wanglab/gogpt-training-data huggingface dataset:
Protein: Kinesin-like protein (Q57WJ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQKSIQDEVRFSSSPRVLRSASRDTHKEMEELPNASSPLLMRRVASLDALPPRPSSRHPRSEGDSVPSVLNPNRQLEDLSRDTQLLNAYGGSDSMPGINKIPVKSFQQHLQGRQFHFAKHRLPQLSNVQSARSVSTPARKGRQSPRCRYNALPALSSSPPRTRRGASFARPYPNKPGTPQSSRAPPRRASARPIASPSSPLAAPLHRADSVIPAAVAEDSSADGKQSAVARTRGGRIRVVVRKRPLPPDEEGCDCVSMDPPNVKVAVRKQRVDLTEYADVNDFTFDDAFGEDKHNEHVFDSCCKELLETTLQGGSASCFAYGQTGSGKTHTMLGNSGERGLYILAAAAIFSSLEKDQEVYASLYEIYCNSLFDLLNNRSPVVVREDHNRRMHITGLTWHAVTSAEELQLLINSGADRRSTGSTTANERSSRSHAVLTIQVRDREDNRFCGTLNLVDLAGSERAADTATNDRQTRQEGAEINKSLLALKECIRALDEKKKHVPFRGSKLTEILRDSFIGNSRTVMIANISASSQNYEHTLNTLRYAFRVKGLSVVNFEPSRARNAPRPLKPVVSDMNPTQGVPQVNAGPLKTTPGRWRSVSSNAFLANRRNVSSGNALVQQRNHVTSSPLRSNNTQGANIASGAGENNFAVYVRQIAGEVVGNIIPQLRADGGRDSSLPSNSDYLQEEGSGVSFNDELIRQLEDRVVARMKLDVIRLVRDTMLRRERAISKLRSENTMLSKLNGALERRAAECAHCRGQNTRQIQQQQN
Protein: N-acetylated alpha-linked acidic dipeptidase-like 2 (A0A0N4SUJ3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MGENEAGLPNMSLQGKKMAYQKVKADLRTSGHSQYLDNDELQATALDLEWDMEKELEEPGFDQFQPDSAEHQNLGHSETLDLHLDSIQPATSPKGRFQRLQEESDCVTHYTRSAPKNNHCSFCYMLKILCIATTLFIFGIIIGYYAHMNCPSDASPSGTNNPQLYQDILKTIKAEDIKKSFRNWLQLYDSKDDMEIAKKIKSHWIALGLEDTQFINYSVLLDFPGSSPGTITLSSTGQCFYPDGQPCREEARGGHSQDLFFSYAAYSAKGTLQGDVIDVSYGTMDDLKRITKLKNTTNQIALLKLGKLPLLYKISLLEKAGFGGALLYIDPCDAAESSVLSSEPFVVTLNPGGDPSTPGYPSHDGSFRKSRTNLTSLLVQPISPSLVKMLISLPKLKMDKDACSPLELPHNEKRTVSLQVQTVTQFKTVSNVVGYLRGLTSPDRYIIVGSNHHAGYSYKGQEWASSTAVITAFIEAMMLRVKKGWRPERTIVFCSWGGTPWGKIGSYEWGEDFVKILQKNAVAYIGLHSPIRGNSSLYPVVSPSLQQLVIEKIKFTCMQRAQCLGANVSSVQIQGDADYFINHLGVPTVQFAYEDIKTLEGPSFLSEAIFPTHATKIEEVDPSFSLHEAITKLSGEVILQIANEPILPFNALDIALGVQNSLKGNEPSVPHLLALASRLRESAELFQSDEMRPANDPKERAPSRVRMLNDILQDLEKNFLVQWVPPGFYRNILYHLDEKTNQFSILKEAWEHCNPQTSNETFQEALSNVLNSINSAHISFKVGLDVFESVLLGKN
Protein: Protein ECM23 (Extracellular mutant protein 23) (SRD1 homolog 2) (Q02710)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in morphogenesis. May be involved in cell wall organization and biogenesis.
Interaction partners:
- Protein GAT3
Sequence:
MLYNKEQGTSGASSSGRRTKFHFDRFVQMVLFIAANPNYCCSVASIPKSGVTPDLKRADILEQKIKSLNSALSPKLKEESRLGGPLHNPSILPAPSFSSLPISSNGKKSLAGYRPKSRKKQTILPNGQPKECATCGDTWTSQWRSGPNGNVELCSRCGIAYRKKMEKKIRSQQSSDDGTKNFIFKNK
Protein: Teleost multiple tissue opsin 2b (R9R6G4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MSEEDRLTLLDEDWSDSPMETLSRAGFIALSVFLGFIMTFGFFNNLVVLVLFCKFKTLRTPVNMLLLNISISDMLVCMFGTTLSFASSVRGRWLLGRHGCMWYGFINSCFGIVSLISLVVLSYDRYSTLTVYHKRAPDYRKPLLAVGGSWLYSLIWTVPPLLGWSSYGLEGAGTSCSVSWTQRTAESHAYIICLFVFCLGLPVLVMVYCYGRLLYAVKQVGKIRKTAARKREYHVLFMVITTVVCYLLCWMPYGVVAMMATFGRPGIISPVASVVPSLLAKSSTVINPLIYILMNKQFYRCFRILFCCQRSLLQNGHSSMPSKTTVIQLNRRVNSNAVACTAQISTGTHNHDCSTHVTERSNPPEVIP
Protein: Protein E6 (P03126)
Organism: Human papillomavirus type 16
Function: Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000269|PubMed:16507364, ECO:0000269|PubMed:22483108}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006, ECO:0000269|PubMed:16507364, ECO:0000269|PubMed:22483108}.
Interaction partners:
Sequence:
MHQKRTAMFQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRHYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL
Protein: Fructoselysine 6-phosphate deglycase (EC 3.5.-.-) (P0AC00)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible conversion of fructoselysine 6-phosphate to glucose 6-phosphate and lysine. Functions in a fructoselysine degradation pathway that allows E.coli to grow on fructoselysine or psicoselysine.
Interaction partners:
- Fructoselysine 6-kinase
- Probable fructoselysine/psicoselysine transporter FrlA
- Fructoselysine 3-epimerase
- Probable fructoselysine utilization operon transcriptional repressor
- Fructose-like permease IIC component 1
- Clamp-binding protein CrfC
Sequence:
MLDIDKSTVDFLVTENMVQEVEKVLSHDVPLVHAIVEEMVKRDIDRIYFVACGSPLNAAQTAKHLADRFSDLQVYAISGWEFCDNTPYRLDDRCAVIGVSDYGKTEEVIKALELGRACGALTAAFTKRADSPITSAAEFSIDYQADCIWEIHLLLCYSVVLEMITRLAPNAEIGKIKNDLKQLPNALGHLVRTWEEKGRQLGELASQWPMIYTVAAGPLRPLGYKEGIVTLMEFTWTHGCVIESGEFRHGPLEIVEPGVPFLFLLGNDESRHTTERAINFVKQRTDNVIVIDYAEISQGLHPWLAPFLMFVPMEWLCYYLSIYKDHNPDERRYYGGLVEY
Protein: Thialysine N-epsilon-acetyltransferase (EC 2.3.1.-) (O17731)
Organism: Caenorhabditis elegans
Function: Catalyzes the N-acetylation of the amino acid thialysine (S-(2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene group substituted with a sulfur. Substrate specificity: thialysine > O-(2-aminoethyl)-L-serine > S-(2-aminoethyl)-D,L-homocysteine. Does not act on polyamines, such as spermidine and spermine, nor on diamines putrescine and cadaverine.
Interaction partners:
Sequence:
MKNFEIVTVTPDHAEQLISMIHELAEFEKMKSSVVNTAEKLRKDIENKAVHGFIAFIGEEPAGMNLFYYAYSTWVGQYLHMEDLYIRPQFRRMGLARTLWKKLAELARDKGIVRLEWAVLDWNKNAIALYDTVDYVNLTKSEGWFTFRMDGAAINKFADE
Protein: Dyslexia-associated protein KIAA0319 homolog (Q5SZV5)
Organism: Mus musculus (Mouse)
Function: Involved in neuronal migration during development of the cerebral neocortex. May function in a cell autonomous and a non-cell autonomous manner and play a role in appropriate adhesion between migrating neurons and radial glial fibers. May also regulate growth and differentiation of dendrites (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5VV43}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q5VV43}. Early endosome membrane {ECO:0000250|UniProtKB:Q5VV43}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q5VV43}.
Interaction partners:
- Doublecortin domain-containing protein 2
- Dynein axonemal assembly factor 4
- Tyrosyl-DNA phosphodiesterase 2
- Acyl-coenzyme A thioesterase 13
Sequence:
MVSPPGVLSSLLLLAAMAGGSSQQCSEGRTYSDAIISPNPETIRIMRVSQTFSVGDCTAACCDLLTCDLAWWFEGSCYLVKCMRSENCEPRTTGPIRSYLTFVRRPVQRPGQLLDYGDMMLSRGSPSGAWGDSLEDLRKDLPFLGKDGGPEETTEYSDEYKDLERGLLQPSNQQDPRGSAEYPDWSLLPSNEGGFNATATGDNSAASMEKLQDPTPHPLDQEQLQALNESTWSPTPGHSSISSVWPSSASPLPTEEGLEGEETLQLQEQPSNSSGKEVPMPSHNPSPASLESSPATTEKNSNFTVTPRSRKHSTPTFPTSTVLTGLTPPPWPLSPTASRTVKALAVSAGDNLVLTLPDREAELKASVEPAPPADTTYSYEWSLMSHPVDFQGKIKQENKPTLHLSQLSVGLYAFRVAVSSENAFGEGYVNVTVMPAARVNQPPVAVVSPQTQELSVPLTSALIDGSQSTDDTEIVSYHWEEVDGPFLGEEFPADTPILRLSNLVPGNYTFRLTITDSDGATNSTTASLVIRDAVDYPPVANAGPNQTITLPQNTIILNGNQSSDDHQIVLYEWFAGPGGESKEMVMQGAQTPYLHLSELQEGEYTFQLMVTDSSGQQSTALVAVTVQAENNQAPVAVAGPDKELVFPVQSATLDGSRSSDDHGIVCYHWEHIRGPSAVEMENVDKAIATVTGLQVGIYHFRLTVRDQQGLSSTSTLTVAVKKENNSPPRAQAGGRHVLILPNNSITLDGSRSTDDRGIVSYLWIRDGQSPAAGDVIGGSDHRAALQLTNLVEGVYTFHLLVTDSQGASDSDAATVEVLPDPKKDGLVELILQVGVEQLTEQQKETLVRQLAVLLNVLDSDVKVLKIQAHTDVSTVIVFYVQSGSPFKVLRAAAVARNLHKRLSKEKEAFLLFKVLRVDTAGCLLKCSGHGHCDPITKRCICSQLWMENLIQRYMWDGESNCEWSVFYVAALALTLTLLTGAVSWLCICCCRRRKRTKIRKKTKYTILDSMDEQERMELRPKYGIKHRSTEHNSSLMVSESEFESDQDTLFSRERMERGVLKGSLNGCARNGVSFGYYSKDR
Protein: Mycobactin import ATP-binding/permease protein IrtA (EC 7.2.2.-) (Iron-regulated transporter A) (P9WQJ9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex IrtAB involved in the import of iron-bound mycobactin (Fe-MBT) and carboxymycobactin (Fe-cMBT) (By similarity). Mycobactins are then reduced by the siderophore interaction domain to facilitate iron release in the bacterial cell (By similarity). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity). Required for replication in human macrophages and in mouse lungs.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:18461140}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:18461140}.
Interaction partners:
- Mycobactin import ATP-binding/permease protein IrtB
- Phenyloxazoline synthase MbtB
- Salicyl-AMP ligase / salicyl-S-ArCP synthetase
- Salicylate synthase
- ESX-3 secretion system protein EccA3
- Protein Rv3402c
- Lysine N-acyltransferase MbtK
- Polyketide synthase Pks13
- Conserved ATPase
- L-lysine N6-monooxygenase MbtG
Sequence:
MARGLQGVMLRSFGARDHTATVIETISIAPHFVRVRMVSPTLFQDAEAEPAAWLRFWFPDPNGSNTEFQRAYTISEADPAAGRFAVDVVLHDPAGPASSWARTVKPGATIAVMSLMGSSRFDVPEEQPAGYLLIGDSASIPGMNGIIETVPNDVPIEMYLEQHDDNDTLIPLAKHPRLRVRWVMRRDEKSLAEAIENRDWSDWYAWATPEAAALKCVRVRLRDEFGFPKSEIHAQAYWNAGRAMGTHRATEPAATEPEVGAAPQPESAVPAPARGSWRAQAASRLLAPLKLPLVLSGVLAALVTLAQLAPFVLLVELSRLLVSGAGAHRLFTVGFAAVGLLGTGALLAAALTLWLHVIDARFARALRLRLLSKLSRLPLGWFTSRGSGSIKKLVTDDTLALHYLVTHAVPDAVAAVVAPVGVLVYLFVVDWRVALVLFGPVLVYLTITSSLTIQSGPRIVQAQRWAEKMNGEAGSYLEGQPVIRVFGAASSSFRRRLDEYIGFLVAWQRPLAGKKTLMDLATRPATFLWLIAATGTLLVATHRMDPVNLLPFMFLGTTFGARLLGIAYGLGGLRTGLLAARHLQVTLDETELAVREHPREPLDGEAPATVVFDHVTFGYRPGVPVIQDVSLTLRPGTVTALVGPSGSGKSTLATLLARFHDVERGAIRVGGQDIRSLAADELYTRVGFVLQEAQLVHGTAAENIALAVPDAPAEQVQVAAREAQIHDRVLRLPDGYDTVLGANSGLSGGERQRLTIARAILGDTPVLILDEATAFADPESEYLVQQALNRLTRDRTVLVIAHRLHTITRADQIVVLDHGRIVERGTHEELLAAGGRYCRLWDTGQGSRVAVAAAQDGTR
Protein: Phospholipase A and acyltransferase 5 (Ca(2+)-independent N-acyltransferase) (iNAT) (EC 2.3.1.-, EC 3.1.1.32, EC 3.1.1.4) (H-rev107-like protein 5) (HRAS-like suppressor 5) (HRSL5) (Rat LRAT-like protein-1) (RLP-1) (Q4KLN5)
Organism: Rattus norvegicus (Rat)
Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17158102}.
Interaction partners:
Sequence:
MIPGHRGPWSAPLCRRLVPAGHSGMGLSPAASGEYGIRLFRVPWPSRPKQISRTASTESSDTQPTNDSASSQALVVQFLPKLPKQDRGLEQARSLRQGQKPEINLELIPSKKRTEMIPSSDSEIEGNLKNQAAESNQKPRPGDLIEIFRIGYEHWAIYVEDDCVVHLAPPSEFEAGSITSIFSNRAVVKYSRLQDVLHGCSWKINNKLDGTYLPLPVDKIIQRTKNMINKIVQYSLIEGNCEHFVNDLRYGVPRSQQVEHVLVEGAKAAGAVLSAVVDSIRPKPITA
Protein: Male-enhanced antigen 1 (MEA-1) (Q64327)
Organism: Mus musculus (Mouse)
Function: May play an important role in spermatogenesis and/or testis development.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- Kelch domain-containing protein 3
Sequence:
MAAVVLGGDTMGPERIFPNQTEDLGPHQGPTEGTGDWSSEEPEEEQEETGAGPAGYSYQPLNQDPEQEEVELAPVGEGEDGAADIQDRIQALGLHLPDPPLESEDEDEEGAAALSSHSSIPMDPEHVELVKRTMAGVSLPAPGVPAWAREISDAQWEDVVQKALQARQASPAWK
Protein: Glucocorticoid receptor (Nuclear receptor subfamily 3 group C member 1) (E5KQF5)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHENVMWLKPESTSHTLI
Protein: Nibrin homolog (Nijmegen breakage syndrome 1 protein) (AtNbs1) (Q0H8D7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the MRE11-RAD50-NBN complex (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex may be involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, and cell cycle checkpoint control. Functions also in the very early stages of meiosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O60934}. Chromosome {ECO:0000250|UniProtKB:O60934}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:O60934}.
Interaction partners:
- Double-strand break repair protein MRE11
- DNA repair protein RAD50
- Serine/threonine-protein kinase ATM
- Serine/threonine-protein kinase ATR
- Chlorophyll a-b binding protein 3, chloroplastic
- Protein BREAST CANCER SUSCEPTIBILITY 1 homolog
- Dentin sialophosphoprotein-like protein
- BRCA1-associated RING domain protein 1
- ATP-dependent DNA helicase 2 subunit KU70
- ATP-dependent DNA helicase 2 subunit KU80
Sequence:
MVWGLFPVDPLSGEDKYYIFSKGIYKVGRKGCDIIINKDKGVSRIHAELTFDATTVSTSRRNKSSSDTSSFVIRVKDCSKYGTFVKTDLGTKDKVHELSNKEKILQDGDVIAFGTGSAIYRLSLIPLVFYLCPSSETFKVDQPVQDAVSSIGARISPTLSEECTHVLLEPRMQVNEALINAILAKKTIILTNWVMLLAEKSICSEIPGYSQYRPSVMVEEALVDVLELNVREKCLEGFTFVLEPTDTYRFGCSFPSLLEVCGAETVTIEDISSMSQDSQFGEINRMICVIPKSAGDKFGRFKHLSLLSRVNEMDLVCAVFSGNLPSTSLIPPSVVISSSCSTDETVVADSEAEEEETTSSVHMIDATEKAETPEKPAAIVIEDSPVTILEETSNLNEFKSVNLLADTESRGHMDEKNSSDSVTIRRDRNDEAETGKSEIIYTQDLIVRDLRSTRKVQSTGGEGVVDFKRFRKGNVTCGNSFSSLIPFAKDPYKEYDSWDVTDFMKEEKKRKQMEAIAEDLFKTEKARKRGTAGSIRGFLSGS
Protein: Penicillin-binding protein 1B (PBP-1b) (PBP1b) (Murein polymerase) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.99.28) (Peptidoglycan TGase) (Peptidoglycan glycosyltransferase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)] (P02919)
Organism: Escherichia coli (strain K12)
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Subcellular location: Cell inner membrane; Single-pass type II membrane protein.
Interaction partners:
- Peptidoglycan D,D-transpeptidase FtsI
- Cell division protein FtsN
- Penicillin-binding protein activator LpoB
- Probable peptidoglycan glycosyltransferase FtsW
- Peptidoglycan D,D-transpeptidase MrdA
- Penicillin-binding protein 1A
- Peptidoglycan glycosyltransferase MrdB
- Cell division coordinator CpoB
- D-alanyl-D-alanine carboxypeptidase DacB
- Penicillin-binding protein activator LpoA
Sequence:
MAGNDREPIGRKGKPTRPVKQKVSRRRYEDDDDYDDYDDYEDEEPMPRKGKGKGKGRKPRGKRGWLWLLLKLAIVFAVLIAIYGVYLDQKIRSRIDGKVWQLPAAVYGRMVNLEPDMTISKNEMVKLLEATQYRQVSKMTRPGEFTVQANSIEMIRRPFDFPDSKEGQVRARLTFDGDHLATIVNMENNRQFGFFRLDPRLITMISSPNGEQRLFVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGASTLTQQLVKNLFLSSERSYWRKANEAYMALIMDARYSKDRILELYMNEVYLGQSGDNEIRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASIYNPWRNPKLALERRNLVLRLLQQQQIIDQELYDMLSARPLGVQPRGGVISPQPAFMQLVRQELQAKLGDKVKDLSGVKIFTTFDSVAQDAAEKAAVEGIPALKKQRKLSDLETAIVVVDRFSGEVRAMVGGSEPQFAGYNRAMQARRSIGSLAKPATYLTALSQPKIYRLNTWIADAPIALRQPNGQVWSPQNDDRRYSESGRVMLVDALTRSMNVPTVNLGMALGLPAVTETWIKLGVPKDQLHPVPAMLLGALNLTPIEVAQAFQTIASGGNRAPLSALRSVIAEDGKVLYQSFPQAERAVPAQAAYLTLWTMQQVVQRGTGRQLGAKYPNLHLAGKTGTTNNNVDTWFAGIDGSTVTITWVGRDNNQPTKLYGASGAMSIYQRYLANQTPTPLNLVPPEDIADMGVDYDGNFVCSGGMRILPVWTSDPQSLCQQSEMQQQPSGNPFDQSSQPQQQPQQQPAQQEQKDSDGVAGWIKDMFGSN
Protein: Diisopropyl-fluorophosphatase (DFPase) (EC 3.8.2.2) (Q7SIG4)
Organism: Loligo vulgaris (Common European squid)
Function: Biological function and substrate unknown. However, it is capable of acting on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including nerve gases).
Interaction partners:
Sequence:
MEIPVIEPLFTKVTEDIPGAEGPVFDKNGDFYIVAPEVEVNGKPAGEILRIDLKTGKKTVICKPEVNGYGGIPAGCQCDRDANQLFVADMRLGLLVVQTDGTFEEIAKKDSEGRRMQGCNDCAFDYEGNLWITAPAGEVAPADYTRSMQEKFGSIYCFTTDGQMIQVDTAFQFPNGIAVRHMNDGRPYQLIVAETPTKKLWSYDIKGPAKIENKKVWGHIPGTHEGGADGMDFDEDNNLLVANWGSSHIEVFGPDGGQPKMRIRCPFEKPSNLHFKPQTKTIFVTEHENNAVWKFEWQRNGKKQYCETLKFGIF
Protein: Nucleoside diphosphate kinase (EC 2.7.4.6) (A8JGW5)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- adenylate kinase
- AAA+ ATPase domain-containing protein
- Ribonucleoside-diphosphate reductase
- CFA20 domain-containing protein
- Inosine triphosphate pyrophosphatase
- Uncharacterized protein
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Thymidylate kinase
- Thymidylate kinase
- Chloroplast ppGpp synthase/degradase
Sequence:
MAANLRYCFISEWLDPASGILWKYQLFYYPESKEVEMVDIKNRRHFLKRTKYEELKPSLLFLGSVVTVFSRQLKLTEYGDEFTRNRMESQSERTLAMIKPDAYKNMGKIINAICQSGFLISKLRIGKLSKEEAGEFYAVHAGKPFVDRLTDFMSSGRVVAMELVAPGAIRKWRELIGPTDSNQARAEAPGSLRAQFGTDKTFNACHGSDAPDTAAEECNFWFGPGRYPGKCDLAAGTTLCLVKPHLVADGAAGLVIDLIQESFEVTAGGLYNLDRNAAAEFLEVYKGVLPAGDFNSMVEQLTSGACIALEVADRDGADAVEPFRQLAGPLDPELGRVLRPASLRARFGLDAVRNGVHCTDLPEDGVLEVNYFFTILPTAS
Protein: Nudix hydrolase 27, chloroplastic (AtNUDT27) (EC 3.6.1.-) (Q9FNH4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use diadenosine 5',5'''-P(1)P(5) pentaphosphate (Ap(5)A) as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18815383}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 48
- Nudix hydrolase
- Nudix hydrolase 20, chloroplastic
- Nudix hydrolase 5
- mRNA-decapping enzyme subunit 2
- Nudix hydrolase 9
- Nudix hydrolase 1
Sequence:
MAVKASGFIGKSAISVHLDFSSFPVKFSCLKQFSVSSPKPLVVLSVALSSPARTVESPPVGYRKNVGICLVSPCRKIFTASKIHIPDTWQMPQGGADEGEDLRNAAFRELREETGVTSAEFIAEIPNWLTYDFPREVKDKLNRKWRTSYKGQAQKWFLFKFTGKEEEINLLGDGTAKPEFKVWSWMLPEQVIEHAVYFKRPVYEHVIKQFNPYFVDEEKDSMNSSKD
Protein: U7 snRNA-associated Sm-like protein LSm11 (P83369)
Organism: Homo sapiens (Human)
Function: Component of the U7 snRNP complex that is involved in the histone 3'-end pre-mRNA processing. Increases U7 snRNA levels but not histone 3'-end pre-mRNA processing activity, when overexpressed. Required for cell cycle progression from G1 to S phases (By similarity). Binds specifically to the Sm-binding site of U7 snRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:12975319}.
Interaction partners:
- U7 snRNA-associated Sm-like protein LSm10
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein-associated proteins B and B'
- Histone RNA hairpin-binding protein
- Zinc finger protein 473
- CASP8-associated protein 2
- Cleavage and polyadenylation specificity factor subunit 3
Sequence:
MEERERGARSAGAGSPARPPSPRLDVSSDSFDPLLALYAPRLPPIPYPNAPCFNNVAEYESFLRTGVRGGGRGRGRARGAAAGSGVPAAPGPSGRTRRRPDAPAPDPERIQRLRRLMVAKEEGDGAAGAGRRGPGRSRKAPRNVLTRMPLHEGSPLGELHRCIREGVKVNVHIRTFKGLRGVCTGFLVAFDKFWNMALTDVDETYRKPVLGKAYERDSSLTLTRLFDRLKLQDSSKKEADSKSAVEDSTLSRYSQTSTWKLASVWGRADTGRGSHKRSRSVPSSLQASAREESRSELSGRTTRTDGSSVGGTFSRATTLSRGQSRKKKRKPKVDYQQVFTRHINQIFIRGENVLLVHLAQ
Protein: Psoriasis susceptibility 1 candidate gene 2 protein (Protein SPR1) (Q9UIG4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Coiled-coil alpha-helical rod protein 1
- Corneodesmosin
Sequence:
MILNWKLLGILVLCLHTRGISGSEGHPSHPPAEDREEAGSPTLPQGPPVPGDPWPGAPPLFEDPPPTRPSRPWRDLPETGVWLPEPPRTDPPQPPRPDDPWPAGPQPPENPWPPAPEVDNRPQEEPDLDPPREEYR
Protein: Regulator of eph expression, isoform A (Q9VQV2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
METSVAGQKPIASAMMCHQQTSSSCAHLMYDQHSSEEELEVINGPSSQAGQHPGTAATGSSCASRISNRGCTSSLDTEAPYEERATTSNSKRSSSTLMVENRKRSLAHSSDDELRNSLEPILTPVNFRTSPPLEAFKPNRSHMMFRSTTPLILSEARCGIENIKLCDNSVNEENGDNGGGGGAANSSKCAKIGALAGNASGTVAATGNGNGGNENEPSVIKACSSSLKMSNSSHHIYQPQPKYSFHYNSSRSSPASTTGLDMEVRSVSPPAKLFHCAISPRRRPSNNASGAAGGATTISPSSASSSSGTTTTHNAANSAGNAANVTAVATQRLQRPHRPCLDFDKMQQVSL
Protein: Glutamate receptor, metabotropic 6b (Metabotropic glutamate receptor 6b) (Zgc:158329) (A1L1T5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTSQLYAPSQSRHHRIIRAPKPHVGSLIHIMWILTMGFTPESQAASSDTQPHSIKIEGDITLGGLFPVHSRGPAGIPCGEVKKEKGIHRMEAMLYALDQINSDPDLLPNITLGARILDTCSRDTYALEQSLTFVQALIQKDNSDVRCSNGEPPIIPKPERVVGVIGASASSVSIMVANVLRLFAIPQISYASTAPELSDNNRYDFFSRVVPPDSFQAQAMVDIVKAMGWNYVSTLASEGNYGESGVDAFIQISREAGGLCIAQAIKIPREPRPGEFDKIIKRLMETSNARGVIIFANEDDIKRVLEAAKRANLTGHFLFVGSDSWGAKISPILNQEDVAEGAVTILPKRASIEGFDQYFTTRSLENNRRNIWFAEFWEDDFKCKLTRPGIRGDGGLRKCTGEERIGRDSGYEQEGKVQFVIDAVYAMAHALHSMHIDLCPGSMGVCDKMDPVDGRMLLTYIRAVNFNGSAGTGVMFNENGDAPGRYDIFQYQLSNTTNPGYKLIGQWTNHLRLSAEDMQWSGGEKLVPDSVCSFPCESGERKRMVKGVPCCWHCELCDGYQFLLDEFNCDMCPFDMRPTPNRTACRPTPIIKLEWSSPWAIIPVFLAVLGILATTGVIATFIRFNDTPIVRASGRELSYVLLTGIFLIYLITFLMIAEPGTVVCAFRRLLLGLGMCISYSAMLTKTNRIYRIFEQGKKSVTPPKFISPTSQLIITFILISVQLLGIFIWFGVVPPHTNVDFDELRPPNPEFARGILKCDMSDLSLIGCLSYSMGLMVTCTVYAIKSRGVPETFNEAKPIGFTMYTTCIIWLAFVPIFFGTSQSTEKMFIQTTTLTVSMSLSATVSLGMLYIPKVYVIIFHPEQNVQKRKRSFKAVAQAATVSTHLSQKSSDKQNGETKVEPDRSQ