wanglab/gogpt-training-data huggingface dataset:
Protein: Atypical chemokine receptor 3 (C-X-C chemokine receptor type 7) (CXC-R7) (CXCR-7) (Chemokine orphan receptor 1) (G-protein coupled receptor 159) (G-protein coupled receptor RDC1 homolog) (RDC-1) (P25106)
Organism: Homo sapiens (Human)
Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Regulates axon guidance in the oculomotor system through the regulation of CXCL12 levels.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31211835}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:22457824}. Recycling endosome {ECO:0000269|PubMed:22457824}. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrestin-dependent manner. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane. {ECO:0000269|PubMed:22457824}.
Interaction partners:
- Stromal cell-derived factor 1
- C-X-C motif chemokine 11
- C-X-C chemokine receptor type 4
- Beta-arrestin-2
- C-C motif chemokine 21
- Probable non-functional immunoglobulin heavy variable 3-16
- Beta-arrestin-1
- Pro-adrenomedullin
- C-X-C motif chemokine 10
- ATP synthase F
Sequence:
MDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCKVTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARAISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALHVTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALEQSTK
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC3 (RNA polymerases I, II, and III subunit ABC3) (DNA-directed RNA polymerase II subunit H) (DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide) (RPB17) (RPB8 homolog) (hRPB8) (P52434)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular location: Nucleus {ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:9852112, ECO:0000269|Ref.6}. Nucleus, nucleolus {ECO:0000305|PubMed:34887565, ECO:0000305|PubMed:36271492}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB11-a
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase III subunit RPC8
Sequence:
MAGILFEDIFDVKDIDPEGKKFDRVSRLHCESESFKMDLILDVNIQIYPVDLGDKFRLVIASTLYEDGTLDDGEYNPTDDRPSRADQFEYVMYGKVYRIEGDETSTEAATRLSAYVSYGGLLMRLQGDANNLHGFEVDSRVYLLMKKLAF
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1 (Oligosaccharyl transferase subunit WBP1) (Oligosaccharyl transferase subunit beta) (P33767)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1724755, ECO:0000269|PubMed:8181570}; Single-pass type I membrane protein {ECO:0000269|PubMed:29301962}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Protein transport protein SEC61
- Protein transport protein SSS1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6
Sequence:
MRTDWNFFFCILLQAIFVVGTQTSRTLVLYDQSTEPLEEYSVYLKDLEQRNYKLEYLDINSTSTTVDLYDKEQRLFDNIIVFPTKGGKNLARQIPVKQLIKFFENEGNILCMSSPGAVPNTIRLFLNELGIYPSPKGHVIRDYFSPSSEELVVSSNHLLNKYVYNARKSEDFVFGESSAALLENREQIVPILNAPRTSFTESKGKCNSWTSGSQGFLVVGFQNLNNARLVWIGSSDFLKNKNQDSNQEFAKELLKWTFNEKSVIKSVHAVHSHADGTSYDEEPYKIKDKVIYSVGFSEWNGEEWLPHIADDIQFELRQVDPYYRLTLSPSGNDSETQYYTTGEFILPDRHGVFTFLTDYRKIGLSFTTDKDVKAIRHLANDEYPRSWEISNSWVYISAICGVIVAWIFFVVSFVTTSSVGKKLETFKKTN
Protein: Glycosyl hydrolase-like protein (EC 3.2.1.-) (Q383P2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Glucosidase 2 subunit beta
- Glucosidase II beta subunit-like
Sequence:
MPAYTGLNGRPIPPGAKRRRHITSALFKTPLLLVPAIFMMILLYYSMRSGRGHRRGLPVPFYDSQETTTSLDDWKKDRSSSGIPGLPPMSDEGRSVIIVPCTASGSINSKLDGQQQVTTEVQFYRTRCQPVVVGKNDERTVKEKGGCSDDVRPIVSIIPQGSEKLYFPKEVLLEEMEEEEQGPQDTVGRFPQRMEKVLSEDGTNGFWLSTSSSGPPIMRCASRALVEPFFSAPLNPQPNWIWGSSGFVVSVLLYTIARDVGKGVVEGSFTFRSREKIHFYGLPLRKKPSAGWIEADDDELDDEAVTGGTLPSGTVPLVYAFGERSVVGILWLNGSPSHAYTTDTADSKSSGMREQTVHFASATGATRVFLLPGPTLEDVLLQYYTLTGFPVFPPLFALGYHHHSVRYRHADDILHVNHMSLSLRLPIDTVGMNLGAVAADDIFAWPRRRIADSLEVQTRLWRDGGHIIVLAVTPTVVPSSGSAAYIEGKEKGYFIFSPLKEGAAFVHLVSGIAKVWIDFLNPRARQWYSEMMEFTRFVGSTNLTHFSLVDNEPMLPRVLGGTDGVTLPSSALHYRGVRHRQVRNVYGMLHSMAAYDGQLSRTNNEYRPFVVTQSYFAGSQRYAAVRLRYRHRRDNDLTLSWARLRETVELCILHSISGLPFVGPDINVPVPNSFWGKKNFDELQVRWYQLSAFLPLFRSDMDVRPRHATILEFPKRTIFRIREAVLFRYTLLPYYYTLFWRSHLYGEPILRPVFLPYEKRGPPPEKGVAMSKESFFVGPDLFVAPVLSAVGEETAWRKEPHHRIRLPPNDLYYDYWTGALQYQGGLVKEPACIRFDKNPPFAEAKHVAPLFLRVGSILPTFTQTRTMRSSHDPANYTLTIALPQLTSELLWASEPVNSSDGRLLAEGELFVDGGDNYVDYNNHSTIRSDFCALRLECRLFPHSYRMEVRLKATVNSSCGKAVEALKANLVELDDPNVYVIDRLRLLFASPSESRFLVRGLPAASENGRQEQMQWKVSYGEIDDNVVEVHNFFVQLSDSLSNESTTHVIAAFDLRL
Protein: Interferon-induced GTP-binding protein Mx1 (Myxoma resistance protein 1) (Myxovirus resistance protein 1) (Q9N0Y3)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Interferon-induced dynamin-like GTPase with antiviral activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15767791}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Binds preferentially to negatively charged phospholipids. {ECO:0000250}.
Interaction partners:
Sequence:
MVNSQGKITDSNPVPNHVLLNGLTDKAEKNQGIGNSLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLINEDEWRGKVSYQDTEMEISDPSEVEVEINKAQDAIAGEGQGISHELISLEVSSPHVPDLTLIDLPGITRVAVGNQPADIGRQTKQLIRKYILKQETINLVVVPCNVDIATTEALSMAQEVDPDGDRTIGILTKPDLVDRGTEGKVVDVAQNLVCHLKKGYMIVKCRGQQDIQDQVSLAEALQKEKDFFEDHPHFRVLLEEGRATVPNLAEKLTSELITHICKTLPLLENQIKENHEKITEELQKYGSDVPEDEHEKMFFLIDKLNAFNQDISSLIQGEESVGEDESRLFTKIRNEFHKWSAVIEKKFQRGYKAIYKQMEKFENRYRGRELPGFVNYKTFEIIIKQQIKELEEPAVDMLHTITDMVQVAFGDISKANFDEFFNLYRTTKSKIEDIKFELEKEAEKSIRLHFQMEQIVYCQDHVYQRALQRVREKDSDEEKKKKTSSMSHDEVSSVNISLSEILEHLLAYRQEATNRISSHIPLIIQYFILQVYGQKLQNGMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLAQARRRLAKFPG
Protein: Protein NifZ (P14889)
Organism: Azotobacter vinelandii
Interaction partners:
Sequence:
MLPQFEYGDEVRLIRNVRNDGTYPGMNTGALLMRRGAVGCVYDVGTYLQDQLIYRVHFLDEGRTIGCREEELILASAPWIPNLFEFRDDVIATRSLAVRGQVLVKRGQLGSIMKVLRDEPELGIQYHVHFGDGLVLQVPEQSLAMADSTAAIEEVLDGI
Protein: SLAM family member 9 (Q9D780)
Organism: Mus musculus (Mouse)
Function: May play a role in the immune response.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MGALLWSLLLLLQEAKGFSGDDEDPEEVIGVLQESINLSLEIPSNEEIKHIDWLFQNNIAIVKPGKKGQPAVIMAVDPRYRGRVSISESSYSLHISNLTWEDSGLYNAQVNLKTSESHITKSYHLRVYRRLSKPHITVNSNISEEGVCNISLTCSIERAGMDVTYIWLSSQDSTNTSHEGSVLSTSWRPGDKAPSYTCRVSNPVSNISSRRISVGSFCADPGYPEKPSMLCLLVKSLFLLLLLAILTVGLCLFRAQKSYETPRVRKLKRNRIKLRKKGKSGPTPV
Protein: Coiled-coil domain-containing protein 186 (Oocyte-testis gene 1 protein) (Q8C9S4)
Organism: Mus musculus (Mouse)
Interaction partners:
- EARP and GARP complex-interacting protein 1
- Syndetin
- Vacuolar protein sorting-associated protein 51 homolog
- Coiled-coil domain-containing protein 138
- RUN domain-containing protein 1
Sequence:
MKIRSRFEEMQSELVPVSMSETEHIASISSDATTEKTSELRDDSCISVSGDESSRLETGAELLSLDSDRILCQTNEHCSQIEVQESHIPDCGSGENSCANTDTCPEDSGQIDDFPGGDFTEQVSKTKEPEQTVTQILAELKSSAPAEAANPKTASASLYDTDCTRKLISEMKTVSASDDLLGEIESELLSAEFAEGHQVPNGLNKGEQALALFEKCVHSRYLQQELTVKQLIKENKNHQELILNICSEKDSLREELRKRTETEKQHMNTIKQLELRIEELNKEIKASKDQLVAQDVTAKNAIQQIHKEMAQRMDQANKKCEEARQEKEAMVMKYVRGEKEALDLRKEKETLERKLRDASKELEKNTNKIKQLSQEKGRLQQLYESKEGETTRLIREIEKLKEEMNSQVIKVKWAQNKLKAEMDSHKETKDKLKETTTKLTQAKEEAEQIRQNCQDMIKTYQESEEIKSNELDAKLRVTKGELEKQMQEKSDQLEMHHAKIKELEDLKRTFKEGMDELRTLRTKAKCLEDERLRTEDELSKYREIINRQKSEIQNLLDKVKITDQLHEQLQSGKQEIEHLKEEMESLNSLINDLQKDIEGSRKRESELLLFTEKLTSKNAQLQSESSALQSQVDNLSCTESQLQSQCQQMGQANRNLESKLLKEEELRKEEVQTLQAELSAAQTEVKALSTQVEELKDELVTQRRKHASNVKDLSKQLQQARRKLEQTENGNHDKDISSMGSRSSSSGSLNARISAEDRSPENTSSSVAVDNFPEVDKAMLIERIVRLQKAHARKNEKIEFMEDHIKQLVEEIRKKTKIIQSYVLREESGTLSSEASDFNKVHLSRRGGIMASLYTSHPADSGLTLELSLEINRKLQAVLEDTLLKNITLKENLQTLGTEIERLIKHQHELEQRTKKA
Protein: Complement C4-B [Cleaved into: Complement C4 beta chain; Complement C4 alpha chain; C4a anaphylatoxin; Complement C4 gamma chain] (P01029)
Organism: Mus musculus (Mouse)
Function: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. Catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0C0L5}. Synapse {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, axon {ECO:0000250|UniProtKB:P0C0L5}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C0L5}.
Interaction partners:
- Membrane cofactor protein
- C4b-binding protein
- Complement receptor type 2
- ABPBG27
- Complement C1s-1 subcomponent
- Complement C1r-A subcomponent
- Complement C1s-1 subcomponent
- Complement C1r-B subcomponent
- Mannan-binding lectin serine protease 2
- Complement decay-accelerating factor, GPI-anchored
Sequence:
MRLLWGLAWVFSFCASSLQKPRLLLFSPSVVNLGTPLSVGVQLLDAPPGQEVKGSVFLRNPKGGSCSPKKDFKLSSGDDFVLLSLEVPLEDVRSCGLFDLRRAPHIQLVAQSPWLRNTAFKATETQGVNLLFSSRRGHIFVQTDQPIYNPGQRVRYRVFALDQKMRPSTDFLTITVENSHGLRVLKKEIFTSTSIFQDAFTIPDISEPGTWKISARFSDGLESNRSTHFEVKKYVLPNFEVKITPWKPYILMVPSNSDEIQLDIQARYIYGKPVQGVAYTRFALMDEQGKRTFLRGLETQAKLVEGRTHISISKDQFQAALDKINIGVRDLEGLRLYAATAVIESPGGEMEEAELTSWRFVSSAFSLDLSRTKRHLVPGAHFLLQALVQEMSGSEASNVPVKVSATLVSGSDSQVLDIQQSTNGIGQVSISFPIPPTVTELRLLVSAGSLYPAIARLTVQAPPSRGTGFLSIEPLDPRSPSVGDTFILNLQPVGIPAPTFSHYYYMIISRGQIMAMGREPRKTVTSVSVLVDHQLAPSFYFVAYFYHQGHPVANSLLINIQSRDCEGKLQLKVDGAKEYRNADMMKLRIQTDSKALVALGAVDMALYAVGGRSHKPLDMSKVFEVINSYNVGCGPGGGDDALQVFQDAGLAFSDGDRLTQTREDLSCPKEKKSRQKRNVNFQKAVSEKLGQYSSPDAKRCCQDGMTKLPMKRTCEQRAARVPQQACREPFLSCCKFAEDLRRNQTRSQAHLARNNHNMLQEEDLIDEDDILVRTSFPENWLWRVEPVDSSKLLTVWLPDSMTTWEIHGVSLSKSKGLCVAKPTRVRVFRKFHLHLRLPISIRRFEQFELRPVLYNYLNDDVAVSVHVTPVEGLCLAGGGMMAQQVTVPAGSARPVAFSVVPTAAANVPLKVVARGVFDLGDAVSKILQIEKEGAIHREELVYNLDPLNNLGRTLEIPGSSDPNIVPDGDFSSLVRVTASEPLETMGSEGALSPGGVASLLRLPQGCAEQTMIYLAPTLTASNYLDRTEQWSKLSPETKDHAVDLIQKGYMRIQQFRKNDGSFGAWLHRDSSTWLTAFVLKILSLAQEQVGNSPEKLQETASWLLAQQLGDGSFHDPCPVIHRAMQGGLVGSDETVALTAFVVIALHHGLDVFQDDDAKQLKNRVEASITKANSFLGQKASAGLLGAHAAAITAYALTLTKASEDLRNVAHNSLMAMAEETGEHLYWGLVLGSQDKVVLRPTAPRSPTEPVPQAPALWIETTAYALLHLLLREGKGKMADKAASWLTHQGSFHGAFRSTQDTVVTLDALSAYWIASHTTEEKALNVTLSSMGRNGLKTHGLHLNNHQVKGLEEELKFSLGSTISVKVEGNSKGTLKILRTYNVLDMKNTTCQDLQIEVKVTGAVEYAWDANEDYEDYYDMPAADDPSVPLQPVTPLQLFEGRRSRRRREAPKVVEEQESRVQYTVCIWRNGKLGLSGMAIADITLLSGFHALRADLEKLTSLSDRYVSHFETDGPHVLLYFDSVPTTRECVGFGASQEVVVGLVQPSSAVLYDYYSPDHKCSVFYAAPTKSQLLATLCSGDVCQCAEGKCPRLLRSLERRVEDKDGYRMRFACYYPRVEYGFTVKVLREDGRAAFRLFESKITQVLHFRKDTMASIGQTRNFLSRASCRLRLEPNKEYLIMGMDGETSDNKGDPQYLLDSNTWIEEMPSEQMCKSTRHRAACFQLKDFLMEFSSRGCQV
Protein: Probable protein phosphatase 2C 25 (AtPP2C25) (EC 3.1.3.16) (Protein phosphatase AP2C1) (O80871)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein phosphatase that negatively regulates defense respones. Inactivates MPK4 and MPK6 MAP kinases involved in stress and defense signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17630279}. Nucleus {ECO:0000269|PubMed:17630279}.
Interaction partners:
- Uncharacterized protein At5g17350
- ARM-repeat/Tetratricopeptide repeat
- Mitogen-activated protein kinase 6
- Germin-like protein subfamily 1 member 15
- Mitogen-activated protein kinase 4
- PHD finger-like domain-containing protein 5A
- Protein SOSEKI 2
- Uncharacterized protein At1g76660
- AT4g32020/F10N7_170
- At1g29190/F28N24_12
Sequence:
MSCSVAVCNSPVFSPSSSLFCNKSSILSSPQESLSLTLSHRKPQTSSPSSPSTTVSSPKSPFRLRFQKPPSGFAPGPLSFGSESVSASSPPGGVLKRKRPTRLDIPIGVAGFVAPISSSAAVAATPREECREVEREGDGYSVYCKRGRREAMEDRFSAITNLHGDRKQAIFGVYDGHGGVKAAEFAAKNLDKNIVEEVVGKRDESEIAEAVKHGYLATDASFLKEEDVKGGSCCVTALVNEGNLVVSNAGDCRAVMSVGGVAKALSSDHRPSRDDERKRIETTGGYVDTFHGVWRIQGSLAVSRGIGDAQLKKWVIAEPETKISRIEHDHEFLILASDGLWDKVSNQEAVDIARPLCLGTEKPLLLAACKKLVDLSASRGSSDDISVMLIPLRQFI
Protein: Varicose, isoform C (Varicose, isoform F) (Q2PDR9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPVETIKMVGLRRDPSKPLGLTVELDEFKQLVVARILAGGVIDKQSMLHVGDVILEVNGTPVRTPDELQVEVSRAKENLTLKIGPNVDEEIKSGRYTVSGGQVKQNGIASLETGKKLTCYMRALFTYNPSEDSLLPCRDIGLPFKSGDILQIINVKDPNWWQAKNITAESDKIGLIPSQELEERRKAFVAPEADYVHKIGICGTRISKRKRKTMYRSVANCEFDKAELLLYEEVTRMPPFRRKTLVLIGVSGVGRRTLKNRLINSDVDKFGAVIPHTSRPKRALEENGSSYWFMDREEMEEAVRNNEFLEYGEHNGNLYGTHLQSIKDVINSGRMCILDCAPNALKILHNSQELMPFVIFVAAPGMEQLKTIYADRRATGSNRNLSFDRQSSIRFSSRRARTLESLASLYEDDDLVATVEESSFVQRKYEKYFDMVIVNEDFDETFRQVVETLDQMSHEEQWVPVNWIY
Protein: Ubiquitin carboxyl-terminal hydrolase 46 (EC 3.4.19.12) (Deubiquitinating enzyme) (Ubiquitin thioesterase) (Ubiquitin-specific-processing protease) (P34547)
Organism: Caenorhabditis elegans
Function: Regulates the abundance of the glr-1 glutamate receptor in the ventral nerve cord by promoting its deubiquitination and preventing its degradation in the lysosome. Contributes to the regulation of embryonic polarity.
Subcellular location: Perikaryon {ECO:0000269|PubMed:21273419}. Cytoplasm {ECO:0000269|PubMed:21273419}. Note=In ventral nerve cord interneurons, localized to discrete puncta within the perikaryon. In the ventral nerve cord, localized diffusely throughout the cytoplasm and to punctate structures.
Interaction partners:
- WD repeat-containing protein 20 homolog
- WD repeat-containing protein 48 homolog
- Glutamate receptor 1
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin carboxyl-terminal hydrolase
- Dol-P-Man:Man
Sequence:
MGATGSSQLEKEISTTESVNNANEHYYGLVNFGNTCYCNSVIQALFFCRPFREKVLNYKQTLKKSGASKDNLVTCLADLFHSIASQKRRVGTIAPKRFITKLKKENELFDNYMQQDAHEFFNYLINTISETLIQEKIAEREKASRHGTLKKGNVTVNLAPATAGLPRSDEKGTSERNGGITVEGNEFLNKSDTTTWIHEIFQGILTNETRCLSCETVSSKDEDFLDLSIDVEQNTSISHCLRVFSETETLCGDQKYFCETCSSKQEAQKRMRIKKPPQLLALHLKRFKFVEPLNRHTKLSYRVVFPLELRLFNVSDDAEYGDRMYDLVATVVHCGATPNRGHYITLVKSNSFWLVFDDDIVEKLEVSSMEEFSGMSTDANIQMPPGNQSAPQKNSESAYILFYQARDYAADDPNHNHKGKNSTHSV
Protein: Galectin-7 (Gal-7) (O54974)
Organism: Mus musculus (Mouse)
Function: Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250}.
Interaction partners:
- Apoptosis regulator Bcl-2
- Mothers against decapentaplegic homolog 3
- Keratin, type II cytoskeletal 5
Sequence:
MSATHHKTSLPQGVRVGTVMRIRGLVPDQAGRFHVNLLCGEEQGADAALHFNPRLDTSEVVFNTKQQGKWGREERGTGIPFQRGQPFEVLLIATEEGFKAVVGDDEYLHFHHRLPPARVRLVEVGGDVQLHSLNIF
Protein: Germ cell-less protein-like 1 (mGcl-1) (DP-interacting protein) (DIP) (Q920G9)
Organism: Mus musculus (Mouse)
Function: Possible function in spermatogenesis. Enhances the degradation of MDM2 and increases the amount of p53 probably by modulating the nucleocytoplasmic transport.
Subcellular location: Nucleus matrix.
Interaction partners:
Sequence:
MGALSSRVLRPAGRTEQPEPTPGAGGAARRSDAGEDAGHSFCYCPGGRKRKRSSGTFCYCHPDSETDDDEDEGDEQQRLLNTPRRKKLKSTSKYIYQTLFLNGENSDIKICALGEEWSLHKIYLCQSGYFSSMFSGSWKESSMNIIELEIPDQNIDIEALQVAFGSLYRDDVLIKPSRVVAILAAACMLQLDGLIQQCGETMKETISVRTVCGYYTSAGTYGLDSVKKKCLEWLLNNLMTHQSVELFKELSINVMKQLIGSSNLFVMQVEMDVYTALKKWMFLQLVPSWNGSLKQLLTETDVWFSKWKKDFEGTTFLETEQGKPFAPVFRHLRLQYIISDLASARIIEQDSLVPSEWLAAVYKQQWLAMLRAEQDSEVGPQEINKEELEGNSMRCGRKLAKDGEYCWRWTGFNFGFDLLVTYTNRYIIFKRNTLNQPCSGSVSLQPRRSIAFRLRLASFDSSGKLICSRATGYQILTLEKDQEQVVMNLDSRLLIFPLYICCNFLYISPEKRTESNRHPENPGH
Protein: Nuclear hormone receptor family member nhr-57 (O16425)
Organism: Caenorhabditis elegans
Function: Orphan nuclear receptor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Hypoxia-inducible factor prolyl hydroxylase
- von Hippel-Lindau tumor suppressor homolog
- Mitochondrial cytochrome c oxidase subunit VIa
- Hypoxia-inducible factor 1
- Paired box protein 3 homolog
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase
- Regulator of hypoxia-inducible factor 1
Sequence:
MLVARERKYCSVCHQLGDGYHFGAIACKACAAFFRRTTSMNLAPKFVCRKKNECVIKMSSRDSCKSCRYAKCLHVGMNPEVVQAIQQAAKQANSPGIESLPSCSSSPASCNSPILSLELGDYDQMTPTLCGVMESYQKLYKKRYDLHAPKLTPRATNYGEFCKIYSNDVYLQFEFLEGSFPQFKEMGGFEKKHVFKYFFVSFLILEMGYRSYQEGTDAIVLANGDFIDTMNLDEFYYDPESLEKCKPTDAMKMYRPNFDQMKRNVFQPLSHQKLSLIEFLALVSLCTWNESLDGQPDCYYPSCRPVRQSVIADLKAFYEKDSPDVDPAYRLSGLLMLLPALERSVELFLQTMEVKRLFRCFPFHDKIYKIIDGQ
Protein: Large ribosomal subunit protein uL15 (50S ribosomal protein L15) (P02413)
Organism: Escherichia coli (strain K12)
Function: This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.
Interaction partners:
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL4
- Elongation factor Tu 1
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein bL35
- Large ribosomal subunit protein uL6
- GTP pyrophosphokinase
- Large ribosomal subunit protein uL30
- DNA-directed RNA polymerase subunit alpha
Sequence:
MRLNTLSPAEGSKKAGKRLGRGIGSGLGKTGGRGHKGQKSRSGGGVRRGFEGGQMPLYRRLPKFGFTSRKAAITAEIRLSDLAKVEGGVVDLNTLKAANIIGIQIEFAKVILAGEVTTPVTVRGLRVTKGARAAIEAAGGKIEE
Protein: Prostaglandin E2 receptor EP2 subtype (PGE receptor EP2 subtype) (PGE2 receptor EP2 subtype) (Prostanoid EP2 receptor) (Q62928)
Organism: Rattus norvegicus (Rat)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Prostaglandin E2 receptor EP4 subtype
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-glucagon
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
- Gastric inhibitory polypeptide
Sequence:
MDNSFNDSRRVENCESRQYLLSDESPAISSVMFTAGVLGNLIALALLARRWRGDTGCSAGSRTSISLFHVLVTELVLTDLLGTCLISPVVLASYSRNQTLVALAPESRACTYFAFTMTFFSLATMLMLFAMALERYLAIGHPYFYRRRVSRRGGLAVLPAIYGVSLLFCSLPLLNYGEYVQYCPGTWCFIQHGRTAYLQLYATVLLLLIVAVLGCNISVILNLIRMQLRSKRSRCGLSGSSLRGPGSRRRGERTSMAEETDHLILLAIMTITFAVCSLPFTIFAYMDETSSRKEKWDLRALRFLSVNSIIDPWVFVILRPPVLRLMRSVLCCRTSLRAPEAPGASCSTQQTDLCGQL
Protein: 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase (HMP-P synthase) (Hydroxymethylpyrimidine phosphate synthase) (EC 2.-.-.-) (Thiamine biosynthesis protein 5) (Thiamine pyrimidine synthase) (Q5ZV75)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP) (Probable). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme (By similarity). The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme (By similarity).
Interaction partners:
- ABC transporter, ATP binding protein
- NADPH-dependent FMN reductase domain protein
- D-amino-acid oxidase
- histidine kinase
- Pyoverdine biosynthesis protein PvcB
- histidine kinase
Sequence:
MAMSSLKSRVTLLLNWYTNPYHTPILVAQQLGFYSEEDIKLAILEPADPSDVTEIVGLGTVDFGVKAMIHTVAAKAKGYPVTSIGTLLDEPPTGLIALKSSGINSFQDIVGKRVGYIGEFGKKIIDDLASLAGIDPTSYKTVRIGMNVTDAIYRDVIDTGIGFINFQKVELEHLCGETVFLRIDQLAGLGCCCFCSIQFIVPEITLQQPELVKGFLRATQRGAAYTTEKPEEAYELLCQAKPQLRTPLYQKIFTRTLPFFSRTLINVDRDWDKVGRYTKHLKIIDEHFDISQCYTNRFLPDTPYSDLKPIACCLEN
Protein: Deoxyhypusine synthase (DHS) (EC 2.5.1.46) (P49366)
Organism: Homo sapiens (Human)
Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Interaction partners:
- Eukaryotic translation initiation factor 5A-1
- Deoxyhypusine hydroxylase
- Eukaryotic translation initiation factor 5A-2
- Eukaryotic translation initiation factor 5A-1-like
- Mitogen-activated protein kinase 3
- Dihydrofolate reductase
- Ornithine decarboxylase
- Spermidine synthase
- Large ribosomal subunit protein uL6
Sequence:
MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMDAFMHEKNED