wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional purine biosynthesis protein ATIC (AICAR transformylase/inosine monophosphate cyclohydrolase) (ATIC) [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR formyltransferase) (AICAR transformylase); Inosine 5'-monophosphate cyclohydrolase (IMP cyclohydrolase) (EC 3.5.4.10) (IMP synthase) (Inosinicase)] (Q9CWJ9)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis. Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR). Also displays cyclohydrolase activity involving the cyclization of FAICAR to IMP. Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54113}.
Interaction partners:
- Adenylosuccinate lyase
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, cytosolic
- Amidophosphoribosyltransferase
- Serine hydroxymethyltransferase, mitochondrial
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
Sequence:
MAPSQLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDAADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMHGSDSKDTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSKGISQMPLRYGMNPHQTPAQLYTLKPKLPITVLNGAPGFINLCDALNAWQLVTELRGAVDIPAAASFKHVSPAGAAVGVPLSEDEARVCMVYDLYPTLTPLAVAYARARGADRMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILSKKKNGNYCVLQMDQSYKPDENEVRTLFGLRLSQKRNNGVVDKSLFSNIVTKNKDLPESALRDLIVATVAVKYTQSNSVCYAKDGQVIGIGAGQQSRIHCTRLAGDKANSWWLRHHPRVLSMKFKAGVKRAEISNAIDQYVTGTIGEGEDLVKWEALFEEVPELLTEAEKKEWVDKLSGVSVSSDAFFPFRDNVDRAKRSGVAYIVAPSGSTADKVVIEACDELGIVLAHTDLRLFHH
Protein: Carboxylesterase 3 (EC 3.1.1.1) (Liver carboxylesterase 31 homolog) (Q6UWW8)
Organism: Homo sapiens (Human)
Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows low catalytic efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin), a prodrug for camptothecin used in cancer therapeutics.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250}.
Interaction partners:
- S-formylglutathione hydrolase
- Hormone-sensitive lipase
- Tumor necrosis factor receptor superfamily member 13C
Sequence:
MERAVRVESGVLVGVVCLLLACPATATGPEVAQPEVDTTLGRVRGRQVGVKGTDRLVNVFLGIPFAQPPLGPDRFSAPHPAQPWEGVRDASTAPPMCLQDVESMNSSRFVLNGKQQIFSVSEDCLVLNVYSPAEVPAGSGRPVMVWVHGGALITGAATSYDGSALAAYGDVVVVTVQYRLGVLGFFSTGDEHAPGNQGFLDVVAALRWVQENIAPFGGDLNCVTVFGGSAGGSIISGLVLSPVAAGLFHRAITQSGVITTPGIIDSHPWPLAQKIANTLACSSSSPAEMVQCLQQKEGEELVLSKKLKNTIYPLTVDGTVFPKSPKELLKEKPFHSVPFLMGVNNHEFSWLIPRGWGLLDTMEQMSREDMLAISTPVLTSLDVPPEMMPTVIDEYLGSNSDAQAKCQAFQEFMGDVFINVPTVSFSRYLRDSGSPVFFYEFQHRPSSFAKIKPAWVKADHGAEGAFVFGGPFLMDESSRLAFPEATEEEKQLSLTMMAQWTHFARTGDPNSKALPPWPQFNQAEQYLEINPVPRAGQKFREAWMQFWSETLPSKIQQWHQKQKNRKAQEDL
Protein: RE13914p (Q8SZ83)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNLILALTTALHLVLVVLAHNPLSTRGESLSDGIRLVMEKRSGDVVHIRPARGTLEAETVASTTNSDTHRTRNNRKPNKPQEHSQQVGAHKSGSRKLVVAENGGALSSQLPQPNHKQGHKNTDKQQRGGGSKQQRGHSQHHGGNRKGPKAATPENGSTCRYAKSAWSNCDHKTNMRSRVLSLRKGEQNCLPTRTIQKKCEKGCRYEKGEWSQCVGGQITREDKLEPEATGGSDQNCNPVRTVSKKCKANGNSSGGKQHGQSRRTKEQKQKDKGASHISS
Protein: Large ribosomal subunit protein bL33 (50S ribosomal protein L33) (P0A7N9)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Alternative ribosome-rescue factor A
- Small ribosomal subunit protein uS10
- GTP pyrophosphokinase
- Large ribosomal subunit protein bL21
- Elongation factor Tu 1
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein bS18
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS11
- Large ribosomal subunit protein bL28
Sequence:
MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK
Protein: Interleukin 12 receptor subunit beta 2 (A0A0A0MTN7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAHTFRGCSLAFMFIITWLLIKAKIDACKRGDVTVKPSHVILLGSTVNITCSLKPRQGCFHYSRRNKLILYKFDRRINFHHGHSLNSQVTGLPLGTTLFVCKLACINSDEIQICGAEIFVGVAPEQPQNLSCIQKGEQGTVACTWERGRDTHLYTEYTLQLSGPKNLTWQKQCKDIYCDYLDFGINLTPESPESNFTAKVTAVNSLGSSSSLPSTFTFLDIVRPLPPWDIRIKFQKASVSRCTLYWRDEGLVLLNRLRYRPSNSRLWNMVNVTKAKGRHDLLDLKPFTEYEFQISSKLHLYKGSWSDWSESLRAQTPEEEPTGMLDVWYMKRHIDYSRQQISLFWKNLSVSEARGKILHYQVTLQELTGGKAMTQNITGHTSWTTVIPRTGNWAVAVSAANSKGSSLPTRINIMNLCEAGLLAPRQVSANSEGMDNILVTWQPPRKDPSAVQEYVVEWRELHPGGDTQVPLNWLRSRPYNVSALISEIPYRVSQNSHPINSLQPRVTYVLWMTALTAAGESSHGNEREFCLQGEDTAALGQAPDRLAHA
Protein: Brevinin-1SE (P85056)
Organism: Lithobates sevosus (Dusky gopher frog) (Rana sevosa)
Function: Mast cell degranulating peptide. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity against the Gram-negative bacterium E.coli K12 and Gram-positive bacterium M.luteus NCT C2665.
Subcellular location: Secreted {ECO:0000269|PubMed:16386333}.
Interaction partners:
Sequence:
FLPLVRGAAKLIPSVVCAISKRC
Protein: Egg-derived tyrosine phosphatase, isoform C (EC 3.1.3.48, EC 3.1.3.64) (A1ZAS8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- phosphatidylinositol-3,5-bisphosphate 3-phosphatase
- phosphatidylinositol-3,5-bisphosphate 3-phosphatase
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Lateral signaling target protein 2 homolog
- Phosphatidylinositol 4-kinase beta
- FIG4 phosphoinositide 5-phosphatase
- Phosphatidylinositol-3-phosphatase SAC1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Putative 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-kinase alpha
Sequence:
MCSLTPNHMVNVTQQHLHDLLETFEKKSFEAAAFEEGTAEYDISKKCEYLFKLDYSLIELDNTNGLLSPRYPGRILIPEYEHGHMAKTLVPGNGLFGQVGGGVGGGGSSGTTATATPLNSSAGSTGSEGVGIQAFVTFANPLQTQQQHPLQQQYPSQQMHPLHAQYPSQQPHPLQQQQQQPSQQQPQNTIYEDQYDIQRMRELVTMAKYARCRQRFAVPVIMYRGKYICRSATLSVMPETYGRKVVDYAYDCLSGGNYTAPNGEENDADSTDESLITHMHDQAQSQFSYDEVIKSDIQLLHTLNVSTIVDLMVENRKIKYFMAVSSSEKADPNKHYKSFNLLSLPYPGCEFFKKFRDNNYMARNLHYNWKQTFNDANINIPNMGPAADIDVAWSEYRDWDLVAITQNYLRATLKYVQEENSGLLIHCISGWDRTPLFVSLVRLSLWADGLIHQSLNAMQMAYFTLAYDWYLFGHQLPDRLKRGEDIMFFCFHVLKFITDEEFSIVEHRKRTKTSSSSGSSVIVIKSDCCDDEPLKDPFTLNCRDYILSFDQDSNDSYSNCSNCDMSITDNFYATTPAQVNPLTSRSPNPKRSRTSPISVPGSNARQRQESTSSNGSWQVVTDTGSIDSMMNGSYMMRFVAQQAADGGGSSNIPLCNGGNGYHCSINAASSGSGSGSGSSISNGSSTHGFANGSSKDVGGSTMASKQCINLRKQRLNAVRAIFIQAYGKTIGLKFKEGSSMNLATFIGNLADQLF
Protein: DNA repair protein RadA (EC 3.6.4.-) (Branch migration protein RadA) (DNA repair protein Sms) (P24554)
Organism: Escherichia coli (strain K12)
Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. Genetic experiments involving combination of radA mutations with mutations in recA, recB, recG, recJ, recQ, ruvA and ruvC show it plays a role in recombination and recombinational repair, probably involving stabilizing or processing branched DNA or blocked replication forks. Is genetically synergistic to RecG and RuvABC. May be involved in recovery of genetic rearrangements during replication fork breakdown. In combination with RadD is important in recovery from double-strand DNA breaks (DSB).
Interaction partners:
- Protein RecA
- Regulatory protein RecX
- DNA repair protein RecN
- DNA helicase II
- Phosphoserine phosphatase
- ATP-dependent DNA helicase RecG
- Single-stranded-DNA-specific exonuclease RecJ
- Holliday junction branch migration complex subunit RuvA
- ATP-dependent DNA helicase RecQ
- DNA replication and repair protein RecF
Sequence:
MAKAPKRAFVCNECGADYPRWQGQCSACHAWNTITEVRLAASPMVARNERLSGYAGSAGVAKVQKLSDISLEELPRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAQQMKTLYVTGEESLQQVAMRAHRLGLPTDNLNMLSETSIEQICLIAEEEQPKLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKDGSLAGPKVLEHCIDCSVLLDGDADSRFRTLRSHKNRFGAVNELGVFAMTEQGLREVSNPSAIFLSRGDEVTSGSSVMVVWEGTRPLLVEIQALVDHSMMANPRRVAVGLEQNRLAILLAVLHRHGGLQMADQDVFVNVVGGVKVTETSADLALLLAMVSSLRDRPLPQDLVVFGEVGLAGEIRPVPSGQERISEAAKHGFRRAIVPAANVPKKAPEGMQIFGVKKLSDALSVFDDL
Protein: Probable ubiquitin carboxyl-terminal hydrolase 1 (EC 3.4.19.12) (Deubiquitinating enzyme 1) (Ubiquitin thioesterase 1) (Ubiquitin-specific-processing protease 1) (Q9USM5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Ubiquitin thioesterase otu2
- Probable ubiquitin carboxyl-terminal hydrolase 2
- Ubiquitin carboxyl-terminal hydrolase 11
- Ubiquitin carboxyl-terminal hydrolase 15
- Ubiquitin carboxyl-terminal hydrolase 14
- AMSH-like protease sst2
- Putative ubiquitin thioesterase otu1
- Ubiquitin carboxyl-terminal hydrolase 6
- Probable ubiquitin carboxyl-terminal hydrolase 1
- Probable ubiquitin carboxyl-terminal hydrolase 7
Sequence:
MASTATQNASTRYSQIWIDQPASLPFQDSINLIKEDKEKWKKEKTAFLIDYDWFEGYVDFIYGEGDNPGPITQWRLLDEKNELKHSLEESIDYSIVSASLWHMLVEWFGLEGLAIERKVLLVGLAAEQKPFVDIYPINFTLHVLFDPINGENTSYSPLYQIDEPYHSDEPYAFSFSRSDTLRSLYKQVMEAFQISDGTSFRLWYLNKSNLSSRFVSLSEFNDQPAIALLSEYAVCMTIFEIDIADGSLLLEFQHPNGEWLSDSITKEQNLTINKEIGLCGLYNLGNSCYMNSALQCMIHTHELTKYFLSDSYEKDINYNNPLGMMGKVALSYASLLKMIHHTADMHSVSPSSFKFIIGEFNTYFSGYRQQDSQEFIAFFLDGLHEDLNRIQIKPYFERPDLFDEHPLHVQRVANQCWDIHTKRNDSIIVQLFQGMYKSTLECSICYQKSTAFDPFMYLTLPLPTSAKWRHKVVYVPPFGTQSPVELYLELLMESTVIQMKFQATEKLQKMGLECGELTACDIYRGKVYKVLKNKDKISKKIHKWDHVVLYGSTANGLTIPIVHGCKRPAMPGSYQSNDVFGFPLQLNVRSRNVLTNDLVKEIVELYRVYAGIDVAIGTLQLGLKRMESKAGKWECIKEIEVKRFEIVEEEEIVIDDKTVIMCLWNDQQYEKLFYNCEWIFEKIQFHMESITLEDCLLEFSKPEQLDLQDSWYCPGCKAFRPATKRLEIWRLPKILVIHLNRFSGHGGDLRRRRKRRDLVVYPVFDLNLKQFLSPFIKDHEWLSSQKSMLYDLYAVDNHHGFMSNGHYTAYARDASSQTFFKFDDTAICEIDPEDIVTSSAYVLFYRAKN
Protein: HIT-type domain-containing protein (Q385E0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RuvB-like helicase
- RuvB-like helicase
- SNF2 DNA repair protein, putative
- Histone H2A
- YEATS domain-containing protein
Sequence:
MVGPRIRNTYAQQLQEERLEKLCDDNAFVNVTDVLRRQRRDAPPANGVASETEFLEESVASATAPSRIHLSRFILEQHRTYLKAMGLNEDEKQHRETKAEGDSSSVSTWSSAASSEKDELVAPPVRGKRMRRDAKPHAEKDKRSGRRTSCGSASGNNDDIECDKDSTTASSDDLARECQYIRSWLLAQGLNSSELRVPPVSYASMTAPPPAHAGGHHLCSVCLLPAGYRCVRCRTALFCSIECHVVHEATRCMKFIV
Protein: PINc domain-containing protein (Q9BL69)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNGDTDASSSRTGAPRKPRPEIQIYRPGMLRQGGSTKSLSSTNEEARPPRPEKLNTTTTTMSGNSRRRSNDTDSVTSRGGSGSTTPDANVINAMNERGGGRNRFEKGYRQQQRTDGPSNYNSTQSLYDTRQHGGYMEYQGNHRSNHRNNGRYSNQQHQQHRQPFERPGGNHYTRGFNERASMRGDGAIARRPQGSRRQRNDSINSTQSEMPPQTGAQLHIDTSFDSASQCGASSNFSMNSLGEAFSFEEMCQNLQNFASMDWSKEVENEFAMQKEQEEEEERRMEQKLQEAAAQEAQKAASPRRNNRRNNRRGGGNSRYHPDESDRESSFGGSIAEEKEEEEAEEELKSGERTPTSVRSGNSYNPRVLYQRTRGANDENHPKRRDAAVEKKPKEPRRYRGEHDDRDDDASEYHGTLENHMSSGRLAGRIQIVQRSQNGTEAGGNRNRQSSEEKPRTYQKRR
Protein: MOB kinase activator 1B (Mob1 homolog 1A) (Mob1A) (Mob1B) (Mps one binder kinase activator-like 1A) (Q7L9L4)
Organism: Homo sapiens (Human)
Function: Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38L.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15067004}. Nucleus {ECO:0000269|PubMed:15067004}.
Interaction partners:
- Serine/threonine-protein kinase LATS1
- Serine/threonine-protein kinase LATS2
- MOB kinase activator 1A
- Serine/threonine-protein kinase 3
- Serine/threonine-protein kinase 38-like
- Protein salvador homolog 1
- Serine/threonine-protein kinase 4
- Serine/threonine-protein kinase 38
- WW domain-containing transcription regulator protein 1
- Transcriptional coactivator YAP1
Sequence:
MSFLFGSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRMAVMLPEGEDLNEWVAVNTVDFFNQINMLYGTITDFCTEESCPVMSAGPKYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDPVIQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLTSKDR
Protein: Protein MGR2 (Q5ABA8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- F1F0 ATP synthase subunit g
- Mitochondrial import inner membrane translocase subunit TIM16
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM21
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit TIM23
- Tom22p
- Mitochondrial import inner membrane translocase subunit TIM14
- Mitochondrial import inner membrane translocase subunit TIM13
- GrpE protein homolog
Sequence:
MPPVQQYQYAGHQPSNWDKFKMGAIMGSTVGVCVGVLFGGFSILQNGAGPNGVMRTLGQYIMGSVGTFGLFMSIGSVIRSESGFQNYEKSMVAMQRAKLRAIYRDE
Protein: Prolargin (Proline-arginine-rich end leucine-rich repeat protein) (P51888)
Organism: Homo sapiens (Human)
Function: May anchor basement membranes to the underlying connective tissue.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Osteomodulin
- Fibromodulin
- Mimecan
- Dermatopontin
- Lumican
- Aggrecan core protein
- Collagen alpha-1
Sequence:
MRSPLCWLLPLLILASVAQGQPTRRPRPGTGPGRRPRPRPRPTPSFPQPDEPAEPTDLPPPLPPGPPSIFPDCPRECYCPPDFPSALYCDSRNLRKVPVIPPRIHYLYLQNNFITELPVESFQNATGLRWINLDNNRIRKIDQRVLEKLPGLVFLYMEKNQLEEVPSALPRNLEQLRLSQNHISRIPPGVFSKLENLLLLDLQHNRLSDGVFKPDTFHGLKNLMQLNLAHNILRKMPPRVPTAIHQLYLDSNKIETIPNGYFKSFPNLAFIRLNYNKLTDRGLPKNSFNISNLLVLHLSHNRISSVPAINNRLEHLYLNNNSIEKINGTQICPNDLVAFHDFSSDLENVPHLRYLRLDGNYLKPPIPLDLMMCFRLLQSVVI
Protein: Regulatory protein zeste (O16114)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVNKQYSATDLEAFMKIAANWQNSNHNLLEGVDIKTEMTQYMNSPSMNMYKKRERTQNWNHQEKKYLLDLCRKDMRIIENKRLDAGLTAVKNKAWKIIHQKFSNQFGTDRTCNRLKEQWRRMKACTRNEILDYNNRLARFGAEVADRKKPSPFTFEVWDFMQEAKKACKSEALDGIDYSKIPLALEEGFEYREDYKFNPEDHDMDDSRTPPQELCDVDIKEEENNETFNETFNHHHLNQSDILGSGERLSVSPNHSISRNGIHEAESPATISTSNVLDSSGAYMAGGGDMSGFQANFNMNNISATLEALNALRSGQFPSAAAAAAAAIHQHQAQAQVAMHHQHNNNNNNNNNNEDDEDSMKPQSKRQRTSSGSMLGSEDQAPVLAPSVPASSDSQALERSGSSNGLTMPGTAVSTNANSSSSNNNNNFELRMFMEMQSKEHMMRMKILEVQLQAAKHSRDLVEINKTLALQKLQLELASKRLPS
Protein: R-spondin-1 (Cysteine-rich and single thrombospondin domain-containing protein 3) (Cristin-3) (mCristin-3) (Roof plate-specific spondin-1) (Q9Z132)
Organism: Mus musculus (Mouse)
Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination (By similarity). Regulates Wnt signaling by antagonizing DKK1/KREM1-mediated internalization of LRP6 through an interaction with KREM1 (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:16543246}. Nucleus {ECO:0000269|PubMed:14732490}. Note=Seems to mainly localize to nucleoli. {ECO:0000269|PubMed:14732490}.
Interaction partners:
- E3 ubiquitin-protein ligase ZNRF3
- Leucine-rich repeat-containing G-protein coupled receptor 5
- E3 ubiquitin-protein ligase RNF43
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 6
- Noggin
- Low-density lipoprotein receptor-related protein 5
- Low-density lipoprotein receptor-related protein 6
- Pro-epidermal growth factor
- Protein Wnt-3a
Sequence:
MRLGLCVVALVLSWTHIAVGSRGIKGKRQRRISAEGSQACAKGCELCSEVNGCLKCSPKLFILLERNDIRQVGVCLPSCPPGYFDARNPDMNKCIKCKIEHCEACFSHNFCTKCQEALYLHKGRCYPACPEGSTAANSTMECGSPAQCEMSEWSPWGPCSKKRKLCGFRKGSEERTRRVLHAPGGDHTTCSDTKETRKCTVRRTPCPEGQKRRKGGQGRRENANRHPARKNSKEPRSNSRRHKGQQQPQPGTTGPLTSVGPTWAQ
Protein: Na(+)/H(+) exchange regulatory cofactor NHE-RF2 (NHERF-2) (NHE3 kinase A regulatory protein E3KARP) (SRY-interacting protein 1) (SIP-1) (Sodium-hydrogen exchanger regulatory factor 2) (Solute carrier family 9 isoform A3 regulatory factor 2) (Tyrosine kinase activator protein 1) (TKA-1) (Q920G2)
Organism: Rattus norvegicus (Rat)
Function: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May also act as scaffold protein in the nucleus.
Subcellular location: Endomembrane system; Peripheral membrane protein. Nucleus. Apical cell membrane. Note=Nuclear, in a punctate pattern. Localizes with EZR and PODXL at the apical cell membrane of glomerular epithelium cells and the sides of the food processes.
Interaction partners:
- Ezrin
- Radixin
- Podocalyxin
- Sodium/hydrogen exchanger 3
- Cystic fibrosis transmembrane conductance regulator
- Moesin
- Lysophosphatidic acid receptor 2
- Chloride anion exchanger
- Thyroid hormone receptor interactor 6
- Apoptosis regulatory protein Siva
Sequence:
MAAPESLRPRLCRLVRGEQGYGFHLHGEKGRRGQFIRRVEPGSPAEAAALRAGDRLVEVNGVNVEGETHHQVVHRIKAVEGQTQLLVVDKETDEELCRRQLTCTEEMAHRGLPPAHNPWEPKPDWACSGSLGSDTGHKDVNGPPRELRPRLCHLRRGPQGYGFNLHSDKSRPGQYIRSVDPGSPASLSGLRAQDRLIEVNGQNVEGLRHAEVVARIKAQEDEARLLVVDPETDEHFKRLRVVPTEDHVEGPLPSPVTNGTSLAQLNGGSVCSSRSDLPGSEKDNEDGSAWKRDPFQESGLHLSPTAAEAKEKARATRVNKRAPQMDWNRKREIFSNF
Protein: D(2) dopamine receptor (Dopamine D2 receptor) (O73810)
Organism: Meleagris gallopavo (Wild turkey)
Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDPLNLSWYNTGDRNWSEPVNESSADQKPQYNYYAVLLTLLIFVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWRFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAAAMPMLYNTRYSSKRRVTVMIACVWVLSFAISSPILFGLNKADERECIIANPAFVVYSSVVSFYVPFIVTLLVYVQIYMVLRRRRKRHTKRSSHGLDSDTHAPLKDKCTHPENVKLGTVIVKSNGSFQVNKRKCEAESHIKMEMEMMSSTSPPERTIVKAAAPSNHQLVVPVASSRSTLDSPGKVEKNGHAKENLHTAKVFEIQSMPNGKTRSTLLKAMNRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNMHCDCNIPPAMYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFMKILHC
Protein: SNW domain-containing protein 1 (G3V3A4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367140}.
Interaction partners:
Sequence:
MALTSFLPAPTQLSQDQLEAEEKARSQRSRQTSLVSSRREPPPYGYRKGWIPRLLEDFGDGGAFPEIHVAQYPLDMGRKKKMSNALAIQVDSEGKIKYDAIARQGQSKDKVIYSKYTDLVPKEVMNADDPDLQRPDEEAIKEITEKTRVALEKSVSQKVAAAMPVRAADKLAPAQYIRYTPSQQGVAFNSGAKQRVIRMVEMQKDPMEPPRFKINKKIPRGPPSPPAPVMHSPSRKMTVKEQQEWKIPPCISNWKNAKGYTIPLDKRLAADGRGLQTVHINENFAKLAEALYIADRKAREAVEMRAQVERKMAQKEKEKHEEKLREMAQKARERRAGIKTHVEKEDGEARERDEIRHDRRKERQHDRNLSRAAPDKRSKLQRNENRDISEVIALGVPNPRTSNEVQYDQRLFNQSKGMDSGFAGGEDEIYNVYDQAWRGGKDMAQSIYRPSKNLDKDMYGDDLEARIKTNRCQAIQLNFSVYTGESKVVHSFFSFSLDLFPTRSFLVQTVDREAEKDQCSLRKILLVWTSFWKKPNSMVALKDPQIAAAPRNTSMKARRGGRNRHRSLQSE
Protein: C-C motif chemokine 25 (Chemokine TECK) (Small-inducible cytokine A25) (Thymus-expressed chemokine) (O35903)
Organism: Mus musculus (Mouse)
Function: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 9
- Atypical chemokine receptor 4
- Atypical chemokine receptor 2
- C-C chemokine receptor type 7
- Stromal cell-derived factor 1
- C-C motif chemokine 5
- C-C motif chemokine
- C-X-C motif chemokine 17
- C-C chemokine receptor type 5
- C-C motif chemokine 27
Sequence:
MKLWLFACLVACFVGAWMPVVHAQGAFEDCCLGYQHRIKWNVLRHARNYHQQEVSGSCNLRAVRFYFRQKVVCGNPEDMNVKRAMRILTARKRLVHWKSASDSQTERKKSNHMKSKVENPNSTSVRSATLGHPRMVMMPRKTNN
Protein: NOP protein chaperone 1 (Q8N5I9)
Organism: Homo sapiens (Human)
Function: Client-loading PAQosome/R2TP complex cofactor that selects NOP58 to promote box C/D small nucleolar ribonucleoprotein (snoRNP) assembly. Acts as a bridge between NOP58 and the R2TP complex via RUVBL1:RUVBL2.
Subcellular location: Nucleus {ECO:0000305|PubMed:33367824}.
Interaction partners:
- Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2
- Nucleolar protein 58
- RuvB-like 1
- Mirror-image polydactyly gene 1 protein
- RuvB-like 2
Sequence:
MEVHGKPKASPSCSSPTRDSSGVPVSKELLTAGSDGRGGIWDRLLINSQPKSRKTSTLQTVRIERSPLLDQVQTFLPQMARANEKLRKEMAAAPPGRFNIENIDGPHSKVIQMDVALFEMNQSDSKEVDSSEESSQDSSENSSESEDEDDSIPSEVTIDNIKLPNSEGGKGKIEVLDSPASKKKK
Protein: Neuropilin (Q6T867)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MDLFAKLCGSLLVLCAALVYGQEEPCGGSFDASDAGYITTPGYPLEYPPHQNCRWVITAPEPSQRIVLNFNPHFELEKLDCRYDFIEIRDGNSDGADLLGRHCSNIAPPAIISSGPVLHIKFVSDYAHQGAGFSLRYEIYKTGSDCSRNFTSPSGVIESPGFPDKYPHNLECTFIIVVPPHMDVTLTFLTFDLENDPLQGSEGECKYDWLEVWDGLPQVGPLIGRHCGTKIPSEIQSSTGILSLSFHTDMAVAKDGFSARYNMTLKEVNDNFHCSNDLGMESGKISDDQISASSSFYDGRWSPRQARLNFDDNAWTPNEDSNKEYIQVDLHFLKVLTGIATQGAVSKETHKSYFVTTFKLEVSTNGEDWMIYRFGKNHKVFHANADPSEVVLNRIPQPVLARFVRIRPQSWKNGIALRFELYGCQITDAPCSEMQGMLSGLLPDSQISASSMRDIHGATGAARLVASRSGWFPSPTQPVAGEEWLQVDLGVPKTVRGIITQGARGVDGSTSAENRAFVRKYKLAHSLNGKDLSYIIDPKTNLPKIFEGNTHYDTPEIRRFDEIVAQFIRVYPERWSPAGIGMRMEILACDLPESTTIPDTATPTIPAQEETSTAHRTPAPTTLSSLGGLCDFEQSMCGWTHDPMSDLKWSMYSSSSPSLDLTHGPDNFGNFLYVEASPMSEPQRARLLSPSVGPERRLVCLLFYYQLRGAGQESLRVLLRDDDQEETLLWTLKGDQGSMWREGRTILPQSPKEYQVVIEGFFERGSRGHIRIDNIHMSSSIELEQCTQPFAAFPPEMTERRPEDLGNNRLFKGRDRIGQEYPFPAWTTPNPSRDPPVTRISEKDNAWLYTLDPILVTIIVMSSLGVLLGAVCAGLLLYCTCSYNGLSSRSTTTLENYNFELYDGIKHKVKINQQRCCSEA
Protein: Lectin [Cleaved into: Lectin beta chain; Lectin alpha chain] (P02870)
Organism: Lens culinaris (Lentil) (Cicer lens)
Function: D-mannose specific lectin.
Interaction partners:
Sequence:
MASLQTQMISFYLIFLSILLTTIFFFKVNSTETTSFSITKFSPDQKNLIFQGDGYTTKGKLTLTKAVKSTVGRALYSTPIHIWDRDTGNVANFVTSFTFVIDAPSSYNVADEFTFFIAPVDTKPQTGGGYLGVFNSKEYDKTSQTVAVEFDTFYNAAWDPSNKERHIGIDVNSIKSVNTKSWNLQNGERANVVIAFNAATNVLTVTLTYPNSLEEENVTSYTLNEVVPLKDVVPEWVRIGFSATTGAEFAAHEVHSWSFHSELGGTSSSKQAADA