wanglab/gogpt-training-data huggingface dataset:
Protein: RNA-directed RNA polymerase (RDRP) (EC 2.7.7.48) (Protein VP1) (P22173)
Organism: Infectious pancreatic necrosis virus (strain Jasper) (IPNV)
Function: RNA-dependent RNA polymerase which is found both free and covalently attached to the genomic RNA. May also contain guanylyl and methyl transferase activities (By similarity).
Subcellular location: Virion {ECO:0000250}. Note=Minor amounts are incorporated in the virion. {ECO:0000250}.
Interaction partners:
Sequence:
MSDIFNSPQNKASILTALMKSTTGDVEDVLIPKRFRPAKDPLDSPQAAAQFLKDNKYRILRPRAIPTMVELETDAALPRLRQMVEDGKLKDTVSVPEGTTAFYPKYYPFHKPDHDEVGTFGAPDITLLKQLTFFLLENDFPTGPETLRQVREAIATLQYGSGSYSGQLNRLLAMKGVATGRNPNKTPKTVGYTNEQLAKLLEQTLPINTPKHEDPDLRWAPSWLINYTGDLSTDKSYLPHVTIKSSAGLPYIGKTKGDTTAEALVLADSFIRDLGRAATSADPEAGVKKTITDFWYLSCGLLFPKGERYTQVDWDKKTRNIWSAPYPTHLLLSMVSTPVMNESKLNITNTQTPSLYGFSPFHGGMDRIMTIIRDSLDNDEDLVMIYADNIYILQDNTWYSIDLEKGEANCTPQHMQAMMYYLLTRGWTNEDGSPRYNPTWATFAMNVAPSMVVDSSCLLMNLQLKTYGQGSGNAFTFLNNHLMSTIVVAEWVKAGKPNPMTKEFMDLEEKTGINFKIERELKNLRETIVEAVETAPQDGYLADGSDLPPIRPGKAVELDLLGWSAIYSRQMEMFVPVLENERLIASAAYPKGLENKALARKPGAEIAYQIVRYEAIRLVGGWNNPLLETAAKHMSLDKRKRLEVKGIDVTGFLDDWNNMSEFGGDLEGITLSEPLTNQTLVDINTPLDSFDPKARPQTPRSPKKTLDEVTTAITSGTYKDPKSAVWRLLDQRTKLRVSTLRDQALALKPASSSVDNWAEATEELAQQQQLLMKANNLLKSSLTETREALETIQSDKIIAGKSNPEKNPGTAANPVVGYGEFSEKIPLTPTQKKNAKRREKQRRNQ
Protein: Pentatricopeptide repeat-containing protein At3g29230 (Q9LS72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat
- Pentatricopeptide repeat-containing protein At4g21190
- Uncharacterized protein At3g49140
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE homolog, chloroplastic
- Protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 3
Sequence:
MTSSLPVRAPSWVSSRRIFEERLQDLPKCANLNQVKQLHAQIIRRNLHEDLHIAPKLISALSLCRQTNLAVRVFNQVQEPNVHLCNSLIRAHAQNSQPYQAFFVFSEMQRFGLFADNFTYPFLLKACSGQSWLPVVKMMHNHIEKLGLSSDIYVPNALIDCYSRCGGLGVRDAMKLFEKMSERDTVSWNSMLGGLVKAGELRDARRLFDEMPQRDLISWNTMLDGYARCREMSKAFELFEKMPERNTVSWSTMVMGYSKAGDMEMARVMFDKMPLPAKNVVTWTIIIAGYAEKGLLKEADRLVDQMVASGLKFDAAAVISILAACTESGLLSLGMRIHSILKRSNLGSNAYVLNALLDMYAKCGNLKKAFDVFNDIPKKDLVSWNTMLHGLGVHGHGKEAIELFSRMRREGIRPDKVTFIAVLCSCNHAGLIDEGIDYFYSMEKVYDLVPQVEHYGCLVDLLGRVGRLKEAIKVVQTMPMEPNVVIWGALLGACRMHNEVDIAKEVLDNLVKLDPCDPGNYSLLSNIYAAAEDWEGVADIRSKMKSMGVEKPSGASSVELEDGIHEFTVFDKSHPKSDQIYQMLGSLIEPPDPGELVAVR
Protein: Myosin, light chain 1, alkali; skeletal, fast (Q6P0G6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function.
Interaction partners:
- Myosin regulatory light chain 2, skeletal muscle isoform A
- Myosin heavy chain, fast skeletal muscle
- Myosin, heavy polypeptide 2, fast muscle specific isoform X1
- Myosin, light chain 9a, regulatory
- Myosin regulatory light polypeptide 9b
- Myosin, light chain 12, genome duplicate 2
- Myosin, light chain 12, genome duplicate 1
- Myosin regulatory light chain 2, skeletal muscle isoform B
- Nebulin.
- Myosin heavy chain 4
Sequence:
MAPKKDAKKPEPPKKAEPAPAPAPAPEPPKADAVDLSGVKLDFTQDQMEDYREAFLLFDRVGDSKVAYNQIADIMRALGQNPTNKEVTKILGNPTADDMVNKRVDFEGFLPMLQVVINNPNKATYDDYVEGLRVFDKEGNGTVMGAELRIVLSTLGEKMSEAEIDALMQGQEDENGCVNYEAFVKHIMSV
Protein: Monocarboxylate transporter 2 (MCT 2) (Solute carrier family 16 member 7) (O60669)
Organism: Homo sapiens (Human)
Function: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:32415067}; Multi-pass membrane protein {ECO:0000269|PubMed:32415067}. Basolateral cell membrane {ECO:0000250|UniProtKB:P53988}; Multi-pass membrane protein {ECO:0000269|PubMed:32415067}. Cytoplasm {ECO:0000250|UniProtKB:O70451}. Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By similarity). {ECO:0000250|UniProtKB:O70451, ECO:0000250|UniProtKB:Q63344}.
Interaction partners:
- Embigin
- Basigin
- Monocarboxylate transporter 4
- Sialin
- Monocarboxylate transporter 3
Sequence:
MPPMPSAPPVHPPPDGGWGWIVVGAAFISIGFSYAFPKAVTVFFKEIQQIFHTTYSEIAWISSIMLAVMYAGGPVSSVLVNKYGSRPVVIAGGLLCCLGMVLASFSSSVVQLYLTMGFITGLGLAFNLQPALTIIGKYFYRKRPMANGLAMAGSPVFLSSLAPFNQYLFNTFGWKGSFLILGSLLLNACVAGSLMRPLGPNQTTSKSKNKTGKTEDDSSPKKIKTKKSTWEKVNKYLDFSLFKHRGFLIYLSGNVIMFLGFFAPIIFLAPYAKDQGIDEYSAAFLLSVMAFVDMFARPSVGLIANSKYIRPRIQYFFSFAIMFNGVCHLLCPLAQDYTSLVLYAVFFGLGFGSVSSVLFETLMDLVGAPRFSSAVGLVTIVECGPVLLGPPLAGKLVDLTGEYKYMYMSCGAIVVAASVWLLIGNAINYRLLAKERKEENARQKTRESEPLSKSKHSEDVNVKVSNAQSVTSERETNI
Protein: Protein BEX2 (Brain-expressed X-linked protein 2 homolog) (Q9WTZ8)
Organism: Mus musculus (Mouse)
Function: Regulator of mitochondrial apoptosis and G1 cell cycle. Regulates the level of PP2A regulatory subunit B and PP2A phosphatase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3MKQ1}. Nucleus {ECO:0000250|UniProtKB:Q9BXY8}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 16
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-4
- Rhombotin-2
- Calmodulin 5
- Olfactory marker protein
Sequence:
MESKVEQGVKNLNMENDHQEKEEKEEKPQDASKRDPIVALPFEAGDYYVPRGGRRRFRVRQPIVHYRWDLMHRVGEPQGRMREENVQRFGDDVRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP
Protein: Nidogen-1 (NID-1) (Entactin) (P10493)
Organism: Mus musculus (Mouse)
Function: Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Laminin subunit gamma-1
- Fibronectin
- Vitronectin
- Agrin
- Laminin subunit beta-1
- Laminin subunit alpha-1
- Laminin subunit alpha-2
- Laminin subunit alpha-5
- Elastin
Sequence:
MLDASGCSWAMWTWALLQLLLLVGPGGCLNRQELFPFGPGQGDLELEAGDDVVSPSLELIGELSFYDRTDITSVYVTTNGIIAMSEPPATEYHPGTFPPSFGSVAPFLADLDTTDGLGNVYYREDLSPFIIQMAAEYVQRGFPEVSFQPTSVVVVTWESVAPYGGPSSSPAEEGKRNTFQAVLASSNSSSYAIFLYPEDGLQFFTTFSKKDESQVPAVVGFSKGLVGFLWKSNGAYNIFANDRESIENLAKSSNAGHQGVWVFEIGSPATAKGVVSADVNLDLDDDGADYEDEDYDLVTSHLGLEDVATPSPSHSPRRGYPDPHNVPRILSPGYEATERPRGVPTERTRSFQLPAERFPQHHPQVIDVDEVEETGVVFSYNTGSQQTCANNRHQCSVHAECRDYATGFCCRCVANYTGNGRQCVAEGSPQRVNGKVKGRIFVGSSQVPVVFENTDLHSYVVMNHGRSYTAISTIPETVGYSLLPLAPIGGIIGWMFAVEQDGFKNGFSITGGEFTRQAEVTFLGHPGKLVLKQQFSGIDEHGHLTISTELEGRVPQIPYGASVHIEPYTELYHYSSSVITSSSTREYTVMEPDQDGAAPSHTHIYQWRQTITFQECAHDDARPALPSTQQLSVDSVFVLYNKEERILRYALSNSIGPVRDGSPDALQNPCYIGTHGCDSNAACRPGPGTQFTCECSIGFRGDGQTCYDIDECSEQPSRCGNHAVCNNLPGTFRCECVEGYHFSDRGTCVAAEDQRPINYCETGLHNCDIPQRAQCIYMGGSSYTCSCLPGFSGDGRACRDVDECQHSRCHPDAFCYNTPGSFTCQCKPGYQGDGFRCMPGEVSKTRCQLEREHILGAAGGADAQRPTLQGMFVPQCDEYGHYVPTQCHHSTGYCWCVDRDGRELEGSRTPPGMRPPCLSTVAPPIHQGPVVPTAVIPLPPGTHLLFAQTGKIERLPLERNTMKKTEAKAFLHIPAKVIIGLAFDCVDKVVYWTDISEPSIGRASLHGGEPTTIIRQDLGSPEGIALDHLGRTIFWTDSQLDRIEVAKMDGTQRRVLFDTGLVNPRGIVTDPVRGNLYWTDWNRDNPKIETSHMDGTNRRILAQDNLGLPNGLTFDAFSSQLCWVDAGTHRAECLNPAQPGRRKVLEGLQYPFAVTSYGKNLYYTDWKTNSVIAMDLAISKEMDTFHPHKQTRLYGITIALSQCPQGHNYCSVNNGGCTHLCLPTPGSRTCRCPDNTLGVDCIERK
Protein: Lactoylglutathione lyase (EC 4.4.1.5) (Glyoxalase I) (Q6XC06)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MATGSEASKAAETVVDWHKQDSKRMLHAVYRVGDLDRTIKYYTECFGMKLLRKRDVPDEKYTNAFLGFGPENTNFAVELTYNYGVDKYDIGTGFGHFAIANDDVYKLAENIKSKGGKITREPGPVKGGSTVIAFAQDPDGYMFELIQRADTPEPLCQVMLRVGDLERSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVLELTYNYGVTEYSKGNAYAQVAIGTNDVYKSAEAVDLATKELGGKILRQPGPLPGINTKIASFVDPDGWKVVLVDNTDFLKELQ
Protein: Protein CLN8 (Q9UBY8)
Organism: Homo sapiens (Human)
Function: Could play a role in cell proliferation during neuronal differentiation and in protection against cell death.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10861296}; Multi-pass membrane protein {ECO:0000269|PubMed:10861296}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:10861296}; Multi-pass membrane protein {ECO:0000269|PubMed:10861296}. Endoplasmic reticulum {ECO:0000269|PubMed:19941651}.
Interaction partners:
- Ceroid-lipofuscinosis neuronal protein 6
- Bis
- Palmitoyl-protein thioesterase 1
- Battenin
- Major facilitator superfamily domain-containing protein 8
- DnaJ homolog subfamily C member 5
- BTB/POZ domain-containing protein KCTD7
- Cathepsin D
- Tripeptidyl-peptidase 1
Sequence:
MNPASDGGTSESIFDLDYASWGIRSTLMVAGFVFYLGVFVVCHQLSSSLNATYRSLVAREKVFWDLAATRAVFGVQSTAAGLWALLGDPVLHADKARGQQNWCWFHITTATGFFCFENVAVHLSNLIFRTFDLFLVIHHLFAFLGFLGCLVNLQAGHYLAMTTLLLEMSTPFTCVSWMLLKAGWSESLFWKLNQWLMIHMFHCRMVLTYHMWWVCFWHWDGLVSSLYLPHLTLFLVGLALLTLIINPYWTHKKTQQLLNPVDWNFAQPEAKSRPEGNGQLLRKKRP
Protein: ER membrane protein complex subunit 8 (Neighbor of COX4) (Protein FAM158B) (O43402)
Organism: Homo sapiens (Human)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22119785}; Peripheral membrane protein {ECO:0000305|PubMed:32439656}; Cytoplasmic side {ECO:0000269|PubMed:32439656}.
Interaction partners:
- Endoplasmic reticulum membrane protein complex subunit 7
- ER membrane protein complex subunit 5
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 10
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 2, mitochondrial
Sequence:
MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPLFHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFSDTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRNDWTNPEINKAVLHLC
Protein: Carboxylic ester hydrolase (EC 3.1.1.-) (Q86L18)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNKLLVFILLLLLLINISFARKRSYIKNTDASIVVTQFGAIKGIVEDTHRVFYGVPFAQPPVNQLRWENPIDLKPWENVRETLTQRSQCAQKCNLGPGVCSPIGTSEDCLYLDVFTPKDATPNSKYPVIVYIPGGAFSVGSGSVPLYDATKFAQSSVIVVNINYRLGVLGFMGTDLMHGNYGFLDQIKALEWVYNNIGSFGGNKEMITIWGESAGAFSVSAHLTSTYSRQYFNAAISSSSPLTVGLKDKTTARGNANRFATNVGCNIEDLTCLRGKSMDEILEAQEKVGLTFGDKILDAFTIWSPVIDGDIIPMQPLTAVKEGKTYDVPTIIGSVKHEAIPFIYSFFQDIVGIDYYRVLVAIVFPLNAMKILPLYPAAPRGQDSRPILSELITDYLFRCPDRYHTVTNAKKLSSPTYHYYYVHVKSTGHSLDACDDKVCHGTELSLFFNSYELMGERLDNDEKELAIDINNYIVNFATTHNPNTGLDVPIQWRQVTSTQNSTLILETTIETKDTFTNDPKCNALDLTYYRNQVRP
Protein: AKT serine/threonine kinase 2 (J3QKW1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDT
Protein: Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (EC 2.4.3.7) (GalNAc alpha-2,6-sialyltransferase III) (ST6GalNAc III) (ST6GalNAcIII) (STY) (Sialyltransferase 7C) (SIAT7-C) (Q8NDV1)
Organism: Homo sapiens (Human)
Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Alpha-2-HS-glycoprotein
Sequence:
MACILKRKSVIAVSFIAAFLFLLVVRLVNEVNFPLLLNCFGQPGTKWIPFSYTYRRPLRTHYGYINVKTQEPLQLDCDLCAIVSNSGQMVGQKVGNEIDRSSCIWRMNNAPTKGYEEDVGRMTMIRVVSHTSVPLLLKNPDYFFKEANTTIYVIWGPFRNMRKDGNGIVYNMLKKTVGIYPNAQIYVTTEKRMSYCDGVFKKETGKDRVQSGSYLSTGWFTFLLAMDACYGIHVYGMINDTYCKTEGYRKVPYHYYEQGRDECDEYFLHEHAPYGGHRFITEKKVFAKWAKKHRIIFTHPNWTLS
Protein: Ferric enterobactin transport protein FepE (P26266)
Organism: Escherichia coli (strain K12)
Function: Part of the ferric enterobactin transport system.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Enterobactin synthase component F
- Iron
- Ferrienterobactin receptor
Sequence:
MSSLNIKQGSDAHFPDYPLASPSNNEIDLLNLISVLWRAKKTVMAVVFAFACAGLLISFILPQKWTSAAVVTPPEPVQWQELEKSFTKLRVLDLDIKIDRTEAFNLFIKKFQSVSLLEEYLRSSPYVMDQLKEAKIDELDLHRAIVALSEKMKAVDDNASKKKDEPSLYTSWTLSFTAPTSEEAQTVLSGYIDYISTLVVKESLENVRNKLEIKTQFEKEKLAQDRIKTKNQLDANIQRLNYSLDIANAAGIKKPVYSNGQAVKDDPDFSISLGADGIERKLEIEKAVTDVAELNGELRNRQYLVEQLTKAHVNDVNFTPFKYQLSPSLPVKKDGPGKAIIVILSALIGGMVACGGVLLRYAMASRKQDAMMADHLV
Protein: SPARC-like protein 1 (Extracellular matrix protein 2) (Matrix glycoprotein Sc1) (P70663)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Myocilin
- Pleiotrophin
- Major prion protein
- Neuroligin-1
- Neurexin-1
Sequence:
MKAVLLLLCALGTAVAIPTSTRFLSDHSNPTTATLVTPEDATVPIAGVEATADIENHPSDKAEKPSALNSEEETHEQSTEQDKTYSFEVDLKDEEDGDGDLSVDPTEGTLTLDLQEGTSEPQQKSLPENGDFPATVSTSYVDPNQRANITKGKESQEQPVSDSHQQPNESSKQTQDLKAEESQTQDPDIPNEEEEEEEDEEEEEEEEPEDIGAPSDNQEEGKEPLEEQPTSKWEGNREQSDDTLEESSQPTQISKTEKHQSEQGNQGQESDSEAEGEDKAAGSKEHIPHTEQQDQEGKAGLEAIGNQKDTDEKAVSTEPTDAAVVPRSHGGAGDNGGGDDSKHGAGDDYFIPSQEFLEAERMHSLSYYLKYGGGEETTTGESENRREAADNQEAKKAESSPNAEPSDEGNSREHSAGSCTNFQCKRGHICKTDPQGKPHCVCQDPETCPPAKILDQACGTDNQTYASSCHLFATKCRLEGTKKGHQLQLDYFGACKSIPACTDFEVAQFPLRMRDWLKNILMQLYEPNPKHGGYLNEKQRSKVKKIYLDEKRLLAGDHPIELLLRDFKKNYHMYVYPVHWQFNELDQHPADRILTHSELAPLRASLVPMEHCITRFFEECDPNKDKHITLKEWGHCFGIKEEDIDENLLF
Protein: Tetratricopeptide repeat domain 39A (U5GXS1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTALDLFLTNQFSEALSYLKPRTKESMYHSLTYATILEMQAMMTFDPQDILLAGNMMKEAQMLCQRHRRKSSVTDSFSSLVNRPTLGQFTEEEIHAEVCYAECLLQRAALTFLQGSSHGGAVRPRALHDPSHACSCPPGPGRQHLFLLQDENMVSFIKGGIKVRNSYQTYKELDSLVQSSQYCKGENH
Protein: Uncharacterized AIM2 family protein C30D10.14 (O14359)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MASCCPTSRGAAASNKSYTFKGKEIENFGGLTTYVVGSTSNTRVLIGFMDIFGLSDQIKEGADKLADDGFTVYLPDFLEGKPLPVTALPPKTPEDQKLCNDFFSTRISPNLHWPKLAKVVEAVRANHGPNVTIGTYGFCWGAKVLVTYPATIDFVGIASCHPSFPDSADAANVHCPVLFLCSKDEDAKIIKEWEEAFKTNPAYAKSSFETFSDMFHGWMAARADLSNPEQRKRFDEGYQKVSSFFQSLM
Protein: Rapamycin-insensitive companion of Tor, isoform B (X2JL73)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASQHSSWRFGKRSKLQLRIKVSQDPEDFYRLDPQRSAAENAFEIYSMLCLEETRDTKRLFLLNALASLCLGARKGSHHSNIRFTTEELLYCLSASLVHTFTQVRAAALRTIRYAISTPNDIKTFNALQLQHLLCRSIDLMLKNDDERVQALKLVRKMLAIAPEDISPAVVRCLVSLADSGIEENDNLLRACLATLAEFAVLNPALLIVCGGVTSITRNVLECHNPRIAESLCGVLLYLLEWPQTRNICGVRLDCLAAPYCDFTYRQSIVDKNKDARELRYTSCRLALLSVLRSWTGTLEFCDPSKPSGLKAIVDALYLNQIEVRKAILDLLYELLTLPQPTWTDDYAVALQAVDPSDFQDTWLLSNGFVSAEGRSILPTLAARAPSVVEQHLALMLYCFLETGLLNALVEVVVSSDQFVSVQATVLIGKILQLMHTHLPPDICCTSPALPTLVSHATLGNQQANAAVAALQNYQKLLRQRPASRSLFLDSIIQGGALIQTRLFRRHLNVQEQAGPVLQLQETAEAAAFAVPPVTQFRGTLDRSRLDSVSSSDESNSQASTSSRSSFRLKHSRVLSQADAHLWDWDVITTILKSNLIRKLDYTQGKFLKRLVDFYKPRNNRFSHQDLVPGQRLPTYVSAGLDLIDVLLSSNELECMRFITDYFSDISQQLAAVTTSNRAHDCLFSPQHMNNTMCQQYFLYIGRMCRTVKGIEVLKNTTVFEYLINLVRVTDHVCYVKLIVSGLNYSYEKLPRQVLEKALTSAKTRGRLYSTQFMAVLLRARLPHFEVWGIPLIINQTRDSDRSVGLAAMDVLEEACHDKYYLEEIVSRWPNLTHRGDAGRLLMARYYSLPRGLNSTMARIEDEIRYWRNGYNKRYVLLVEADTHSSLTLHIRNEDGYYSRRNCNQRPQTVPPNVAPHLYGQMAQTGQGMTALRKHGDLPQLLELLRRAKCTDDAECLELKAAIWALAHASTHSNGIEYFVELNARLYEKLIVLVTKCEVYSVRATCFSALGLIAGTQAGANILFKLNWLSVRHDKNTMWPVHQPEDWMSSQYTPVRHYYEDVPADNMTMMDDYIERFYETGSDFWHMLADQTDASGGGGGVAGTVVGMHPIVQDPNATITTTDSVRTTTDDVHPRMLVGVAAKSKTLPEGSNLRQGKHQRSLSESKTTDVISLLGSGVGTMSGAVLYPTPYQHRIRYNSCTDSNTSGVSSCESVTGRTAAAYAAAANELQQFPLSPIPSMSNLLESDELFRRNQLATSMLPSTLSPMAMKGYVQLRSLRKHSRPVFSESSAEFYDFAEILDTPEVQMRKLDWTHSHRRLKVRSLDRQLSDVYRRLSADELNVLLPTLNAPKFLPPNDLKGPCYAGICLPKNVLDLFPTRNLSRTYVSRDIQDQDIVGINLLNTMLRPQCLNDSLTNEGGDESSVISSLSDVSSASRRQTRQLQQGAKHSRSLCLHCARSPRQQRNDSGSHSNGGGGASLAPCELYSSAAAALVAAGIQAGPVLAKKSGSSAQGASAALGADISFHSPESMLSEDSLPDRLTASILYNVQRLANPVSAKQSKMALLELKQKHPHAFQDICLYSEACKTIGRSSYRMIARRFLQELFLDLNFDSFYVEPQLIIGARKFSAEEKAEATAPTAMQAMPFKQTILKPKPAAQLASVYETSWENLLMDQSPRINKSSPADQPANAQTKAKARNQLHIDDTESSLSSTDGENDSGEDVCDGSGAGTQASSVTTAHTALPTGNSNRSSIGTCTASQLVPGAATSNSAGAGTSASDNASTSLKNENRQFTRGRFYTLELDLSCTKNKFPIKNRSQRTPTPPPIESLIESKPTVQTDVNTSALPIMQRTGGSNDSSSALRYSTVTKSLSASMARPVGSLYCEKRLQSSKSEAVLDEVAKARRASGGVGLTTVRDNS
Protein: Centrosomal protein 43 (FGFR1 oncogene partner) (O95684)
Organism: Homo sapiens (Human)
Function: Required for anchoring microtubules to the centrosomes. Required for ciliation.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:16690081, ECO:0000269|PubMed:28659385}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385, ECO:0000269|PubMed:32946374}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:28659385}. Note=Associated with gamma-tubulin (PubMed:16314388). Localizes on both mother and daughter centrioles (PubMed:28428259, PubMed:28625565). Localizes to an axial position on the mother centriole (PubMed:28625565). Localizes to the distal end of the centriole partly on the subdistal appendage region (PubMed:28659385). {ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Centrosome-associated protein 350
- Centrosomal protein of 19 kDa
- Ribonuclease T2
- Fibroblast growth factor receptor 1
- Centriolin
- FGFR1 oncogene partner 2
- Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit gamma
- Unconventional myosin-XVIIIa
Sequence:
MAATAAAVVAEEDTELRDLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVENKTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIRRCQQKEKGPTTGEGALDLSDVHSPPKSPEGKTSAQTTPSKIPRYKGQGKKKTSGQKAGDKKANDEANQSDTSVSLSEPKSKSSLHLLSHETKIGSFLSNRTLDGKDKAGLCPDEDDMEGDSFFDDPIPKPEKTYGLRKEPRKQAGSLASLSDAPPLKSGLSSLAGAPSLKDSESKRGNTVLKDLKLISDKIGSLGLGTGEDDDYVDDFNSTSHRSEKSEISIGEEIEEDLSVEIDDINTSDKLDDLTQDLTVSQLSDVADYLEDVA
Protein: Putative caffeoyl-CoA O-methyltransferase At1g67980 (EC 2.1.1.104) (Trans-caffeoyl-CoA 3-O-methyltransferase) (CCoAMT) (CCoAOMT) (Q9C9W3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers (By similarity).
Interaction partners:
- Shikimate O-hydroxycinnamoyltransferase
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Chalcone synthase
- AT5g57840/MTI20_9
- Spermidine hydroxycinnamoyl transferase
- 4-coumarate--CoA ligase 4
- 4-coumarate--CoA ligase 1
- 4-coumarate--CoA ligase 2
- 4-coumarate--CoA ligase 3
Sequence:
MANEIPTKGILKSEALKQYIMETSAYPREHELLKELRKATVQKYGNLSEMEVPVDEGHFLSMLVKIMNAKNTIEIGVFTGYSLLTTALALPEDGRITAIDIDKEAYEVGLEFIKKAGVDHKINFIHSDGLKALDQLVNDKCEFDFAFADADKSSYVNFHERLLKLVKVGGIIAFDNTLWFGFVAEDEDGVPEHMREYRAALIEFNKKLALDPRVEVSQISIGDGITLCRRLV
Protein: Sodium/potassium-transporting ATPase subunit beta-2 (Adhesion molecule in glia) (AMOG) (Sodium/potassium-dependent ATPase subunit beta-2) (P14231)
Organism: Mus musculus (Mouse)
Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.
Subcellular location: Cell membrane; Single-pass type II membrane protein.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit beta-3
- Phospholemman
- Protein ATP1B4
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MVIQKEKKSCGQVVEEWKEFVWNPRTHQFMGRTGTSWAFILLFYLVFYGFLTAMFSLTMWVMLQTVSDHTPKYQDRLATPGLMIRPKTENLDVIVNISDTESWGQHVQKLNKFLEPYNDSIQAQKNDVCRPGRYYEQPDNGVLNYPKRACQFNRTQLGDCSGIGDPTHYGYSTGQPCVFIKMNRVINFYAGANQSMNVTCVGKRDEDAENLGHFVMFPANGSIDLMYFPYYGKKFHVNYTQPLVAVKFLNVTPNVEVNVECRINAANIATDDERDKFAGRVAFKLRINKT
Protein: Beta-lactamase HcpA (EC 3.5.2.6) (Cysteine-rich 28 kDa protein) (O25001)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Slowly hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives. May be involved in the synthesis of the cell wall peptidoglycan.
Subcellular location: Secreted {ECO:0000269|PubMed:9596777}.
Interaction partners:
Sequence:
MLGNVKKTLFGVLCLGTLCLRGLMAEPDAKELVNLGIESAKKQDFAQAKTHFEKACELKNGFGCVFLGAFYEEGKGVGKDLKKAIQFYTKGCELNDGYGCNLLGNLYYNGQGVSKDAKKASQYYSKACDLNHAEGCMVLGSLHHYGVGTPKDLRKALDLYEKACDLKDSPGCINAGYIYSVTKNFKEAIVRYSKACELKDGRGCYNLGVMQYNAQGTAKDEKQAVENFKKGCKSSVKEACDALKELKIEL