wanglab/gogpt-training-data huggingface dataset:
Protein: Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24] (Q9Y5R2)
Organism: Homo sapiens (Human)
Function: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity).
Subcellular location: [Matrix metalloproteinase-24]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3. {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed matrix metalloproteinase-24]: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Also shed from cell surface as soluble proteinase, by a proteolytic cleavage. {ECO:0000250}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Metalloproteinase inhibitor 1
Sequence:
MPRSRGGRAAPGPPPPPPPPGQAPRWSRWRVPGRLLLLLLPALCCLPGAARAAAAAAGAGNRAAVAVAVARADEAEAPFAGQNWLKSYGYLLPYDSRASALHSAKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERQPRPPRPPLGDRPSTPGTKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCNQKEVERRKERRLPQDDVDIMVTINDVPGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV
Protein: Tumor necrosis factor (TNF-a) (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) [Cleaved into: Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form] (C1K3N5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401, ECO:0000256|RuleBase:RU368112}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401, ECO:0000256|RuleBase:RU368112}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000256|RuleBase:RU368112}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:0000256|RuleBase:RU368112}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000256|RuleBase:RU368112}; Single-pass type II membrane protein {ECO:0000256|RuleBase:RU368112}.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000256|RuleBase:RU368112}.
Interaction partners:
Sequence:
STESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
Protein: Protein gustavus (A1Z6E0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. Nucleus {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}. Note=Component of the cytoplasmic ribonucleoprotein (RNP) bodies which concentrate at the perinuclear region of the nurse cell and in punctate aggregates throughout the cytoplasm. Some cortical enrichment of these aggregates is also observed. At stage 7, accumulates in the anterior cytoplasm of the oocyte, whereas during stage 10 accumulates at the posterior pole. This posterior distribution is not maintained in later developmental stages. {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}.
Interaction partners:
- ATP-dependent RNA helicase vasa
- Elongin-C
- RING-box protein 2
- Suppressor of cytokine signaling at 16D, isoform B
- Suppressor of cytokine signaling at 36E, isoform D
- Elongin-B
- Ell-associated factor Eaf
- LP02169p
- AF4/FMR2 family member lilli
- Cullin-5
Sequence:
MGQKISGGVKTVSRNDSQSTFKPIIPRELQADFVKPARIDILLDMPPASRDLQLKHSWNSEDRSLNIFVKEDDKLTFHRHPVAQSTDCIRGKVGLTKGLHIWEIYWPTRQRGTHAVVGVCTADAPLHSVGYQSLVGSTEQSWGWDLGRNKLYHDSKNCAGVTYPAILKNDEAFLVPDKFLVALDMDEGTLSFIVDQQYLGIAFRGLRGKKLYPIVSAVWGHCEITMRYIGGLDPEPLPLMDLCRRTIRQKIGRTNLEEHIQQLQLPLSMKTYLLYKNRR
Protein: Histidine triad nucleotide binding protein 1 (F1RKI3)
Organism: Sus scrofa (Pig)
Interaction partners:
- Carboxypeptidase
Sequence:
MADEIAKAQAARPGGDTIFGKIIRKEIPAKIIYEDDQCLAFHDISPQAPTHFLVIPKKHISQISAAEDDDESLLGHLMIVGKKCAADLGLKKGYRMVVNEGSDGGQSVYHVHLHVLGGRQMNWPPG
Protein: Ceramide transporter 1 (A0A2R8YE59)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
Protein: DNA polymerase zeta subunit 2 (DNA polymerase zeta Rev7 subunit) (DNA polymerase zeta processivity subunit) (Revertibility protein 7) (Q9VNE1)
Organism: Drosophila melanogaster (Fruit fly)
Function: As the accessory component of the DNA polymerase zeta complex, involved in translesion DNA synthesis (TLS) and various DNA repair mechanisms. Promotes the apurinic/apyrimidinic (AP) endonuclease activity of Rrp1 and is therefore likely to be involved in the base excision repair (BER) pathway responsible for repair of DNA lesions. It does not appear to influence the synthesis activity of the catalytic component Dmpol-zeta.
Interaction partners:
- DNA repair protein Rev1
- DNA polymerase zeta catalytic subunit
- DNA polymerase delta subunit 2
- Kelch-like protein diablo
- Regulatory protein zeste
- DNA polymerase delta subunit 3
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit 1
- DNA polymerase alpha catalytic subunit
- DNA polymerase iota
Sequence:
MQAEIKADIIVEAMEVLVNHILYVRGIYPSHIFKMKRMYNSPIYVSIFPPLNNYLAGVLKSAQELLRRRELQCLELIVYQKENEKLESYKMQLETQRSGLPAEDHLMEFEQNMRSVIYKISQRLNQAPKLPAGSCQFKVHLHTTQEAFIRFSHDSQYQEFPWLQTQKTESQATGRTVYLLPLARVDDLGLKMDVLIVN
Protein: Uncharacterized protein (Q389I8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYLAVFQEFAHSKVLERIQSEDICRVDVAPMPCSSAKSEEELAVVRASAKLIIEDPEKENEEAVEAALATLGGLGFSITHRHPVTSAGCPMRDRVILTYTG
Protein: Protein phosphatase 1, regulatory subunit 13B (D4A6A8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGEGGCHLAEVWRGSERPIPCDHMMYEHLQKWGPRREEVKFFLRHEDSPTESSEQGARQSQEQRTQRNVMNVPGEKHTENGEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKKGKLNGFQSYNGRLTGPAAVELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKRISELRERLYGKKIQAPEPCEWDIITTVTPEHIRPGRCCGSLYPGDPVKPQSLTIASSAAHGRSKSANDGNWPTLKQNSASVKSTQMAGGDWKDSGMEGTLKQGAISSQPLPLSALGATDKLGIEIGKGPPPIPGVGKPLPPSYGTYPSPGPLGPGSTSSLERRKEGSLPRPAAGPPSRQKPAPLPPAGSAPQPSSSQQIQQRISVPPSPTYPPAGPPAFPAGDGKPELPLTVAIRPFLADKGSRPQSPRKGPQTVNSSSIYSMYLQQATPPKNYQPPAHGTLNKSVKAVYGKPVLPSGSASPSPLPFLHGSLGTGTTQPQPPSECAEKEAEPEGPSVPGEGSTVESLPRPLSPTKLTPIVHSPLRYQSDADLEALRRKLANAPRPLKKRSSITEPEGPGGPNIQKLLYQRFNTLAGGMEGTPFYQPSPSQDFVGTLADVDNGNTNANGNLDESFPPRPTAPLPDELAPSSDANDNELPSPEPEELICPQTTHQTAEPTEDNNNNVATVPSTEQIPSPVAEAPSEEDQVPPAPLSPVVHPPTASASKRTNLKKPNSERTGHGLRVRFNPLALLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWTPLHCAASCNSVHLCKQLVESGAAIFASTISDIETAADKCEEMEEGYIQCSQFLYGVQEKLGVMNKGIVYALWDYEAQNNDELSFHEGDAITILRRKDENETEWWWARLGDREGYVPKNLLGLYPRIKPRQRTLA
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q38G18)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFLGTVMKATTITCFALKLLSMAVLGSQDPQSTAAITDACTEIRYMLNVRQHFDQQIRNLAQAAEELHSQSKVLRLAAAKHVGTKKGLAYTLLAGLAAARESQAQKHLTEWTPKFTNAIQELSARIAVTDSGRTSGGAPTEKYGSAETDATTDQRHGATQRCKVSLTLTPSAPAKCSTASSEEKLKKAASELPALDKLKLIQTKLFGQYKAEVNLQSKGSSAVTRPIAGNAGCESASGASTDSVDMKFLTLSKPAPEFDTPKIEEDAGCREPNQQNDIHVHTAETLIHALCRARKFPTTNQQKLGPESLDSISSDSTAQEIALRLSNKYKKDQPENQRQEAVKDLLGKGTDSIQTKWLNDLSKTDSTLKLQDDAQPISIDAASQTDFDKALALFTAQAYQRAVKQEKTSVTENPSKKTDTEDKTEEKKDGDNKTTAADCKASSETNCDKTKCDWNAEKKQCKVKEGAAVISAVIKSPLLLEFLLLA
Protein: ATP-dependent DNA helicase II subunit 2 (EC 3.6.4.12) (ATP-dependent DNA helicase II subunit Ku80) (Pombe Ku80) (Q9HGM8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12424244}. Chromosome, telomere {ECO:0000269|PubMed:12424244}.
Interaction partners:
- ATP-dependent DNA helicase II subunit 1
- DNA ligase 4
- Double-strand break repair protein rad32
- Exodeoxyribonuclease 1
- DNA repair and recombination protein rad22
- DNA ligase 3
- DNA endonuclease ctp1
- Telomerase reverse transcriptase
- DNA repair protein rhp51
- DNA ligase 1
Sequence:
MSDKECTVFVLDLGKDMGTCHHGRSHSDLEWTLSYFHDELSHKFLANRKTDVVGIVGYKCDDTKNDLAEQEAYWNISVLYPIQTALFSKLQSVSQTLKPSNTMQGDLISAIVVSFDLMARHCKKNKWKKKMIVLTAARGIIDFSDYIGIAEQLLQHDVFLGVYGVDFDQEDINYSEPLKESQKKENEVRIQEFVESCHGQYCTFQQIYNNIGKPWVRKVRPVAIFRGTFSIGNRDSKDTSISIQVERYPRTRLTKPPTSSAFYENDMSKNYECLNIENSNVENKSMESDAVSTVRSYMVRDPKTNDSFEVKREDLESGYSYGRTIVPISRSDEDVLALDTIPGYEILGFIPKSSLPIYYTISDTNIIVPKDDFESKLNFSAFVQSLEREHRYALARFVSKDKGVPVLLVLMPYVEFKRHYLVDIQLPFAEDVRPYSFSEFEKLSNEEDMRQIDFAVSNYIDNMDLDSSDCGFNPPFEPENTFSMIPHRLQQAISYYANSPEGDLPQPNIYLTRYTNPPKSLLDNCILDLKLIKEKLTVNVPVKPKYSSQETAFDTGAPISEEQIEELLNSGLDEQEGEKLLVLHVSEKDPVGTFTEVLKNPFGLEDALTEMEKVIKNLIDKSKYDLALQSLQSLRLHSILEDEVERFNEYLTRLKKDVMQNNKPKENELINKIRSSGLDIILHDELTRHDNFNNI
Protein: Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic (AtFTSHI5) (Protein EMBRYO DEFECTIVE 2458) (Protein FTSH INACTIVE PROTEASE 5) (F4J3N2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for plastid development during embryogenesis. Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex (Probable).
Subcellular location: Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein Ycf2
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 4, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic
- ATP-dependent zinc metalloprotease FTSH 12, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 1, chloroplastic
- Malate dehydrogenase, chloroplastic
- Protein TIC 100
- Protein TIC 56, chloroplastic
- Inner membrane localized protein
- Protein TIC 20-I, chloroplastic
Sequence:
MDFISASSLSSPFSTQLSPIYLSSGIVSLKPRHRVKNRNFGSRESNNKSRKIVPIRGCFGFSGSFLRSKQSDYGSEAVSESLRLCGEGNELVLSSEYNSAKTRESVIQFVTKPLVYALFCIAIGLSPIRSFQAPALAVPFVSDVIWKKKKERVREKEVVLKAVDHEFSDYTRRLLETVSVLLKTIEIVRKENGEVAEVGAALDAVKVEKEKLQKEIMSGLYRDMRRLRKERDLLMKRADKIVDEALSLKKQSEKLLRKGAREKMEKLEESVDIMESEYNKIWERIDEIDDIILKKETTTLSFGVRELIFIERECVELVKSFNRELNQKSFESVPESSITKLSRSEIKQELVNAQRKHLEQMILPNVLELEEVDPFFDRDSVDFSLRIKKRLEESKKLQRDLQNRIRKRMKKFGEEKLFVQKTPEGEAVKGFPEAEVKWMFGEKEVVVPKAIQLHLRHGWKKWQEEAKADLKQKLLEDVDFGKQYIAQRQEQVLLDRDRVVSKTWYNEDKSRWEMDPMAVPYAVSRKLIDSARIRHDYAVMYVALKGDDKEFYVDIKEYEMLFEKFGGFDALYLKMLACGIPTSVHLMWIPMSELSLQQQFLLVTRVVSRVFNALRKTQVVSNAKDTVLEKIRNINDDIMMAVVFPVIEFIIPYQLRLRLGMAWPEEIEQTVGSTWYLQWQSEAEMNFKSRNTEDFQWFLWFLIRSSIYGFVLYHVFRFLKRKVPRLLGYGPFRRDPNVRKFWRVKSYFTYRKRRIKQKRKAGIDPIKTAFDRMKRVKNPPIPLKNFASIESMREEINEVVAFLQNPKAFQEMGARAPRGVLIVGERGTGKTSLALAIAAEARVPVVNVEAQELEAGLWVGQSAANVRELFQTARDLAPVIIFVEDFDLFAGVRGKFVHTKQQDHESFINQLLVELDGFEKQDGVVLMATTRNHKQIDEALRRPGRMDRVFHLQSPTEMERERILHNAAEETMDRELVDLVDWRKVSEKTTLLRPIELKLVPMALESSAFRSKFLDTDELLSYVSWFATFSHIVPPWLRKTKVAKTMGKMLVNHLGLNLTKDDLENVVDLMEPYGQISNGIELLNPTVDWTRETKFPHAVWAAGRALITLLIPNFDVVENLWLEPSSWEGIGCTKITKVTSGGSAIGNTESRSYLEKKLVFCFGSHIASQMLLPPGDENFLSSSEITKAQEIATRMVLQYGWGPDDSPAVYYATNAVSALSMGNNHEYEMAGKVEKIYDLAYEKAKGMLLKNRRVLEKITEELLEFEILTHKDLERIVHENGGIREKEPFFLSGTNYNEALSRSFLDVGDPPETALLSAPT
Protein: GPI ethanolamine phosphate transferase 1 (EC 2.-.-.-) (A0A1W2PQR8)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}.
Interaction partners:
Sequence:
MHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSLCKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMSMTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
Protein: CRISPR system Cascade subunit CasE (EC 3.1.-.-) (CasE endoRNase) (crRNA endonuclease) (Q46897)
Organism: Escherichia coli (strain K12)
Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).
Interaction partners:
- CRISPR system Cascade subunit CasC
- CRISPR system Cascade subunit CasB
- CRISPR system Cascade subunit CasD
- CRISPR system Cascade subunit CasA
- CRISPR-associated endoribonuclease Cas2
- CRISPR-associated endonuclease Cas1
- CRISPR-associated endonuclease/helicase Cas3
Sequence:
MYLSKVIIARAWSRDLYQLHQGLWHLFPNRPDAARDFLFHVEKRNTPEGCHVLLQSAQMPVSTAVATVIKTKQVEFQLQVGVPLYFRLRANPIKTILDNQKRLDSKGNIKRCRVPLIKEAEQIAWLQRKLGNAARVEDVHPISERPQYFSGDGKSGKIQTVCFEGVLTINDAPALIDLVQQGIGPAKSMGCGLLSLAPL
Protein: Oxysterol-binding protein (Q8I7N6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSSDEDGYDFGDSNEDFDEIYNNAEEHDIGNVQQDHGSVLMHLLSQVSVGMDLTKVTLPTFILERRSLLEMYADFFAHPDLFIATNGNDSAEKRMIAVVRYYLNSFYAARKSGVAKKPYNAILGETFRCRYSVPNSSLSGKKTESGPWPGSDEKQLTFIAEQVSHHPPISAFYAEMPSEGISFNAHIYTKSSFLGLSIGVASIGEGILTLHNYGDEQYTITFPSGYGRSIMSTPWFEFGGKVKVECEKTGYRADIEFLTKPFFGGKPHRIQGSICRDGAKKPVLTLRGEWNGTMYAKTQNGEEYVFVDVKAKPEVKKECVPVMQQGKRESRRLWRHVTAALLRNRIQTATTSKRFIEQRQRKEAKERLESGEKWTPLLFDTTDKDGEWMYKQKFGVRKAV
Protein: Protein WVD2-like 5 (Q94C48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Microtubule-associated protein (MAP) that regulates the orientation of interphase cortical microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8GYX9}.
Interaction partners:
- At1g23060/T26J12_16
- La-related protein 1C
- Protein ETHYLENE INSENSITIVE 3
Sequence:
MDPESIMAADGTDSAPANGGLAMENVCVKENGAVSVETVDTTSESQNENSANSSTLDTIEHVKEAAEGTQVEHVDDSKCMKGEKAQRKPRHEKLSGGKNNSSVHIKKSKEGKSADAKVAASNGSVAPNVQTTNPLKSKSFNGREAQVTKQGKHDSAPAESADGEKVKPKSQKKQAHETSEDDTQSSNSPKADDGKPRKVGALPNYGFSFKCDQRAEKRKEFYVKLEEKTHAKEEEINSMQAKSKETQEAELRMLRKSLNFKATPMPSFYQEPQPPKTELKKIPPTRPKSPKLGRKKTASGADSEETQTPRLGRLSLDERASKDNPTAKGIMPTVDLKKQPVRKSLPRLPSQKTVLPDGKPAPAKAAIIPAKVRPEKKKLEKDAETVNQTSHPTEEEAQVTVSSNADVEDSHETVSPRMNEDRADKSIEVSEAVAVEH
Protein: MYB transcription factor (Myb domain protein 85) (Myb family transcription factor) (Myb-like protein) (Putative transcription factor) (Q94GA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- NAC domain-containing protein 12
- NAC domain-containing protein 73
- NAC domain-containing protein 10
- Homeobox protein knotted-1-like 7
- NAC domain-containing protein 43
- NAC domain-containing protein 66
- NAC domain-containing protein 30
- Cellulose synthase A catalytic subunit 8
- NAC domain-containing protein 37
- Cytochrome P450 84A1
Sequence:
MGRQPCCDKLGVKKGPWTVEEDKKLINFILTNGHCCWRALPKLAGLRRCGKSCRLRWTNYLRPDLKRGLLSHDEEQLVIDLHANLGNKWSKIASRLPGRTDNEIKNHWNTHIKKKLLKMGIDPMTHQPLNQEPSNIDNSKTIPSNPDDVSVEPKTTNTKYVEISVTTTEEESSSTVTDQNSSMDNENHLIDNIYDDDELFSYLWSDETTKDEASWSDSNFGVGGTLYDHNISGADADFPIWSPERINDEKMFLDYCQDFGVHDFGF
Protein: Tuberous sclerosis 1 protein homolog (Q09778)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Together with tsc2, required for uptake of various amino acids from the environment and for proper conjugation. Involved in induction of gene expression of permeases and genes required for meiosis upon nitrogen starvation. May act as a GTPase-activating protein (GAP) for the small GTPase rhb1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Tuberous sclerosis 2 protein homolog
- GTP-binding protein rhb1
- Uncharacterized protein C1711.08
- Serine/threonine-protein kinase tor1
- Heat shock protein sti1 homolog
- Serine/threonine-protein kinase tor2
- Transcription factor prr1
- Protein wos2
- Uncharacterized protein C18B11.11
- 40 kDa peptidyl-prolyl cis-trans isomerase
Sequence:
MPLQSLVKALWNVLHEEESEGYPDLTELIAEVESYQQRYPKQNPTNSQKIRHILDEIYEKTPFNNTRRRILWLAVLKTVIPLLILDRQAVGEWWDQIFFPFLNSPTQLKPVFSDLKSILFYILIFHDEDEWGGDLRRECAEETITRLVDLYVSKAIENLGDVESQEQRNQTIECLVNVLVHYGIQRPKELSSCFCHHFLNPPTRIPILSVMVEVIRRQGPRLYEIPQTGFYDLVLKCAEFDTSPILLSYALSFILMILSHICNSLDDSLYRLFCIYLRFSMIDPTSGFPSSTASGNWEVFHDFMSTYASTTTSQTDSSYNDVHDIVGSSQPDYLESLDYSQLFSILYALYPINFLEFLRDPKLYASKHNFQIRYSFNQELLSTKSDGLLGRHLAHSNFLKYTAETELTDKSRWTRLDSIAVVALCNSLNAVGIAESVMDPFGGKLPTTYEETSSATGLLAYPNESHDIASEPFSISWPQNPSISGSVHSATTFDKAQLSNTEDSYDNISHGTSYSEGVSSIHMVKGERGSNNLELTSESLSSTNDTIRRLQRDLLFLQNELRFEKFVRQQHLQNIGKLHREHILDMAVESERQKLLLTNKRYKAQIELLNSEIDKHRSESQAALNRRVKWENDFNNKIKALREEKKAWKSEESELKSSIESLISQLESIRNSQIDIAFSKNQLELKLQLYETKLKEYEQHLSCVNISKKQVSSSSDTSFGNTKMDSSMILSNSEAVSDEQERELIESEKHRMKLESENLHLQANIELLKKDLEAINVVYEAKIFDLEKRLSSEANAPELHNPVNLNYDAQLSKISEIKENYDELLTRYRELEGKFLESQAEVEELKNFQKPLVDTGSSIHSSPGLQQSKFIIRNDSLHPKVGPPRRQSTDTSRSTFRQY
Protein: Pyruvate kinase 2 (PK 2) (EC 2.7.1.40) (P52489)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be used by cells under conditions in which the level of glycolytic flux is very low.
Interaction partners:
- NAD-dependent malic enzyme, mitochondrial
- Enolase 1
- Enolase 2
- Enolase-related protein 1
- Glucose-6-phosphate isomerase
- Pyruvate kinase 1
- Enolase-related protein 3
- ATP-dependent 6-phosphofructokinase subunit alpha
- Pyruvate decarboxylase isozyme 3
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Sequence:
MPESRLQRLANLKIGTPQQLRRTSIIGTIGPKTNSCEAITALRKAGLNIIRLNFSHGSYEFHQSVIENAVKSEQQFPGRPLAIALDTKGPEIRTGRTLNDQDLYIPVDHQMIFTTDASFANTSNDKIMYIDYANLTKVIVPGRFIYVDDGILSFKVLQIIDESNLRVQAVNSGYIASHKGVNLPNTDVDLPPLSAKDMKDLQFGVRNGIHIVFASFIRTSEDVLSIRKALGSEGQDIKIISKIENQQGLDNFDEILEVTDGVMIARGDLGIEILAPEVLAIQKKLIAKCNLAGKPVICATQMLDSMTHNPRPTRAEVSDVGNAVLDGADCVMLSGETAKGDYPVNAVNIMAATALIAESTIAHLALYDDLRDATPKPTSTTETVAAAATAAILEQDGKAIVVLSTTGNTARLLSKYRPSCPIILVTRHARTARIAHLYRGVFPFLYEPKRLDDWGEDVHRRLKFGVEMARSFGMVDNGDTVVSIQGFKGGVGHSNTLRISTVGQEF
Protein: Serine protease (Q57ZL3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIRHGLTGPPASSDPSDAVLSGIYPLYFRDEFLGSCIAIAPRILITAGHHFNSLKDDVGDLHLLDAASEGEITVVYVSKDRVHDLLVLWVSADLNWVPLRGFQPPVGARVATVWLSTKWPHDTIVSPGTVIEVNRGNCVVRGTVSTTGSSGSPVVDQFGDHIVGMHLISNTRDGSRVSGFISSRMIVSALVAMGVPCREVER
Protein: Putative xanthine dehydrogenase FAD-binding subunit XdhB (EC 1.17.1.4) (Q46800)
Organism: Escherichia coli (strain K12)
Function: Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism).
Interaction partners:
- Putative xanthine dehydrogenase molybdenum-binding subunit XdhA
- Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA
- Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC
- Aldehyde oxidoreductase molybdenum-binding subunit PaoC
- Probable hypoxanthine oxidase XdhD
- Guanine deaminase
- Adenine deaminase
- Aldehyde oxidoreductase FAD-binding subunit PaoB
- Putative oxidoreductase YgfK
- Xanthine-guanine phosphoribosyltransferase
Sequence:
MFDFASYHRAATLADAINLLADNPQAKLLAGGTDVLIQLHHHNDRYRHIVDIHNLAELRGITLAEDGSLRIGSATTFTQLIEDPITQRHLPALCAAATSIAGPQIRNVATYGGNICNGATSADSATPTLIYDAKLEIHSPRGVRFVPINGFHTGPGKVSLEHDEILVAFHFPPQPKEHAGSAHFKYAMRDAMDISTIGCAAHCRLDNGNFSELRLAFGVAAPTPIRCQHAEQTAQNAPLNLQTLEAISESVLQDVAPRSSWRASKEFRLHLIQTMTKKVISEAVAAAGGKLQ