wanglab/gogpt-training-data huggingface dataset:
Protein: D-mannonate dehydratase (ManD) (EC 4.2.1.8) (A5V6Z0)
Organism: Rhizorhabdus wittichii (strain DSM 6014 / CCUG 31198 / JCM 15750 / NBRC 105917 / EY 4224 / RW1) (Sphingomonas wittichii)
Function: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- PFAM: Mannitol dehydrogenase, C-terminal domain
- PFAM: Mandelate racemase/muconate lactonizing enzyme, N-terminal domain protein
- 2-keto-3-deoxygluconate kinase
- Uronate isomerase
- PFAM: PfkB domain protein.
- PFAM: ribulose-phosphate 3-epimerase
- TIGRFAM: sugar-phosphate isomerase, RpiB/LacA/LacB family
Sequence:
MKITGARVIVTCPDRNFVTLKIETDEGLTGIGDATLNGRELAVASYLTDHVIPCLIGRDAHRIEDIWNYLYRGAYWRRGPVTMSAIAAVDTALWDIKAKAAGLPLYQLLGGRSRDGVMVYGHANGRDIEETTDEVARYIEMGYRAIRAQTGVPGLASTYGVSSDKMYYEPADAALPTENIWSTEKYLDHVPKLFDRLRDRFGFDHHLLHDVHHRLTPIEAGRLGKSLEPYRLFWMEDATPAENQEAFRLIRQHTVTPLAVGEVFNTIWDAKDLIQNQLIDYIRATVVHAGGISHLRRIADLAALYQVRTGCHGATDLSPVCMGAALHFDIWVPNFGVQEYMRHTEATDAVFPHAYSFASGYMTPGDVPGHGVEIDEKLAAKYPYKPCSLPVNRLEDGTLWHW
Protein: Sepiapterin reductase (EC 1.1.1.153) (O76752)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Dihydropteridine reductase
- 6-pyruvoyl tetrahydrobiopterin synthase
- Tryptophan 5-hydroxylase 2
- Protein henna
- Tyrosine 3-monooxygenase
- Dihydrofolate reductase
- LD24696p
- RE21057p
- BcDNA.GH10614
- AT18092p
Sequence:
MDLKQRTYLLVTGASRGIGREFAQQLAKRIKAEGSMVTLLGRNQTLLQESKAEIVATVPDLSVQTYSLELETAKTEDFTKILEASGGKNNFERAIVIHNAGTVGDTSKRAKEIGDTDFLQRYYHSNVFSAISLNCEFMRVFKGIPKLVVNLSTLAAIAPISSMAHYCTVKAAREMYFRVLATEESAEDTLVLNYAPGVIDTQMTVQVQREAHDPAVVAMFREQRESKTMLTPAQTTERFIKVLEAFKFKSGDHVDYRDEQF
Protein: Parvalbumin beta (Dark muscle parvalbumin) (saba-DPA) (White muscle parvalbumin) (allergen Sco j 1) (P59747)
Organism: Scomber japonicus (Chub mackerel)
Function: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
Interaction partners:
Sequence:
MAFASVLKDAEVTAALDGCKAAGSFDHKKFFKACGLSGKSTDEVKKAFAIIDQDKSGFIEEEELKLFLQNFKAGARALSDAETKAFLKAGDSDGDGKIGIDEFAAMIKG
Protein: Ground-like domain-containing protein (O01465)
Organism: Caenorhabditis elegans
Interaction partners:
- Ground-like domain-containing protein
- Warthog protein 1
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
- Ground-like domain-containing protein
Sequence:
MILPLLLSLFIFLPDVAEGNCHDHRYGVPSKSCKRVKDPTFQIRGDIRIVPMWEFILMKEPSEKRVKRSTSFRNGTLRSVHSGGNHGLPVDSLPTSNKNLNQANSFIKTPVLHQLLIQPIDSSAPASPVQRHIIQSQGKPTIGQLPIHVNKSKINTNHKTKRQGVYSALAQPPPAAKWGNNRPSYQNPTPSYQQGYPQQFPAPQRQQQYQPQPQTTNYNQAPQRPLYIPPPPPKLQVYPPQQLAENPYQTRNGVNNYRSRNSYGTNNRKHGRNGKKGKSSKMCKMCRKLSEEDESEEKEMACDLCSKSRRKGKKKGKSLRDGMVGGRRKSSKSSEDSDDHDDSMEGEGGGTENFTNDDENGADDYEDDGESTTIKPNAVSQPTILDFVERSKQQNKLMRIPVYRGKKLEAESNGTSGAYEDGDDNGEHNREEEEESSQYSSNIRDMEQPTKYSSKPNVKYSYPPKDTLPLQTCFHNPSGYVCCNLELNNVVESTYKEVRELPNFNPCNLQLIANKVQRASERMFGHPFESIVSHADFAQNINFSGDLVCKLEIDGKYMIAYGTPYHADDAVGPQGPDGKPLPVRSLKL
Protein: (R)-specific enoyl-CoA hydratase (EC 4.2.1.119) (3-hydroxyacyl-thioester dehydratase HtdY) (Dehydrogenase (EC 1.-.-.-)) (Q11198)
Organism: Mycobacterium tuberculosis
Interaction partners:
Sequence:
MAIDPNSIGAVTEPMLFEWTDRDTLLYAIGVGAGTGDLAFTTENSHGIDQQVLPTYAVICCPAFGAAAKVGTFNPAALLHGSQGIRLHAPLPAAGKLSVVTEVADIQDKGEGKNAIVVLRGRGCDPESGSLVAETLTTLVLRGQGGFGGARGERPAAPEFPDRHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFATQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARFTKPVFPGETLSTVIWRTEPGRAVFRTEVAGSDGAEARVVLDDGAVEYVAG
Protein: Kinesin-like protein (A0A140VKG5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MASQFCLPESPCLSPLKPLKPHFGDIQEGIYVAIQRSDKRIHLAVVTEINRENYWVTVEWVEKAVKKGKKIDLETILLLNPALDSAEHPMPPPPLSPLALAPSSAIRDQRTATKWVAMIPQKNQTASGDSLDVRVPSKPCLMKQKKSPCLWEIQKLQEQREKRRRLQQEIRARRALDVNTRNPNYEIMHMIEEYRRHLDSSKISVLEPPQEHRICVCVRKRPLNQRETTLKDLDIITVPSDNVVMVHESKQKVDLTRYLQNQTFCFDHAFDDKASNELVYQFTAQPLVESIFRKGMATCFAYGQTGSGKTYTMGGDFSGTAQDCSKGIYALVAQDVFLLLRNSTYEKLDLKVYGTFFEIYGGKVYDLLNWKKKLQVLEDGNQQIQVVGLQEKEVCCVEEVLNLVEIGNSCRTSRQTPVNAHSSRSHAVFQIILKSGRIMHGKFSLVDLAGNERGADTTKASRKRQLEGAEINKSLLALKECILALGQNKPHTPFRASKLTLVLRDSFIGQNSSTCMIATISPGMTSCENTLNTLRYANRVKKLNVDVRPYHRGHYPIGHEAPRMLKSHIGNSEMSLQRDEFIKIPYVQSEEQKEIEEVETLPTLLGKDTTISGKGSSQWLENIQERAGGVHHDIDFCIARSLSILEQKIDALTEIQKKLKLLLADLHVKSKVE
Protein: Sodium-coupled neutral amino acid transporter 5 (Solute carrier family 38 member 5) (System N transporter 2) (Q3U1J0)
Organism: Mus musculus (Mouse)
Function: Symporter that cotransports neutral amino acids and sodium ions, coupled to an H(+) antiporter activity. Releases L-glutamine and glycine from astroglial cells and may participate in the glutamate/GABA-L-glutamine cycle and the NMDA receptors activation (By similarity). In addition, contributes significantly to L-glutamine uptake in retina, namely in ganglion and Mueller cells therefore, participates in the retinal glutamate-glutamine cycle. The transport activity is pH sensitive, Li(+) tolerant, bidirectional and associated with large uncoupled fluxes of protons (By similarity). Moreover functions in both direction and is associated with large uncoupled fluxes of protons (By similarity). The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+) (By similarity). May have a particular importance for modulation of net hepatic glutamine flux (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18689705}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at astroglial membrane. {ECO:0000250|UniProtKB:A2VCW5}.
Interaction partners:
- Sodium-coupled neutral amino acid transporter 3
Sequence:
MAISCAVGMEMQEPKMNGTLSAGAAAGYRQEREGFLPTTRNPATGRKPVQFLDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMAHTGVIFFLALLLCIALLSSYSIHLLLTCASVVGIRAYEQLGQRAFGPAGKVVVAIIICLHNVGAMSSYLFIIKSELPLVIGTFLHMDPEGDWFLKGNLLIILVSLLIILPLALMKHLGYLGYTSSLSLTCMLFFLISVIYKKFQIGCDVSHNDTVVEAEQAPLQAFNSSCEAELFTVDSQMSYTVPIMAFAFVCHPEVLPIYTELCRPTQRRMQAVANMSIGAMFIMYGLTATFGYLTFYSTVKAEMLEMYTQEDMLILCVRLAVLLAVTLTVPVVLFPIRRALQQLLFPSKAFSWLRHVAIALILLILVNILVICVPTIRDIFGFIGSTSAPSLIFILPSVFYLRIVPTEVEPLFSWPKIQALCFGVLGVLFMAISLGFMFANWATGQSRMSGH
Protein: E3 ubiquitin-protein ligase RNF19A (EC 2.3.2.31) (Double ring-finger protein) (Dorfin) (Gametogenesis-expressed protein GEG-154) (RING finger protein 19A) (UBCM4-interacting protein 117) (UIP117) (XY body protein) (XYbp) (P50636)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10585566}. Note=Expressed primarily in the XY body of pachytene spermatocytes and in the centrosome of somatic and germ cells in all phases of the cell cycle.
Interaction partners:
Sequence:
MQEQEISFIFKYNEGLCMNIDSDSILMSILDMSLHQQMGSDRDLQSSTSSVSLPSVKKAPKQRRISIGSLFRRKKDSKRKSRELNGGVDGIASIESIHSEMCADKNSIFSTNTSSDNGLTSISKQIGDFIECPLCLLRHSKDRFPDIMTCHHRSCVDCLRQYLRIEISESRVNISCPECTERFNPHDIRLILSDDVLMEKYEEFMLRRWLVADPDCRWCPAPDCGYAVIAFGCASCPKLTCGREGCGTEFCYHCKQIWHPNQTCDAARQERAQSLRLRTIRSSSISYSQESGAAADDIKPCPRCAAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLVGAPVGIALIAGIAIPAMIIGIPVYVGRKIHNRYEGKDVSKHKRNLAIAGGVTLSVIVSPVVAAVTVGIGVPIMLAYVYGVVPISLCRSGGCGVSAGNGKGVRIEFDDENDINVGGTNAAIDTTSVAEARHNPSIGEGSVGGLTGSLSASGSHMDRIGTIRDNLSETASTMALAGASITGSLSGSAMVNCFNRLEVQADVQKERCSLSGESGTVSLGTVSDNASTKAMAGSILNSYIPLDREGNSMEVQVDIESKPFKFRHNSGSSSVDDSGATRGHTGGASSGLPEGKSSATKWSKEATGGKKSKSGKLRKKGNMKINETREDMDAQLLEQQSTNSSEFEAPSLSDSMPSVADSHSSHFSEFSCSDLESMRTSCSHGSSDCHARFTAVNTLPEVENDRLENSPHQCSSALLSKAASCSDVPQPSHAADEHGTSRSGGKPMVDLCFGDALRETNNNHSHQTADLKVAVQTEI
Protein: N-terminal acetyltransferase B complex subunit MDM20 (NatB complex subunit MDM20) (Dislikes extra CIN8 protein 1) (Mitochondrial distribution and morphology protein 20) (Q12387)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic subunit of the NatB N-terminal acetyltransferase, which catalyzes acetylation of the amino-terminal methionine residues of all proteins beginning with Met-Asp or Met-Glu and of some proteins beginning with Met-Asn or Met-Met. NatB acetylates TPM1 protein and regulates tropomyocin-actin interactions. MDM20 is required for mitochondrial inheritance during budding and together with TPM1, is essential for the integrity and assembly of actin cables. Genetically interacts with CIN8.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- N-terminal acetyltransferase B complex catalytic subunit NAT3
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-terminal acetyltransferase A complex catalytic subunit ARD1
- N-alpha-acetyltransferase NAT5
- N-terminal acetyltransferase A complex subunit NAT1
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- Tropomyosin-1
- N-alpha-acetyltransferase 40
Sequence:
MSDKIQEEILGLVSRSNFKQCYAKLGQLQKQFPNALYFKILETYVKFKQSPGKFDYNKLLEEPYGLKGTTITGDTRSLEFLHNFFVELGKYDEALHVYERGNFKFPSYELSYHWFMKALEDSNYNQMSKASLQLAKYSDSGNLPKRAYYFWNAISILAVSRFQENTLSDPKKILLSRLARQSLLDLKPFQNVQEIIVYCLVLDELFPQSREISEEIVAITFANFDTSVNLYLKNFILKHTKLLNSPQKLFEVCSKLIEKGLDDYELITNLIDAAYKLSKSKDEVKQWIDENLGDSRNTRLARLKLDIMYTDSVSESSLSYYLSKYHNKPCCSIDLNHYSGHINIDMLKSIMSKYDPEDKDLIHHCNILELGLIGSDSINNYNKFKGTLEKKSVTDYSSCSTFLLEIVKDKCKKTNPELKDVLLCITILENYQAKDPHNFDTMCWLIVLYMYLGLVPDAYFHFINLKIKNVQTDSLDYMIFSRFSTLFPNKQSDFYSKTFHEHNNLYDTSLANLPRYIQVAFERNSYSKILGMLEMRDKLMKSYTRWTKTLENLQFSRLCNDKRGHLLQKLHEDWRSLEMTQSVSFSDNRDFSILDENFAQFLNRGKILEYANLNEESIFLTLIRELIIEALPNGEKTEQISALLKKLPSINLEELLNNNLTEVESASFLIFFEIYENNGKNLHDLISRLMKVPINAKQNWMVSHTYLTKMATLKTLDSLKRIKDKEIQKLIKNSLKELRSCCDDVFKGYSKALVQAYEELKKDECGNLLKELDVKAENVKNIKNSLLGIQKSVRNL
Protein: Universal minicircle sequence binding protein (UMSBP), putative (Q38AZ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADNMQMSNARTCYNCGQPGHMSRECPNARSGGNMGGGRSCYNCGQPDHISRDCPNARTGGNMGGGRSCYNCGRPGHISRDCPNARSGGNMGGGRACYHCQQEGHIARECPNAPADAAAGGRACFNCGQPGHLSRACPVK
Protein: RNA-binding protein RO60 (60 kDa SS-A/Ro ribonucleoprotein homolog) (Ro sixty-related protein) (Q9RUW8)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: Binds to several small RNAs that accumulate during recovery from UV irradiation. Contributes to the resistance of D.radiodurans to ultraviolet irradiation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P10155}.
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease PH
Sequence:
MKNLLRAINPLNRPQTERLDERQVRNNAGGFVYTVSDESRLTRFLVLGVDGGTFYASAQKHTVQATDFVRELVQRDAALALRVTLDVVRGQRAPKADPALLVLALIAKTAPNAADRKAAWDALPEVARTGTMLLHFLAFADALGGWGRLTRRGVANVYETADVDKLALWAVKYKARDGWSQADALRKAHPKTDDAARNAVLKFMVDGVLPKVDSPALRVIEGHLKATEAQTDAAAAALMQEYRLPLEAVPTHVRGAEVYRAAMQTNGLTWLLRNLGNLGRVGVLTPNDSATVQAVIERLTDPAALKRGRIHPLDALKARLVYAQGQGVRGKGTWLPVPRVVDALEEAFTLAFGNVQPANTRHLLALDVSGSMTCGDVAGVPGLTPNMAAAAMSLIALRTEPDALTMGFAEQFRPLGITPRDTLESAMQKAQSMSFGGTDCAQPILWAAQERLDVDTFVVYTDNETWAGQVHPTVALDQYAQKMGRAPKLIVVGLTATEFSIADPQRRDMLDVVGFDAAAPNVMTAFARGEV
Protein: DNA mismatch repair protein MLH3 (MutL protein homolog 3) (F4JN26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in DNA mismatch repair (MMR), correcting insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of the MutLbeta heterodimer, which probably forms a ternary complex with the MutSbeta heterodimer that initially recognizes the DNA mismatches. This complex is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in promoting meiotic crossing-over and is involved in maintaining the genetic stability of simple sequence repeats by correction of frameshift intermediates.
Subcellular location: Nucleus {ECO:0000269|PubMed:16467846, ECO:0000269|PubMed:16856855}.
Interaction partners:
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein MSH2
- DNA mismatch repair protein MSH6
- DNA mismatch repair protein MSH7
- DNA mismatch repair protein MSH4
- DNA mismatch repair protein MSH3
- DNA mismatch repair protein MSH5
- DNA mismatch repair protein MSH1, mitochondrial
- Exonuclease 1
- Crossover junction endonuclease MUS81
Sequence:
MKTIKPLPEGVRHSMRSGIIMFDMARVVEELVFNSLDAGATKVSIFVGVVSCSVKVVDDGSGVSRDDLVLLGERYATSKFHDFTNVETASETFGFRGEALASISDISLLEVRTKAIGRPNGYRKVMKGSKCLHLGIDDDRKDSGTTVTVRDLFYSQPVRRKYMQSSPKKVLESIKKCVFRIALVHSNVSFSVLDIESDEELFQTNPSSSAFSLLMRDAGTEAVNSLCKVNVTDGMLNVSGFECADDWKPTDGQQTGRRNRLQSNPGYILCIACPRRLYEFSFEPSKTHVEFKKWGPVLAFIERITLANWKKDRILELFDGGADILAKGDRQDLIDDKIRLQNGSLFSILHFLDADWPEAMEPAKKKLKRSNDHAPCSSLLFPSADFKQDGDYFSPRKDVWSPECEVELKIQNPKEQGTVAGFESRTDSLLQSRDIEMQTNEDFPQVTDLLETSLVADSKCRKQFLTRCQITTPVNINHDFMKDSDVLNFQFQGLKDELDVSNCIGKHLLRGCSSRVSLTFHEPKLSHVEGYESVVPMIPNEKQSSPRVLETREGGSYCDVYSDKTPDCSLGSSWQDTDWFTPQCSSDRGCVGIGEDFNITPIDTAEFDSYDEKVGSKKYLSSVNVGSSVTGSFCLSSEWSPMYSTPSATKWESEYQKGCRILEQSLRLGRMPDPEFCFSAANNIKFDHEVIPEMDCCETGTDSFTAIQNCTQLADKICKSSWGHADDVRIDQYSIRKEKFSYMDGTQNNAGKQRSKRSRSAPPFYREKKRFISLSCKSDTKPKNSDPSEPDDLECLTQPCNASQMHLKCSILDDVSYDHIQETEKRLSSASDLKASAGCRTVHSETQDEDVHEDFSSEEFLDPIKSTTKWRHNCAVSQVPKESHELHGQDGVFDISSGLLHLRSDESLVPESINRHSLEDAKVLQQVDKKYIPIVACGTVAIVDQHAADERIRLEELRTKVLAGKARTVTYLSADQELVLPEMGYQLLQSYSEQIRDWGWICNITVEGSTSFKKNMSIIQRKPTPITLNAVPCILGVNLSDVDLLEFLQQLADTDGSSTIPPSVLRVLNSKACRGAIMFGDSLLPSECSLIIDGLKQTSLCFQCAHGRPTTVPLVDLKALHKQIAKLSGRQVWHGLQRREITLDRAKSRLDNAKS
Protein: Potassium voltage-gated channel protein Shaw (Shaw2) (P17972)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL43
- 40S ribosomal protein S24
- Large ribosomal subunit protein eL21
- FI01658p
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS13
Sequence:
MNLINMDSENRVVLNVGGIRHETYKATLKKIPATRLSRLTEALANYDPILNEYFFDRHPGVFAQVLNYYRTGKLHYPTDVCGPLFEEELEFWGLDSNQVEPCCWMTYTQHRDTQETLAVLDRLDLDTEKPSEEELARKFGFEEDYYKGTISWWQEMKPRIWSLFDEPYSSNAAKTIGVVSVFFICISILSFCLKTHPDMRVPIVRNITVKTANGSNGWFLDKTQTNAHIAFFYIECVCNAWFTFEILVRFISSPNKWEFIKSSVNIIDYIATLSFYIDLVLQRFASHLENADILEFFSIIRIMRLFKLTRHSSGLKILIQTFRASAKELTLLVFFLVLGIVIFASLVYYAERIQPNPHNDFNSIPLGLWWALVTMTTVGYGDMAPKTYIGMFVGALCALAGVLTIALPVPVIVSNFAMYYSHTQARAKLPKKRRRVLPVEQPRQPRLPGAPGGVSGCGTPGSGPHSGPMGSGGTGPRRMNNKTKDLVSPKSDMAFSFD
Protein: Toll-like receptor 1 (Toll/interleukin-1 receptor-like protein) (TIL) (CD antigen CD281) (Q9EPQ1)
Organism: Mus musculus (Mouse)
Function: Participates in the innate immune response to microbial agents. Specifically recognizes diacylated and triacylated lipopeptides. Cooperates with TLR2 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Forms the activation cluster TLR2:TLR1:CD14 in response to triacylated lipopeptides, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity). Acts as a coreceptor for M.tuberculosis lipoproteins LprG, LpqH and PhoS1 (pstS1), in conjunction with TLR2 and for some but not all lipoproteins CD14 and/or CD36. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11095740, ECO:0000269|PubMed:17998391}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:11095740}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:Q15399}. Golgi apparatus {ECO:0000250|UniProtKB:Q15399}. Note=Does not reside in lipid rafts before stimulation but accumulates increasingly in the raft upon the presence of the microbial ligand. In response to triacylated lipoproteins, TLR2:TLR1 heterodimers are recruited in lipid rafts, this recruitment determine the intracellular targeting to the Golgi apparatus. {ECO:0000250|UniProtKB:Q15399}.
Interaction partners:
- Toll-like receptor 6
- Toll-like receptor 2
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 4
- Toll/interleukin-1 receptor domain-containing adapter protein
- Stress-70 protein, mitochondrial
- Platelet glycoprotein 4
- Scavenger receptor class B member 1
- Toll-like receptor 5
- Integrin alpha-M
Sequence:
MTKPNSLIFYCIIVLGLTLMKIQLSEECELIIKRPNANLTRVPKDLPLQTTTLDLSQNNISELQTSDILSLSKLRVLIMSYNRLQYLNISVFKFNTELEYLDLSHNELKVILCHPTVSLKHLDLSFNAFDALPICKEFGNMSQLQFLGLSGSRVQSSSVQLIAHLNISKVLLVLGDAYGEKEDPESLRHVSTETLHIVFPSKREFRFLLDVSVSTTIGLELSNIKCVLEDQGCSYFLRALSKLGKNLKLSNLTLNNVETTWNSFINILQIVWHTPVKYFSISNVKLQGQLAFRMFNYSDTSLKALSIHQVVTDVFSFPQSYIYSIFANMNIQNFTMSGTHMVHMLCPSQVSPFLHVDFTDNLLTDMVFKDCRNLVRLKTLSLQKNQLKNLENIILTSAKMTSLQKLDISQNSLRYSDGGIPCAWTQSLLVLNLSSNMLTGSVFRCLPPKVKVLDLHNNRIMSIPKDVTHLQALQELNVASNSLTDLPGCGAFSSLSVLVIDHNSVSHPSEDFFQSCQNIRSLTAGNNPFQCTCELRDFVKNIGWVAREVVEGWPDSYRCDYPESSRGTALRDFHMSPLSCDTVLLTVTIGATMLVLAVTGAFLCLYFDLPWYVRMLCQWTQTRHRARHIPLEELQRNLQFHAFVSYSGHDSAWVKNELLPNLEKDDIQICLHERNFVPGKSIVENIINFIEKSYKSIFVLSPHFIQSEWCHYELYFAHHNLFHEGSDNLILILLAPIPQYSIPTNYHKLKTLMSRRTYLEWPTEKNKHGLFWANLRASINVKLVNQAEGTCYTQQ
Protein: Protein WFDC9 (Q8NEX5)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- WAP four-disulfide core domain protein 13
Sequence:
MKPWILLLVMFISGVVMLLPVLGSFWNKDPFLDMIRETEQCWVQPPYKYCEKRCTKIMTCVRPNHTCCWTYCGNICLDNEEPLKSMLNP
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q57U91)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365081}.
Interaction partners:
- MI domain-containing protein
- Peptidyl-prolyl cis-trans isomerase
- ATP-dependent DEAD/H RNA helicase, putative
- peptidylprolyl isomerase
- Peptidyl-prolyl cis-trans isomerase
- Peptidyl-prolyl cis-trans isomerase
- RNA helicase
- Peptidyl-prolyl cis-trans isomerase
- RNA-binding protein, putative
- Uncharacterized protein
Sequence:
MPSSSLSSPHPLVTAAILLETSLGELVVDLYGADCPVATAELVNLCRCKYFNGCIATEVVPDNVMILAHPVEELRRQTFASLLEASGQCHQLGGDTASDGRAVKQLIYNEWKRMRRHTAQLRRNSGASGKAEAGRLEFVPQSASNAVGAIRRSGLLLLEVPKVDGGGSNDEVSPKMQLLITLSNRHQDYFEDNFMVLGEVREGNNVVEKMRVAPHRRLTSVSGITTRPSRLIRIRHMTVLPTAGTDAFADISHRDRRKTMEENNLSSRLAQVGCFRHWATLGAVQAANKGLVSLLKREASKSTARKGRKGSSDETESFSGCEFLVIPEDSAQGGARNFPNHDTNNGDDYDILSVKYNSHFHGDYLSSDDDTDGDGNFGSRKEREKRQQEKMRLHQDKLNETRALTLNLLDGIGDASGELKPEGNVLFVCRLNPLTTSEGLEMCFSQFGKVKSVQVIRDSKTGDSLCYGFVEFADEETCYRAHQKMDNALIDDRRIHVDFSQSVSKLWMEKQRELRKRVRQ
Protein: Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (EC 3.6.1.17) (Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase) (Ap4A hydrolase) (Ap4Aase) (Diadenosine tetraphosphatase) (Nucleoside diphosphate-linked moiety X motif 2) (Nudix motif 2) (P50584)
Organism: Sus scrofa (Pig)
Function: Catalyzes the asymmetric hydrolysis of diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield AMP and ATP. Exhibits decapping activity towards FAD-capped RNAs and dpCoA-capped RNAs in vitro (By similarity).
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase
- CTP synthase
- Adenylate cyclase type 9
- CTP synthase
- Nucleoside diphosphate kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Nucleoside diphosphate kinase
- Alkaline phosphodiesterase I
- Adenylate cyclase type 8
Sequence:
MALRACGLIIFRRRLIPKVDNTAIEFLLLQASNGIHHWTPPKGHVEPGESDLQTALRETQEEAGIDAGQLTIIEGFRKELNYVAWEKPKTVIYWLAEVKDYDVEVRLSREHQAYRWLGLDEACQLAQFKDMKAVLQEGHQFLCSMAA
Protein: Trans-4-hydroxy-L-proline dehydratase (EC 4.2.1.172) (Glycyl radical enzyme) (Hyp dehydratase) (A0A031WDE4)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Function: Glycine radical enzyme that catalyzes the dehydration of the non-proteinogenic amino acid trans-4-hydroxy-L-proline (Hyp) to produce delta(1)-pyrroline-5-carboxylate (P5C). Is involved in the anaerobic degradation of 4-hydroxyproline.
Interaction partners:
Sequence:
MARGTFERTKKLREESINAEPHISIERAVLMTEAYKKYEGSVEIPVLRALSFKHYIENRTLSINDGELIVGEKGDSPNGAPTYPEICCHTMEDLEVMHNRDIINFSVSEEARKIHKEEIIPFWKKRQTRDKIINAMTPEWLAAYEAGMFTEFMEQRAPGHTVCGDTIYKKGFLDLKKDIEARLKELDFLNDLDAYNKKADLEAMAIACDAMVILGKRYAEKARQMAEEETDEAKKKDLLLIAETCDVVPAHKPETYHQAIQMYWFVHIGVTTELNIWDAFTPGRLDQHLNPFYERDVENGILDRDRAQELLECLWVKFNNQPAPPKVGITLKESSTYTDFANINTGGINPDGQDGVNEVSYIILDVMDEMKLIQPSSNVQISKKTPQKFLKRACEISRKGWGQPAFYNTEAIVQELMEAGKTIEDARLGGTSGCVETGCFGKEAYVLTGYMNIPKILELTLNNGYDPISKKQIGIETGDPRNFQSYEELFEAFKKQLHYMIDIKIEGNAVIENICAKHMPCPLMSTIVDDCIEKGKDYQRGGARYNTRYIQGVGIGTITDSLTAIKYNVFDKKKFDMDTLLKALDANFEGYEAILNLVSNKTPKYGNDDDYADEIMQEIFNAYYNEVTGRPTVCGGEYRVDMLPTTCHIYFGEIMGASPNGRLCAKPVSEGISPEKGGDTNGPTAVIKSCAKMDHIKTGGTLLNQRFAPSVVQGEKGLDNMANLVRAYFNMDGHHIQFNVFDKNVLLEAQKNPQDYKDLIVRVAGYSDHFNNLSRTLQDEIIGRTEQTF
Protein: Misexpression suppressor of ras 4 (Q9GU55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEALDQQQAKLTSNRDDGEAGRGSETGSEEGTGAGAAAGEEDDIEELHYVLDQAKEENESHQHGQNNNAKGNEDGKPKKNDDVIDVTMANGQGFKDTPEEETTGTEETAETEETAETEEAEQAEESLLNSRKSTDTPVDLGANCLTTGSPSKDLVKQELVEDKSEELKEPTSISLNEQFLDDIELKTEVEDKSDSLSETHMEFLTDSEEQPSESLGANHESEIDEKVDHFQPKESDSNEVEDKYFQSANEDSESEIEETVYTPPVINLETDSESGDKEFISIKDNESPVLEIEGGTEKSQTSGDLYQADVGEYASTAPPEVDETTSQTIGVPSLEGSDTLDSPSLTMDVDLPCSEDGAPPNVIKIESDMEDEAHSDSVKLKEHTVEVVPLIKLNGAHKALKEEKLEDGEVEEVEDPGEELEDPKEQSVITNHTGNNTKEEDTTASQVSALPLILPVGTTRSRSISSRSSTVSSASQPHLVIDHPESEHNAKPPALKLSLKRRRSKSSSVSQPEKQTKVEAGGFVSSLLLQRLQSNSNVIPPAISTESQQVLSCAKCNLQFDFERFQELNKHQAQCSGIQSANSSQLSQKQERFFRCSQCCSVHQCWHFFLHMREVHRRYICLYCNHVYPSVEKLSLHLENKHDIDQSHFAKDAWDQQQSKEDRARHLVCCTCQATFVQGSEFEDHDCSQLMQPCALCNQKGGHIIGCKNNKRKPTKRRRKVRRPPEPPLPVSQEAVEQPVPVEAIPEQLPQQLHLQSDIQNPFPAENIPAPEPVEDPPAPPIPKLVVPKIMLRVPKEFQKSVDAALSSTDTEDEELETAQPVEEAVSAPPEDLPFDAPPPPPPALSYDDSTSSKLNRVLAELERTKLDIERTKADIITKKQSKIIMANAHLENVVPQVVDPPQHLQPQQEEQRRWSLTPPASPHNNHVNLPEPPPALITEFQGQPDAVRRNSLGSDCMDMDDSLNAPEMEGSRDFTEAQKETLEPAPPSQDTQTADEPLAIQPLPPADGIMVAGPDTHTVDLQLDRPLDRFSMVDFVRLCLKSVYSLCLYCNHARRIAVNVKQLVIHLIGQHRFTATVDSITAEELYAETIVTKLKSFLRTSKTSI