAHGKPSGILAPVEADARRYLEWGATFVAVGSDLGVFRSATQKLADTFKK
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 1 (Protein acetyltransferase BLOC1S1) (A0A8I5ZSQ1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLSRLLKEHQAKQNERKELQEKRRREAITAATCLTEALVDHLNVGVAQAYMNQRKLDHEVKTLQVQAAQFAKQTGQWIGMVENFNQALKGSLVW
Protein: Myotubularin-related protein 11 (Cisplatin resistance-associated protein) (hCRA) (Inactive phosphatidylinositol 3-phosphatase 11) (A4FU01)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWWGGRGQSFNIAPQKEEPEMGSVQENRMPEPRSRQPSSCLASRCLPGEQILAWAPGVRKGLEPELSGTLICTNFRVTFQPCGWQWNQDTPLNSEYDFALVNIGRLEAVSGLSRVQLLRPGSLHKFIPEEILIHGRDFRLLRVGFEAGGLEPQAFQVTMAIVQARAQSNQAQQYSGITLSKAGQGSGSRKPPIPLMETAEDWETERKKQAARGWRVSTVNERFDVATSLPRYFWVPNRILDSEVRRAFGHFHQGRGPRLSWHHPGGSDLLRCGGFYTASDPNKEDIRAVELMLQAGHSDVVLVDTMDELPSLADVQLAHLRLRALCLPDSSVAEDKWLSALEGTRWLDYVRACLRKASDISVLVTSRVRSVILQERGDRDLNGLLSSLVQLLSAPEARTLFGFQSLVQREWVAAGHPFLTRLGGTGASEEAPVFLLFLDCVWQLLQQFPADFEFSEFFLLALHDSVRVPDTLTFLRNTPWERGKQSGQLNSYTQVYTPGYSQPPAGNSFNLQLSVWDWDLRYSNAQILQFQNPGYDPEHCPDSWLPRPQPSFMVPGPPSSVWLFSRGALTPLNQLCPWRDSPSLLAVSSRWLPRPAISSESLADQEWGLPSHWGACPLPPGLLLPGYLGPQIRLWRRCYLRGRPEVQMGLSAPTISGLQDELSHLQELLRKWTPRISPEDHSKKRDPHTILNPTEIAGILKGRAEGDLG
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (Complex I subunit B13) (Complex I-13kD-B) (CI-13kD-B) (NADH-ubiquinone oxidoreductase 13 kDa-B subunit) (Q16718)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase flavoprotein 3, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Cytochrome b-c1 complex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
Sequence:
MAGVLKKTTGLVGLAVCNTPHERLRILYTKILDVLEEIPKNAAYRKYTEQITNEKLAMVKAEPDVKKLEDQLQGGQLEEVILQAEHELNLARKMREWKLWEPLVEEPPADQWKWPI
Protein: Protein UshA [Includes: UDP-sugar hydrolase (EC 3.6.1.45) (UDP-sugar diphosphatase) (UDP-sugar pyrophosphatase); 5'-nucleotidase (5'-NT) (EC 3.1.3.5)] (P07024)
Organism: Escherichia coli (strain K12)
Function: Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.
Subcellular location: Periplasm. Note=Exported from the cell, except a small proportion that is internally localized.
Interaction partners:
- 5'/3'-nucleotidase SurE
- 5'-deoxynucleotidase YfbR
- Uridine kinase
- Pyrimidine 5'-nucleotidase YjjG
- Thymidine kinase
- 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
- GMP/IMP nucleotidase YrfG
- Thymidine phosphorylase
- Adenosine deaminase
- Trifunctional NAD biosynthesis/regulator protein NadR
Sequence:
MKLLQRGVALALLTTFTLASETALAYEQDKTYKITVLHTNDHHGHFWRNEYGEYGLAAQKTLVDGIRKEVAAEGGSVLLLSGGDINTGVPESDLQDAEPDFRGMNLVGYDAMAIGNHEFDNPLTVLRQQEKWAKFPLLSANIYQKSTGERLFKPWALFKRQDLKIAVIGLTTDDTAKIGNPEYFTDIEFRKPADEAKLVIQELQQTEKPDIIIAATHMGHYDNGEHGSNAPGDVEMARALPAGSLAMIVGGHSQDPVCMAAENKKQVDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADFEFRNGEMKMVNYQLIPVNLKKKVTWEDGKSERVLYTPEIAENQQMISLLSPFQNKGKAQLEVKIGETNGRLEGDRDKVRFVQTNMGRLILAAQMDRTGADFAVMSGGGIRDSIEAGDISYKNVLKVQPFGNVVVYADMTGKEVIDYLTAVAQMKPDSGAYPQFANVSFVAKDGKLNDLKIKGEPVDPAKTYRMATLNFNATGGDGYPRLDNKPGYVNTGFIDAEVLKAYIQKSSPLDVSVYEPKGEVSWQ
Protein: Double-strand break repair protein (F8W7U8)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR000882}.
Interaction partners:
Sequence:
MSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTLDEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVNFGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVEKIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNRSKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAVKKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKIEEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFRHREQKEKTGEEINFGKLITKPSEGTTLRVEDLVKQYFQTAEKNVQLSLLTERGMGEAVQEFVDKEEKDAIEELVKYQLEKTQRFLKERHIDALEDKIDEEVRRFRETRQKNTNEEDDEVREAMTRARALRSQSEESASAFSADDLMSIDLAEQMANDSDDSISAATNKGRGRGRGRRGGRGQNSASRGGSQRGRDTGLETSTRSRNSKTAVSASRNMSIIDAFKSTRQQPSRNVTTKNYSEVIEVDESDVEEDIFPTTSKTDQRWSSTSSSKIMSQSQVSKGVDFESSEDDDDDPFMNTSSLRRNRR
Protein: Vacuolar ATPase assembly integral membrane protein VPH2 (Protein VMA12) (P32341)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vacuolar ATPase assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9325326}; Multi-pass membrane protein {ECO:0000269|PubMed:9325326}.
Interaction partners:
- Vacuolar ATPase assembly protein VMA22
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit d
- V-type proton ATPase subunit F
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit c
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit e
- Vacuolar ATPase assembly integral membrane protein VMA21
- V0 assembly protein 1
Sequence:
MFEIKLNDRITEFLRKFKNSAKSNEGIDEDIDLFLKRHAIPMQSLLFYVKEYRKDSDLQCSIKELLKPLEFEFKPKAVRGLHYSEDFKKKLEFLKYQEQELEYQSMVKRSKSVFSLQEDDELTPSQINKQIKEQVTTVFNVLVSVISVVVAIWYWTGSSTNFPVHVRLLLCLFFGILVLVADVVVYNSYLKKLEEAKVKEKTKVEKKKVLSKITL
Protein: AT5g08500/MAH20_6 (Transmembrane CLPTM1 family protein) (Q8VZJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Non-race specific disease resistance protein
- Nuclear pore complex protein GP210
- Uncharacterized GPI-anchored protein At1g61900
- Pyridoxal 5'-phosphate synthase subunit PDX1.1
- Ribonuclease H2 subunit A
Sequence:
MAPPAGQTAAVAEAAGADGAPPQQQRGFGSTISGIVRIAVFWYFASKFFSPKQKPMDPTAPSQLMTNLFHKGESLDMWFYLSEQEKFNDFGNDRALYWHETNIPYAVWTPESIRTKSLTYYPSETLQNNGSLYAHIFFARSGFPIDPTDPEYQPLNSFSRTHAVATYFPKQKKNKKKSLLGSPKDSDESEPEVEKVGDKKSDPKEEVPVEWISLWKPNVTINLVDDFTHYSQNGVPPNIAPHLLVEPTTGNYYPTIYFNEFWLLRDKFIPVNETVSELPLNLEISPISMMKWQLFQQVDQSFQMQRSYGSMLDGESDELKKVFLEGNPYLLGITMFVSMLHSVFDFLAFKNDIQFWNKNKSMEGLSAKSVVLNFICQFVIFLYLLDNDTSWMILASSGVGVCIEFWKIGKAMRIEVDRSGMIPRLRFHDRESYASNKTKEYDDIAIKFLSYVLLLLVIGLSIYSLAYERHKSWYSWILSSLTSCVYMFGFIMMCPQLFINYKLKSVAHLPWRQMTYKFLNTIIDDLFAFVIKMPILHRLSVFRDDVIFLIYLYQRWVYPVDKTRVNEFGFGGEDETAEKKLITEKEEEDKKTN
Protein: Vacuolar protein-sorting-associated protein 36 (ESCRT-II complex subunit VPS36) (Q6DDF4)
Organism: Xenopus laevis (African clawed frog)
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.
Subcellular location: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
Interaction partners:
Sequence:
MDRFSWCTGLLDIDETLVIQQRGVRLSDGEEKTKFDSGTLLLTTHRLIWRDQKNHDFCIAFPLSQIVFTEEQAGGIGKSAKIVVHLHPATPNKEPGPYQTSRYSYVKLSFREHGQIEFQRRLAEELTQRRWERLSASASPSMQMNKGPQTGRIKAVGIVGIERKLEEKRKETDKNISEAFEDLSKLMEKAKEMVELSKSIATKIKDKQGDISEDETIRFKSYLLSMGIANPVTRETHGSGTHYHMQLAKQLATMLQAPLEERGGIMSLTEVYCLVNRARGMELLSPEDLVNACKMLESLKLPIRLRVFDSGVMVIEHQSHNEEEMVASALETVSEKGSLTSEEFAKIVGMSVLLAKERLLLAENMGHLCRDDSVEGLRFYPNLFLTQS
Protein: PHD finger protein 1 (Q6MGC9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAQLPRLSRLGAPSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGSSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSKLLSALNSHKDRFISGREIKKRKCLFGLHARTPPPVELLTGDGSPTSFPSGQGPGGGVSRPLGKRRKSEPEPLRRRQKGKVEELGPPTAAHSRHGSQEQRALQASESPPPPSPNQSYQGSSGYNFRPTDARCLPSSPIRMFASFHPSASTAGTSGDSEPPDRSPLELHIGFPTDIPKSSPHSVTASSSSVPALTPGLSRHSLPPSPLCRSLSPGTGGGVRGGVSYLSRGDPVRVLARRVRPDGSVQYLVEWGGGGIF
Protein: Exportin-6 (Exp6) (Ran-binding protein 20) (Q96QU8)
Organism: Homo sapiens (Human)
Function: Mediates the nuclear export of actin and profilin-actin complexes in somatic cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:14592989}. Cytoplasm {ECO:0000269|PubMed:14592989}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:14592989}.
Interaction partners:
- Profilin-1
- Profilin-4
- Profilin-3
- Importin-9
- E3 SUMO-protein ligase RanBP2
- Exportin-7
- Exportin-4
- Exportin-2
- Actin, cytoplasmic 1
- Dynein axonemal assembly factor 5
Sequence:
MASEEASLRALESLMTEFFHDCTTNERKREIEELLNNFAQQIGAWRFCLYFLSSTRNDYVMMYSLTVFENLINKMWLGVPSQDKMEIRSCLPKLLLAHHKTLPYFIRNKLCKVIVDIGRQDWPMFYHDFFTNILQLIQSPVTTPLGLIMLKTTSEELACPREDLSVARKEELRKLLLDQVQTVLGLLTGILETVWDKHSVTAATPPPSPTSGESGDLLSNLLQSPSSAKLLNQPIPILDVESEYICSLALECLAHLFSWIPLSASITPSLLTTIFHFARFGCDIRARKMASVNGSSQNCVSGQERGRLGVLAMSCINELMSKNCVPMEFEEYLLRMFQQTFYLLQKITKDNNAHTVKSRLEELDESYIEKFTDFLRLFVSVHLRRIESYSQFPVVEFLTLLFKYTFHQPTHEGYFSCLDIWTLFLDYLTSKIKSRLGDKEAVLNRYEDALVLLLTEVLNRIQFRYNQAQLEELDDETLDDDQQTEWQRYLRQSLEVVAKVMELLPTHAFSTLFPVLQDNLEVYLGLQQFIVTSGSGHRLNITAENDCRRLHCSLRDLSSLLQAVGRLAEYFIGDVFAARFNDALTVVERLVKVTLYGSQIKLYNIETAVPSVLKPDLIDVHAQSLAALQAYSHWLAQYCSEVHRQNTQQFVTLISTTMDAITPLISTKVQDKLLLSACHLLVSLATTVRPVFLISIPAVQKVFNRITDASALRLVDKAQVLVCRALSNILLLPWPNLPENEQQWPVRSINHASLISALSRDYRNLKPSAVAPQRKMPLDDTKLIIHQTLSVLEDIVENISGESTKSRQICYQSLQESVQVSLALFPAFIHQSDVTDEMLSFFLTLFRGLRVQMGVPFTEQIIQTFLNMFTREQLAESILHEGSTGCRVVEKFLKILQVVVQEPGQVFKPFLPSIIALCMEQVYPIIAERPSPDVKAELFELLFRTLHHNWRYFFKSTVLASVQRGIAEEQMENEPQFSAIMQAFGQSFLQPDIHLFKQNLFYLETLNTKQKLYHKKIFRTAMLFQFVNVLLQVLVHKSHDLLQEEIGIAIYNMASVDFDGFFAAFLPEFLTSCDGVDANQKSVLGRNFKMDRDLPSFTQNVHRLVNDLRYYRLCNDSLPPGTVKL
Protein: Multidrug resistance protein homolog 65 (EC 7.6.2.2) (P-glycoprotein 65) (Q00748)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit alpha
- Sodium/potassium-transporting ATPase subunit beta-1
- G-protein coupled receptor moody
- ABC-type xenobiotic transporter
- Multidrug resistance protein homolog 49
- Uncharacterized protein, isoform A
Sequence:
MERDEVSTSSSEGKSQEEAPMAEGLEPTEPIAFLKLFRFSTYGEIGWLFFGFIMCCIKALTLPAVVIIYSEFTSMLVDRAMQFGTSSNVHALPLFGGGKTLTNASREENNEALYDDSISYGILLTIASVVMFISGIFSVDVFNMVALRQVTRMRIKLFSSVIRQDIGWHDLASKQNFTQSMVDDVEKIRDGISEKVGHFVYLVVGFIITVAISFSYGWKLTLAVSSYIPLVILLNYYVAKFQGKLTAREQESYAGAGNLAEEILSSIRTVVSFGGEKSEVQRYENFLVPARKASQWKGAFSGLSDAVLKSMLYLSCAGAFWYGVNLIIDDRNVENKEYTPAILMIAFFGIIVGADNIARTAPFLESFATARGCATNLFKVIDLTSKIDPLSTDGKLLNYGLRGDVEFQDVFFRYPSRPEVIVHRGLNIRIRAGQTVALVGSSGCGKSTCVQLLQRFYDPVFGSVLLDDLDIRKYNIQWLRSNIAVVGQEPVLFLGTIAQNISYGKPGATQKEIEAAATQAGAHEFITNLPESYRSMIGERGSQLSGGQKQRIAIARALIQNPKILLLDEATSALDYQSEKQVQQALDLASKGRTTIVVSHRLSAIRGADKIVFIHDGKVLEEGSHDDLMALEGAYYNMVRAGDINMPDEVEKEDSIEDTKQKSLALFEKSFETSPLNFEKGQKNSVQFEEPIIKALIKDTNAQSAEAPPEKPNFFRTFSRILQLAKQEWCYLILGTISAVAVGFLYPAFAVIFGEFYAALAEKDPEDALRRTAVLSWACLGLAFLTGLVCFLQTYLFNYAGIWLTTRMRAMTFNAMVNQEVGWFDDENNSVGALSARLSGEAVDIQGAIGYPLSGMIQALSNFISSVSVAMYYNWKLALLCLANCPIIVGSVILEAKMMSNAVVREKQVIEEACRIATESITNIRTVAGLRREADVIREYTEEIQRVEVLIRQKLRWRGVLNSTMQASAFFAYAVALCYGGVLVSEGQLPFQDIIKVSETLLYGSMMLAQSLAFTPAFSAALIAGHRLFQILDRKPKIQSPMGTIKNTLAKQLNLFEGVRYRGIQFRYPTRPDAKILNGLDLEVLKGQTVALVGHSGCGKSTCVQLLQRYYDPDEGTIHIDHDDIQHDLTLDGVRTKLGIVSQEPTLFERSIAENIAYGDNRRSVSMVEIIAAAKSANAHSFIISLPNGYDTRMGARGTQLSGGQKQRIAIARALVRNPKILLLDEATSALDLQSEQLVQQALDTACSGRTCIVIAHRLSTVQNADVICVIQNGQVVEQGNHMQLISQGGIYAKLHKTQKDH
Protein: Checkpoint protein HUS1 (mHUS1) (Q8BQY8)
Organism: Mus musculus (Mouse)
Function: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates. The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O60921}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O60921}. Note=In discrete nuclear foci upon DNA damage. DNA damage induces its nuclear translocation. Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:O60921}.
Interaction partners:
- Cell cycle checkpoint control protein RAD9A
- Cell cycle checkpoint protein RAD1
- Cell cycle checkpoint protein RAD17
- Serine/threonine-protein kinase ATR
- DNA topoisomerase 2-binding protein 1
- Cell cycle checkpoint control protein RAD9B
- Replication factor C subunit 2
- ATR-interacting protein
- Replication factor C subunit 4
- Replication factor C subunit 3
Sequence:
MKFRAKIVDLACLNHFTRVSNMIAKLAKTCTLRISPEKLNFILCDKLASGGVSMWCELEQENFFSEFQMEGVSEENNEIYLELTSENLSRALKTAQNSRALKIKLTNKHFPCLTVSVELVSSSSSSRIVVHDIPIKVLPRRLWKDLQEPSIPDCDVSICLPALKMMKSVVEKMRNISNQLVIEANLKGELNLKIETELVCVTTHFKDLENPLLPSDSVSQNRHPEDMAKVHIDIKKLLQFLAGQQVTPTKAVCNIVNNRTVHFDLLLEDVSLQYFIPALS
Protein: Meiotically up-regulated gene 2 protein (Q9URV3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKKENWQKIENVYLLGKKIDKAKRMANKGESNTNMLSTEENIVKAKAVSRKKPVDVSYAGLARHESHVDTDYHGQALNTDNQDPKNYQARSFVKENELYESSQDCGHSRLAQILSEENQIKRLPQSDNTTTERIIENNPNYSNKPSKLKRALSGENSVFSIHQRNTLSPSSNLPRIPSDLYDIKQFLENLDARSFKSDMDLKRSQNMRRRATGYPAIVVPFLNGSLPQADLPPLRTIEDIDNLTREQCLTFIQGYGIPIDSSDTVYLKEKLRDAIGMRAFTDMSFEMNSFHLESPR
Protein: Histone-lysine N-methyltransferase (EC 2.1.1.355) (B1H256)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009343}.
Interaction partners:
Sequence:
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGVSKKNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSENTWEPRQNLKCVRILKQFHKDLERELVRRHRRSKPPRHLDPNLANYLVQKAKQRRALQRWEQELNAKRSHLGRITVENEVDLDGPPRSFVYINEYRVGEGITLNQVAVGCECQDCLLAPTGGCCPGASLHKFAYNDQGQVRLKAGQPIYECNSRCCCGYDCPNRVVQKGIRYNLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIWAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTTACRKYLF
Protein: Calcitonin gene-related peptide 1 (CGRP1) (Calcitonin gene-related peptide) (CGRP) (P30880)
Organism: Sus scrofa (Pig)
Function: CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P06881}.
Interaction partners:
Sequence:
SCNTATCVTHRLAGLLSRSGGMVKSNFVPTDVGSEAF
Protein: At3g14060 (Q9LVJ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDPHLVITAASSAFRWPSSRRKIYLRRRKPQVVRLGGKNSTPRGSFSLKKVVTRMRLKWLRLYYVRLVKKIKAYYRTIVKEFEEAGAATIQQRMTVETAAFAAPGLGLSFCPMSGYVDQPRFFLV
Protein: 3-hydroxyanthranilate 3,4-dioxygenase (EC 1.13.11.6) (3-hydroxyanthranilate oxygenase) (3-HAO) (3-hydroxyanthranilic acid dioxygenase) (HAD) (Biosynthesis of nicotinic acid protein 1) (P47096)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03019, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Kynurenine 3-monooxygenase
- Kynureninase
- High-affinity nicotinic acid transporter
- Indoleamine 2,3-dioxygenase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Catalase T
- Peroxisomal catalase A
- Uridine nucleosidase
Sequence:
MFNTTPINIDKWLKENEGLLKPPVNNYCLHKGGFTVMIVGGPNERTGYHINPTPEWFYQKKGSMLLKVVDETDAEPKFIDIIINEGDSYLLPGNVPHSPVRFADTVGIVVEQDRPGGENDKIRWYCSHCRQVVHESELQMLDLGTQVKEAILDFENDVEKRTCFHCKTLNYARPQSN
Protein: Glucan endo-1,3-beta-glucosidase GII (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase GII) ((1->3)-beta-glucanase isoenzyme GII) (Beta-1,3-endoglucanase GII) (P15737)
Organism: Hordeum vulgare (Barley)
Function: May provide a degree of protection against microbial invasion of germinated barley grain through its ability to degrade fungal cell wall polysaccharides. Hydrolyzes laminarin in vitro.
Interaction partners:
Sequence:
MARKDVASMFAAALFIGAFAAVPTSVQSIGVCYGVIGNNLPSRSDVVQLYRSKGINGMRIYFADGQALSALRNSGIGLILDIGNDQLANIAASTSNAASWVQNNVRPYYPAVNIKYIAAGNEVQGGATQSILPAMRNLNAALSAAGLGAIKVSTSIRFDEVANSFPPSAGVFKNAYMTDVARLLASTGAPLLANVYPYFAYRDNPGSISLNYATFQPGTTVRDQNNGLTYTSLFDAMVDAVYAALEKAGAPAVKVVVSESGWPSAGGFAASAGNARTYNQGLINHVGGGTPKKREALETYIFAMFNENQKTGDATERSFGLFNPDKSPAYNIQF
Protein: Transcription factor JunB (Transcription factor AP-1 subunit JunB) (P17275)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[GC]TCA-3'. Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to an AP-1 consensus sequence and its transcriptional activity (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor Jun
- Fos-related antigen 1
- Protein FosB
- Transcription factor JunD
- Fos-related antigen 2
- Protein c-Fos
- Basic leucine zipper transcriptional factor ATF-like
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 8
- Early growth response protein 1
Sequence:
MCTKMEQPFYHDDSYTATGYGRAPGGLSLHDYKLLKPSLAVNLADPYRSLKAPGARGPGPEGGGGGSYFSGQGSDTGASLKLASSELERLIVPNSNGVITTTPTPPGQYFYPRGGGSGGGAGGAGGGVTEEQEGFADGFVKALDDLHKMNHVTPPNVSLGATGGPPAGPGGVYAGPEPPPVYTNLSSYSPASASSGGAGAAVGTGSSYPTTTISYLPHAPPFAGGHPAQLGLGRGASTFKEEPQTVPEARSRDATPPVSPINMEDQERIKVERKRLRNRLAATKCRKRKLERIARLEDKVKTLKAENAGLSSTAGLLREQVAQLKQKVMTHVSNGCQLLLGVKGHAF