wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear pore complex protein NUP58 (Nucleoporin 58) (Protein TRANSCURVATA1) (Q8RWH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in nucleocytoplasmic trafficking. May have regulatory roles in the gibberellin pathway, in auxin signaling and in light perception.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:21189294, ECO:0000269|PubMed:23840761}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP62
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP1
- Nuclear pore complex protein NUP88
- Amino-terminal region of chorein
- Nuclear pore complex protein NUP96
- Nuclear pore complex protein NUP214
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP160
- Nuclear pore complex protein NUP93A
Sequence:
MSFFPPQQQQTPQPLFQTQQTSLFQPQQTNSIFSQSQPQQTNSIFSQSQPQQTNSIFSQPQQQQQTSLFQPQQFQQQQQQLNQQQQQQVQQQLYLFTNDKAPANYSTKWADLHPDSQKLLLQIEEKILEHRSESQRLDQCSRLYDSSVSSEGFEFDASRIVQELGGINTAMDRQKAVLHELMIVAKDMLRNAEIAVRSFMMLQPRFPHWKQGGGVVSVGSQPSQGQGTNPAPASSGQQQAVTTTVQVSDFYRGIPKKPTAFLLQTVVRFEKYLNECRQWVEELEQLLALDSDKYSRHASLLESLPKVMSNVHDFFVHVAAKVESIHQYIESMRTSYLADQRRRGECHDPFLEADRRETAKQEAAAKRVHPTLHLPASTTSTQPSTQVAGLIASSATPGGSNPPQTSVPTSNPSSGAGFSFLNTPASGPSSSLFATPSSTAPTSSLFGPSPTPTQTPLFGSSPASTFGSTQSLFGQTTPSLTMPSQFGGATPGSGASFGSMTKSSRPKSRTTRR
Protein: poly(A)-specific ribonuclease (EC 3.1.13.4) (Q96IQ6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPAATVDHSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLGLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMISGVVLCEGVKWLSFHSGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGNAYEEEANKQS
Protein: Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) (P50282)
Organism: Rattus norvegicus (Rat)
Function: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P14780}.
Interaction partners:
- Metalloproteinase inhibitor 1
- Metalloproteinase inhibitor 3
- CD44 antigen
- Neutrophil gelatinase-associated lipocalin
- Metalloproteinase inhibitor 2
- Vascular endothelial growth factor A
- Proto-oncogene tyrosine-protein kinase Src
- Cathepsin G
- Endothelin-1
- NADPH oxidase 2
Sequence:
MSPWQPLLLVLLALGYSFAAPHQRQPTYVVFPRDLKTSNLTDTQLAEDYLYRYGYTRAAQMMGEKQSLRPALLMLQKQLSLPQTGELDSETLKAIRSPRCGVPDVGKFQTFDGDLKWHHHNITYWIQSYTEDLPRDVIDDSFARAFAVWSAVTPLTFTRVYGLEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGAVVPTYFGNANGAPCHFPFTFEGRSYLSCTTDGRNDGKPWCGTTADYDTDRKYGFCPSENLYTEHGNGDGKPCVFPFIFEGHSYSACTTKGRSDGYRWCATTANYDQDKADGFCPTRADVTVTGGNSAGEMCVFPFVFLGKQYSTCTSEGRSDGRLWCATTSNFDADKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYHYHEDSPLHEDDIKGIHHLYGRGSKPDPRPPATTAAEPQPTAPPTMCSTAPPMAYPTGGPTVAPTGAPSPGPTGPPTAGPSEAPTESSTPDDNPCNVDVFDAIADIQGALHFFKDGRYWKFSNHGGNQLQGPFLIARTWPAFPSKLNSAFEDPQPKKIFFFLWAQMWVYTGQSVLGPRSLDKLGLGSEVTLVTGLLPRRGGKALLISRERIWKFDLKSQKVDPQSVTRLDNEFSGVPWNSHNVFQYQDKAYFCHDKYFWRVSFHNRVNQVDHVAYVTYDLLQCP
Protein: Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I) (Q8C196)
Organism: Mus musculus (Mouse)
Function: Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P31327}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P31327}. Cell membrane {ECO:0000269|PubMed:34799567}; Peripheral membrane protein {ECO:0000305}; Extracellular side {ECO:0000269|PubMed:34799567}. Note=Localizes to the cell surface of hepatocytes. {ECO:0000269|PubMed:34799567}.
Interaction partners:
- Ornithine transcarbamylase, mitochondrial
- Argininosuccinate synthase
- Glutamine synthetase
- Glutamate dehydrogenase 1, mitochondrial
- Glutaminase liver isoform, mitochondrial
- Glutaminase kidney isoform, mitochondrial
- N-acetylglutamate synthase, mitochondrial
- Multifunctional protein CAD
- Argininosuccinate lyase
- NAD-dependent protein deacylase sirtuin-5, mitochondrial
Sequence:
MTRILTACKVVKTLKSGFGFANVTTKRQWDFSRPGIRLLSVKAKTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEALTDPAYKGQILTMANPIIGNGGAPDTTARDELGLNKYMESDGIKVAGLLVLNYSNDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQSVDFVDPNKQNLIAEVSTKDVKVFGKGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTQMEYDGLLIAGGPGNPALAQPLIQNVKKILESDRKEPLFGISTGNIITGLAAGAKSYKMSMANRGQNQPVLNITNRQAFITAQNHGYALDNTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVSPGPTDTEYLFDSFFSLIKKGKGTTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQADAVYFLPITPQFVTEVIKAERPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESMEDALKAADTIGYPVMIRSAYALGGLGSGICPNKETLIDLGTKAFAMTNQILVERSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSVNVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSVDGFTPRLPMNKEWPANLDLKKELSEPSSTRIYAIAKALENNMSLDEIVRLTSIDKWFLYKMRDILNMDKTLKGLNSDSVTEETLRKAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDIKFDEHGIMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACNGCIISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFANSVGYPCLLRPSYVLSGSAMNVVFSEDEMKRFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKEGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGESIDEKRLPTLEQPIIPSDYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIALLTNFQVTKLFAEAVQKSRTVDSKSLFHYRQYSAGKAA
Protein: Tail spike protein (TSP) (Endo-1,3-alpha-L-rhamnosidase) (EC 3.2.1.-) (Endorhamnosidase) (Q9XJP3)
Organism: Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage SfVI)
Function: Non-covalently bound to the neck of the phage capsid and mediating attachment of the viral particle to host cell-surface polysaccharide. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide.
Subcellular location: Virion {ECO:0000269|PubMed:6284}.
Interaction partners:
Sequence:
MTDIITNVVIGMPSQLFTMARSFKAVANGKIYIGKIDTDPVNPENQIQVYVENEDGSHVPASQPIVINAAGYPVYNGQIVKFVTEQGHSMAVYDAYGSQQFYFQNVLKYDPDQFGPDLIEQLAQSGKYSQDNTKGDAMIGVKQPLPKAVLRTQHDKNKEAISILDFGVIDDGVTDNYQAIQNAIDAVASLPSGGELFIPASNQAVGYIVGSTLLIPGGVNIRGVGKASQLRAKSGLTGSVLRLSYDSDTIGRYLRNIRVTGNNTCNGIDTNITAEDSVIRQVYGWVFDNVMVNEVETAYLMQGLWHSKFIACQAGTCRVGLHFLGQCVSVSVSSCHFSRGNYSADESFGIRIQPQTYAWSSEAVRSEAIILDSETMCIGFKNAVYVHDCLDLHMEQLDLDYCGSTGVVIENVNGGFSFSNSWIAADADGTEQFTGIYFRTPTSTQSHKIVSGVHINTANKNTAANNQSIAIEQSAIFVFVSGCTLTGDEWAVNIVDINECVSFDKCIFNKPLRYLRSGGVSVTDCYLAGITEVQKPEGRYNTYRGCSGVPSVNGIINVPVAVGATSGSAAIPNPGNLTYRVRSLFGDPASSGDKVSVSGVTINVTRPSPVGVALPSMVEYLAI
Protein: IkappaB kinase (EC 2.7.11.10) (Q6INT1)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKERLGTGGFGYVLRWIHQDTGEQVAIKQCRQELSPKNRERWCLEIQIMKKLNHPNVVSAREVPDGLQKLAPNDLPLLAMEYCEGGDLRKYLNQFENCCGLKEGPIRTLLSDISSALRYLHENRIIHRDLKPENIVLQPGPQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQKKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHGKVREKSNEHIVVYDDLTGAVKFSSVLPTPNHLSGILAGKLERWLQCMLMWHQRQRGTDPQNPNVGCFQALDSILSLKLLSVMNMVSGRVHTYPVTENENLQNLKSWLQQDTGIPEEEQELLQASGLALNSAQPLTQYVIDCTVIDGRQGEGDLIFLFDNRKTVYEPQISLPAHPESVSIVLQDPKRPLTYTHLRRVWGQIWQTIRALKEDCARLLQGQRTSMVNLLRYNTELSKKKNSMTSECEQLKAKLDFFRSSIQIDLEKYSEQMEFGITSEKLLSAWREMEQAVELCGREREVQALVDKMMALQTDSVDLQRNPLGRKHRGTLDDLEEQARDLYRRLRERPRDQRTPGDSNDMVRLLILAIQSFEKRVILIYDQLSKTVVCKRKALELSPKVKEVMNLMREDEKIVVRRQEKRQQELWNLLKIACSKVRGPVSGSPDSLGTSRMPGPSQLLSQPPVLSVSLAQEYVKKSEDLRSESLNLCSQLESSMRSFMKEQDGSLMSLDWSWLLQQEEESGASPITTS
Protein: Proline-rich protein 34 (Q9NV39)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPASATAAWHCPPLCLPPLPASAPTSPPNPATRPAPGPGRRARCPQSAHPAPTRGALTFWAPGSWPRVLLVPRSPGPVLRAPRLPHPAARARRRAWHGARLPGSPARAGRTFQRGLVSNSWAHAIFLPRPPNVLELQV
Protein: Glutamate receptor ionotropic, kainate glr-3 (Q21415)
Organism: Caenorhabditis elegans
Function: Ionotropic glutamate receptor (By similarity). Activation by glutamate requires additional verification. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Receptor-type guanylate cyclase gcy-8
- C2H2-type domain-containing protein
Sequence:
MFWIAKTLIAFLILLKTDCYKIAIPANLIDEVNPVLEFVDFRVQVIPYETKPLWRIKQESFKIVGISIENGLFSVCNCLILGASAIILPEQYDGHLAAAAIVQSIADNTNVPCVSLHLSPPTRPSTHLHPHLNAKSLAVAAFIKREKWKDVVVVFEEPDELLEITDMITAGHFDPDSFSSQLVRLKHGDDYGNELKHIKNKLDRYRIVINIPLQKALHFLEQAANMSMCGVLYHYVVMDMDLVTVDIDSIRGIEDCNITSFGVHDVNSEYIEDIRQEIVHKSSIRLPKKGVPYTTSIWIDTLRLLIRSMKSIQIWDEPRCGSSWKSGSDIKKRFFENPLAGISGDLHWAPSGERSNYTLHVYRRTLSFQKFAEWSSRTRRIASSEAVVIANSSEKLTLEGKHLKISVYLEAPFVMITSNGSYEGYCIDLLHKIANILKFTYTIQKVRDNAYGSKESNGKWSGMVGELQRGDADLAVASLTISYGRSEVIDFTVPYMHLGISILFKKPRIRDSDWFKFMDPLSTQVWIMTFASYFVVSVAIWIIAKISPYEQFERDEDNGQYKPVDNQFSLRNSFWFTVCSLMQQGSELCPRAASTRLLTGIWWFFALILISSYTANLAAVLTTRRMETPIENADDLAAQTKIKYGTLGRGSTMSFFNESKIETYERMWQLMSSSPGLFVQSSKEGIARVKSSDYAYLMESSMLEYAVERDCELMQIGGLIDQKGYGIGLPKGSPYRELISTAILRLQEKTELTELKEKWWKDKSVVCEQPKRKDQDDGESIGGIFIILVVGLVLTAVLVIFELITTRKPSPAQSQVIRHVNVIPSFKLGFFRWNVN
Protein: Alpha/beta hydrolase domain-containing protein aho-3 (EC 3.1.2.22) (Abnormal hunger orientation protein 3) (Q21221)
Organism: Caenorhabditis elegans
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins (By similarity). Acts in sensory neurons including AWC to regulate starvation-induced thermotaxis plasticity and salt learning behavior.
Subcellular location: Cell membrane {ECO:0000305|PubMed:22512337}; Lipid-anchor {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side {ECO:0000305|PubMed:22512337}. Cytoplasmic vesicle membrane {ECO:0000305|PubMed:22512337}; Lipid-anchor {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side {ECO:0000305|PubMed:22512337}. Note=In neurons, localizes to the sensory endings and to cytoplasmic punctate structures. {ECO:0000269|PubMed:22512337}.
Interaction partners:
Sequence:
MSSGAPSGSSMSSTPGSPPPRAGGPNSVSFKDLCCLFCCPPFPSSIVSKLAFMPPEPSYTITEDNKLVLIEGRAAWPHQEVDMANCVEMRITRTRRRNRVACTMIRPLPNSHFTLLFSHGNAVDLGQMTSFLYGLGFHLNCNVFSYDYSGYGCSTGKPSEKNLYADITAAFELLKSEFGVPKEKIILYGQSIGTVPSVDLASREDLAALVLHSPLMSGMRVAFPGTTTTWCCDAFPSIEKVPRVKCPTLVIHGTDDEVIDFSHGVSIYERCPTSVEPLWVPGAGHNDVELHAAYLERLRSFIDMEASAIRVTAPITNATSTNSRTISNGTSS
Protein: 3-deoxy-D-manno-octulosonic acid transferase (Kdo transferase) (EC 2.4.99.12) (EC 2.4.99.13) (Bifunctional Kdo transferase) (Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (P0AC75)
Organism: Escherichia coli (strain K12)
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:1577828}; Single-pass membrane protein {ECO:0000305|PubMed:1577828}; Cytoplasmic side {ECO:0000305|PubMed:1577828}.
Interaction partners:
- Tetraacyldisaccharide 4'-kinase
- Lipid A biosynthesis lauroyltransferase
- 3-deoxy-manno-octulosonate cytidylyltransferase
- Lipid A biosynthesis palmitoleoyltransferase
- Lipid-A-disaccharide synthase
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
- Phosphopantetheine adenylyltransferase
- UDP-3-O-
- 2-dehydro-3-deoxyphosphooctonate aldolase
Sequence:
MLELLYTALLYLIQPLIWIRLWVRGRKAPAYRKRWGERYGFYRHPLKPGGIMLHSVSVGETLAAIPLVRALRHRYPDLPITVTTMTPTGSERVQSAFGKDVQHVYLPYDLPDALNRFLNKVDPKLVLIMETELWPNLIAALHKRKIPLVIANARLSARSAAGYAKLGKFVRRLLRRITLIAAQNEEDGARFVALGAKNNQVTVTGSLKFDISVTPQLAAKAVTLRRQWAPHRPVWIATSTHEGEESVVIAAHQALLQQFPNLLLILVPRHPERFPDAINLVRQAGLSYITRSSGEVPSTSTQVVVGDTMGELMLLYGIADLAFVGGSLVERGGHNPLEAAAHAIPVLMGPHTFNFKDICARLEQASGLITVTDATTLAKEVSSLLTDADYRSFYGRHAVEVLYQNQGALQRLLQLLEPYLPPKTH
Protein: Calcitonin gene-related peptide type 1 receptor (CGRP type 1 receptor) (Calcitonin receptor-like receptor) (Q68EK2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Receptor for calcitonin-gene-related peptide (CGRP) (By similarity). Receptor specificity may be modulated by accessory proteins. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16602}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q16602}.
Interaction partners:
- Receptor activity-modifying protein 1
- Receptor
- Pro-adrenomedullin
- Calca protein
- Si:ch73-334d15.2.
- Islet amyloid polypeptide
- G_PROTEIN_RECEP_F2_4 domain-containing protein
- Receptor activity modifying protein 3.
- Calcitonin gene-related peptide type 1 receptor
Sequence:
MTASCWTICLFLLGSVTEFIVLASPEVNESQQQHPQNVYHDIGVTRNKIVTAQFECYQKIMKDNSQDRRGPVCNRTWDGWLCWDDTEAGITSEQHCPDYFQDFDPTEMVTKICTESGQWFLHPESNRTWTNFTRCNLHTTEGRRTAMNLFYLALIGHGLSLTSLFISLGIFFHFKSLSCQRITLHKNLFFSFVLNSIITIIWLTAVANNQELVQQNPISCKISQFIHLYIFGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYLLGWGFPLIPATIHAVARSYYYNDNCWISSNTSLLYIIHGPICAAMLVNLFFLLNIVRVLITKLKVTHQAKSSLYMKAVRATLILVPLLGIQYVLLPYKPSGRVSAEIYDYIMHILMHYQGLLVATIFCFFNGEVQAVLRRHWNQYRIQFGSTITQSDALRSASYTASSITEVQGCYSIDGHTEHLNGKNYHDFDNAIIKPENPFA
Protein: Rho guanine nucleotide exchange factor TIAM2 (SIF and TIAM1-like exchange factor) (T-lymphoma invasion and metastasis-inducing protein 2) (TIAM-2) (Q6ZPF3)
Organism: Mus musculus (Mouse)
Function: Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP-dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Activates specifically RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14550769}. Cell projection, lamellipodium {ECO:0000269|PubMed:14550769}. Cell projection, filopodium {ECO:0000269|PubMed:14550769}. Cell projection, growth cone {ECO:0000269|PubMed:11707441, ECO:0000269|PubMed:14550769}. Cell projection, neuron projection {ECO:0000269|PubMed:11707441, ECO:0000269|PubMed:14550769}. Perikaryon {ECO:0000269|PubMed:11707441}.
Interaction partners:
Sequence:
MGNSESQYTFQGSKNHSNTVTGAKQKPCSLKIRSVHAKDEKSLHGWTHGSSGAGYKSRSLARSCLSHFKNHQPYATRLSGPTCKVSKGTTYSKHRANTPGNDFQGNSGAFLPENGFHYVDRESEESHITSNGHLLTCYGRKESLASTPPGEDHRSPRVLIKTLGKLDGCLRVEFHNGGNPHKGTSEDPSGPVRLLRYSPTLASETCPVRETRRHSAAGSPSSQRPSPTDSRLRSSKGSSLSSESSWYDSPWGNAGEVSEVEGSFLAPSTPDPSLPSSFPPSDTKKPFNQSSSLSSLRELYKDPNLGCRSPSGTCLSSNEYISSQVSLNNRVSFASDMDVPSRVDHRDPLHYSSFTLPCRKSKALTEDAAKKDTLKARMRRFSDWTGSLSRKKRKLQEPRSMEGSEYFDSHSDGLNAEGQVPAQTSSLLWSGGSAQTLPHRSESTHAISVDPLRQNIYENFMRELEMSRSNTEHVETSTETMESSSESVSSLEQLDLLFEKEQGVVRKAGWLFFKPLVTLQKERKLELVARRKWKQYWVTLKGCTLLFYETYGKNSTEQNSAPRCALFAEDSIVQSVPEHPKKEHVFCLSNSCGDVYLFQATSQTDLENWVTAIHSACASLFAKKHGKEDTVRLLKSQTRSLLQKIDMDSKMKKMAELQLSVVSDPKNRKAIENQIRQWEQNLEKFHMDLFRMRCYLASLQGGELPNPKSLLAATSRPSKLALGRLGVLSVSSFHALVCSRDDSTLRKRTLSLTQRGKSKKGIFSSLKGLDTLARKGREKRASITQMFDSSHSHGFLGTQLPQKSTNSNKAHDLHLYGSAVDSALRDSMWEVQTYVHFQDNEGVTVTIKPEHRVEDVLALVCKMRQLEPTHYGLQLRKVVDKSVEWCVPALYEYMQEQVYDEIEVFPLSVYDVQLTKTGDMTDFGFAVTVQVDEHQHLNRIFISDVLPDSLAYGGGLRKGNEITSLNGEPVSDLDIQQMEALFSEKSVGLTLVARPVTTRRTLCASWSDSDLFSRDQKSLPPSPNQSQLLEEFLDNFRKTATSDFSNVPEITTGLKRSQTEGTLDQVPHREKMEQTFLSADQIAELCRDLNNTHTNSMEAPTESHDPPPRPLARHLSDADRLRKVIQELVDTEKSYVKDLSCLFELYLEPLQNETFLTQDEMESLFGSLPEMLEFQKVFLETLEDAISASSDFSVLETPSQFRKLLFSLGGSFLYYADHFKLYSGFCANHIKVQRVLERAKTDKAFKAFLDARNPTKQHSSTLESYLIKPVQRVLKYPLLLKELVSLTDHESEEHYHLTEALKAMEKVASHINEMQKIYEDYGMVFDQLVAEQSGTEKEVTELSMGELLMHSTVSWLNPFLSLGKARKDIELTVFVFKRAVILVYKENCKLKKKLPSNSRPAHNSADLDPFKFRWLIPISALQVRLGNTAGTENNSTWELIHTKSEIEGRPETIFQLCCSDSENKTSIVKVIRSILRENFRRHIKCELPLEKTCKDRLVPLKNRVPVSAKLASSRSLKGLRTSSSSEWPSEPSKGNSLDSDECSLSSGTQSSGCPVAESRRDSKSTELEKDAQEGLAEFPDGLIKESDILSDEDEDFHHPLKQGSPTKDIEIQFQRLKISEESDVHPVGQQPLTESGEQPKLVRGHFCPIKRKANSTKRGRGTLLKAQTRHQSLDSHPETASIDLNLVLEREFSVQSLTSVVNEEGFYETQSHGKS
Protein: Interleukin-17 receptor E (IL-17 receptor E) (IL-17RE) (Q8NFR9)
Organism: Homo sapiens (Human)
Function: Specific functional receptor for IL17C. May be signaling through the NF-kappa-B and MAPK pathways. May require TRAF3IP2 /ACT1 for signaling. May be a crucial regulator in innate immunity to bacterial pathogens. Isoform 2 and isoform 4 may be either cytoplasmic inactive or dominant active forms. Isoform 3 and isoform 5 may act as soluble decoy receptors.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted {ECO:0000305}.
Interaction partners:
- Interleukin-17 receptor A
- Interleukin-17C
- Interleukin-17 receptor B
- Interleukin-17F
- Interleukin-17 receptor D
- Interleukin-17 receptor C
- Interleukin-17B
- Interleukin-25
- Interleukin-17D
- Interleukin-17A
Sequence:
MGSSRLAALLLPLLLIVIDLSDSAGIGFRHLPHWNTRCPLASHTDDSFTGSSAYIPCRTWWALFSTKPWCVRVWHCSRCLCQHLLSGGSGLQRGLFHLLVQKSKKSSTFKFYRRHKMPAPAQRKLLPRRHLSEKSHHISIPSPDISHKGLRSKRTQPSDPETWESLPRLDSQRHGGPEFSFDLLPEARAIRVTISSGPEVSVRLCHQWALECEELSSPYDVQKIVSGGHTVELPYEFLLPCLCIEASYLQEDTVRRKKCPFQSWPEAYGSDFWKSVHFTDYSQHTQMVMALTLRCPLKLEAALCQRHDWHTLCKDLPNATARESDGWYVLEKVDLHPQLCFKFSFGNSSHVECPHQTGSLTSWNVSMDTQAQQLILHFSSRMHATFSAAWSLPGLGQDTLVPPVYTVSQARGSSPVSLDLIIPFLRPGCCVLVWRSDVQFAWKHLLCPDVSYRHLGLLILALLALLTLLGVVLALTCRRPQSGPGPARPVLLLHAADSEAQRRLVGALAELLRAALGGGRDVIVDLWEGRHVARVGPLPWLWAARTRVAREQGTVLLLWSGADLRPVSGPDPRAAPLLALLHAAPRPLLLLAYFSRLCAKGDIPPPLRALPRYRLLRDLPRLLRALDARPFAEATSWGRLGARQRRQSRLELCSRLEREAARLADLG
Protein: BAHD acyltransferase DCR (EC 2.3.1.-) (Protein DEFECTIVE IN CUTICULAR RIDGES) (Protein PERMEABLE LEAVES 3) (Q9FF86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for incorporation of 9(10),16-dihydroxy-hexadecanoic acid into cutin.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19626137, ECO:0000269|PubMed:19828672}.
Interaction partners:
- BAHD acyltransferase BIA1
- Protein ECERIFERUM 2
- At3g10570
- Protein PELOTA 2
- D-isomer specific 2-hydroxyacid dehydrogenase family protein
- Glycerol-3-phosphate 2-O-acyltransferase 6
- Protein ECERIFERUM 26
- Cytosolic sulfotransferase 10
- 3-ketoacyl-CoA synthase 6
- Serine carboxypeptidase-like 5
Sequence:
MKIKIMSKTHVKPTKPVLGKKQFHLTTFDLPYLAFYYNQKFLLYKFQNLLDLEEPTFQNEVVENLKDGLGLVLEDFYQLAGKLAKDDEGVFRVEYDAEDSEINGVEFSVAHAADVTVDDLTAEDGTAKFKELVPYNGILNLEGLSRPLLAVQVTKLKDGLAMGLAFNHAVLDGTSTWHFMSSWAEICRGAQSISTQPFLDRSKARDTRVKLDLTAPKDPNETSNGEDAANPTVEPPQLVEKIFRFSDFAVHTIKSRANSVIPSDSSKPFSTFQSLTSHIWRHVTLARGLKPEDITIFTVFADCRRRVDPPMPEEYFGNLIQAIFTGTAAGLLAAHGPEFGASVIQKAIAAHDASVIDARNDEWEKSPKIFQFKDAGVNCVAVGSSPRFRVYEVDFGFGKPETVRSGSNNRFNGMMYLYQGKAGGISIDVEITLEASVMEKLVKSKEFLLSEEEEEDDGKKLTNGNGHVNGNGNGYVNGNGNGFV
Protein: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (PDP 1) (EC 3.1.3.43) (Protein phosphatase 2C) (Pyruvate dehydrogenase phosphatase catalytic subunit 1) (PDPC 1) (Q9P0J1)
Organism: Homo sapiens (Human)
Function: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19184109}.
Interaction partners:
- Pyruvate dehydrogenase protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Protein phosphatase PTC7 homolog
- Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Secreted frizzled-related protein 4
- PH domain leucine-rich repeat-containing protein phosphatase 1
- Protein phosphatase 1A
Sequence:
MPAPTQLFFPLIRNCELSRIYGTACYCHHKHLCCSSSYIPQSRLRYTPHPAYATFCRPKENWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSILGFDSNQLPANAPIEDRRSAATCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNSLRTYWQELIDLNTGESTDIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNERELERLKLEHPKSEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYHTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRTKMSSVFEDQNAATHLIRHAVGNNEFGTVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQE
Protein: Platelet-derived growth factor receptor-like protein (A4JYS7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGHSWFLRTVLLLFALPEGWSKPVITPDAPHLVILKGKQLYLRCHDDADVNAGRVRWLRDKGRRIEGELKDDEASVILLNITETQHMGNYTCENTETEEKSSIYIYVKDLGSAFVRRMVNDLQVRKGEEITLPCLVTDPAVSHLSLQTCNGSALPAALTFITHPQGGITIRNVSKAFEGCYFCAGQLDQKPVKSREYNLVVRLGE
Protein: Processive diacylglycerol beta-glycosyltransferase (EC 2.4.1.-) (Beta-diglycosyldiacylglycerol synthase) (Beta-DGS) (DGlyDAG synthase) (Beta-monoglycosyldiacylglycerol synthase) (Beta-MGS) (MGlyDAG synthase) (Glycosyl-beta-1,6-glycosyldiacylglycerol synthase) (UDP-galactose:1,2-dioleoylglycerol 3-beta-D-galactosyltransferase) (UDP-glucose:1,2-dioleoylglycerol 3-beta-D-glucosyltransferase) (Q9ZB73)
Organism: Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) (Mycoplasmoides genitalium)
Function: Processive glycosyltransferase involved in the biosynthesis of both the non-bilayer-prone beta-monoglycosyldiacylglycerol and the bilayer-forming membrane lipid beta-diglycosyldiacylglycerol. These components contribute to regulate the properties and stability of the membrane. Catalyzes sequentially the transfers of glucosyl or galactosyl residues from UDP-Glc or UDP-Gal to diacylglycerol (DAG) acceptor to form the corresponding beta-glycosyl-DAG (3-O-(beta-D-glycopyranosyl)-1,2-diacyl-sn-glycerol), which then acts as acceptor to give beta-diglycosyl-DAG product (3-O-(beta-D-glycopyranosyl-beta-(1->6)-D-glycopyranosyl)-1,2-diacyl-sn-glycerol). Dioleoylglycerol (DOG) is a preferred sugar acceptor than 3-O-(beta-D-glucopyranosyl)-1,2-dioleoyl-sn-glycerol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21835921}.
Interaction partners:
- Uncharacterized glycosyltransferase MG025
- Co-chaperonin GroES
- Uncharacterized glycosyltransferase MG060
- UTP--glucose-1-phosphate uridylyltransferase
- Chaperonin GroEL
Sequence:
MDKLVSILVPCYKSKPFLKRFFNSLLKQDLNQAKIIFFNDNVADETYEVLQKFKKEHNNLAIEVYCDKQNEGIGKVRDKLVNLVTTPYFYFIDPDDCFNNKNVIKEIVESIKKEDFDLGVLKSMVYLCFLKHDFIIKFLPLKGIFQGRVKLINNNNVNKLNYIKNNDQYIWNIVINTDFFRKLNLTFESRLFEDIPIWYPMFFSSQKIVFIDVIGTNYFIRNDSLSTTISAPRYLNLIQCYEKLYVNLSQNGSLASFIDPNHKIEARFWRRQMFVWFALFSFEYFKKNFSESKKILEKLFVFLEKNGVYERVFQTKNQGIYYIWVQRLKYFKHVLESKSDN