wanglab/gogpt-training-data huggingface dataset:
Protein: PTS system trehalose-specific EIIBC component (EIIBC-Tre) (EII-Tre) [Includes: Trehalose-specific phosphotransferase enzyme IIB component (EC 2.7.1.201) (PTS system trehalose-specific EIIB component); Trehalose permease IIC component (PTS system trehalose-specific EIIC component)] (P36672)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in trehalose transport at low osmolarity.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00426, ECO:0000305|PubMed:2160944}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00426}.
Interaction partners:
- Trehalose-6-phosphate hydrolase
- PTS system glucose-specific EIIA component
- HTH-type transcriptional regulator TreR
- Phosphocarrier protein HPr
- Trehalose-6-phosphate synthase
- Trehalose-6-phosphate phosphatase
- PTS system N-acetylglucosamine-specific EIICBA component
- PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component
- PTS system fructose-specific EIIB'BC component
- 6-phospho-beta-glucosidase
Sequence:
MMSKINQTDIDRLIELVGGRGNIATVSHCITRLRFVLNQPANARPKEIEQLPMVKGCFTNAGQFQVVIGTNVGDYYQALIASTGQAQVDKEQVKKAARHNMKWHEQLISHFAVIFFPLLPALISGGLILGFRNVIGDLPMSNGQTLAQMYPSLQTIYDFLWLIGEAIFFYLPVGICWSAVKKMGGTPILGIVLGVTLVSPQLMNAYLLGQQLPEVWDFGMFSIAKVGYQAQVIPALLAGLALGVIETRLKRIVPDYLYLVVVPVCSLILAVFLAHALIGPFGRMIGDGVAFAVRHLMTGSFAPIGAALFGFLYAPLVITGVHQTTLAIDLQMIQSMGGTPVWPLIALSNIAQGSAVIGIIISSRKHNEREISVPAAISAWLGVTEPAMYGINLKYRFPMLCAMIGSGLAGLLCGLNGVMANGIGVGGLPGILSIQPSYWQVFALAMAIAIIIPIVLTSFIYQRKYRLGTLDIV
Protein: 2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 (Diphthamide biosynthesis protein 2) (Diphtheria toxin resistance protein 2) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2) (P32461)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1. Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 2-
- Diphthamide biosynthesis protein 3
- Elongation factor 2
- Diphthine methyl ester synthase
- Diphthine--ammonia ligase
- Diphthine methyltransferase
- Diphthamide biosynthesis protein 4
- Protein KTI13
- NADH-cytochrome b5 reductase 1
- ATP-dependent RNA helicase DBP7
Sequence:
MEVAPALSTTQSDVAFQKVETHEIDRSSYLGPCYNSDELMQLISAYYNVEPLVGYLEQHPEYQNVTLQFPDDLIKDSSLIVRLLQSKFPHGKIKFWVLADTAYSACCVDEVAAEHVHAEVVVHFGDACLNAIQNLPVVYSFGTPFLDLALVVENFQRAFPDLSSKICLMANAPFSKHLSQLYNILKGDLHYTNIIYSQVNTSAVEEKFVTILDTFHVPEDVDQVGVFEKNSVLFGQHDKADNISPEDYHLFHLTTPQDPRLLYLSTVFQSVHIFDPALPGMVTGPFPSLMRRYKYMHVARTAGCIGILVNTLSLRNTRETINELVKLIKTREKKHYLFVVGKPNVAKLANFEDIDIWCILGCSQSGIIVDQFNEFYKPIITPYELNLALSEEVTWTGKWVVDFRDAIDEIEQNLGGQDTISASTTSDEPEFDVVRGRYTSTSRPLRALTHLELEAADDDDSKQLTTRHTASGAVIKGTVSTSASALQNRSWKGLGSDFDSTEVDNTGADIEEGISGVARGYGFDREDAMKKENK
Protein: ATP synthase F(0) complex subunit a (F-ATPase protein 6) (Proton-conducting channel, ATP synthase F(0) complex subunit a) (P00848)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase F
- Cytochrome c oxidase subunit 3
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
Sequence:
MNENLFASFITPTMMGFPIVVAIIMFPSILFPSSKRLINNRLHSFQHWLVKLIIKQMMLIHTPKGRTWTLMIVSLIMFIGSTNLLGLLPHTFTPTTQLSMNLSMAIPLWAGAVITGFRHKLKSSLAHFLPQGTPISLIPMLIIIETISLFIQPMALAVRLTANITAGHLLMHLIGGATLVLMNISPPTATITFIILLLLTILEFAVALIQAYVFTLLVSLYLHDNT
Protein: Esterase (EC 3.1.1.-) (Early nodule-specific protein homolog) (Latex allergen Hev b 13) (allergen Hev b 13) (Q7Y1X1)
Organism: Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Function: Has lipase and esterase activities. May be involved in plant defense.
Interaction partners:
Sequence:
MEFPETNNNPIITLSFLLCMLSLAYASETCDFPAIFNFGDSNSDTGGKAAAFYPLNPPYGETFFHRSTGRYSDGRLIIDFIAESFNLPYLSPYLSSLGSNFKHGADFATAGSTIKLPTTIIPAHGGFSPFYLDVQYSQFRQFIPRSQFIRETGGIFAELVPEEYYFEKALYTFDIGQNDLTEGFLNLTVEEVNATVPDLVNSFSANVKKIYDLGARTFWIHNTGPIGCLSFILTYFPWAEKDSAGCAKAYNEVAQHFNHKLKEIVAQLRKDLPLATFVHVDIYSVKYSLFSEPEKHGFEFPLITCCGYGGKYNFSVTAPCGDTVTADDGTKIVVGSCACPSVRVNWDGAHYTEAANEYFFDQISTGAFSDPPVPLNMACHKTESLRTLASV
Protein: KAT8 regulatory NSL complex subunit 1 (A0A3B3IT55)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAMAPALTDAAAEAHHIRFKLAPPSSTLSPGSAENNGNANILIAANGTKRKAIAAEDPSLDFRNNPTKEDLGKLQPLVASYLCSDVTSVPSKESLKLQGVFSKQTVLKSHPLLSQSYELRAELLGRQPVLEFSLENLRTMNTSGQTALPQAPVNGLAKKLTKSSTHSDHDNSTSLNGGKRALTSSALHGGEMGGSESGDLKGGMTNCTLPHRSLDVEHTTLYSNNSTANKSSVNSMEQPALQGSSRLSPGTDSSSNLGGVKLEGKKSPLSSILFSALDSDTRITALLRRQADIESRARRLQKRLQVVQAKQVERHIQHQLGGFLEKTLSKLPNLESLRPRSQLMLTRKAEAALRKAASETTTSEGLSNFLKSNSISEELERFTASGIANLRCSEQAFDSDVTDSSSGGESDIEEEELTRADPEQRHVPLRRRSEWKWAADRAAIVSRWNWLQAHVSDLEYRIRQQTDIYKQIRANKGLIVLGEVPPPEHTTDLFLPLSSEVKTDHGTDKLIESVSQPLENHGAPIIGHISESLSTKSCGALRPVNGVINTLQPVLADHIPGDSSDAEEQLHKKQRLNLVSSSSDGTCVAARTRPVLSCKKRRLVRPNSIVPLSKKVHRNSTIRPGCDVNPSCALCGSGSINTMPPEIHYEAPLLERLSQLDSCVHPVLAFPDDVPTSLHFQSMLKSQWQNKPFDKIKPPKKLSLKHRAPMPGSLPDSARKDRHKLVSSFLTTAKLSHHQTRPDRTHRQHLDDVGAVPMVERVTAPKAERLLNPPPPVHDPNHSKMRLRDHSSERSEVLKHHTDMSSSSYLAATHHPPHSPLVRQLSTSSDSPAPASSSSQVTASTSQQPVRRRRGESSFDINNIVIPMSVAATTRVEKLQYKEILTPSWREVDLQSLKGSPDEENEEIEDLSDAAFAALHAKCEEMERARWLWTTSVPPQRRGSRSPISPELHSAPLTPVARDTPRHLASEDTRCSTPELGLDEQSVQPWERRTFPLAHSPQAECEDQLDAQERAARCTRRTSGSKTGRETEAAPTSPPIVPLKSRHLVAAATAQRPTHR
Protein: Always early (Q2PNP9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRIKPGVASKRTENFTKKPSNISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGNSFEGMVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRENSSHLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: Phosphatidylserine decarboxylase proenzyme 2 (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 2 beta chain; Phosphatidylserine decarboxylase 2 alpha chain] (P53037)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Phosphatidylethanolamine produced by PSD2 is insufficient to completely provide the PtdEtn pool required by mitochondria under respiratory conditions. PSD2 is also involved in the PtdSer transport step to the site of PtdEtn synthesis on the Golgi/endosome membranes. Required for normal heavy metal resistance.
Subcellular location: Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:7890739}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:11104779, ECO:0000305|PubMed:20016005}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:24366873}. Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:20016005}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:11104779, ECO:0000305|PubMed:20016005}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:24366873}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Choline/ethanolaminephosphotransferase 1
- Lysophospholipid acyltransferase
- Phosphatidylethanolamine N-methyltransferase
- Phospholipase D1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol transfer protein PDR17
- Triacylglycerol lipase 5
Sequence:
MRIIKGRKRGKNKKPTLILKIHVIQAENIEALKTFNCNPVCFVTTNTFYSQKTNKLKNSNTHWNQTLRIKLPRNPTSEWLRIIVYDALPTGAPPTTPSRPRTTTANTSSSTLSNSGLSSHSHSSRNLNVTSKGNQTSTSINSVSSSATPAPSHSSSSLSTTGPGSTHKNRINSYLYLGEAKISLLDLFKRKDTTTSYKFSIEAQRYHLYDMKGGKDQDSLNCNFLVGDILLGFKLECNVKRTPTFQAFNAWRNELNTYLGRIDRNKARMRSSSSLPPPLEDMLSNSSAVSGNEIRREKPYSDTDLAHDEEVNAEDEIDAEESIEDMNSSGSICTERRYDIDNDTIFDSISEVVSLNDEELDILNDFEEADHPNVPDINVHDIDEDTRISLSSMITALDEYDIVEPEDVAKLPAVSENDITSVDDEESENQQESDEEFDIYNEDEREDSDFQSKEYIGSRLLHLQRGKHNKSYANYLYRRAKSNFFISKKEHAMGVVFMHIGAIKNLPALRNRLSKTNYEMDPFIVISFGRRVFKTSWRKHTLNPEFNEYAAFEVFPHETNFAFSIKVVDKDSFSFNDDVAKCELAWFDMLQQQQHENEWIPYEIPLDLTVEPAHAPKQPVLYSSFKYVSYPFLKKSFWKEAVDTSVNLERLDIIQVMLYLERLGSFTMADSFELFQHFNKSAWAGQSITRSQLVEGLQSWRKSTNFKRIWTCPRCMRSCKPTRNARRSKLVLENDLITHFAICTFSKEHKTLKPSYVSSAFASKRWFSKVLIKLTYGKYALGSNNANILVQDRDTGIIIEEKISAHVKLGMRIIYNGKSPESKKFRSLLKTLSIRQGKKFDSTASAKQIEPFIKFHSLDLSQCRDKDFKTFNEFFYRKLKPGSRLPESNNKEILFSPADSRCTVFPTIQESKEIWVKGRKFSIKKLANNYNPETFNDNNCSIGIFRLAPQDYHRFHSPCNGTIGKPVYVDGEYYTVNPMAVRSELDVFGENIRVIIPIDSPQFGKLLYIPIGAMMVGSILLTCKENDVVESGQELGYFKFGGSTIIIIIPHNNFMFDSDLVKNSSERIETLVKVGMSIGHTSNVNELKRIRIKVDDPKKIERIKRTISVSDENAKSTGNVTWEYHTLREMMNKDFAGL
Protein: Replication-associated protein G2P (Rep) (EC 3.1.21.-) (EC 6.5.1.1) (G2P) (Gene 2 protein) (P69546)
Organism: Enterobacteria phage f1 (Bacteriophage f1)
Function: Isoform G2P plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates at the 3'-OH of the cleavage site. After one round of rolling circle synthesis, protein G2P is linked to the newly synthesized ssDNA and joins the ends of the displaced strand to generate a circular single-stranded molecule ready to be packed into a virion.
Interaction partners:
Sequence:
MIDMLVLRLPFIDSLVCSRLSGNDLIAFVDLSKIATLSGMNLSARTVEYHIDGDLTVSGLSHPFESLPTHYSGIAFKIYEGSKNFYPCVEIKASPAKVLQGHNVFGTTDLALCSEALLLNFANSLPCLYDLLDVNATTISRIDATFSARAPNENIAKQVIDHLRNVSNGQTKSTRSQNWESTVTWNETSRHRTLVAYLKHVELQHQIQQLSSKPSAKMTSYQKEQLKVLSNPDLLEFASGLVRFEARIETRYLKSFGLPLNLFDAIRFASDYNSQGKDLIFDLWSFSFSELFKAFEGDSMNIYDDSAVLDAIQSKHFTITPSGKTSFAKASRYFGFYRRLVNEGYDSVALTMPRNSFWRYVSALVECGIPKSQLMNLSTCNNVVPLVRFINVDFSSQRPDWYNEPVLKIA
Protein: Small ribosomal subunit protein uS12 (40S ribosomal protein S23) (P62266)
Organism: Homo sapiens (Human)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays an important role in translational accuracy.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}. Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SA96}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}. Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q6SA96, ECO:0000269|PubMed:25957688}.
Interaction partners:
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL18
Sequence:
MGKCRGLRTARKLRSHRRDQKWHDKQYKKAHLGTALKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVANVSLLALYKGKKERPRS
Protein: Exocyst complex component Sec3, putative (Eurofung) (Q5BG68)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Exocyst complex component Sec8
- Exocyst complex component Sec6, putative
- Exocyst complex component SEC5
- Exocyst complex component Sec10, putative
- Exocyst complex component SEC15
- Exocyst complex component exo84
- Exocyst complex protein exo70
- Uncharacterized protein
Sequence:
MNGHDRPRGPLGDPVPQRDPRRRAESRAGGHGGPGDGASRAEKFEDEKRRIVQSCFSKKDSDGALVESYITHVRIMEDGAYPSSPPPPNSSPENKKARVIIVAVRRSGRVRMHKARENNDGSFSIGKTWMLDDLSAIKSYNAIVPSSPQEELQKQWASNVGFLVTVGKPYYWHAKSPKEKDFFIGSLVKIYKKYTGGKMPDLIGFDERELQLLLGPHYSGGKGPSSGSSNTEGSFVPPRPPSSQGNRPQSPHWARARSRDSPKRRPNEEDLPIRAQRSREQMSRPSTAQSGKSGPPPFAPPQHPPPVLPVDQGDRPPPRAMERLAGDPKTPKIAPVSPLEPKIREIPSSLRTAHSRENISKEAEEVNLSSVQTEPRPPSSRSGKMVPEPRPIVRSENSSSSIPEARRLNDDIVPGLAPSELRVKEPKRGSETPSSTSKGQPTSLAGDQLSSSNNLQLADVPPGLLAGLPASNNATSAKPVETPQQVSEREEPEEPVAESKAPSSPISPPEALQENDEDDPDAHRPGLGPMIKKKSNKDVAGAFRKAANAYGAFKPRSGGAGARLLAAAKKQAASEGPDGITSVVPAPSLVRRVEEPAKTTTEERPEETATVPPVSETPEIPSTDAPPVPAPPVPAPTVPEPNIQEPPRVEITEAVADATVAPSLDAPKNMPEAVAVRADERSRSVSPSPRDRRRRRHEDNTVKYCQALGLDPKVLGDRGVEFDDILTDLGWNGRLSDEKKIEDLEADVRREIGRVEATSWLGNLEQQEGKVDQLAKLIDKTIEECEELDNLLTLYSHELNTLRDDVSYIETQSQGLQVQTANQKLLHSELQTLLKTLSISVNDLQPLKEASLSNIDGLRETELALSTLYKAMLTIDPDIWHNKKRLDAAGGHGTVGVYADTEIGQMRAIKDKKEEYRFYSSSFLQRLRQFMGIAYQVAAQKRADAAANSQKDPMKLDGSARAYARRELWVYSALTLFAREVSGPEWQGLITLYEQQAKQSYQAEFRDNNMAWKRTARKMTGEEQELLFTHQDKEKEAEGITTAARKLTVRRGKTIRAAAGLRLPSADKQHGRLEPFEVFAGTLQETVKMISEEQNFLVRFFHLTSLSNTDFADIVASGAPDERAVPDFTIKQSPDPDRGMAKKVEQAMDELYSFWPMDMQNLVDWSIKADPLQGIGILFAIEKTIADFDDTNQDFIIHSLQKLHSRLIGLFNRFVDEQIRGIEETKVKINKRKGVISFMRIFPNFSVAVENMLSDPSSEFYDIRLNVNEAYDRINRAMWESLKFIAKEAPGQSATVAAAAGSGDPEDKEILNYHILLIENMNHYIEEVDIRNLPVLERWRNRAQEDMREHMRLYLDSVIYRPLGKLLEFVDSVEGLAATTSNPTDIASRPSHSRSVAKRVLAAYDAKEIRRGIEMLKKRVEKHFGDADDPGLSRSLVIKVLRECESRYEQAYDRTQHVIRAVYEGQLELEWRKEDVAATFRK
Protein: PBP domain-containing protein (Q9I5N7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Filamentous haemagglutinin FhaB/tRNA nuclease CdiA-like TPS domain-containing protein
- DNA repair protein
- Phosphate transport system permease protein PstA
- ShlB/FhaC/HecB family hemolysin secretion/activation protein
- Glycosyltransferase
- Energy transducer TonB
- Glycosyltransferase
Sequence:
MLKPMFGVVALTLLTSHTTLGATVTGGGASMPAKLYKGSADSILPINFSYAASGSGIGKTAFLMNNPMLLGATTGTVHYIGSDSILSSSELSAYSTNYRGAYGPLIQIPLAGTAVTIPYKKPDITDLNLTSAQLCDAFSGAKVTWGQLLGNPADRTPIRIVYQRGGSGATELLTRHLNSVCPTRFATNSIFTNARLPAGGALPSNWVAVQPYESVRNAVDNVSGSIGYEGPDGVDLSDNSKIARVNGLLPTLANRVIAVRSVAPPGVAADRADPSKWIPVFVNPNAGYSIVGYTNFVFGQCYKDATVAADLRAFLTQHYGGTTTNRAVADHRFVPLVASWKSAIMSAFITGTSENLAINNPSVCNGKGRP
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FV88)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Ribosomal RNA-processing protein 43
- glycerol kinase
Sequence:
MESIHDAMSDILGKDQHNGRHGDNHSRRPGRRGSNTGSNYDFERQSMEYEPSVMPHTNYIPEYRLGRDDNTIFPIQEVIPNSQDAMEELAARSRRQRAATATINANNNDFQRNNDGLGGHGENGDEIHGEEDLDIDDPLRDNVPMMVKPKILHQNPQTPTVLPSTFHPISKWSSVKRYYLKEFLAEFLGTMMMVFFGQCIDIQVNAGAQIQRNQYLAYVERLNRTKAVTNDTLEILNALPLLVSTTTSGTADNVPKNWAAAVVMGYFAAGGSAISGAHLNPAATVTTFFFRGFPARKMPFYFAGQLLGGFMACLLSYIYYKRVIMEGYPHWYESETVAGFFVTSPKPYLSTERQITSEFMCTAAMQLCVFALTDPYTSLSADIFPLLLFLMALVVNSSMSFQTGSAMNAARDLGPRLALWALGFDRKNLWIHHHRYFWVPMIVPFWGSMTGALLYDFCIYQGHESPVNWPLSLYKEKFMKLWHRRPGWKNRTRKRRTSDLSDFSYQNDDDDNLTDNDFKDKPKTAKTNVKPNQGGNPADEAGKFVRFQSVSQRGGRSRHNNSTTILEEDSIETASLGHSQSDSVDNSDKHSIHNATDEKVSY
Protein: Catenin alpha-2 (Alpha N-catenin) (Q61301)
Organism: Mus musculus (Mouse)
Function: May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Required for proper regulation of cortical neuronal migration and neurite growth. It acts as negative regulator of Arp2/3 complex activity and Arp2/3-mediated actin polymerization. It thereby suppresses excessive actin branching which would impair neurite growth and stability (By similarity). Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16457793}; Peripheral membrane protein {ECO:0000305|PubMed:16457793}; Cytoplasmic side {ECO:0000305|PubMed:16457793}. Cytoplasm {ECO:0000269|PubMed:16457793}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:15034585}. Cell junction, adherens junction {ECO:0000269|PubMed:16457793, ECO:0000269|PubMed:16691566}. Cell projection, axon {ECO:0000269|PubMed:16457793, ECO:0000269|PubMed:16691566}. Nucleus {ECO:0000250|UniProtKB:P26232}.
Interaction partners:
- Catenin beta-1
- Vinculin
- Cadherin-1
- Afadin
- Cadherin-2
- Alpha-actinin-1
- Tight junction protein 1
- Alpha-actinin-4
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
Sequence:
MTSATSPIILKWDPKSLEIRTLTVERLLEPLVTQVTTLVNTSNKGPSGKKKGRSKKAHVLAASVEQATQNFLEKGEQIAKESQDLKEELVAAVEDVRKQGETMRIASSEFADDPCSSVKRGTMVRAARALLSAVTRLLILADMADVMRLLSHLKIVEEALEAVKNATNEQDLANRFKEFGKEMVKLNYVAARRQQELKDPHCRDEMAAARGALKKNATMLYTASQAFLRHPDVAATRANRDYVFKQVQEAIAGISSAAQATSPTDEAKGHTGIGELAAALNEFDNKIILDPMTFSEARFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMNNTGRKEKGDPLNIAIDKMTKKTRDLRRQLRKAVMDHISDSFLETNVPLLVLIEAAKSGNEKEVKEYAQVFREHANKLVEVANLACSISNNEEGVKLVRMAATQIDSLCPQVINAALTLAARPQSKVAQDNMDVFKDQWEKQVRVLTEAVDDITSVDDFLSVSENHILEDVNKCVIALQEGDVDTLDRTAGAIRGRAARVIHIINAEMENYEAGVYTEKVLEATKLLSETVMPRFAEQVEVAIEALSANVPQPFEENEFIDASRLVYDGVRDIRKAVLMIRTPEELEDDSDFEQEDYDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEEKAKIAEQVEIFHQEKSKLDAEVAKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVINAAKKIAEAGSRMDKLARAVADQCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELIVSGTGVQSTFTTFYEVDCDVIDGGRASQLSTHLPTCAEGAPIGSGSSDSSMLDSATSLIQAAKNLMNAVVLTVKASYVASTKYQKVYGTAAVNSPVVSWKMKAPEKKPLVKREKPEEFQTRVRRGSQKKHISPVQALSEFKAMDSF
Protein: Phospholipase A-2-activating protein (PLA2P) (PLAP) (Q9Y263)
Organism: Homo sapiens (Human)
Function: Plays a role in protein ubiquitination, sorting and degradation through its association with VCP. Involved in ubiquitin-mediated membrane proteins trafficking to late endosomes in an ESCRT-dependent manner, and hence plays a role in synaptic vesicle recycling (By similarity). May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. Plays a role in cerebellar Purkinje cell development (By similarity). Positively regulates cytosolic and calcium-independent phospholipase A2 activities in a tumor necrosis factor alpha (TNF-alpha)- or lipopolysaccharide (LPS)-dependent manner, and hence prostaglandin E2 biosynthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:28007986}. Cytoplasm {ECO:0000269|PubMed:27753622, ECO:0000269|PubMed:28007986}. Synapse {ECO:0000250|UniProtKB:P27612}. Note=Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. {ECO:0000269|PubMed:27753622}.
Interaction partners:
- Ubiquitin thioesterase OTU1
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Transitional endoplasmic reticulum ATPase
- Polyubiquitin-C
- UBX domain-containing protein 6
- Nuclear protein localization protein 4 homolog
- Polyubiquitin-B
- NSFL1 cofactor p47
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MTSGATRYRLSCSLRGHELDVRGLVCCAYPPGAFVSVSRDRTTRLWAPDSPNRSFTEMHCMSGHSNFVSCVCIIPSSDIYPHGLIATGGNDHNICIFSLDSPMPLYILKGHKNTVCSLSSGKFGTLLSGSWDTTAKVWLNDKCMMTLQGHTAAVWAVKILPEQGLMLTGSADKTVKLWKAGRCERTFSGHEDCVRGLAILSETEFLSCANDASIRRWQITGECLEVYYGHTNYIYSISVFPNCRDFVTTAEDRSLRIWKHGECAQTIRLPAQSIWCCCVLDNGDIVVGASDGIIRVFTESEDRTASAEEIKAFEKELSHATIDSKTGDLGDINAEQLPGREHLNEPGTREGQTRLIRDGEKVEAYQWSVSEGRWIKIGDVVGSSGANQQTSGKVLYEGKEFDYVFSIDVNEGGPSYKLPYNTSDDPWLTAYNFLQKNDLNPMFLDQVAKFIIDNTKGQMLGLGNPSFSDPFTGGGRYVPGSSGSSNTLPTADPFTGAGRYVPGSASMGTTMAGVDPFTGNSAYRSAASKTMNIYFPKKEAVTFDQANPTQILGKLKELNGTAPEEKKLTEDDLILLEKILSLICNSSSEKPTVQQLQILWKAINCPEDIVFPALDILRLSIKHPSVNENFCNEKEGAQFSSHLINLLNPKGKPANQLLALRTFCNCFVGQAGQKLMMSQRESLMSHAIELKSGSNKNIHIALATLALNYSVCFHKDHNIEGKAQCLSLISTILEVVQDLEATFRLLVALGTLISDDSNAVQLAKSLGVDSQIKKYSSVSEPAKVSECCRFILNLL
Protein: Small ribosomal subunit protein uS19c (30S ribosomal protein S19, chloroplastic) (P0C478)
Organism: Oryza sativa (Rice)
Function: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MTRKKTNPFVAHHLLAKIEKVNMKEEKETIVTWSRASSILPAMVGHTIAIHNGKEHIPIYITNPMVGRKLGEFVPTRHFTSYESARKDTKSRR
Protein: MAM domain-containing glycosylphosphatidylinositol anchor protein 1 (Ig6M) (P85171)
Organism: Rattus norvegicus (Rat)
Function: Required for radial migration of cortical neurons in the superficial layer of the neocortex (By similarity). Plays a role in the formation or maintenance of inhibitory synapses. May function by inhibiting the activity of NLGN2.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15019943}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15019943}. Note=Associated with lipid rafts. {ECO:0000250|UniProtKB:Q8NFP4, ECO:0000269|PubMed:15019943}.
Interaction partners:
- Neuroligin-2
Sequence:
MEVTCLLLLALIPFHCRGQGVYAPAQAQIVHAGQACVVKEDNISERVYTIRESDTLVLQCLVTGHPRPQVRWTKTAGSASDKFQETSVFNETLRIERIARTQGGRYYCKAENGVGVPAIKSIRVDVQYLDEPVLTVHQTVSDVRGNFYQEKTVFLRCTVSSNPPARFIWKRGSDTLSHSQDNGVDIYEPLYTQGETKVLKLKNLRPQDYASYTCQVSVRNVCGIPDKSITFQLTNTTAPPTLKLSVNETLVVNPGENVTVQCLLTGGDPLPQLHWSHGPGPLPLGALAQGGTLSIPSVQARDSGYYNCTATNNVGNPAKKTVNLLVRSLKNATFQITPDMIKESENIQLGQDLKLSCHVDAVPQEKVNYQWFKNGKPARTSKRLLVTRNDPELPAVTSSLELIDLHFSDYGTYLCVASFPGSPVPDLSVEVNISSETVPPTISVPKGRAVVTVREGSPAELQCEVRGKPRPPVLWSRVDKEAALLPSGLALEETPDGKLRVERVSREMSGTYRCQTARYNGFNVRAREAQVQLTVHFPPEVEPSSQDVRQALGRPVLLRCSLLRGSPQRIASAVWRFKGQLLPPPPVLPAAAAEGPDHAELRLDALTRDSSGNYECSVSNDVGSATCLFQVSAKAYSPEFYFDTPNPTRSHKLSKNYSYVLQWTQREPDAVDPVLNYRLSIRQLNQHNAMVKAIPVRRVEKGQLLEYTLTDLRVPHSYEIHLTPYTTFGAGDMASRVIHYTEPINSPSLSDNTCHFEDEKICGYTQDLTDNFDWTRQNALTQNPKRSPNTGPPTDISGTPEGYYMFIETSRPRELGDRARLVSPLYNASAKFYCVSFFYHMYGKHIGSLNLLVRSRNKGTLDTHAWSLSGNKGNVWQQAHVPINPSGPFQIIFEGVRGSGYLGDIAIDDVTLKKGECPRRQMDPNKVVVMPGSGAPRLSSLQLWGSMTIFLLALQR