wanglab/gogpt-training-data huggingface dataset:
Protein: Amyloid beta A4 precursor protein-binding family B member 1-interacting protein (APBB1-interacting protein 1) (Proline-rich EVH1 ligand 1) (PREL-1) (Proline-rich protein 73) (Rap1-GTP-interacting adapter molecule) (RIAM) (Retinoic acid-responsive proline-rich protein 1) (RARP-1) (Q7Z5R6)
Organism: Homo sapiens (Human)
Function: Appears to function in the signal transduction from Ras activation to actin cytoskeletal remodeling. Suppresses insulin-induced promoter activities through AP1 and SRE. Mediates Rap1-induced adhesion.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with ENA/VASP proteins at lamellipodia tips and focal adhesions, and F-actin at the leading edge. At the membrane surface, associates, via the PH domain, preferentially with the inositol phosphates, PtdIns(5)P and PtdIns(3)P. This binding appears to be necessary for the efficient interaction of the RA domain to Ras-GTPases (By similarity). {ECO:0000250}.
Interaction partners:
- Vasodilator-stimulated phosphoprotein
- Talin-2
- Talin-1
- Ras-related protein Rap-1A
- Profilin-4
- Profilin-3
- Profilin-1
- Ras-related protein Rap-1b
- Src kinase-associated phosphoprotein 1
- Ena/VASP-like protein
Sequence:
MGESSEDIDQMFSTLLGEMDLLTQSLGVDTLPPPDPNPPRAEFNYSVGFKDLNESLNALEDQDLDALMADLVADISEAEQRTIQAQKESLQNQHHSASLQASIFSGAASLGYGTNVAATGISQYEDDLPPPPADPVLDLPLPPPPPEPLSQEEEEAQAKADKIKLALEKLKEAKVKKLVVKVHMNDNSTKSLMVDERQLARDVLDNLFEKTHCDCNVDWCLYEIYPELQIERFFEDHENVVEVLSDWTRDTENKILFLEKEEKYAVFKNPQNFYLDNRGKKESKETNEKMNAKNKESLLEESFCGTSIIVPELEGALYLKEDGKKSWKRRYFLLRASGIYYVPKGKTKTSRDLACFIQFENVNIYYGTQHKMKYKAPTDYCFVLKHPQIQKESQYIKYLCCDDTRTLNQWVMGIRIAKYGKTLYDNYQRAVAKAGLASRWTNLGTVNAAAPAQPSTGPKTGTTQPNGQIPQATHSVSAVLQEAQRHAETSKDKKPALGNHHDPAVPRAPHAPKSSLPPPPPVRRSSDTSGSPATPLKAKGTGGGGLPAPPDDFLPPPPPPPPLDDPELPPPPPDFMEPPPDFVPPPPPSYAGIAGSELPPPPPPPPAPAPAPVPDSARPPPAVAKRPPVPPKRQENPGHPGGAGGGEQDFMSDLMKALQKKRGNVS
Protein: C-type lectin domain family 2 member D (C-type lectin-related protein B) (Clr-b) (Lectin-like transmembrane protein) (Osteoclast inhibitory lectin) (Q91V08)
Organism: Mus musculus (Mouse)
Function: Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Binds high molecular weight sulfated glycosaminoglycans.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14990792, ECO:0000269|PubMed:16751398}; Single-pass type II membrane protein {ECO:0000269|PubMed:14990792}.
Interaction partners:
- Killer cell lectin-like receptor subfamily B member 1B allele B
- Killer cell lectin-like receptor subfamily B member 1C
- Killer cell lectin-like receptor subfamily B member 1B allele A
- Killer cell lectin-like receptor subfamily B member 1
- Killer cell lectin-like receptor subfamily B member 1A
Sequence:
MCVTKASLPMLSPTGSPQEVEVGKILQGKRHGTISPESCAKLYCYYGVIMVLTVAVIALSVALSATKTEQIPVNKTYAACPQNWIGVENKCFYFSEYPSNWTFAQAFCMAQEAQLARFDNQDELNFLMRYKANFDSWIGLHRESSEHPWKWTDNTEYNNTIPIRGEERFAYLNNNGISSTRIYSLRMWICSKLNSYSLHCQTPFFPS
Protein: DNA mismatch repair protein MSH7 (AtMSH7) (MutS protein homolog 7) (Q9SMV7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Forms the heterodimer MutS gamma (MSH2-MSH7 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. MutS gamma recognizes specifically the T/G single base mismatch, but not trinucleotide insertion-deletion loops (IDL).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein PMS1
- DNA mismatch repair protein MLH3
- DNA mismatch repair protein MSH2
- DNA mismatch repair protein MSH5
- Proliferating cellular nuclear antigen 1
- Proliferating cell nuclear antigen 2
- DNA mismatch repair protein MSH3
- Exonuclease 1
- Exonuclease 1
Sequence:
MQRQRSILSFFQKPTAATTKGLVSGDAASGGGGSGGPRFNVKEGDAKGDASVRFAVSKSVDEVRGTDTPPEKVPRRVLPSGFKPAESAGDASSLFSNIMHKFVKVDDRDCSGERSREDVVPLNDSSLCMKANDVIPQFRSNNGKTQERNHAFSFSGRAELRSVEDIGVDGDVPGPETPGMRPRASRLKRVLEDEMTFKEDKVPVLDSNKRLKMLQDPVCGEKKEVNEGTKFEWLESSRIRDANRRRPDDPLYDRKTLHIPPDVFKKMSASQKQYWSVKSEYMDIVLFFKVGKFYELYELDAELGHKELDWKMTMSGVGKCRQVGISESGIDEAVQKLLARGYKVGRIEQLETSDQAKARGANTIIPRKLVQVLTPSTASEGNIGPDAVHLLAIKEIKMELQKCSTVYGFAFVDCAALRFWVGSISDDASCAALGALLMQVSPKEVLYDSKGLSREAQKALRKYTLTGSTAVQLAPVPQVMGDTDAAGVRNIIESNGYFKGSSESWNCAVDGLNECDVALSALGELINHLSRLKLEDVLKHGDIFPYQVYRGCLRIDGQTMVNLEIFNNSCDGGPSGTLYKYLDNCVSPTGKRLLRNWICHPLKDVESINKRLDVVEEFTANSESMQITGQYLHKLPDLERLLGRIKSSVRSSASVLPALLGKKVLKQRVKAFGQIVKGFRSGIDLLLALQKESNMMSLLYKLCKLPILVGKSGLELFLSQFEAAIDSDFPNYQNQDVTDENAETLTILIELFIERATQWSEVIHTISCLDVLRSFAIAASLSAGSMARPVIFPESEATDQNQKTKGPILKIQGLWHPFAVAADGQLPVPNDILLGEARRSSGSIHPRSLLLTGPNMGGKSTLLRATCLAVIFAQLGCYVPCESCEISLVDTIFTRLGASDRIMTGESTFLVECTETASVLQNATQDSLVILDELGRGTSTFDGYAIAYSVFRHLVEKVQCRMLFATHYHPLTKEFASHPRVTSKHMACAFKSRSDYQPRGCDQDLVFLYRLTEGACPESYGLQVALMAGIPNQVVETASGAAQAMKRSIGENFKSSELRSEFSSLHEDWLKSLVGISRVAHNNAPIGEDDYDTLFCLWHEIKSSYCVPK
Protein: Histone superfamily protein (A8MRL0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFFLLLSPRSDFTTIEFRVLSHSSLKIKMARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSHAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) (P18894)
Organism: Mus musculus (Mouse)
Function: Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:1686595}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14920}. Presynaptic active zone {ECO:0000250|UniProtKB:O35078}. Secreted {ECO:0000269|PubMed:27670111, ECO:0000269|PubMed:33484270}. Note=Transiently present in the cytosol before being delivered to the peroxisomes (By similarity). In the cerebellum, a fraction of protein localizes to the presynaptic active zone, where its activity is regulated by protein BSN (By similarity). Secreted into the lumen of the small intestine (PubMed:27670111, PubMed:33484270). {ECO:0000250|UniProtKB:O35078, ECO:0000250|UniProtKB:P14920, ECO:0000269|PubMed:27670111, ECO:0000269|PubMed:33484270}.
Interaction partners:
- Alanine--glyoxylate aminotransferase
- Peroxisomal sarcosine oxidase
- Sarcosine dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Glycine dehydrogenase
- Trans-L-3-hydroxyproline dehydratase
- L-threonine aldolase
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- 5-aminolevulinate synthase, non-specific, mitochondrial
Sequence:
MRVAVIGAGVIGLSTALCIHERYHPTQPLHMKIYADRFTPFTTSDVAAGLWQPYLSDPSNPQEAEWSQQTFDYLLSCLHSPNAEKMGLALISGYNLFRDEVPDPFWKNAVLGFRKLTPSEMDLFPDYGYGWFNTSLLLEGKSYLPWLTERLTERGVKLIHRKVESLEEVARGVDVIINCTGVWAGALQADASLQPGRGQIIQVEAPWIKHFILTHDPSLGIYNSPYIIPGSKTVTLGGIFQLGNWSGLNSVRDHNTIWKSCCKLEPTLKNARIVGELTGFRPVRPQVRLEREWLHFGSSSAEVIHNYGHGGYGLTIHWGCAMEAANLFGKILEEKKLSRLPPSHL
Protein: FI23916p1 (Q9W259)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIKARDSTRLLLISLLIGQLYVSCAGSPIDADVKGTDYQDDEYEYGDDTDDDDTQIIDVTKNHAEQEAPPYFDVTDLRVEAKPGDDVILNCDARNFQLSNAVVWYKNRIIIANGQNPISQRVQCMLNNSILLRNVSPEDSDDYYCEILPQRVRQHTALRVGARLSILCDDRDITDRSQTFRQGDHHKLECRTYLPDNATIKWSFNDLNGQPSSVDNQNGVIILDNVDEKNAGDYQCLADDGSRHPPHGTVHIDVQYSPIVSTHRHNVNTEKGATAELYCNYRAKPIGRSYFIKDGKTLQLSDKYSLKDSVHNDHNRTTLIVREVTDSDLGEYLCQVENAIGSNEVKVHVSYNPETPQFEDMTVEGNKVTLHWLVRSHQLLSEAMLDYQLTGSYTWSTVQVLETHRHNNTDNIWKITHQLELSRGVWHARVKTKNTKGWSHFSNDHVFEIPEDSEVDKDEEVELPPDEIVQAGIMPMSKGAASSMQRLNVGVILLAALLLRVRL
Protein: Epididymis-specific alpha-mannosidase (EC 3.2.1.24) (Alpha-1,6-mannosidase) (Mannosidase alpha class 2B member 2) (Q9Y2E5)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Alpha-mannosidase 2C1
- Lysosomal alpha-mannosidase
Sequence:
MGQLCWLPLLAPLLLLRPPGVQSAGPIRAFVVPHSHMDVGWVYTVQESMRAYAANVYTSVVEELARGQQRRFIAVEQEFFRLWWDGVASDQQKYQVRQLLEEGRLEFVIGGQVMHDEAVTHLDDQILQLTEGHGFLYETFGIRPQFSWHVDPFGASATTPTLFALAGFNAHLGSRIDYDLKAAMQEARGLQFVWRGSPSLSERQEIFTHIMDQYSYCTPSHIPFSNRSGFYWNGVAVFPKPPQDGVYPNMSEPVTPANINLYAEALVANVKQRAAWFRTPHVLWPWGCDKQFFNASVQFANMDPLLDHINSHAAELGVSVQYATLGDYFRALHALNVTWRVRDHHDFLPYSTEPFQAWTGFYTSRSSLKGLARRASALLYAGESMFTRYLWPAPRGHLDPTWALQQLQQLRWAVSEVQHHDAITGTESPKVRDMYATHLASGMLGMRKLMASIVLDELQPQAPMAASSDAGPAGHFASVYNPLAWTVTTIVTLTVGFPGVRVTDEAGHPVPSQIQNSTETPSAYDLLILTTIPGLSYRHYNIRPTAGAQEGTQEPAATVASTLQFGRRLRRRTSHAGRYLVPVANDCYIVLLDQDTNLMHSIWERQSNRTVRVTQEFLEYHVNGDVKQGPISDNYLFTPGKAAVPAWEAVEMEIVAGQLVTEIRQYFYRNMTAQNYTYAIRSRLTHVPQGHDGELLCHRIEQEYQAGPLELNREAVLRTSTNLNSQQVIYSDNNGYQMQRRPYVSYVNNSIARNYYPMVQSAFMEDGKSRLVLLSERAHGISSQGNGQVEVMLHRRLWNNFDWDLGYNLTLNDTSVVHPVLWLLLGSWSLTTALRQRSALALQHRPVVLFGDLAGTAPKLPGPQQQEAVTLPPNLHLQILSIPGWRYSSNHTEHSQNLRKGHRGEAQADLRRVLLRLYHLYEVGEDPVLSQPVTVNLEAVLQALGSVVAVEERSLTGTWDLSMLHRWSWRTGPGRHRGDTTSPSRPPGGPIITVHPKEIRTFFIHFQQQ
Protein: Phosphatidylinositol 4-kinase type 2 (EC 2.7.1.67) (Q8I0B7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein {ECO:0000256|RuleBase:RU367084}.
Interaction partners:
Sequence:
MPKNNIKSFLSQVPLPNAIAAKYQEPSEPRDDEQPTTSKDALESSSSVPSASAAYACICCEHKCPLEKDFLESQSDKEGDPPFLVNSPSMARDSKDTVTVQIAAPRCNCANCPLRNLYDPLFSEIVAKAEGAIENGVLPERIYQGSSGSYFVKDASHQCLAVFKPKDEEPYGRLNPKWTKWMHKLCCPCCFGRACLIPNQGYLSESGASLVDRKLNLNVVPKTRVVRLVAESFNYARIDRQKAKLKKRIKEHYPSAHFNRMSLPLKTGSFQLFVEGYKDADYWLRRFESEPLPPSVAKSFQLQFERLVVLDYIIRNTDRGNDNWLIKYVAPKITTQVGGTGGRTMHGVVTPKLPNALGASKIVDLNEPPQASPKPTTGGRPSNHLAGGAATSAQQDSSSLASSEDEPSSRSPPTSEPDWNVVNSAFIRIAAIDNGLAFPFKHPDSWRAYPYHWAWLPQAKIPFSEEIKEQVLPQLSDMNFVEEICTELLYLFQQDRGFDKRLFERQMSVMRGQILNLTQALRDGKSPVQLVQMPAVIVERSSGSRFFSFTQRFQNKSPFFSWC
Protein: V-set and transmembrane domain containing 2 like (D3ZDJ6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- M-phase phosphoprotein 8
Sequence:
MGAPLAAALGALHYLALFLQLGGATRPAGHAPWDNHVSGHALFTETPHDMTARTGEDVEMACSFRGSGSPSYSLEIQWWYLRSHRDWTDKQTWASNQLKASQQEDSGKDATKISVVKVVGSNISHKLRLSRVKPTDEGTYECRVIDFSDGKARHHKVKAYLRVQPGENSVLQLPDAPPAAPAPPPKPGRELRKRSLPEACSL
Protein: Hydroxymethylglutaryl-CoA synthase (Q57YL2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 3-hydroxy-3-methylglutaryl coenzyme A reductase
- hydroxymethylglutaryl-CoA lyase
- Enoyl-CoA hydratase/Enoyl-CoA isomerase/3-hydroxyacyl-CoA dehydrogenase, putative
- Succinyl-CoA:3-ketoacid-coenzyme A transferase
- propanoyl-CoA C-acyltransferase
- Methylglutaconyl-CoA hydratase, mitochondrial, putative
- Squalene monooxygenase
- squalene synthase
- Lanosterol 14-alpha-demethylase
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MRRTVRSLAGISGMSVYTPPCRVALKEWCNWTGNDWKKVSNVVGDSFRVPSNNENAYTMAASAVLRLILNYEVDPSRVGFLGFGTESSSDNSAGAVIVRGMVDKALKELGMPALSRHCEVPEFKHACLGGVYALKGAARYAEVDGGDDKLAIVVASDIAEYALGSTGEQTQGAGSVAMLVQKTPRLLELNTKAAGSASDYRGPDFRKPYRRHFIKEYGSTAENGKIPDFPVFSGPYSTLVYLDEVTAAVENMLSRLNQEPADYYDSVSALFFHRPYHMMPVQAMSFLYTRGLARSTAETHKTFFEELCGKAKVDSSAVRAELDKVPNYFEVIDEGKEPKDAFTMTNKVAKVLRSEKVFADFLGSKMSLGSTTMANFGNLYTASLPCWLAAGCEDAYSRKIDITGKPMVMIGYGSGDASEAIPITPVKGWEEAAAKINLSEALGNSINLTEEQYKGLHTGSLKDDFAADKRQKEFVVDRIGTRNEAAFQDIGIEYYRFVK
Protein: Beta-1,2-xylosyltransferase 1 (Cxt1p) (EC 2.4.1.-) (Q5K8R6)
Organism: Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Function: Beta-1,2-xylosyltransferase that plays a key role in capsule polysaccharide synthesis by transferring xylose to alpha-1,3-dimannoside in a beta-1,2-linkage. Also mediates glycosylation of glycosphingolipids; constitutes the unique xylosyltransferase responsible for adding xylose to glycosphingolipids.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPLNLPFSSPLKLPLPRRFIILILSASILILFLHTFAPSTLPPVLTPNLPHHEPDASYFSPSKWLPPILNPNAPTRPLEFDEDGQCLFLSPFDALSAAEKARARVLSLDEISPGIVRADAPPAEGTDADPDFDDEFSELSNATRKMPAGLTHPILGLLRDGEAKWNSMVTMQSQTLEQAVDVYMDRWGRRPPKGFDEWWHFAKANNVLLPDEYDPIMNSLLPFYALPIDTLKERLVEAEKIPETFTLIVHDGKVELKWNDDYSRDTWWASRPRADSQINLMEPFIKHIGTFRATFTIHDQPSILLDHERQEELLTAARHGKISTHPNELDRAEQNWRKACPPDSPLNKGEEELEAPDSFISSHLAAMDICQHPSYMENHGMLLEEKNSDSHPKPHTKLYPILVPSKTALNGDIPVTPIGKDGRRDDIGHDPEWNRKSGKLYWRGLATGLQHNKKAGAKWRQSHRERLHFLANDKSDTYTEVLSPVGSSGEAELARMPLRELGQYYMDVKLAGGNWQCDWGDGTCEEMEKEIDFAPKDSSERSNDFKYVFDTDGNAWSSRFPRLMASNNVVIKSTVFPEWNTNSLPEWYAYVPSKMDYSDLFSIMTFFRGTPSGRGAHDEVARRIALNGQCWVERTWRREDLQAYMFRLYLEYARLTSPDRDNGKMDYVSTQKKASKEADDVPAAADIETPVIDQ
Protein: Glycosyltransferase WbpY (Q9HTB9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- D-rhamnosyltransferase WbpZ
- ABC subunit of A-band LPS efflux transporter
- GDP-6-deoxy-D-mannose reductase
- Alginate biosynthesis protein AlgA
- Transport permease protein
- Glycosyltransferase WbpX
- GDP-mannose 4,6-dehydratase
- Class I SAM-dependent methyltransferase
- Glycosyltransferase
- Acyltransferase 3 domain-containing protein
Sequence:
MRIAVNARILQAPRTGIGHYLVELLGALQAHADFEFSLFHGWGWSGDLPAAALPGYSRLSPWLRNLPGAYRARRWLEQRRFDSGRPPVDLYHEPSLWPLDFDGPMLMTLHDLTHLHYPATQPAARLREIERRLARGMEKARLILTDSQAIADEAQAYFGLPRERFVVAPLGHAARFRPRDRESLREPLRAHGLVPRGYFLCVGTLEPRKNLSLALRAHGQLPAAVRQRFPLMIVGMPGWESRSLDDELRQALASGTVRLLGYLPDERVAELMSGARALVFPSIYEGFGLPVLEAMASGTPVLLTRLSAMPEVAGEAGSYIDPDDANGLSDMLVRMTEDTVYWECCREAGLRRAEQFSWKRCANLTAAAYRRAVEG
Protein: GEO07164p1 (GH08251p) (Q9VTA5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ejaculatory bulb-specific protein 2
Sequence:
MKFLLVCTLILGLAFFMASALPQLNNEAPMVGDDHHHHPVVRSVHFAEDVQAQHKHDDVACCG
Protein: Retinal guanylyl cyclase 2 (RETGC-2) (EC 4.6.1.2) (Guanylate cyclase 2F, retinal) (Guanylate cyclase F) (GC-F) (Rod outer segment membrane guanylate cyclase 2) (ROS-GC2) (O02740)
Organism: Bos taurus (Bovine)
Function: Responsible for the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors. Plays an essential role in phototransduction, by mediating cGMP replenishment. May also participate in the trafficking of membrane-asociated proteins to the photoreceptor outer segment membrane (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:9175772}; Single-pass type I membrane protein {ECO:0000255}. Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:Q5SDA5}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Guanylyl cyclase-activating protein 1
- Guanylyl cyclase-activating protein 2
- Retinal guanylyl cyclase 1
- Inosine triphosphate pyrophosphatase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Bis
- Pyruvate kinase
- Pyruvate kinase
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
Sequence:
MFLAPWPFSHLMLWFVTLGRQRGQHGLASFKLLWCLWLLVLMSLPLQVWAPPYKIGVVGPWTCDPLFSKALPEIAAQLATERINKDPALDLGHSLEYVIFNEDCQASRALSSFISHHQMASGFIGPANPGYCEAASLLGNSWDKGIFSWACVNYELDSKNSHPTFSRTLPSPIRVLLTVMKYFQWAHAGVISSDEDIWVHTAYRVASALRSRGLPVGVVLTTGQDSQSIQKALQQIRQADRIRIIIMCMHSTLIGGETQTHLLEWAHDLQMTDGTYVFVPYDTLLYSLPYKHTPYKVLRNNPKLREAYDAVLTITVESQEKTFYQAFEEAAARGEIPEKLESDQVSPLFGTIYNSIYFIAQAMNNAMKENGWASAASLVQHSRNVQFYGFNQLIRTDANGNGISEYVILDTNWKEWELHSTYTVDMETELLRFGETPIHFPGGRPPRADAQCWFADGRICQGGINPTFALMVCLALLIALLSINGFAYFIRHRINKIQLIKGPNRILLTLEDVTFINPHFGSKRGSHASVSFQITSEVQSGRSPRLSFSSGSLTPATCENSNIAIYEGDWVWLKKFPSGNFGDIKSVESSASDIFEMMKDLRHENINPLVGFFYDSGVFAIVTEFCSRRSLEDILMNQDVKLDWMFKSSLLLDLIKGMKYLHHREFAHGRLKSRNCVVDGRFVLKVTDYGFNDILETLRLSQEEPSAEELLWTAPELLRAPRGSRLRSFAGDVYSFAIIMQEVMVRGTPFCMMDLPAKEIIERIKKPPPVYRPVVPPEHAPPECLQLMKQCWAEAAEQRPTFDEIFNQFKTFNKGKKTNIIDSMLRMLEQYSSNLEDLIQERTEELEIEKQKTEKLLTQMLPPSVAESLKKGCTVEPEGFDLVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPKRNGMRHAAEIANMSLDILSSVGTFKMRHMPEVPVRIRIGLHSGPVVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVSHSTVTILRTLGEGYEVELRGRTELKGKGTEETFWLVGKKGFTKPLPVPPPVGKDGQVGHGLQSVEIAAFQRRKQKSSW
Protein: Cartilage matrix protein (Matrilin-1) (P51942)
Organism: Mus musculus (Mouse)
Function: Cartilage matrix protein is a major component of the extracellular matrix of non-articular cartilage. It binds to collagen.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Aggrecan core protein
- Cartilage oligomeric matrix protein
Sequence:
MKVTSGPAFALCSLLLLLLLLLQVPDSLSLVPQPRGHLCRTRPTDLVFVVDSSRSVRPVEFEKVKVFLSQVIESLDVGPNATRVGLVNYASTVKPEFPLRAHGSKASLLQAVRRIQPLSTGTMTGLALQFAITKALSDAEGGRARSPDISKVVIVVTDGRPQDSVRDVSERARASGIELFAIGVGRVDKATLRQIASEPQDEHVDYVESYNVIEKLAKKFQEAFCVVSDLCATGDHDCEQLCVSSPGSYTCACHEGFTLNSDGKTCNVCRGGGSGSATDLVFLIDGSKSVRPENFELVKKFINQIVDTLDVSDRLAQVGLVQYSSSIRQEFPLGRFHTKKDIKAAVRNMSYMEKGTMTGAALKYLIDNSFTVSSGARPGAQKVGIVFTDGRSQDYINDAARKAKDLGFKMFAVGVGNAVEEELREIASEPVADHYFYTADFKTINQIGKKLQKQICVEEDPCACESILKFEAKVEGLLQALTRKLEAVSGRLAVLENRII
Protein: Inositol hexakisphosphate kinase 3 (InsP6 kinase 3) (EC 2.7.4.21) (Inositol hexaphosphate kinase 3) (Q96PC2)
Organism: Homo sapiens (Human)
Function: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11502751}.
Interaction partners:
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
- Inositol-pentakisphosphate 2-kinase
- Inositol hexakisphosphate kinase 1
- Inositol hexakisphosphate kinase 2
- Inositol-trisphosphate 3-kinase B
- Inositol-trisphosphate 3-kinase A
Sequence:
MVVQNSADAGDMRAGVQLEPFLHQVGGHMSVMKYDEHTVCKPLVSREQRFYESLPLAMKRFTPQYKGTVTVHLWKDSTGHLSLVANPVKESQEPFKVSTESAAVAIWQTLQQTTGSNGSDCTLAQWPHAQLARSPKESPAKALLRSEPHLNTPAFSLVEDTNGNQVERKSFNPWGLQCHQAHLTRLCSEYPENKRHRFLLLENVVSQYTHPCVLDLKMGTRQHGDDASEEKKARHMRKCAQSTSACLGVRICGMQVYQTDKKYFLCKDKYYGRKLSVEGFRQALYQFLHNGSHLRRELLEPILHQLRALLSVIRSQSSYRFYSSSLLVIYDGQEPPERAPGSPHPHEAPQAAHGSSPGGLTKVDIRMIDFAHTTYKGYWNEHTTYDGPDPGYIFGLENLIRILQDIQEGE
Protein: Achaete-scute homolog 1b (Zash-1b) (Q90260)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional regulator. May mediate transcription activation by binding to the E box-containing promoter (By similarity). Involved in neurogenesis. Involved in maintaining rhombomere boundaries in the hindbrain, probably via up-regulation of delta expression. May mediate transcription activation by binding to the E box-containing promoter.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEATVVATTQLTQDSFYQPFSESLEKQDRECKVLKRQRSSSPELLRCKRRLTFNGLGYTIPQQQPMAVARRNERERNRVKQVNMGFQTLRQHVPNGAANKKMSKVETLRSAVEYIRALQQLLDEHDAVSAVLQCGVPSPSVSNAYSAGPESPHSAYSSDEGSYEHLSSEEQELLDFTTWFDRYESGASMATKDWC
Protein: Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A (EC 2.4.1.155) (Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase) (GlcNAc-T V) (GNT-V) (Mannoside acetylglucosaminyltransferase 5) (N-acetylglucosaminyl-transferase V) [Cleaved into: Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A (Secreted beta-1,6-N-acetylglucosaminyltransferase V) (Secreted GNT-V)] (P97259)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2. Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration. MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity). Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:8910328}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q09328}.; SUBCELLULAR LOCATION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A]: Secreted {ECO:0000250|UniProtKB:Q09328}.
Interaction partners:
Sequence:
MAFFTPWKLSSQKLGFFLVTFGFIWGMMLLHFTIQQRTQPESSSMLREQILDLSKRYIKALAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVNGTGANSTNSTTAVPSLVSLEKISVADIINGVQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDGTSCSFFIYLSEVENWCPRLPWRAKNPYEEADHNSLAEIRTDFNILYSMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKILVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFKKTLGPSWVHYQCMLRVLDSFGTEPEFNHASYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFSPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNREEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQENQLICEPSFFQHLNKEKDLLKYRVTCQSSELYKDILVPSFYPKSKHCVLQGDLLLFSCAGAHPTHQRICPCRDFIKGQVALCKDCL
Protein: Type III secretion chaperone SycN (Q9I329)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Type III secretion outer membrane protein PopN
- Type III secretory apparatus protein PcrD
- Regulatory protein PcrH
- Uncharacterized protein
- Type III secretion system effector delivery regulator TyeA domain-containing protein
- Uncharacterized protein
- Regulator in type III secretion
- Translocation protein in type III secretion
- Type III secretion protein PcrV
- Transcriptional regulator protein PcrR
Sequence:
MDWVELAVAQFCQDLRVSVPAPLARVVQLDFEDSGTLQLERHGEQLSLWLACDLAWHQAYRGTLRALRLCHARAAGSLPLRCAWSGESRLLLCITLEARQVGMPTLHQALQALRSARSEVLAA