wanglab/gogpt-training-data huggingface dataset:
Protein: Preprotein translocase protein (Q0P9G0)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
- Protein translocase subunit SecD
- Protein-export membrane protein SecF
- Protein translocase subunit SecE
- Membrane protein insertase YidC
- hydroxymethylpyrimidine kinase
- Protein translocase subunit SecA
- Protein-export membrane protein SecG
- Leucine--tRNA ligase
- Transcription-repair-coupling factor
- Lipoprotein
Sequence:
MAENSILTSLLPLVVLFAIFYFLVIRPQQKQAKAHKQMLESLQKGDKIITNGGLICEVVKPEEDFIKVKLNEDNVTAKISREFIAKKIDA
Protein: Proteasome-activating nucleotidase 1 (PAN 1) (Proteasomal ATPase 1) (Proteasome regulatory ATPase 1) (Proteasome regulatory particle 1) (D4GUJ7)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-terminus of the proteasomal ATPase functions like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates (Probable). Is also able to cleave other nucleoside triphosphates including GTP and TTP, but the rate of hydrolysis is 4- to 5-fold slower than for ATP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00553}.
Interaction partners:
- Proteasome subunit alpha 1
- Glycerol kinase
- Proteasome subunit beta
- Desampylase
- Proteasome subunit alpha 2
- Proteasome-activating nucleotidase 2
- Probable metalloprotease HVO_1016
- Large ribosomal subunit protein eL40
- DNA double-strand break repair Rad50 ATPase
Sequence:
MMTDTVDDVDLPYDKDSASQQEKITALQERLEVLETQNEEMRDKLLDTNAENNKYQQKLERLTHENKKLKQSPLFVATVQEITDEGVIIKQHGNNQEALTEVTDEMREELEPDARVAVNNSLSIVKRLDKETDVRARVMQVEHSPDVTYEDIGGLEEQMQEVRETVEMPLDRPEMFAEVGIDPPSGVLLYGPPGTGKTMLAKAVANQTNASFIKMAGSELVHKFIGEGAKLVRDLFEVARENEPAVIFIDEIDAIASKRTDSKTSGDAEVQRTMMQLLAEMDGFDERGNIRIIAATNRFDMLDPAILRPGRFDRLIEVPKPNEDGREIIFQIHTRKMNVSDDVDFVELAEMADNASGADIKAVCTEAGMFAIRDDRTEIFMQDFVDAWEKIQQEASDETEVSRAFA
Protein: Ribonucleotide reductase regulatory TP53 inducible subunit M2B (D4ADQ1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ribonucleoside-diphosphate reductase
- Adenylate kinase 9
- Ribonucleoside-diphosphate reductase subunit M2
- GTP:AMP phosphotransferase AK3, mitochondrial
- Nucleoside diphosphate kinase B
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase 6
- Guanylate kinase
- Nucleoside diphosphate kinase A
- UMP-CMP kinase
Sequence:
MGDPERPEAARPEEGEQLCPETKENEVRSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQASFWTAEEVDLSKDLPHWNKLKSEEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVMEIIVDAVKIEQEFLTEALPVGLIGMNCVLMKQYIEFVADRLLGELGFSKIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
Protein: Ktr system potassium uptake protein A (K(+)-uptake protein KtrA) (O32080)
Organism: Bacillus subtilis (strain 168)
Function: Catalytic subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Ktr system potassium uptake protein B
- Ktr system potassium uptake protein D
- Potassium transporter KimA
- Carbamoyl phosphate synthase arginine-specific small chain
- Probable ABC transporter permease protein YqgI
- Cyclic di-AMP receptor A
- Cyclic-di-AMP phosphodiesterase PgpH
- Cyclic-di-AMP phosphodiesterase GdpP
- UPF0750 membrane protein YxkD
Sequence:
MGRIKNKQFAVIGLGRFGGSICKELHRMGHEVLAVDINEEKVNAYASYATHAVIANATEENELLSLGIRNFEYVIVAIGANIQASTLTTLLLKELDIPNIWVKAQNYYHHKVLEKIGADRIIHPEKDMGVKIAQSLSDENVLNYIDLSDEYSIVELLATRKLDSKSIIDLNVRAKYGCTILAIKHHGDICLSPAPEDIIREQDCLVIMGHKKDIKRFENEGM
Protein: Leucine-rich repeat and fibronectin type-III domain-containing protein 4 (D4ABX8)
Organism: Rattus norvegicus (Rat)
Function: Promotes neurite outgrowth in hippocampal neurons. May play a role in redistributing DLG4 to the cell periphery (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase S
- Interleukin-1 receptor accessory protein-like 1
- Receptor-type tyrosine-protein phosphatase F
- Netrin-G1
- Disks large homolog 4
- Interleukin-1 receptor accessory protein
- Disks large homolog 1
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
- Adhesion G protein-coupled receptor L3
Sequence:
MAPPLLLLLLASGAAACPLPCVCQNLSESLSTLCAHRGLLFVPPNVDRRTVELRLADNFIQALGPPDFRNMTGLVDLTLSRNAITRIGARSFGDLESLRSLHLDGNRLVELGSSSLRGPVNLQHLILSGNQLGRIAPGAFDDFLDSLEDLDVSYNNLRQVPWAGIGSMPALHTLNLDHNLIDALPPGVFAQLSQLSRLDLTSNRLATLAPDPLFSRGRDAEASPSPLVLSFSGNPLHCNCELLWLRRLARPDDLETCASPPTLAGRYFWAVPEGEFSCEPPLIARHTQRLWVLEGQRATLRCRALGDPVPTMHWVGPDDRLVGNSSRAWAFPNGTLEIGVTGAGDAGAYTCIATNPAGEATARVELRVLALPHGGNTSAEGGRPGPSDIAASARTAAEGEGTLESEPAVQVTEVTATSGLVSWGPGRPADPVWMFQIQYNSSEDETLIYRIVPASSQHFLLKHLVPGADYDLCLLALSPAAGPSDLTATRLLGCAHFSTLPATPLCHALQAHVLGGTLTVAVGGVLVAALLVFTVALLVRGRGAGNGRLPLKLSHVQSQTNGGTSPMPKSHPPRSPPPRPQRSCSLDLGDTGGCYGYARRLGGAWARRSHSVHGGLLGAGCRGMGGSAERLEESVV
Protein: LIM domain transcription factor LMO4 (Breast tumor autoantigen) (LIM domain only protein 4) (LMO-4) (P61968)
Organism: Homo sapiens (Human)
Function: Transcription cofactor. Plays a role in establishing motor neuron identity, in concert with MNX1, acting, at least in part, to disrupt LDB1-LHX3 complexes thereby negatively modulating interneuron genes in motor neurons.
Interaction partners:
- LIM domain-binding protein 1
- Single-stranded DNA-binding protein 3
- DNA endonuclease RBBP8
- Single-stranded DNA-binding protein 2
- Single-stranded DNA-binding protein 4
- Isopentenyl-diphosphate delta-isomerase 2
- LIM domain-binding protein 2
- Insulin gene enhancer protein ISL-2
- Breast cancer type 1 susceptibility protein
Sequence:
MVNPGSSSQPPPVTAGSLSWKRCAGCGGKIADRFLLYAMDSYWHSRCLKCSCCQAQLGDIGTSCYTKSGMILCRNDYIRLFGNSGACSACGQSIPASELVMRAQGNVYHLKCFTCSTCRNRLVPGDRFHYINGSLFCEHDRPTALINGHLNSLQSNPLLPDQKVC
Protein: Alpha-1,2-mannosyltransferase ALG9 (EC 2.4.1.259) (EC 2.4.1.261) (Asparagine-linked glycosylation protein 9) (Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (P53868)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15987956}; Multi-pass membrane protein {ECO:0000269|PubMed:16847258}.
Interaction partners:
- Dol-P-Man:Man
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- SAGA complex/transcription factor TFIID complex subunit TAF10
- Transcription factor tau 95 kDa subunit
- Putative endoplasmic reticulum mannosidase MNL2
- Dol-P-Glc:Glc
Sequence:
MNCKAVTISLLLLLFLTRVYIQPTFSLISDCDETFNYWEPLNLLVRGFGKQTWEYSPEYSIRSWAFLLPFYCILYPVNKFTDLESHWNFFITRACLGFFSFIMEFKLHREIAGSLALQIANIWIIFQLFNPGWFHASVELLPSAVAMLLYVGATRHSLRYLSTGSTSNFTKSLAYNFLASILGWPFVLILSLPLCLHYLFNHRIISTIRTAFDCCLIFSLTAFAVIVTDSIFYGKLAPVSWNILFYNVINASEESGPNIFGVEPWYYYPLNLLLNFPLPVLVLAILGIFHLRLWPLWASLFTWIAVFTQQPHKEERFLYPIYGLITLSASIAFYKVLNLFNRKPILKKGIKLSVLLIVAGQAMSRIVALVNNYTAPIAVYEQFSSLNQGGVKAPVVNVCTGREWYHFPSSFLLPDNHRLKFVKSGFDGLLPGDFPESGSIFKKIRTLPKGMNNKNIYDTGKEWPITRCDYFIDIVAPINLTKDVFNPLHLMDNWNKLACAAFIDGENSKILGRAFYVPEPINRIMQIVLPKQWNQVYGVRYIDYCLFEKPTETTN
Protein: Cyclin 6 (Q381B4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine/threonine-protein kinase, putative
- Cyclin-dependent kinases regulatory subunit
- Telomerase-associated protein, putative
- Uncharacterized protein
- Cell division cycle protein, putative
- Uncharacterized protein
- Uncharacterized protein
- cyclin-dependent kinase
- Cyclin
- Rev7, putative
Sequence:
MNPTALREVSNLSTGSGDVKQRLAQRRSANLESCRYPYSSSAVRHGSGSLLSLRSSLYSPVGTAGKESSVSPHADRLRENNPVYCSDVIKDITTMYMESEKEAIYGQVLPSPRYLTYQPEINEKMRMILVDWLIDVHLKFKLHPETLYLTVSIVDRYLSSVNTRRTTGRYIPRSKLQLVGITAILLAAKYEEIWPPEVKECVYICANTYTRDEVIRMEREMCTELSFRFTVPTPFPFIVRLLDVVEGLERQQQTQQLSHQLQQIQSQSQSQSQQTQMQASQSQPQSLSRSRSQSRSQPRSDEECTAYVLQLRHTAFFFLDHGMLDYKCLQFSPSQQAKAALFLALVTLHMKEQGSSYVLNNDIIWTRQLQYYSKAQVRDFKACARTMLDFVSYVSTTRYQSVRRKYSSSKYGEVAKLTMPSEVPDF
Protein: Interferon-induced 35 kDa protein homolog (IFP 35) (Ifi-35) (Q9D8C4)
Organism: Mus musculus (Mouse)
Function: Acts as a signaling pathway regulator involved in innate immune system response. In response to interferon IFN-alpha, associates in a complex with transcriptional regulator NMI to regulate immune response; the complex formation prevents proteasome-mediated degradation of IFI35 and correlates with IFI35 dephosphorylation (By similarity). In complex with NMI, inhibits virus-triggered type I interferon/IFN-beta production (By similarity). In complex with NMI, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of the NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries. Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation when actively released by macrophage to the extracellular space during cell injury and pathogen invasion (By similarity). Macrophage-secreted IFI35 activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P80217}. Nucleus {ECO:0000250|UniProtKB:P80217}. Secreted {ECO:0000250|UniProtKB:P80217}. Note=Cytoplasmic IFI35 localizes in punctate granular structures (By similarity). Nuclear localization increased following IFN-alpha treatment (By similarity). Extracelullar following secretion by macrophage (By similarity). {ECO:0000250|UniProtKB:P80217}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL14
Sequence:
MSVTLQTVLYSLQEEQARLKMRLQELQQLKRERTGSPGAKIPFSVPEVPLVFQGQTKQGRQVPKFVVSNLKVCCPLPEGSALVTFEDPKVVDRLLQQKEHRVNLEDCRLRVQVQPLELPVVTNIQVSSQPDNHRVLVSGFPAGLRLSEEELLDKLEIFFGKAKNGGGDVETREMLQGTVMLGFADEEVAQHLCQIGQFRVPLDRQQVLLRVSPYVSGEIQKAEIKFQQAPHSVLVTNIPDVMDAQELHDILEIHFQKPTRGGGEVEALTVVPSGQQGLAIFTSESS
Protein: Insulin-like growth factor-binding protein 2-A (IGF-binding protein 2-A) (IGFBP-2-A) (IGFBP-2a) (Q9PTH3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted.
Interaction partners:
- Insulin-like growth factor 2a.
- Insulin-like growth factor 2
- Insulin-like growth factor 1
- Insulin
- G protein-coupled receptor 22b.
- Insulin
- Pregnancy-associated plasma protein A, pappalysin 1a.
Sequence:
MLSYVSCGLLLALVTFHGTARSEMVFRCPSCTAERQAACPMLTETCGEIVREPGCGCCPVCARQEGEQCGVYTPRCSSGLRCYPKPDSELPLELLVQGLGRCGRKVDTEPTGSAEPREVSGEVQDPLDIGLTEVPPIRKPTKDSPWKESAVLQHRQQLKSKMKYHKVEDPKAPHAKQSQCQQELDQVLERISKITFKDNRTPLEDLYSLHIPNCDKRGQYNLKQCKMSVNGYRGECWCVNPHTGRPMPTSPLIRGDPNCNQYLDGQEMDPSVDPPN
Protein: IP11267p (Mos oncogene) (Q1EC11)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Female sterile
- Mitosis initiation protein fs
- Tubulin alpha-4 chain
- pH-sensitive chloride channel 2
- Vitellogenin receptor Yl
- Deubiquitinase otu
- Cyclin J, isoform A
Sequence:
MGDLLLNTPKRKQLLKDGPPVPTRCQVLGRGAYGTVFKAIYRDRSVAVKIIRAQAASTLHNESHLLNLEHRNIVRLLKLESAADFGLVIMECPRGQSLQRIVDTLALPLMHRVLITLDVVAALRYCHSQNVLHLDVKPTNILVALGTKSSITCNSSKIKVKRSYICKLCDFGSSIEMGEFCAWQEPSVAKGTLRYMSPEALRSDTLTEASDIYSLGITMWQLQARRLPYHTLDCNETIAYQVVKHELRPDNYHQLKILALDSPIDCDWDLAHESTANVICRRANTSARRNLSLDPSYTVGRDLKKKRHRNRLALHFDSPAPEGSACSESAYSQLYKSCWVSAPELRLSSIQLKHELEFILCHST
Protein: Mitogen-activated protein kinase 4a (EC 2.7.11.24) (MAP kinase 4a) (PpMPK4a) (A9T142)
Organism: Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens)
Function: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for innate immunity triggered by pathogen-associated molecular patterns (PAMPs). Involved in resistance to necrotrophic fungi B.cinerea and A.brassicicola. Involved in the transduction of signals from chitosan perception to the activation of defense genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27268428}. Nucleus {ECO:0000269|PubMed:27268428}. Note=Localization to the cytoplasm and nucleus does not change significantly following chitin treatment. {ECO:0000269|PubMed:27268428}.
Interaction partners:
Sequence:
METSSGTPELKVISTPTYGGHYVKYVVAGTDFEVTARYKPPLRPIGRGAYGIVCSLFDTVTGEEVAVKKIGNAFDNRIDAKRTLREIKLLRHMDHENVVAITDIIRPPTRENFNDVYIVYELMDTDLHQIIRSNQALTEDHCQYFLYQILRGLKYIHSANVLHRDLKPTNLLVNANCDLKIADFGLARTLSETDFMTEYVVTRWYRAPELLLNCSAYTAAIDIWSVGCIFMELLNRSALFPGRDYVHQLRLITELIGTPEDRDLGFLRSDNARRYIKHLPRQSPIPLTQKFRGINRSALDLVEKMLVFDPAKRITVEAALAHPYLASLHDINDEPASVSPFEFDFEEPSISEEHIKDLIWREALDCSLGPDDMVQ
Protein: Corticosteroid-binding globulin (CBG) (Serpin A6) (Transcortin) (Q06770)
Organism: Mus musculus (Mouse)
Function: Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species.
Subcellular location: Secreted.
Interaction partners:
- Cannabinoid receptor 2
- Albumin
- Mannose-6-phosphate isomerase
- G-protein coupled receptor 55
- Transient receptor potential cation channel subfamily V member 1
- Sex hormone-binding globulin
- Glucocorticoid receptor
- Transient receptor potential cation channel subfamily V member 2
Sequence:
MSLALYTCLFWLCTSGLWTTQAVTDEDSSSHRDLAPTNVDFAFNLYKRLVALNSDKNTLISPVSISMALAMLSLSTRGSTQYLENLGFNMSKMSEAEIHQGFQYLNSLLQQSDTGLEMNMGNVMFLLQNLKLKDSFLADTKHYYESEALTIPSKDWTKAGEQINNHVKNKTQGKIEHVVSDLDSSATLILINYIFLKGIWKLPFSPENTREEDFYVNETSTVKVPMMVQSGNISYFRDSAIPCQMVQMNYVGNGTTFIILPDQGQMDTVVAALNRDTIDRWGKLMIPRQMNLYIPKFSMSDTYDLQDVLADVGIKDLFTNQSDFADTTKDTPLTLTVLHKAMLQLDEGNVLPAATNGPPVHLPSESFTLKYNRPFIFLAFDKYTWSSLMMSQVMNPA
Protein: (thale cress) hypothetical protein (A0A178WA11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAKYNEIAKKKREAKADRKRAIHGDPLTNKLKTRTPVPSVSGKRQRKLLRKWRREQKDMVEKGLVTMEDVEMASAQAASEDSKKSPRKFSVKKSLKLNKLNNKGKKKKNQKASGEKSADCMLE
Protein: Syncrip, isoform I (A0A0B4KH21)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNKFVSHNLGRDPYRTFSPEMYPLSSPLGPHGTEMAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYGSWSWAWNHSTAWQSRWPTWQHQSSGGPNSATGGGSGSGGGTGGGGGSSAGGHRSGGAGSNRGVPWGVANASQRSWHPARQAATKFTSWSCIQNIHGG
Protein: Inner membrane protein YccS (P75870)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane protein YccF
Sequence:
MLSPLLKRYTWNSAWLYYARIFIALCGTTAFPWWLGDVKLTIPLTLGMVAAALTDLDDRLAGRLRNLIITLFCFFIASASVELLFPWPWLFAIGLTLSTSGFILLGGLGQRYATIAFGALLIAIYTMLGTSLYEHWYQQPMYLLAGAVWYNVLTLIGHLLFPVRPLQDNLARCYEQLARYLELKSRMFDPDIEDQSQAPLYDLALANGLLMATLNQTKLSLLTRLRGDRGQRGTRRTLHYYFVAQDIHERASSSHIQYQTLREHFRHSDVLFRFQRLMSMQGQACQQLSRCILLRQPYQHDPHFERAFTHIDAALERMRDNGAPADLLKTLGFLLNNLRAIDAQLATIESEQAQALPHNNDENELADDSPHGLSDIWLRLSRHFTPESALFRHAVRMSLVLCFGYAIIQITGMHHGYWILLTSLFVCQPNYNATRHRLKLRIIGTLVGIAIGIPVLWFVPSLEGQLVLLVITGVLFFAFRNVQYAHATMFITLLVLLCFNLLGEGFEVALPRVIDTLIGCAIAWAAVSYIWPDWQFRNLPRMLERATEANCRYLDAILEQYHQGRDNRLAYRIARRDAHNRDAELASVVSNMSSEPNVTPQIREAAFRLLCLNHTFTSYISALGAHREQLTNPEILAFLDDAVCYVDDALHHQPADEERVNEALASLKQRMQQLEPRADSKEPLVVQQVGLLIALLPEIGRLQRQITQVPQETPVSA
Protein: Tubulin glycylase 3C (EC 6.3.2.-) (Q23FE2)
Organism: Tetrahymena thermophila (strain SB210)
Function: Probable glycylase which modifies tubulin, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues within the C-terminal tail of tubulin.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:19531357}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19531357}. Note=Mainly present in assembling locomotory cilia.
Interaction partners:
Sequence:
MSSLDEGLKQMSQQEYRNEEQNQEGNQEDLNNQNDHNLNNNELDSLSSPPSDNYNEEEFEQEDDIKPDIKIYQNASQNNISQTQRISQTQLPQQQGGGGKRNSSLLQKEHYHQKNQEIIQKLMEKKKKEQEEKEKKELKLKKREDKLRKRMLEEAAKIREQKEVNLESQTEQSDHSNVTKSKKLKFKSVQDIYQLVVIQGKYQREQLTDKQQQELNEFESRLNEEKTTIIKMQQVYRSRQITFLEELKKKQEKKKQEEEQQKLKQEKIQTKLREQYENVNSNLYAETELFKQKKQEITKVSTQKQLVRASSAEGDKEKDDKKDIAKKIQQKNQEYIEKLKEKKRQEIAKEEEEKKKKEQLKEKMKDFVLVNIKKDIENGVFFVDVPEKKPKKEKKKNESKEDNIQITSPKLNSTKSLSSQITRKTNDAKKVEKLPKIKDSNKENHSKERNEDNEEGDDGEYECDEGDEGASDGEDEDDGNGSAIKRKLRKYPFITDLELWKKKQRLPADIKVFIVTGGYHDISKALKKRGWIANPDTKSPCYNFRWSLQTKDIDYENLKDFQIVNHFQKSACITTKVGLCKSLRNLVWHENVDIDTFYPRCFDLNDTEDFENFVEEFKSSKAESILKRYMRMYFEKDPDIEKIKKQAVIAFNVCERKMKELDEIIDDPNSIQLITKKEWNILSADELTEEKLAQKKYEQWLERIEGKNKQKPKKKKKKSKKDKQQGDTEKKEEEEGEAEDEEEDEEDEEEEEKQMDEFTLKVHQILKRYKVKYPQDCLTGEDNVWIIKPAGLSRGRGITCYNNLVEILDHVKSKESQWVIQKYIENPLIIKKRKFDIRVWILVTDWNPLTIWHYTDCYVRFSVDDYDTENLQNKFTHLTNNMVSKLKQRDEKDDITELGSMYFKENFINYLKEKEGYDVFTDKIEPQIVRAIIMSLKSVQDNIENRKNSIEMYGYDFMVDDLYNTWLIEINSSPSMEYSTPVTERLVKAVSEDIVKVVIDYGMEKSKKARKNIETGAFKRIYKGKYVEEKTNVVGLNLICEGVALKKGKKNSNVAKVNNLKPNFS
Protein: G-protein coupled receptor 55 (Q9Y2T6)
Organism: Homo sapiens (Human)
Function: May be involved in hyperalgesia associated with inflammatory and neuropathic pain (By similarity). Receptor for L-alpha-lysophosphatidylinositol (LPI). LPI induces Ca(2+) release from intracellular stores via the heterotrimeric G protein GNA13 and RHOA. Putative cannabinoid receptor. May play a role in bone physiology by regulating osteoclast number and function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18757503}; Multi-pass membrane protein {ECO:0000269|PubMed:18757503}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-12
- Cannabinoid receptor 1
- Transient receptor potential cation channel subfamily V member 1
- Glucose-dependent insulinotropic receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Fatty-acid amide hydrolase 1
- Beta-arrestin-2
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Cannabinoid receptor 2
Sequence:
MSQQNTSGDCLFDGVNELMKTLQFAVHIPTFVLGLLLNLLAIHGFSTFLKNRWPDYAATSIYMINLAVFDLLLVLSLPFKMVLSQVQSPFPSLCTLVECLYFVSMYGSVFTICFISMDRFLAIRYPLLVSHLRSPRKIFGICCTIWVLVWTGSIPIYSFHGKVEKYMCFHNMSDDTWSAKVFFPLEVFGFLLPMGIMGFCCSRSIHILLGRRDHTQDWVQQKACIYSIAASLAVFVVSFLPVHLGFFLQFLVRNSFIVECRAKQSISFFLQLSMCFSNVNCCLDVFCYYFVIKEFRMNIRAHRPSRVQLVLQDTTISRG
Protein: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4 (EC 2.4.1.102) (Core 2-branching enzyme 3) (Core2-GlcNAc-transferase 3) (C2GnT3) (E9Q649)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- C1GALT1-specific chaperone 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- Mucin-6
- Alpha-1,4-N-acetylglucosaminyltransferase
Sequence:
MKIFRCCFKYTLQQKLFILLLTLWLFSLLKLLNVGRLLFPQRDIYLVEYSLSTSPFVRNRFPESGDAARDNVNCSGVYEHEPLEIGKSLEIRRRSIIDLEDGDVVAMTSDCDVYQTLRQYHEKLVSREEEDFPIAYSLVVHKDAIMVERLIRAIYNQHNLYCIHYDLKSPDTFKAAMNNLAKCFPNIFIASKLETVEYAHISRLQADWNCLSDLLKSSVQWKYVINLCGQDFPLKSNFELVTELKSLQGRNMLETVRPPSAKTERFTYHHELRQVPYDYMKLPVKTNVSKGAPPHNIQVFVGSAYFVLSRAFVKYIFNSSLVEDFFAWSKDTYSPDEHFWATLIRIPGIPGGISSSSQDVSDLQSKTRLVKWFYYEGFLYPNCTGSHLRSVCIYGAAELRWLLNEGHWFANKFDSKVDPILMKCLAEKLEEQQRKLIALSSEKFMTEGTRQSHTL
Protein: Catalase B (EC 1.11.1.6) (Q877A8)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide through its degradation into water and oxygen.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- catalase
- Catalase
- catalase
- Catalase
- Catalase
- Oxidase FUB9
- Oxidase FUB9
- Oxidase FUB9
- Oxidase FUB9
- 3-hydroxyanthranilate 3,4-dioxygenase
Sequence:
MRALSLASLIGIASAACPYMTGELERRDTGTDDATAATEEFLSQYYMADNDTFLTSDVGGPIEDQNSLQVGDRGPTLLEDFIFRQKIQRFDHERVPERAVHARGVGAHGVFTSYGDYSNITAASFLGAEGKETPVFVRFSTVAGSRGSSDLARDVHGFATRFYTDEGNFDIVGNNIPVFFIQDAILFPDLIHAVKPRGDNEIPQAATAHDSAWDFFSQQPSSLHTLLWAMSGHGIPRSLRHVDGFGIHTFRFVTDNGDSKLVKFHWKSLQGKASMVWEEAQQVSGKNPDFMRQDLFEAIEAGRYPEWELGVQIMDEEDQLKFGFDLFDPTKIVPEEYVPITKLGKMTLNRNPRNYFAETEQVMFQPGHIVRGVDFTEDPLLQGRLFSYLDTQLNRHGGPNFEQLPINQPRVPVHNNNRDGAGQMFIPLNPNAYSPNTLNKGSPKQANQTVGKGFFTAPGRESTGRFTRAVSPSFEDVWSQPRLFYNSLTPAEQQFVVDAIRFENSNVKSSVVRNNVIIQLNRVSNDLARRVARAIGVEEPEADPTYYHNNKTTDVGTFGQKLKKLDGLKVGFLASVETPASIEAASELSKQLSEDGVDVVVVAERLSDGVDQTYSGSDAIQFDAVIVAPGAEGLFSTFSFTAPSNATSSSTLFPAGRPLQIVIDGFRFGKPVGAVGSAATALKNAGIQTSRDGVYVDKSVTSGFVDGIKDGLRTFKFLDRFKLDH
Protein: RutC family protein UK114 (Q9V3W0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Molecular chaperone. Seems to fulfill an ATP-independent, HSP70-like function in protein folding. May protect essential factors of cell proliferation during heat shock. No role in calpain activation.
Interaction partners:
Sequence:
MSTIVRKLISTANAAKPVAPYNQAVVADRTVYVSGCLGLDKDTMKLVPGGPTEQAQKALENLEAVLKAADSGVDKVIKNTVFLKDLNDFGAVNEVYKRVFNKDFPARSCFQVAKLPMDALVEIECIALTGSVETKTVQ