wanglab/gogpt-training-data huggingface dataset:
Protein: Junction plakoglobin a (Gamma-catenin) (Plakoglobin) (Plakoglobin-1a) (Q9PVF7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, desmosome {ECO:0000269|PubMed:10456847, ECO:0000269|PubMed:18682726}. Cell membrane {ECO:0000269|PubMed:15494018, ECO:0000269|PubMed:26938059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14923}. Cytoplasm {ECO:0000269|PubMed:10456847}. Cell junction {ECO:0000269|PubMed:10456847, ECO:0000269|PubMed:29376824}. Cell junction, adherens junction {ECO:0000269|PubMed:10456847, ECO:0000269|PubMed:18682726, ECO:0000269|PubMed:27760340}. Nucleus {ECO:0000269|PubMed:15494018}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P14923}. Note=Localized in the ooplasm during the initial stages of oogenesis. {ECO:0000269|PubMed:10456847}.
Interaction partners:
Sequence:
MEMHMGEAPGSVKVTEWQQSYYGTDSGIHSGATTVRSDDDGTEYSSKKFTYTTTFTENPAEVESQLNMTRAQRVRAAMFPETVMEGSVIHSTQIDPSQQTNVQKLAEPSQQLKAAIVHLINYQDDAELATRAIPELTKLLNDEDQLVVNKAAMIVNQLTRKEASRRALMQSPQMVAAVVRAMQNTTDMETTRATASILHNLSHQREGLLAIFKSGGIPALVRMLSSPMDSVLFYAITTLHNLLLHQEGAKMAVRLADGLQRMVPLLKKSNPKFLAITTDCLQLLSYGNQESKLIILANGGPEGLVNIMRTYNYEKLLWTTSRVLKVLSVCPSNKPAIVDAGGMQALGKHLSGSSQRLMQNCLWTLRNLSDAATKQDGMENLLQVLVGLLSADDINMLTCATGVLSNLTCNNTRNKTQVTQSNGVEALIHTILRASSKQDVIEPAVCALRHLTSRHPEAETAQNAVRMHYGIPAIVKLLNQPYHWPVVKAVVGLIRNLALCPANQAPLRDADAIPKLVTLLSKAHQDAQKPGSSAQRSYQDGVRMEEIVEGCTGALHIMARDPMNRGTIASMDTIPLFVQLLYSPLDNVKRVAAGVLCELALDKQSAEIIDAEGASAPLMELLHSSNEGIATYAAAVLYRTAEDKNPDYKKRVSVELTHSLFKHDPEAWEMAHNTVMDPVLGDEELDGYGPAGYGGYADGMHMDPLDPEMQDDFRSGMPYNSMARVYHDY
Protein: Protein kinase superfamily protein (F4JPT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAVTSLLDTVFRRRKKKSTEFISYTAVFEFDLDTIKAATNDFSELVGRGGFGFVYKGRLQNGQEIAVKILSTSSIRTERQFHNELIILSKLKHKNLINLLGFCTKRDQHGLVYEFMPNSSLDCFILDPHRAAQLNWEMCRNIIDGIARGLRYLHEESGLWVVHRDIKPGNILLDSDLKPKIVGFELARTMQQGENAAETTEIVGTVGYLDPEYIRSGRVSVKSDVYAFGVTILTIISRRKAWSVDGDSLIKYVRRCWNRGEAIDVIHEVMREEEREYSISEILRYIHIALLCVDENAERRPNIDKVLHWFSCFSTPLPDPTFGNRFLVEEETNWPWSPSLSPGHSSVTSPISSR
Protein: Cystatin cpi-2 (A0A0K0IP23)
Organism: Brugia malayi (Filarial nematode worm)
Function: Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Also acts as an asparaginyl endopeptidase inhibitor. In the human host, inhibits CTSL/cathepsin L, CTSS/cathepsin S, CTSB/cathepsin B and asparaginyl endopeptidase LGMN/AEP which may cause defects in both antigen and MHC class II invariant chain CD74/Ii processing.
Interaction partners:
Sequence:
MMSTMSIKEGLLVILLSLFLFDTTALIHRREIPHMESKGQMQRGQVLLGGWQERSPEDNEILELLPSVLTKVNQQSNDEYHLMPIKLLNVSSQVVAGVKYKMEVQVARSECKKSASEQVNLKTCKKLEGHPDQVMTLEVWEKPWEDFLQVNILETKVLSSV
Protein: Phosphosulfolactate synthase (EC 4.4.1.19) ((2R)-phospho-3-sulfolactate synthase) (PSL synthase) (Q57703)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the addition of sulfite to phosphoenolpyruvate (PEP) to yield (2R)-phospho-3-sulfolactate (PSL).
Interaction partners:
- Uncharacterized protein MJ0120
- Uncharacterized protein MJ0119
- Uncharacterized ABC transporter ATP-binding protein MJ0121
- 2-phosphosulfolactate phosphatase
- L-sulfolactate dehydrogenase
- Uncharacterized protein MJ0664
- Probable hydrogenase maturation factor HypB
Sequence:
MKAFEFLYEDFQRGLTVVLDKGLPPKFVEDYLKVCGDYIDFVKFGWGTSAVIDRDVVKEKINYYKDWGIKVYPGGTLFEYAYSKGKFDEFLNECEKLGFEAVEISDGSSDISLEERKNAIKRAKDNGFMVLTEVGKKMPDKDKQLTIDDRIKLINFDLDAGADYVIIEGRESGKGIGLFDKEGKVKENELDVLAKNVDINKVIFEAPQKSQQVAFILKFGSSVNLANIAFDEVISLETLRRGLRGDTFGKV
Protein: Rubredoxin-NAD(+) reductase (RdxR) (EC 1.18.1.1) (P42454)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.
Subcellular location: Cytoplasm.
Interaction partners:
- Rubredoxin
- Nitrate reductase, large subunit
- EstB protein
- HTH-type transcriptional regulator EstR
Sequence:
MHPIVIIGSGMAGYTLAREFRKLNPEHELVMICADDAVNYAKPTLSNALSGNKAPEQIPLGDAEKMSTQLKLQILSETWVKAINPETHELKLEKNGQETIQPYSKLVLAVGANPTRLAIAGDGSDDIHVVNSLIDYRAFRENLAKRQDKRVVILGAGLIGCEFANDLQHTGHQVTVIDLSPRPLGRLLPAHIADAFQKNLEESGIHFVLSTTVEKVSKINDGQDYAVTLANGQTLVADIVLSAIGLQPNIDLAKHAGVHTSRGILTNSLLETNLEDIYAIGDCAEVNGTLLPYVMPIMQQARALAKTLSGETTHVHYPAMPVAVKTPAAPLTVLPVPVDVDVNWETEEFEDGMLAKAIDNTDTLRGFVLLGATAGKQRLTLTKLVPDLIPAQL
Protein: Homeobox transcription factor phx1 (Q10328)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Trnascription factor that regulates the expression of the homocitrate synthase (HCS) lys4.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Homocitrate synthase, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim22
- Mitochondrial import inner membrane translocase subunit tim9
- Serine/threonine-protein kinase sck2
- Uncharacterized transporter SPBPB10D8.05c
Sequence:
MRSYSNPENGGQINDNINYSEKRPTMLPENLSLSNYDMDSFLGQFPSDNNMQLPHSTYEQHLQGEQQNPTNPNYFPPEFDENKVDWKQEKPKPDAPSFADNNSFDNVNSSKLTNPSPVQPNIVKSESEPANSKQNEVVEATSVEKAKENVAHESGTPESGGSTSAPKSKKQRLTADQLAYLLREFSKDTNPPPAIREKIGRELNIPERSVTIWFQNRRAKSKLISRRQEEERQRILREQRELDSLNQKVSQAFAHEVLSTSPTSPYVGGIAANRQYANTLLPKPTRKTGNFYMKSGPMQSSMEPCIAESDIPIRQSLSSTYYNSLSPNAVPVSSQRKYSASSYSAIPNAMSVSNQAFDVESPPSSYATPLTGIRMPQPESDLYSYPREVSPSSGGYRMFGHSKPSSYKASGPVRPPNMATGHMRTSSEPTSYDSEFYYFSCTLLVIGLWKRLRASPQDLMCFYSPPKKLFAYLIQFQGIQYRIEYSFFVIESIHVFRVEEPLLNELSATASSRDKPAPNEYWLQMDIQLSVPPVFHMITSEGQGNCTDFTEGNQASEVLLHSLMGRATSMFQMLDRVRRASPELGSVIRLQKGLNPHQFLDPQWANQLPRQPDSSVFDHQGRNPPIQGLSHDTSSEYGNKSQFKRLRSTSTPARQDLAQHLLPPKTNTEGLMHAQSVSPITQAMKSANVLEGSSTRLNSYEPSVSSAYPHHNLALNLDNTQFGELGTSNISYPLSAPSDVGSLPRASNSPSRPVMHPNTQGINTEIKDMAAQFPNSQTGGLTPNSWSMNTNVSVPFTTQNREFGGIGSSSISTTMNAPSQQLSQVPFGDVSLATENSVPSYGFEVPSEESVYAQARTNSSVSAGVAPRLFIQTPSIPLASSAGQDSNLIEKSSSGGVYASQPGASGYLSHDQSGSPFEDVYSPSAGIDFQKLRGQQFSPDMQ
Protein: Growth hormone-releasing hormone receptor (GHRH receptor) (Growth hormone-releasing factor receptor) (GRF receptor) (GRFR) (Q02643)
Organism: Homo sapiens (Human)
Function: Receptor for GRF, coupled to G proteins which activate adenylyl cyclase. Stimulates somatotroph cell growth, growth hormone gene transcription and growth hormone secretion.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Somatoliberin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Homeobox protein prophet of Pit-1
- Somatotropin
- Guanine nucleotide-binding protein G
- Growth hormone secretagogue receptor type 1
- Pituitary-specific positive transcription factor 1
- Prolactin
- Growth hormone receptor
Sequence:
MDRRMWGAHVFCVLSPLPTVLGHMHPECDFITQLREDESACLQAAEEMPNTTLGCPATWDGLLCWPTAGSGEWVTLPCPDFFSHFSSESGAVKRDCTITGWSEPFPPYPVACPVPLELLAEEESYFSTVKIIYTVGHSISIVALFVAITILVALRRLHCPRNYVHTQLFTTFILKAGAVFLKDAALFHSDDTDHCSFSTVLCKVSVAASHFATMTNFSWLLAEAVYLNCLLASTSPSSRRAFWWLVLAGWGLPVLFTGTWVSCKLAFEDIACWDLDDTSPYWWIIKGPIVLSVGVNFGLFLNIIRILVRKLEPAQGSLHTQSQYWRLSKSTLFLIPLFGIHYIIFNFLPDNAGLGIRLPLELGLGSFQGFIVAILYCFLNQEVRTEISRKWHGHDPELLPAWRTRAKWTTPSRSAAKVLTSMC
Protein: leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (A0A6I8PIV1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDEEEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGASLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRDDMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVDGFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQYLMEVTHDLRLRLKNYMMPAKGKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFEANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVLMENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGHFSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTPISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH
Protein: Neuraminidase (EC 3.2.1.18) (P03468)
Organism: Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Function: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. {ECO:0000255|HAMAP-Rule:MF_04071}.
Interaction partners:
Sequence:
MNPNQKIITIGSICLVVGLISLILQIGNIISIWISHSIQTGSQNHTGICNQNIITYKNSTWVKDTTSVILTGNSSLCPIRGWAIYSKDNSIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPVGEAPSPYNSRFESVAWSASACHDGMGWLTIGISGPDNGAVAVLKYNGIITETIKSWRKKILRTQESECACVNGSCFTIMTDGPSDGLASYKIFKIEKGKVTKSIELNAPNSHYEECSCYPDTGKVMCVCRDNWHGSNRPWVSFDQNLDYQIGYICSGVFGDNPRPEDGTGSCGPVYVDGANGVKGFSYRYGNGVWIGRTKSHSSRHGFEMIWDPNGWTETDSKFSVRQDVVAMTDWSGYSGSFVQHPELTGLDCMRPCFWVELIRGRPKEKTIWTSASSISFCGVNSDTVDWSWPDGAELPFSIDK
Protein: Nitric oxide synthase, inducible (EC 1.14.13.39) (Inducible NO synthase) (Inducible NOS) (iNOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2) (Q06518)
Organism: Rattus norvegicus (Rat)
Function: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. {ECO:0000250|UniProtKB:P35228}.
Interaction partners:
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-1
- Arginase-1
- RAC-alpha serine/threonine-protein kinase
- Arginase-2, mitochondrial
- Argininosuccinate lyase
- Argininosuccinate synthase
- RAC-beta serine/threonine-protein kinase
- Ornithine transcarbamylase, mitochondrial
Sequence:
MACPWKFLFRVKSYQGDLKEEKDINNNVEKTPGAIPSPTTQDDPKSHKHQNGFPQFLTGTAQNVPESLDKLHVTPSTRPQHVRIKNWGNGEIFHDTLHHKATSDISCKSKLCMGSIMNSKSLTRGPRDKPTPVEELLPQAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATKMAWRNAPRCIGRIQWSNLQVFDARSCSTASEMFQHICRHILYATNSGNIRSAITVFPQRSDGKHDFRIWNSQLIRYAGYQMPDGTIRGDPATLEFTQLCIDLGWKPRYGRFDVLPLVLQAHGQDPEVFEIPPDLVLEVTMEHPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINAAVLHSFQKQNVTIMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYYYQIEPWKTHIWQDEKLRPRRREIRFTVLVKAVFFASVLMRKVMASRVRATVLFATETGKSEALARDLAALFSYAFNTKVVCMEQYKANTLEEEQLLLVVTSTFGNGDCPSNGQTLKKSLFMMKELGHTFRYAVFGLGSSMYPQFCAFAHDIDQKLSHLGASQLAPTGEGDELSGQEDAFRSWAVQTFRAACETFDVRSKHCIQIPKRYTSNATWEPEQYKLTQSPESLDLNKALSSIHAKNVFTMRLKSLQNLQSEKSSRTTLLVQLTFEGSRGPSYLPGEHLGIFPGNQTALVQGILERVVDCSSPDQTVCLEVLDESGSYWVKDKRLPPCSLRQALTYFLDITTPPTQLQLHKLARFATEETHRQRLEALCQPSEYNDWKFSNNPTFLEVLEEFPSLRVPAAFLLSQLPILKPRYYSISSSQDHTPSEVHLTVAVVTYRTRDGQGPLHHGVCSTWINNLKPEDPVPCFVRSVSGFQLPEDPSQPCILIGPGTGIAPFRSFWQQRLHDSQHRGLKGGRMTLVFGCRHPEEDHLYQEEMQEMVRKGVLFQVHTGYSRLPGKPKVYVQDILQKELADEVFSVLHGEQGHLYVCGDVRMARDVATTLKKLVAAKLNLSEEQVEDYFFQLKSQKRYHEDIFGAVFSYGAKKGNTLEEPKGTRL
Protein: Class I diterpene synthase 2, chloroplastic (VacTPS2) ((13S)-vitexifolin A synthase) (EC 4.2.3.-) (9,13-epoxylabda-14-ene synthase) (EC 4.2.3.189) (Viteagnusin D synthase) (EC 4.2.3.-) (A0A2K9RFZ2)
Organism: Vitex agnus-castus (Chaste tree)
Function: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase the catalyzes the conversion of peregrinol diphosphate to viteagnusin D and 9,13(R)-epoxy-labd-14-ene, and of syn-copalyl diphosophate to vitexifolin A.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSLRFNLIVTPFSNHRIRNRRETFPAQEFPVATSKSAVKVKCNLITSTDLVGKVREKINGKVDNSLEVPAIHPVDIPSNLCMIDTLERLGVDRYFQSEIDGVLEETYRLWQQKEKDIFADVTCRAMAFRLLRVKGYEVSSDELAPYADQAHVNLQISDVTAVIELYRASQERIYEEESTLEKLHAWTSTYLKQQLVSGTISDKKLHKQVEYYLKNYHGILDLVGIRRSLDLYDIDHYQILKAADRFRTICKDLLAFSRQDFNNCQAQYQRELQLLQRWYEDCRLDKLNYGRDVLRISYFVSSAIIGDPELSDARLAFAKYCVLTTCIDDFFDHAGSREESYRILELVKEWKEKPAEDYGSKEVEFLFTAVYNTVNELAEMAYVEQGRCVKSLLIKLWVELLTSFKKELDSWTDDTALSLDEYLSSSWVSITSRINILTSIQFLGLKLSEEMLSSQECTDLCRHGSLVVRLLNDMQTFEKERRENTKNSVSILLEAPKHEGAITEEEVISKIKEIVEQNRRKLMQMVYQRGTIFPRKCKDVFLKSCRGGYYLYSNGDEFTSPVQIMEDMKLCYEPLTFHPLEANNGGNKN
Protein: Inositol-tetrakisphosphate 1-kinase (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase) (Inositol-triphosphate 5/6-kinase) (Ins(1,3,4)P(3) 5/6-kinase) (EC 2.7.1.159) (Q13572)
Organism: Homo sapiens (Human)
Function: Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Also acts as an inositol polyphosphate phosphatase that dephosphorylates Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that interconverts the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain. Plays an important role in MLKL-mediated necroptosis. Produces highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which bind to MLKL mediating the release of an N-terminal auto-inhibitory region leading to its activation. Essential for activated phospho-MLKL to oligomerize and localize to the cell membrane during necroptosis.
Interaction partners:
- Inositol polyphosphate multikinase
- Inositol-pentakisphosphate 2-kinase
- Multiple inositol polyphosphate phosphatase 1
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- Inositol-trisphosphate 3-kinase A
- Inositol polyphosphate 1-phosphatase
- Inositol-trisphosphate 3-kinase B
- Inositol-trisphosphate 3-kinase C
- Inositol polyphosphate 5-phosphatase K
- Inositol polyphosphate-4-phosphatase type I A
Sequence:
MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGMEVVQLNLSRPIEEQGPLDVIIHKLTDVILEADQNDSQSLELVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYMEDDRICSPPFMELTSLCGDDTMRLLEKNGLTFPFICKTRVAHGTNSHEMAIVFNQEGLNAIQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPESSSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFPGYEGVSEFFTDLLNHIATVLQGQSTAMAATGDVALLRHSKLLAEPAGGLVGERTCSASPGCCGSMMGQDAPWKAEADAGGTAKLPHQRLGCNAGVSPSFQQHCVASLATKASSQ
Protein: Pepsin A-5 (EC 3.4.23.1) (Pepsinogen-5) (P0DJD9)
Organism: Homo sapiens (Human)
Function: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
Subcellular location: Secreted.
Interaction partners:
- Pepsin A-4
- Pepsin A-3
- Vitamin K-dependent protein C
- Lactoylglutathione lyase
Sequence:
MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDKSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGETIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNVPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA
Protein: Ras-related protein Rab-11A (EC 3.6.5.2) (Q76NM4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
- 1-phosphatidylinositol 4-kinase
- GDP dissociation inhibitor, putative
- Rab GDP dissociation inhibitor
- Ras-related protein Rab-1A
Sequence:
MAMKEDYYDYLFKIVLIGDSGVGKSNLLSRFTRDEFNLESKSTIGVEFATKSIQLKNNKIIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDITKKNSFENIEKWLKELRDNADSNIVILLVGNKSDLKHLRVINDNDATQYAKKEKLAFIETSALEATNVELAFHQLLNEIYNVRQKKQATKNDDNLSIQPRGKKINVDDDNDKNETKKKNKCC
Protein: Protein SMG9 (Protein smg-9 homolog) (O46080)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing nonC and recruited to stalled ribosomes (By similarity).
Interaction partners:
- Nonsense-mediated mRNA decay factor SMG8
- Serine/threonine-protein kinase Smg1
- Probable ATP-dependent RNA helicase DDX56
- LD30822p
- Serine/threonine-protein kinase mTor
- RNA-binding protein 8A
Sequence:
MADPRRRFRNKKRDEACSGLLAPVTIARREDAARMMQPKILLKKDRDREQETWDRERDKDRKLERDREAEPSPSCYPDTPPALKTMIVNRTGEVRPADRCQMPLAGGALVQGSGQLSAVPSSSVCAALVSSVPTSRDKGSCSGGAGTAGTSAGAPNALQELQPPRMNRPTPLIVANGIFNANARKLFHKTNTDFTVIGVLGGQSSGKSTLLNLLAAERSLDYDYYQHLFSPEADECIFATRHKLKPNNGQKSILRPRTETLQFFITRERHILLDTPPLMPVGKDSDHQDLYSLGTMAQLLSVCHILILVIDGLALEQLRLINAALRLRPTLHCKGYVRDHMPQVVFVRARAHRIDFEIQQRERLDKKLAYLYGPTGLPIYRGRGDARCLNTFLLPEVSSNKATAFHSCLGELVRQFRERILGCTRISMCHTSTELSEAIWFEILAESARKAAPHFEKIYAEIKLRHLDTRCQWRSDNWRTFSSNAES
Protein: DNA mismatch repair protein MSH1, mitochondrial (MutS protein homolog 1) (P25846)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Important for mitochondrial DNA (mtDNA) stability and repair. Recognizes and binds to base-base and small insertion-deletion mismatches in mtDNA. ATP binding and hydrolysis is crucial for function. Binding to a mismatched base pair attenuates ATP hydrolysis. Also involved in proper sorting of mtDNA during mtDNA transmission.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15611870, ECO:0000269|PubMed:7961998}.
Interaction partners:
- DNA mismatch repair protein MSH3
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein MLH3
- DNA mismatch repair protein MSH6
- DNA mismatch repair protein PMS1
- DNA mismatch repair protein MLH2
- DNA damage-inducible protein DIN7
- N-glycosylase/DNA lyase
- Cruciform cutting endonuclease 1, mitochondrial
Sequence:
MKHFFRLPTAFRPISRVSLRYSSTDTAQPKISKLKISFNKISESNSEKKDNLGSIDTRNCLSTQQDDKLSSTEPSKASLPPSLQYVRDLMDLYKDHVVLTQMGSFYELYFEQAIRYAPELNISLTNRAYSHGKVPFAGFPVHQLSRHLKMLVNNCGYSVTIAEQFKKKDVADNEANKFYRRVTRIVTPGTFIDEAFENLRENTYLLNIEFPENCMSQVADTSLKVGICWCDVSTGEIFVQQVYLRDLVSAITRIQPKEILLDERLLEFHIESGTWYPELVELKKFFIKYQKMPSQHRTIESFYGLFNLGGKEATERQLKIQFQTFTQKELAALRNTLIYVSNHLPDFSINFQIPQRQLATAIMQIDSRTSTALELHSTVRDNNKKGSLLSSIRRTVTPSGTRLLSQWLSGPSLDLKEIKKRQKIVAFFKDNRDITETLRTMLKKVNDLSRILQKFSFGRGEALELIQMARSLEVSREIRKYLLNNTSLMKATLKSQITQLTESLNFEKNLIDDILKFLNEEELAKSQDAKQNADVTRMLDIDVKDKKESNKDEIFELRDFIVNPSFNTKLRKLHDTYQGVWQKKTEYNALLKGFFVGDLGAKTFTLKERQNGEYALHVTGTASSLKKIDELISKSTEYHGSCFHILQKSSQTRWLSHKIWTDLGHELELLNLKIRNEEANIIDLFKRKFIDRSNEVRQVATTLGYLDTLSSFAVLANERNLVCPKVDESNKLEVVNGRHLMVEEGLSARSLETFTANNCELAKDNLWVITGPNMGGKSTFLRQNAIIVILAQIGCFVPCSKARVGIVDKLFSRVGSADDLYNEMSTFMVEMIETSFILQGATERSLAILDEIGRGTSGKEGISIAYATLKYLLENNQCRTLFATHFGQELKQIIDNKCSKGMSEKVKFYQSGITDLGGNNFCYNHKLKPGICTKSDAIRVAELAGFPMEALKEAREILG
Protein: Suppressor of organelle fusion 2 (WD repeat-containing protein 81 homolog sorf-2) (Q10122)
Organism: Caenorhabditis elegans
Function: Together with sorf-1 negatively regulates the levels of phosphatidylinositol 3-phosphate (PtdIns3P) to enable the conversion of early endosomes to late endosomes. Binds to sorf-1 and the sorf-1-sorf-2 complex likely acts through bec-1, a non-catalytic subunit of phosphatidylinositol 3-kinase (PI3K), to suppress PI3K activity, thereby negatively regulating endosomal PtdIns3P levels.
Subcellular location: Early endosome {ECO:0000305|PubMed:26783301}. Late endosome {ECO:0000305|PubMed:26783301}. Cytoplasm {ECO:0000269|PubMed:26783301}.
Interaction partners:
- Suppressor of organelle fusion 1
- SAC domain-containing protein
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar fusion protein CCZ1 homolog
- CLaudin-like in Caenorhabditis
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1
- Beclin homolog
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Myotubularin-related protein 5
- UV radiation resistance-associated gene protein-like
Sequence:
MPEEEFEWNESKLNALSEILTQWAPHDELKLENVILEAKMAWIHESTDAVALEKEFEKLLNTSFDPLMDYEEHQRVKNGVCSPAKSTKLDWITKWANIAEKLSISHINCSKAPHKTINFQRLQILPNMTSILAIAHTEADNVILIYGHTKEGIDFQTVLRHSYSNIPDGSLQTIHFLTKNLLDLYSQLFSRKITAEFKTRHFRCLPSFWLQYDVLAPIFEQFRAPRAPRIPLDEATSNWANRKWENYQYLTYLNDITGRVRGEVHNHPIFPWVCDFSEENGGFRQLNRTKYRLCKGDDQLREMYSREPSHHVPELLSDIGYMVYRARVEPKDNLCRHVRRKWVPEEYPSTMSRMYQWTPDECIPEFYDDPSIFNSCHPDMADLRFPEFVSSPQEFIEWHRKMLEHEEVSMNLHRWIDLVFGFNLAIDNSKNALNLHLCFVEKNRRGLRTTGMVQLFNRPHPIRMPLNYDPKLDNYHLKMESFGFGMTSEHRKEPEVEPDEDSHYQIYQKIKKVRRLRHNTYFSSMVSAMEVMAQIVLAPHLAGRFDDPDHIRRCIQLYSYRIPANYRRLFDFLFNTEQDFPDCDEFSFFVSVRLNIPTKILNFSEEFGKCVSLHILRKLDVIPPFSKRSQLIILKEVESLKKSIRLCDHMEQCVVAAFQQLLEDEEACIQSVHRLMPVITRSLSQSALEDLINPMIELIQCETSVKLLDRRFLMHVSICYGTHTFLDLFLPPIVEACASMNCDRSVVAKESIMWLAKRYGPVICAKFISSNVLRIMASCYEAFEMVGLEQQPKAVFNVVLQGDETCSRIESLLSEIVLTYSVTFITVQFLPFCVDLIEQFHKRSSVQLEPGLVSVFRIVELSIRSMSDHQLMNYLEEFIIQKVIYRVLTILLDASFQFSSMRVRIIIICKVCQLLHSITQKIGTENTRIYANQPFKLMFSTFSEIYETDEELRINLRKRPSENTLFEVPLWMVEDVVDKFAKEWGVPFLSSFCDDPAFLIPFVSNSSSSSSPPASIAHSPPSAFTAYSLGGMSSGNRLFSLSASSPVNSVNSLGGLSFCDSGSLSAVWCARVSAAVCGVDNYRFDHLSLCNYTGHQEKIRKLAAISNENSFVSASSDKTVKLWSIKPELDEIGCQWTYQKHTRPVHDITILADNSIASTDGVLHVWDPFRTTLLAQMEWDSKEGSGGNIMRVENVDRHILSAICSLHSTVKLFDSRVGGWTCELKVSPGPGLTRAITVRDKGNKMAVALSNGTLAILDARNGKINALAQTNSTHTVSVNWLSDTRLLVCDADECGIFLETNPRAHIVRKLQDPVSAACLTDNSLVTLQNGTILRVYRNSGELQIETKIRPDELPGTPTAVLPLPLNCSYLIGSSHGAIRLMC