wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase delta 4, accessory subunit (Q6P6U6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- DNA polymerase delta catalytic subunit
- DNA polymerase delta subunit 2
- DNA polymerase delta 3, accessory subunit.
- DNA polymerase epsilon subunit 4
- DNA polymerase epsilon subunit
- DNA polymerase epsilon catalytic subunit
- DNA polymerase epsilon subunit 3
- DNA polymerase alpha catalytic subunit
- DNA polymerase zeta catalytic subunit
- Mitotic spindle assembly checkpoint protein MAD2B
Sequence:
MGRKRFITDSYPVVKKREGPPGHNKGELAPELGEDTQSLSQEETELELLRQFDLAWQYGPCTGITRLQRWHRAEQMGLKPPVEVYQVLKTHPEDSRFQCSLWHLYPL
Protein: Outer envelope membrane protein 7 (AtOEP7) (Q9SVC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:11595795, ECO:0000269|PubMed:17337631, ECO:0000269|PubMed:18715957, ECO:0000269|PubMed:21730198}; Single-pass membrane protein {ECO:0000269|PubMed:11595795}. Note=The targeting to chloroplasts is facilitated by AKR2A and HSP17.8. {ECO:0000269|PubMed:18193034, ECO:0000269|PubMed:21730198}.
Interaction partners:
- Ankyrin repeat domain-containing protein 2A
- Protein CHUP1, chloroplastic
- Translocase of chloroplast 34, chloroplastic
- 22 kDa peroxisomal membrane protein
- Protein TOC75-3, chloroplastic
- UPF0548 protein At2g17695
- Translocase of chloroplast 159, chloroplastic
- Translocase of chloroplast 33, chloroplastic
- Mitochondrial import receptor subunit TOM20-1
- non-specific serine/threonine protein kinase
Sequence:
MGKTSGAKQATVVVAAMALGWLAIEIAFKPFLDKFRSSIDKSDPTKDPDDFDTAATATTSKEGL
Protein: Cytochrome b-c1 complex subunit 6, mitochondrial (Complex III subunit 6) (Complex III subunit VIII) (Cytochrome c1 non-heme 11 kDa protein) (Mitochondrial hinge protein) (Ubiquinol-cytochrome c reductase complex 11 kDa protein) (P07919)
Organism: Homo sapiens (Human)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00127}; Peripheral membrane protein {ECO:0000250|UniProtKB:P00127}; Intermembrane side {ECO:0000250|UniProtKB:P00127}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome b-c1 complex subunit 9
- Cytochrome b-c1 complex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MGLEDEQKMLTESGDPEEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSHTEEDCTEELFDFLHARDHCVAHKLFNNLK
Protein: UDP-N-acetylmuramoylalanine--D-glutamate ligase (EC 6.3.2.9) (D-glutamic acid-adding enzyme) (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase) (Q97RU8)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}.
Interaction partners:
Sequence:
MKVIDQFKNKKVLVLGLAKSGESAARLLDKLGAIVTVNDGKPFEDNPAAQSLLEEGIKVITGGHPLELLDEEFALMVKNPGIPYNNPMIEKALAKGIPVLTEVELAYLISEAPIIGITGSNGKTTTTTMIGEVLTAAGQHGLLSGNIGYPASQVAQIASDKDTLVMELSSFQLMGVQEFHPEIAVITNLMPTHIDYHGSFSEYVAAKWNIQNKMTAADFLVLNFNQDLAKDLTSKTEATVVPFSTLEKVDGAYLEDGQLYFRGEVVMAANEIGVPGSHNVENALATIAVAKLRDVDNQTIKETLSAFGGVKHRLQFVDDIKGVKFYNDSKSTNILATQKALSGFDNSKVVLIAGGLDRGNEFDELVPDITGLKKMVILGQSAERVKRAADKAGVAYVEATDIADATRKAYELATQGDVVLLSPANASWDMYANFEVRGDLFIDTVAELKE
Protein: Spectrin repeat containing nuclear envelope protein 1 (A0A5F9ZH86)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
XIEQIIAQGEQLIEKSEPLDAAIIEEELDELRRYCQEVFGRVERYHKKLIRLPPSSNLSLSLAQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESAMSRALPSEDEEGQDDKDFYLRGAVGLSGDHSALESQIRQLGKALDDSRFQIQQTENIIRSKTPTGPELDTSYKGYMKLLGECSSSIDSVKRLEHKLKEEEESLPGFVNLHSTETQTAGVIDRWELLQAQALSKELRMKQNLQKWQQFNSDLNSIWAWLGDTEEELEQLQRLELSTDIQTIELQIKKLKELQKAVDHRKAIILSINLCSPEFTQADSKESRDLQDRLSQMNGRWDRVCSLLEEWRGLLQDALMQCQGFHEMSHGLLLMLENIDRRKNEIVPIDSNLDAEILQDHHKQLMQIKHELLESQLRVASLQDMSCQLLVNAEGTDCLEAKEKVHVIGNRLKLLLKEVSRHIKELEKLLDVSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKTVHKRWLRFLPF
Protein: Transcriptional activator plp-1 (Pur-alpha-like protein 1) (Q94230)
Organism: Caenorhabditis elegans
Function: Probable transcription activator. Binds telomeric DNA containing repeats of the sequence, 5'-TTAGGC-3'. Binds to end-1 promoter, activating end-1 expression, which is required for endoderm specification during embryonic development.
Subcellular location: Nucleus {ECO:0000269|PubMed:19084000}. Chromosome {ECO:0000269|PubMed:16267406, ECO:0000269|PubMed:19084000}. Note=localizes to nuclei of interphase cells throughout early embryogenesis. Localizes to the nucleus in a lit-1 dependent manner. Transiently asymmetrically localizes during telophase of the dividing EMS cell with higher levels in the future E cell nucleus and low or undetectable levels in that of the MS cell. {ECO:0000269|PubMed:19084000}.
Interaction partners:
- Multidrug resistance protein mrp-7
Sequence:
MSDGSVERGTKRAEDSLATHQLTVQYKRYYIDVNENTRGRYIKIAELGTNYKSRIILSIVAAKAIVSEISKMLALIDEPSTGEHAPKESSLIKSETLNVDGRKFYVDLKENVRGRFLRIAQMPMNPRQTRQQIAIPSDGIAEIHKVLTEYLAKFGEGHEQENTNTPKITAENKSFLFHSGKNDRGEFVRISEIKLNSGYRNAITVPMSALVDFRKELDNIIANQGK
Protein: UV excision repair protein RAD23 (P32628)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a central role both in proteasomal degradation of misfolded proteins and DNA repair. Central component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA repair protein RAD4
- Peptide-N
- DNA repair protein RAD7
- 26S proteasome regulatory subunit RPN10
- E4 ubiquitin-protein ligase UFD2
- DNA repair protein RAD16
- 26S proteasome regulatory subunit RPN1
- Ubiquitin domain-containing protein DSK2
- Polyubiquitin
- Ubiquitin carboxyl-terminal hydrolase RPN11
Sequence:
MVSLTFKNFKKEKVPLDLEPSNTILETKTKLAQSISCEESQIKLIYSGKVLQDSKTVSECGLKDGDQVVFMVSQKKSTKTKVTEPPIAPESATTPGRENSTEASPSTDASAAPAATAPEGSQPQEEQTATTERTESASTPGFVVGTERNETIERIMEMGYQREEVERALRAAFNNPDRAVEYLLMGIPENLRQPEPQQQTAAAAEQPSTAATTAEQPAEDDLFAQAAQGGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD
Protein: Envelope glycoprotein B (gB) (P06436)
Organism: Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1)
Function: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress (By similarity). Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation).
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04032}.
Interaction partners:
Sequence:
MRQGAARGCRWFVVWALLGLTLGVLVASAAPSSPGTPGVAAATQAANGGPATPAPPAPGPAPTGDTKPKKNKKPKNPPPPRPAGDNATVAAGHATLREHLRDIKAENTDANFYVCPPPTGATVVQFEQPRRCPTRPEGQNYTEGIAVVFKENIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRSTAKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGTTVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTSYAADRFKQVDGFYARDLTTKARATAPTTRNLLTTPKFTVAWDWVPKRPSVCTMTKWQEVDEMLRSEYGGSFRFSSDAISTTFTTNLTEYPLSRVDLGDCIGKDARDAMDRIFARRYNATHIKVGQPQYYLANGGFLIAYQPLLSNTLAELYVREHLREQSRKPPNPTPPPPGASANASVERIKTTSSIEFARLQFTYNHIQRHVNDMLGRVAIAWCELQNHELTLWNEARKLNPNAIASATVGRRVSARMLGDVMAVSTCVPVAADNVIVQNSMRISSRPGACYSRPLVSFRYEDQGPLVEGQLGENNELRLTRDAIEPCTVGHRRYFTFGGGYVYFEEYAYSHQLSRADITTVSTFIDLNITMLEDHEFVPLEVYTRHEIKDSGLLDYTEVQRRNQLHDLRFADIDTVIHADANAAMFAGLGAFFEGMGDLGRAVGKVVMGIVGGVVSAVSGVSSFMSNPFGALAVGLLVLAGLAAAFFAFRYVMRLQSNPMKALYPLTTKELKNPTNPDASGEGEEGGDFDEAKLAEAREMIRYMALVSAMERTEHKAKKKGTSALLSAKVTDMVMRKRRNTNYTQVPNKDGDADEDDL
Protein: Dickkopf WNT-signaling pathway inhibitor 1b (Dickkopf-like protein 1) (Dickkopf-related protein 1b isoform X1) (Dickkopf1) (Q9PWH3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMHIAMLSTACLIFMGCIKVAGSTMLNSNAIKVGSGAAGASHPVSPSPDVSLLDSLNFALDTPQPLICESDEECGGEEFCFQSRGVCLQCKKRRKRCIRDAMCCPGNHCSNGVCIPNDPDMIQQLGMEEFVSIAHENSTALMPKVSTQGSPQNQMLKGLEGENCLRSSDCAEGLCCARHFWSKICKPVLKEGQVCTKHKRKGTHGLEIFQRCDCGEGLSCRTQRGDGGKASRSLHTCQRH
Protein: Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (MyHC-2a) (Myosin heavy chain IIa) (MyHC-IIa) (Myosin heavy chain, skeletal muscle, adult 2) (G3UW82)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, myofibril {ECO:0000269|PubMed:28752107}. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin-1
- Myosin light chain 1/3, skeletal muscle isoform
- Titin
- Myosin-4
- Myosin light chain 3
- Troponin T, fast skeletal muscle
- Troponin C, skeletal muscle
- Actin, alpha skeletal muscle
- Troponin I, fast skeletal muscle
- Myosin, light chain 12A, regulatory, non-sarcomeric
Sequence:
MSSDAEMAVFGEAAPYLRKSEKERIEAQNRPFDAKTSVFVAEPKESFVKGTIQSKDAGKVTVKTEAGATLTVKEDQIFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNDEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQGLNSADLLKALCYPRVKVGNEYVTKGQTVEQVTNAVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNETVVGLYQKSSVKTLAYLFSGAQTAEAEASSGGAAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQYIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQAMCRGFLARVEYQKMVERRESIFCIQYNIRAFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDDLAKSEAKRKELEEKMVSLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDERLKKKEFEMSNLQSKIEDEQAIGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQVSELKSKEEEQQRLINDLTTQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEVKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKYEETHAELEASQKEARSLGTELFKMKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHIRVVESMQSTLDAEIRSRNDAIRIKKKMEGDLNEMEIQLNHSNRMAAEALRNYRNTQGILKDTQLHLDDALRGQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLSKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKIISEE
Protein: Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Prolyl 4-hydroxylase subunit beta) (Q2HWU2)
Organism: Macaca fuscata fuscata (Japanese macaque)
Function: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07237}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P07237}. Melanosome {ECO:0000250|UniProtKB:P07237}. Cell membrane {ECO:0000250|UniProtKB:P09103}; Peripheral membrane protein {ECO:0000305}. Note=Highly abundant. In some cell types, seems to be also secreted or associated with the plasma membrane, where it undergoes constant shedding and replacement from intracellular sources. Localizes near CD4-enriched regions on lymphoid cell surfaces. Colocalizes with MTTP in the endoplasmic reticulum. {ECO:0000250|UniProtKB:P07237}.
Interaction partners:
Sequence:
MLRRALLCLAVAAAPGLYADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKYNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEEVAFDENKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAIKVHSFPTLKFFPASVDRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL
Protein: Adhesion G protein-coupled receptor L3 (Calcium-independent alpha-latrotoxin receptor 3) (CIRL-3) (Latrophilin-3) (Q9Z173)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells. Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q80TS3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80TS3}. Cell projection, axon {ECO:0000250|UniProtKB:Q80TS3}. Cell junction {ECO:0000250|UniProtKB:Q80TS3}.
Interaction partners:
- Leucine-rich repeat transmembrane protein FLRT3
- Teneurin-2
- Teneurin-4
- Teneurin-3
- Netrin receptor UNC5D
- Netrin receptor UNC5C
- Netrin receptor UNC5A
- Vascular endothelial growth factor A
- Guanine nucleotide-binding protein G
- Unc-5 family C-terminal like
Sequence:
MCPPQLFILMMLLAPVVHGGKHNERHPALAAPLRHAEHSPGGPLPPRHLLQQPAAERSTAHRGQGPRGTARGVRGPGAPGAQIAAQAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDFGPLDSRSGPVHHGQVSYISPPIHLDSDLERPPVRGISTTGPLGMGSTTTSTTLRTTTWNLGRSTTPSLPGRRNRSTSTPSPAIEVLDVTTHLPSAASQIPAMEESCEAVEAREIMWFKTRQGQVAKQSCPAGTIGVSTYLCLAPDGIWDPQGPDLSNCSSPWVNHITQKLKSGETAANIARELAEQTRNHLNAGDITYSVRAMDQLVGLLDVQLRNLTPGGKDSAARSLNKLQKRERSCRAYVQAMVETVNNLLQPQALNAWRDLTTSDQLRAATMLLDTVEESAFVLADNLLKTDIVRENTDNIQLEVARLSTEGNLEDLKFPENTGHGSTIQLSANTLKQNGRNGEIRVAFVLYNNLGPYLSTENASMKLGTEAMSTNHSVIVNSPVITAAINKEFSNKVYLADPVVFTVKHIKQSEENFNPNCSFWSYSKRTMTGYWSTQGCRLLTTNKTHTTCSCNHLTNFAVLMAHVEVKHSDAVHDLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNINYEDNRPFIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRTHCCSGKSTESSIGSGKTSGSRTPGRYSTGSQSRIRRMWNDTVRKQSESSFITGDINSSASLNRGSYLPCIQACVTYLEGLLNNARDTSVMDTLPLNGNHGNSYSIAGGEYLSNCVQIIDRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNRNMMNKLVDNLGSGSEDDAIVLDDAASFNHEESLGLELIHEESDAPLLPPRVYSTDNHQPHHYSRRRLPQDHSESFFPLLTDEHTEDPQSPHRDSLYTSMPALAGVPAADSVTTSTQTEAAAAKGGDAEDVYYKSMPNLGSRNHVHPLHAYYQLGRGSSDGFIVPPNKDGASPEGTSKGPAHLVTSL
Protein: Uncharacterized tRNA/rRNA methyltransferase LasT (EC 2.1.1.-) (P37005)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized tRNA/rRNA methyltransferase YfiF
- tRNA
- tRNA
- Uncharacterized protein YafE
- Uncharacterized protein YbdN
Sequence:
MRITIILVAPARAENIGAAARAMKTMGFSDLRIVDSQAHLEPATRWVAHGSGDIIDNIKVFPTLAESLHDVDFTVATTARSRAKYHYYATPVELVPLLEEKSSWMSHAALVFGREDSGLTNEELALADVLTGVPMVADYPSLNLGQAVMVYCYQLATLIQQPAKSDATADQHQLQALRERAMTLLTTLAVADDIKLVDWLQQRLGLLEQRDTAMLHRLLHDIEKNITK
Protein: ATP-dependent protease subunit HslV (EC 3.4.25.2) (Heat shock protein HslV) (P0A7B8)
Organism: Escherichia coli (strain K12)
Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. The complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as RpoH and SulA. In addition, small hydrophobic peptides are also hydrolyzed by HslV. HslV has weak protease activity even in the absence of HslU, but this activity is induced more than 100-fold in the presence of HslU. HslU recognizes protein substrates and unfolds these before guiding them to HslV for hydrolysis. HslV is not believed to degrade folded proteins.
Subcellular location: Cytoplasm.
Interaction partners:
- ATP-dependent protease ATPase subunit HslU
- ATP-dependent Clp protease ATP-binding subunit ClpX
- ATP-dependent Clp protease proteolytic subunit
- Chaperone protein HtpG
- Protein GrpE
- Chaperone protein DnaK
- Chaperone protein DnaJ
- Chaperone protein ClpB
- Co-chaperonin GroES
- Lon protease
Sequence:
MTTIVSVRRNGHVVIAGDGQATLGNTVMKGNVKKVRRLYNDKVIAGFAGGTADAFTLFELFERKLEMHQGHLVKAAVELAKDWRTDRMLRKLEALLAVADETASLIITGNGDVVQPENDLIAIGSGGPYAQAAARALLENTELSAREIAEKALDIAGDICIYTNHFHTIEELSYKA
Protein: Integrator complex subunit 11 (Int11) (EC 3.1.27.-) (Cleavage and polyadenylation-specific factor 3-like protein) (CPSF3-like protein) (Q503E1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalytic component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. Mediates the snRNAs 3' cleavage.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5TA45}. Cytoplasm {ECO:0000250|UniProtKB:Q5TA45}.
Interaction partners:
- Integrator complex subunit 3
- Integrator complex subunit 5
- Integrator complex subunit 4
- Integrator complex subunit 9
- Integrator complex subunit 1
- Integrator complex subunit 7
- Integrator complex subunit 6
- Integrator complex subunit 2
- Integrator complex subunit 12
- Integrator complex subunit 10
Sequence:
MPDIKVTPLGAGQDVGRSCILVSIGGKNIMLDCGMHMGFNDDRRFPDFSYITQNGRLTEFLDCVIISHFHLDHCGALPYMSEMVGYDGPIYMTHPTKAICPILLEDFRKITVDKKGETNFFTSQMIKDCMKKVVPLNLHQTVQVDDELEIKAYYAGHVLGAAMVQIKVGSESVVYTGDYNMTPDRHLGAAWIDKCRPDILISESTYATTIRDSKRCRERDFLKKVHETVERGGKVLIPVFALGRAQELCILLETFWERMNLKAPIYFSTGLTEKANHYYKLFITWTNQKIRKTFVQRNMFEFKHIKAFDRSYADNPGPMVVFATPGMLHAGQSLQIFKKWAGNEKNMVIMPGYCVQGTVGHKILNGQKKLEMEGRATLDVKLQVEYMSFSAHADAKGIMQLIRMAEPRNMLLVHGEAKKMEFLKDKIEQEFSISCFMPANGETTTIVTNPSVPVDISLNLLKREMALGGPLPDAKRPRTMHGTLIMKDNSLRLVSPEQALKELGLNEHQLRFTCRVQLHDPHSDTDTLSRIYTHLKSVLKSYSIQHVPDGTVIVESIVIKVTSSAEEPNLKVILLSWSYQDEELGSFLSTLLKKGLPS
Protein: Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 3 (Na(+)/K(+)-transporting ATPase subunit beta-1-interacting protein 3) (Protein FAM77D) (Q3URJ8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGCCTGRCSLVCLCALQLLSALERQIFDFLGFQWAPILGNFLHIIVVILGLFGTIQYRPRYIMVYTVWTALWVTWNVFIICFYLEVGGLSKDTDLMTFNISVHRSWWREHGPGCVRRVLPPSAHGMMDDYTYVSVTGCVVDFQYLEVIHSAVQILLSLVGFVYACYVISISMEEEDTCRNK
Protein: UDP-glucose 6-dehydrogenase (EC 1.1.1.22) (A8WGP7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- UDP-glucuronic acid decarboxylase 1
- UDP-glucose 4-epimerase
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
- Hyaluronan synthase 2
- Hexosyltransferase
- Hyaluronan synthase 3
- Glucuronokinase with putative uridyl pyrophosphorylase
- NAD
Sequence:
MFQIKKICCIGAGYVGGPTCSVIASMCPEITVTVVDVNESRIKAWNSDTLPIYEPGLNEVVLSCRGKNLFFSTDIDSAIKEADLVFISVNTPTKTYGMGKGRAADLKFIEACARRIVEVSDGYKIVTEKSTVPVRAAESIRRIFDANTKPSLNLQVLSNPEFLAEGTAVKDLKEPDRVLIGGDETPEGQRAISALCAVYEHWVPKTRIITTNTWSSELSKLAANAFLAQRISSINSISALCESTGADVEEVARAIGMDQRIGSKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVASYWQQVIDMNEYQRKRFACRIIDCLFNTVTGKKIALLGFSFKKDTGDTRESSSIYISKYLMDEGAKLHIYDPKVLKEQIIQDLSQPGISGDNPERVSDLVTVTVDPYEACESAHALVICTEWDMFKDLDYEKIYHKMLKPAFIFDGRRVLDHLHTQLQNVGFQIETIGKKVMTRIPFTTSGGVPRITEPPVKKSKA
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 (Ribophorin-2) (A0A0B4LFR4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU366029}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU366029}.
Interaction partners:
Sequence:
MLKLGLVIFCVLVASGPTWSARTVDSHLGQKDLSRLQKVFVDGFGSSDLQSIFFSSLNIQLTDATQKEPLCKKIATLHSESKLNSFEKDYYYIGASRNLGCSAKIDEGLLSKVYSSLNSELGSSQEIFYRVVTHKVLGVEINEATQEKLVKRLQELLKKDDTLSGLGYAFNVAPLLGASASFIANRVEDAIVQADEVDGKLLQFEGGLSITSLIINGAFGVSKTFNKPVPITADQAVKFANYFLSRRSVQTAKGAHVLIEALKTISGADKIAPVCVQLIGNGQLDAQSPTLNVAVVDLLGKPLSPAPKVINAKVIRKKDSSVLADKITVASKSSDKTTYVADLASLKPARGVYQAELSADGVYTQTLQFKVLGRVKVQSLEVGIAESDASAATRKQSVTYPGKLQEVLSADSTQKLLLKAVLVDESTSKPLAVHQAFVRLYNKKTDKEIIFVAEQDSSKAYKFDMDVGNNGKNFNYQSGTYSIYLTVGDSSLSNSFEWLVAEVQLKFNEDKVKPKNTSGPLPEIIHQFRVPDKRPPRIVSDIFTGLCITPLVLLFVFWGKLGINVSNLTLAPSTIGFHLGFGGILVLFFVFWLQLNMFQTLRLLIPIAVFTFLAGNRLLRRLYAQRNSKASAS