wanglab/gogpt-training-data huggingface dataset:
Protein: Protein smoothened (P56726)
Organism: Mus musculus (Mouse)
Function: G protein-coupled receptor that probably associates with the patched protein (PTCH) to transduce the hedgehog's proteins signal. Binding of sonic hedgehog (SHH) to its receptor patched is thought to prevent normal inhibition by patched of smoothened (SMO) (By similarity). Required for the accumulation of KIF7, GLI2 and GLI3 in the cilia. Interacts with DLG5 at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16136078, ECO:0000269|PubMed:33886552}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:16136078, ECO:0000269|PubMed:19464178, ECO:0000269|PubMed:21659505, ECO:0000269|PubMed:23831757, ECO:0000269|PubMed:25644602}. Note=Cilium localization is promoted by SHH and is required for activity. {ECO:0000269|PubMed:16136078, ECO:0000269|PubMed:19464178}.
Interaction partners:
- Sonic hedgehog protein
- Protein patched homolog 1
- Suppressor of fused homolog
- Indian hedgehog protein
- Protein patched homolog 2
- Beta-arrestin-2
- Kinesin-like protein KIF3A
- Limbin
- Beta-arrestin-1
- EvC complex member EVC
Sequence:
MAAGRPVRGPELAPRRLLQLLLLVLLGGPGRGAALSGNVTGPGPHSASGSSRRDVPVTSPPPPLLSHCGRAAHCEPLRYNVCLGSALPYGATTTLLAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATRGPCAIVERERGWPDFLRCTPDHFPEGCPNEVQNIKFNSSGQCEAPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRFGEPTSSETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSIKSNHPGLLSEKAASKINETMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKKPIPDCEIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGHSDDEPKRIKKSKMIAKAFSKRRELLQNPGQELSFSMHTVSHDGPVAGLAFDLNEPSADVSSAWAQHVTKMVARRGAILPQDVSVTPVATPVPPEEQANMWLVEAEISPELEKRLGRKKKRRKRKKEVCPLRPAPELHHSAPVPATSAVPRLPQLPRQKCLVAANAWGTGESCRQGAWTLVSNPFCPEPSPHQDPFLPGASAPRVWAQGRLQGLGSIHSRTNLMEAEILDADSDF
Protein: FI19801p1 (A1Z7H7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- trypsin
- GH01508p
Sequence:
MSWLISAVFLLLSLCAFSMGQDTISAMCLSDERCTSLKRCEDSDDSGRRGIRPRSSRICGTQRVCCEKAQLDSYDRWLVERTTTVPSTIRNKVSSVLEPPPNESCGQNMECVPRKLCRDNIINDSGISLINPRISPIQCSKSLYRCCAVDQKVDDSESPYLVKQANFKYKNCGYSNPKGLIPDNDKFPYSEDVSIFGEFPWMVGIFTGRQEFLCGGTLIHPRLVVTTSHNLVNETVDTLVARAGDWDLNSLNEPYPHQGSRIKEIIMHSEFDPNSLYNDIALLLLDEPIRLAPHIQPLCLPPPESPELTNQLLSVTCYATGWGTKEAGSDKLEHVLKRINLPLVEREECQAKLRNTRLEARFRLRPSFICAGGDPGKDTCKGDGGSPLFCQMPGEMDRYQLVGIVSWGVECAVEDIPAVYVNVPHLRGWIDEKIRGLGIVLQAQ
Protein: Leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (P07813)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Arginine--tRNA ligase
- Lysine--tRNA ligase, heat inducible
- Lysine--tRNA ligase
- Methionine--tRNA ligase
- Proline--tRNA ligase
- Isoleucine--tRNA ligase
- Glutamate--tRNA ligase
- Glutamine--tRNA ligase
- Asparagine--tRNA ligase
- Cysteine--tRNA ligase
Sequence:
MQEQYRPEEIESKVQLHWDEKRTFEVTEDESKEKYYCLSMLPYPSGRLHMGHVRNYTIGDVIARYQRMLGKNVLQPIGWDAFGLPAEGAAVKNNTAPAPWTYDNIAYMKNQLKMLGFGYDWSRELATCTPEYYRWEQKFFTELYKKGLVYKKTSAVNWCPNDQTVLANEQVIDGCCWRCDTKVERKEIPQWFIKITAYADELLNDLDKLDHWPDTVKTMQRNWIGRSEGVEITFNVNDYDNTLTVYTTRPDTFMGCTYLAVAAGHPLAQKAAENNPELAAFIDECRNTKVAEAEMATMEKKGVDTGFKAVHPLTGEEIPVWAANFVLMEYGTGAVMAVPGHDQRDYEFASKYGLNIKPVILAADGSEPDLSQQALTEKGVLFNSGEFNGLDHEAAFNAIADKLTAMGVGERKVNYRLRDWGVSRQRYWGAPIPMVTLEDGTVMPTPDDQLPVILPEDVVMDGITSPIKADPEWAKTTVNGMPALRETDTFDTFMESSWYYARYTCPQYKEGMLDSEAANYWLPVDIYIGGIEHAIMHLLYFRFFHKLMRDAGMVNSDEPAKQLLCQGMVLADAFYYVGENGERNWVSPVDAIVERDEKGRIVKAKDAAGHELVYTGMSKMSKSKNNGIDPQVMVERYGADTVRLFMMFASPADMTLEWQESGVEGANRFLKRVWKLVYEHTAKGDVAALNVDALTENQKALRRDVHKTIAKVTDDIGRRQTFNTAIAAIMELMNKLAKAPTDGEQDRALMQEALLAVVRMLNPFTPHICFTLWQELKGEGDIDNAPWPVADEKAMVEDSTLVVVQVNGKVRAKITVPVDATEEQVRERAGQEHLVAKYLDGVTVRKVIYVPGKLLNLVVG
Protein: Chitin synthase 1 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase 1) (P30597)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable UDP-N-acetylglucosamine pyrophosphorylase
- Chitin synthase-like protein 2
- NEDD8-conjugating enzyme ubc12
- Putative polysaccharide deacetylase
Sequence:
MRRWFKKTLPRPPDEEESAGLTNKDIVETNHLYPTITNLSLNSDTSSILFDKNKKPLKPKIIIPDKEFDLDYYLKDETESIQSPFEGFTAQPNFSNFNKQGNTMNREANFQRTNEKIQRNKSIKRVKLFHGNLILDCPIPKKLLVTLPQQTEREFAYMRYSAATCDPQDFSKSLFTLRQPLFFQPRKTEICIAITMYNEDEVLFARTMHSVMKNISHLCTRKNSQVWGKDAWKKVVVCIISDGRTKIHPRTLAYLAAIGVYQDGIAKNQVNDKEVKAHIYEYTTQLSIDPNLKFKGSDRGIVPVQMIFCLKEKNQKKLNSHLWFFQAFCPILKPEVCILLDAGTRPGDQSIYHLWKSFDLNPQVAGACGEIVVMKGKLGSGLINPLVATQNFEYKMSNILDKPVESVFGFISVLPGAFSAYRFEALQNDSQGNGPLASYFKGELQNTGKSGIFEANMYLAEDRILCFELVSKKNEAWILHYVKSAYADTDVPDRIPEFVLQRRRWLNGSFFAAAYAICHYYRFFRTSHTISRKFMLSIEFIYQLATIVFGWFNIGNFFIIFYILTSSLASTSANFLPGEILFRIAIWIYASLLVTCFVLALGNRPHGSPNFYLSMVIMYSILMGYLLFCSGWIAYRAISDAIHNASSTSSSYTSALLNSNVFINIVISLSSTYGMYLVVSIISFDPWHMFTSFVQYIFLSIMYTNVLNVYAFCNTHDVSWGTKGDHFTNNDLGVARLLQKGADVEIAIPTNQSDIDAKYEDAVKLLASPSLEFNSPIINHGEQEDFYKNFRTYVVLTWILSNLFLVGIVLSIPKINGISISNNETSAYLSFLLWSVVAFSVFRFIGCIFYLFIRLCTGE
Protein: LD25803p (Q8MSW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFFQRAHHASLELFTKGLSIQDQYTEVLQEYLKDSHLLCVFVLLSHPAARGELRLKSTDPKVPPILTSNYLTESEDVATLMRGIRYIESLEQTKAFQDHLAEIARIPIKECDQIENYRSEEYWRCYAKYFTVTCYHQSGTVKMGPDYDNEACVSQRLKVHGLENLRVADASIMPAVVSANTNAATVMIGERAAHFIQEDYQGEAVGANGGLWVPHMHADEF
Protein: Candida glabrata strain CBS138 chromosome C complete sequence (Q6FWS6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- glycerol kinase
- Ribosomal RNA-processing protein 43
- Mitogen-activated protein kinase HOG1
Sequence:
MSHQQGGSKNPNAMSDLNEYLSNEDRNSQERNDRDDFDVEMQEYTPQPFKRPTASYIPEYIGTSNQFPIQEVVPNTNIPIHQLMENHSAAQSPNRPSSPVNNSNMNNLSGDMSTAAATSVNVNTTSNTDHLRARDHTTVSANVLNLGHLYKNNYGNNNDDGDHISVQEGVTNDSESKQYGTRRDRATSFISRLAGGGDDGSPNDPNPGNASVPIIVKPKTLYQNPQTPTVLPSTYHPINRWSLVKSGVLKEFLAEFMGTMVMIIFGSAVVIQVLSGGKAQQDSYLAAMDALSQSDLSAGEKMAFENLTKLVSSVSAGTFDDIALGWAAAVVMGYFCAGGSAISGGHLNPIITLANFVYRGFPAKKIPFYFFGQLFGAYVGGLIAYGYYKKVISETFPDHFNSETVVSMFCVVPKPYLSSARQFVSEFLCGAMLVACTFALTDPYTSLSGDVFPLMLFLLIFMCNSGLGYQTGTAMNMARDLGPRMALYTVGFSRKLLWTSHHHFFWVPICAPFIGALTGGLVYDIFIYQGHESPVNWPFSLYKETFQRWWFKRPGWQRRNKARRMSDLSEISYAEDEDLDNTYTGTRFPRVTKTKSYHSSHNTDEKKVQFKSVQRDKPHNQNMAAVLDDESSLETASLGDSYIEQYSSKNSN
Protein: Dis1/XMAP215 protein AlpA (Eurofung) (Q5B1Q9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Probable kinetochore protein ndc80
- EB1 homolog
- Kinesin-like protein
- Protein kinase domain-containing protein
- Uncharacterized protein
- Probable kinetochore protein nuf2
- Tubulin beta-2 chain
- Tubulin beta-1 chain
- Clip 170 homolog
- Mitotic spindle checkpoint protein
Sequence:
MPEGEEDFSSLPFPDRFAHKNWKVRKGGYEDAKQQFEKTGDESDPIFAQFQDASLWKGAVTDSNVAAQQDGLAAYCAFLQYGGPAGCARTRGATVPGIVEKGLPQTRPAAKASALEALLLCVELDKPEAVIEEILPVLSHKVPKVIAATLAGLTAIYHNFGCKVVDPKPVLKALPKVFGHADKNVRAEAQNLTVELYRWLKEAMKPVFWAELKPVQQQDLEKLFESVKQEPPPKQERLTRAQQAEVDAGAGGGSEPGEAGGEDDYGEDDGGEVDAFDLAEPIDVFPKIPKDFHEQLGSSKWKDRKEALDALYSALNVPKIKDGPFDEIVRGLAKCMKDANVAVVTVAANCIDLLAKGTRSAFVKHRPTVMPPIMERLKEKKQTVADALGQALDAVFIATTLSDCLEDILEFVKHKNPQVKQETVKFLIRCLRNTRDVPSKPEVKSIADAATKLLTDSSEVNRAGGAEILGTLMKIMGERAMTPFLDGLDDIRKTKIKEYFETAEVKAKDRPKPIVGPPKAAPPSAKKPVGTKKPLGLKKPAAAAPPPPVEEPAPAPSPSKPATKAVPSKRTLPTPGGALKKKLGGPGGLASPQKRVISPPSEEQPQQPPVSKFGLGRGLAGRPIARPPAPAEPAPAPAAPAVSGLTAIERAELEELRLEKERLVRLNEELRSEKAKLSTTIGELQNQNAQLIEDHTRDVLSIKAKETQLTRARSDAEAADQNVQKQKREIERLKRELSRALRSGSMSSPTAIPDQFGMAMPDPGSLYQDPNNAHSAVARSGLHMGPRFESTRPRSYASASPSEEKENGLESPGLGRRKFSPTFGNPYSGMASPTRSSLVGSGSASGEEQPTRSTEPAENWRRAAEVTSQLKARIEQMKVKQGLIGRQPAQR
Protein: Bacteriocin divergicin M35 (P84962)
Organism: Carnobacterium divergens (Lactobacillus divergens)
Function: Bacteriocin with antibacterial activity against many strains of L.monocytogenes, L.seeligeri, L.welshimeri, L.grayi, L.murayi, L.ivanovii, L.innocus, C.divergens and C.piscocola. No antibacterial activity was detected against L.lactis, P.acidilactici, P.pentosaceus, L.salivarius, L.delbruekii, L.acidophilus, L.plantarum, L.casei, L.rhamnosus, S.thermophilus, P.freudenreichii, B.breve and E.coli.
Subcellular location: Secreted {ECO:0000269|PubMed:15541799}.
Interaction partners:
Sequence:
TKYYGNGVYCNSKKCWVDWGTAQGCIDVVIGQLGGGIPGKGKC
Protein: Transcription factor 7 (E5RG75)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYKETVYSAFNLLMHYPPPSGAGQHPQPQPPLHKANQPPHGVPQLSLYEHFNSPHPTPAPADISQKQVHRPLQTPDLSGFYSLTSGSMGQLPHTVSWFTHPSLMLGSGVPGHPAAIPHPAIVPPSGKQELQPFDRNLKTQAESKAEK
Protein: Low affinity immunoglobulin gamma Fc region receptor III-B (Fc-gamma RIII-beta) (CD16-I) (Fc-gamma RIII) (Fc-gamma RIIIb) (FcRIII) (FcRIIIb) (FcR-10) (IgG Fc receptor III-1) (CD antigen CD16b) (O75015)
Organism: Homo sapiens (Human)
Function: Receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1825220}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1825220}. Secreted. Note=Secreted after cleavage.
Interaction partners:
- T-cell surface glycoprotein CD3 zeta chain
- High affinity immunoglobulin epsilon receptor subunit gamma
- B-lymphocyte antigen CD19
- Neural cell adhesion molecule 1
- Tumor necrosis factor receptor superfamily member 8
- Tyrosine-protein kinase SYK
- Low affinity immunoglobulin gamma Fc region receptor III-A
- Myeloid cell surface antigen CD33
- T-cell surface glycoprotein CD4
- Integrin alpha-M
Sequence:
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYSVLEKDSVTLKCQGAYSPEDNSTQWFHNENLISSQASSYFIDAATVNDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVNITITQGLAVSTISSFSPPGYQVSFCLVMVLLFAVDTGLYFSVKTNI
Protein: Phosphodiesterase (EC 3.1.4.-) (Q3TTI9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRPLTCIMYAIFQERDLLKTFKISSDTFVTYMMTLEDHYHSDVAYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEEHCDIFQNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSPSPPLDERSRDCQGLMEKFQFELTLEEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLEETDIDIATEDKSPIDT
Protein: Insulin-like growth factor-binding protein 1 (IBP-1) (IGF-binding protein 1) (IGFBP-1) (P21743)
Organism: Rattus norvegicus (Rat)
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. Promotes cell migration (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P08833}.
Interaction partners:
- Insulin-like growth factor 2
- Insulin-like growth factor 1
- Insulin-2
- Insulin-1
- Insulin-like growth factor-binding protein 6
- Secreted phosphoprotein 24
- Insulin-like growth factor 1 receptor
- Insulin-like growth factor-binding protein 4
- Cation-independent mannose-6-phosphate receptor
- Pappalysin-1
Sequence:
MPEFLTVVSWPFLILLSFQVRVVAGAPQPWHCAPCTAERLELCPPVPASCPEISRPAGCGCCPTCALPLGAACGVATARCAQGLSCRALPGEPRPLHALTRGQGACVLEPAAPATSSLSGSQHEEAKAAVASEDELAESPEMTEEQLLDSFHLMAPSREDQPILWNAISTYSSMRAREITDLKKWKEPCQRELYKVLERLAAAQQKAGDEIYKFYLPNCNKNGFYHSKQCETSLDGEAGLCWCVYPWSGKKIPGSLETRGDPNCHQYFNVQN
Protein: Peroxidase 31 (Atperox P31) (EC 1.11.1.7) (ATP41) (Q9LHA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- Leucine-rich repeat receptor-like protein kinase PXC2
- 1-
Sequence:
MASLKSLFLLFLFFFTAQSRLTTNFYSKTCPRFLDIIRDTITNKQITNPTTAAAVIRLFFHDCFPNGCDASVLISSTAFNTAERDSSINLSLPGDGFDVIVRAKTALELACPNTVSCSDIISVATRDLLITVGGPYYDVFLGRRDSRTSKSSLLTDLLPLPSTPISKIIQQFESKGFTVQEMVALSGAHSIGFSHCKEFVGRVGRNNTGYNPRFAVALKKACANYPKDPTISVFNDIMTPNKFDNMYYQNLKKGLGLLESDHGLYSDPRTRYFVDLYAKNQDLFFKDFAKAMQKLSLFGIQTGRRGEIRRRCDAIN
Protein: Pfmc-2TM Maurer's cleft two transmembrane protein (Q8IIY1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MFHYIYKIYIFTIILCASNLFNNNVVEIGTYKLSYHNGGIQFRMLAQKNDNKKSFGNTLTNILFKDKKKKNLDPQISSLVSLVDNMDITQEKKDKIKNLSLKYINSRDVKEKNESINELQKYSNNEECKEQMDSYLMHLRMQNDIKCLKRKNLWNNIGINSITLSLIIIMIMIACMFAICNAPQYIYVPASFLLIFIIYIVARYFPDMKIGFKKLKTKLNTFFQNKKQITK
Protein: beta-N-acetylhexosaminidase (EC 3.2.1.52) (G5EFL1)
Organism: Caenorhabditis elegans
Interaction partners:
- Alpha-
- Beta-1,4-galactosyltransferase galt-1
- Alpha-
- Alpha-
- Beta-hexosaminidase A
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase
- Exostosin-like-3 homolog
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Fucosyltransferase
- Alpha-galactosidase
Sequence:
MFPMRCIRRRSIDFVLKGVILTTICLFLFHMTSSYPKGGISQRALDSMQKEPQTPVLVQKRENFEESIDVAVEQESKKENPFVNQQASTENAKPITQEVKIERPSRDNEFYKNVVIHFDLKGAPPKVDYFLDLLRLIAKGGATGILLEWEDMFPWTGKLEQFKNTDAYSESDVDMILSEATKLKLDVIPLVQTFGHLEWILKYEEMRKYRENDAYPQVLCLGNEEGVEFVREMIRQVAKKHAKYGIPFFHIGADEAFEFGVCQESLDWIKKNGKNGRKQLLALAHLKAIAEFAKQQTGDSTQILAWHDMLKDFDSRLIKNLELGQIIQPVVWDYSENIITLNDYIFSALAENFPTMWASSAYKGANYPSASTSEVRHYETNNRNWIRTKQNQERKFKNGFQGIIVTGWQRYDHLAGLCETLPIGTASMMLQMQIALNAPALDLEGTRQKAATLLECQGFNVDGVKVVSNQCKYRGFQTYLIYQSEVPNLFARIDSELSKNHHLMGWANRYNRKYNISQNWYHREMLPFVQQLVGQYDRVESDLRASMKDLYFENTIDEFIYENLGEMSEKLHGYLEEIQRLDKLRAWPKRHFPIKK
Protein: Ras-like protein 2 (EC 3.6.5.2) (P01120)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP.
Subcellular location: Cell membrane; Lipid-anchor.
Interaction partners:
- Inhibitory regulator protein IRA2
- Adenylate cyclase
- Serine/threonine-protein kinase SCH9
- Cell division control protein 25
- Serine/threonine-protein kinase RIM15
- Transcriptional activator/repressor GIS1
- cAMP-dependent protein kinase type 1
- Zinc finger protein MSN4
- Zinc finger protein MSN2
- cAMP-dependent protein kinase type 3
Sequence:
MPLNKSNIREYKLVVVGGGGVGKSALTIQLTQSHFVDEYDPTIEDSYRKQVVIDDEVSILDILDTAGQEEYSAMREQYMRNGEGFLLVYSITSKSSLDELMTYYQQILRVKDTDYVPIVVVGNKSDLENEKQVSYQDGLNMAKQMNAPFLETSAKQAINVEEAFYTLARLVRDEGGKYNKTLTENDNSKQTSQDTKGSGANSVPRNSGGHRKMSNAANGKNVNSSTTVVNARNASIESKTGLAGNQATNGKTQTDRTNIDNSTGQAGQANAQSANTVNNRVNNNSKAGQVSNAKQARKQQAAPGGNTSEASKSGSGGCCIIS
Protein: GM14169p (Q95S25)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDDIRSSIDDMMDRFNDSITHSAPKKLLFNRLSASFDLGVSPNKRRRERESPERSLNDTASSLNMPANDSMASLQNSKLRTELIETKGIVIQLRNEIEKKSREHKEAILLAENKSTALKDQCDITSKKNLELQDDLKALRKRELVLKNEASRATAELNQLRLKFDESTLKLQKEKYLQKEDARDVHLCINNELSEYRRIAQRADLELQSTRNELERLRQLNEELQARASGFEQLRANHEKQTQSLKVANDRIQELEFEIQSYSDWKEVVKTSRERLASVPDLLAEVEHLRSHNKHLNTLIGDKLLLEEQVYDYKTRLEREEGARAEAASLQVKLLHMEQELKEWVKVAQDHCLANTLVSPMALRSRIEQLLKEDIIHVAEKTSSASDTKHLNTTIRDLEHKCAIYLKNIEDLNIGLKRHKNFKERLQRKLITVSKERDFYKQLVENFDKDTTLSNASVADMTQDMQVRVRMEVLERTVTGYKDMCATLEREIQSLRQQELVNEPAGEGYDSVKKELDTLRMENDRLRRRKEELEMEMMHRCLRGDFNMKDFKVVHFSENPAAEAYESTKNMMEKLQAEIERLKRRNKKLEDDNEQRLNETTSTGGMTLNFKEFNQLQAELESANGKMRKMRDCFKAAREEFRDVCYMLLGYRIDRIGANSNYRISSMFAEGPDDYLDISLNESNCLALLESPYSHTFNPPIDQQLAASNFPAFFSALTLELFQKATVTMT
Protein: DENN domain-containing protein 2C (Q68D51)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form.
Interaction partners:
Sequence:
MDVGFSRTTVQTLSRSHCKNIKQKISQWEGRANGISNPEKWCPKDFGVRYNCHQEIRLKKNPIAERKSKNLDVTSRENVGLDINENTKSHDQSENENKKHEYDDTHFFKNESESNWVCSRVKEIESCKEDVLDPETSLPPGNFYTSQILWKKIEALPPDKLLNLALEHCDSSEKELNFRVLDSSYGITKSLENIYSEPEGQECGPSINPLPKPRRTFRYLSESGVTPYKERNCDKKYCENNSCAQSSLASSQEPEPKKYGGKIRGRSKRKSFEFEDIQHFRNRNSQTIREELGRNSGSALYYTQSEDNIYEDIIYPTKENPYEDIPVQPLPMWRSPSAWKLPPAKSAFKAPKLPPKPQFLHRKTMEVKNSQAYLRSKLTKDTTLPVTLTEWKLFRAGEVANTKRKNLPRLVLKIDDIFESKRGKKKVKLHSYTGKELPPTKGETSGNESDAEYLPKNRHKRLAQLQPSSKRNPHYQTLERDLIELQEQQLFELFVVVSLQKKPSGISYIPQVIQQFPGKDDHGYKQSKDMEERLKVIPKFCFPDSKDWMPTSELKSETFSFVLTGEDGSRWFGYCKKLLPVGKGKRLPEVYCMVSRLGCFNLFSKILDEVEKRREMSPALVYPFMRSVMEAPFPAPGRTITVKSYLPGAGDESIELCRPLDSRLEHVDFKCLFKCLSVCHLIRVCASLLLERRVIFVANSLSTLSKCGHAVVATLYPFTWQHTYIPVLPASMIDIVCSPTPFLIGILSCSLPQLQDLPIEEVLIVDLCADKFLQEVSDEDEILPPKLQAALMQILEERNEILTQEQNFSQDVTLNSLVSEAFVRFFVELVGHYSLNMTVTERGERVFQREPFRKSHTSRSVRHFLDLFMETQMFAGFIQDRELRKSGVKGLFEIRAIQYLETIPESEPSGMNRILRSLGSKMKFLQKK
Protein: Orexin/Hypocretin receptor type 1 (Hypocretin receptor type 1) (Orexin receptor type 1) (Ox-1-R) (Ox1-R) (Ox1R) (O43613)
Organism: Homo sapiens (Human)
Function: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26950369, ECO:0000269|PubMed:9491897}; Multi-pass membrane protein {ECO:0000269|PubMed:26950369}.
Interaction partners:
- Hypocretin neuropeptide precursor
- Orexin receptor type 2
- Oxidation resistance protein 1
- Pro-MCH
- Ataxin-3-like protein
- Corticotropin-releasing factor receptor 1
- Proenkephalin-B
Sequence:
MEPSATPGAQMGVPPGSREPSPVPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFVVALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGHALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAIMVPQAAVMECSSVLPELANRTRLFSVCDERWADDLYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSDQLGDLEQGLSGEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVLKRVFGMFRQASDREAVYACFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSCCLPGLGPCGSLKAPSPRSSASHKSLSLQSRCSISKISEHVVLTSVTTVLP
Protein: Double-strand-break repair protein rad21-like protein 1 (A2AU37)
Organism: Mus musculus (Mouse)
Function: Meiosis-specific component of some cohesin complex required during the initial steps of prophase I in male meiosis. Probably required during early meiosis in males for separation of sister chromatids and homologous chromosomes. Replaces RAD21 in premeiotic S phase (during early stages of prophase I), while RAD21 reappears in later stages of prophase I. Involved in synaptonemal complex assembly, synapsis initiation and crossover recombination between homologous chromosomes during prophase I. Not required for meiosis in females in young mice, while it is required later as mice age.
Subcellular location: Nucleus {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Chromosome {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Note=In meiotic chromosomes, localized along axial elements in early meiosis: detectable on the axial elements in leptotene, and stays on the axial/lateral elements until mid pachytene. It then disappears and is replaced with RAD21. Compared to REC8, has mutually exclusive loading sites on the chromosomes: REC8 and RAD21L form distinct cohesin-enriched domains along the axial elements. {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21743440}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Cohesin subunit SA-3
- Structural maintenance of chromosomes protein 1B
- Structural maintenance of chromosomes protein 1A
- Meiotic recombination protein REC8 homolog
- Cohesin subunit SA-2
- Cohesin subunit SA-1
- Nipped-B-like protein
- Sister chromatid cohesion protein PDS5 homolog B
- Wings apart-like protein homolog
Sequence:
MFYTHVLMSKRGPLAKIWLAAHWEKKLTKAHVFECNLEITIQKIISPKVKIALRTSGHLLLGVVRIYNRKAKYLLADCSEAFLKMKMTFRPGLVDLPKENFEAAYNTITLPEEFHDFEIYNINEIDISEPLAQNQSRPEEITLREEYSNDLLFQAGSFGDEPEILRRHSFFDDNILMNSSGLVVEHSSGSFAEEKSLFFDNGDGFGDEGAAGEMIDNLLQDESTFLEEAYLNKEVSLPPELPSSIMVEPGNSDDQCIPEDEEINEITLLSNEDEGFTLDPIDDLDIADRRRRKKRRLLVDPVKEISSKAMHRQLASFMDTLMVLDLAPPTQRLMMWKKRGGVDMLLSTATQDLINDELKMLFTKCFLSSDYKLAKLTLKESVRKEVGNQQIAEPSVMGEPNSHSELDQPQDWKDVTDESVGSFQENVNMNVNSEQDILGMISPAVEGLSSMNGSLAQENCPAELESSGSKQNTEAEKWNQRLFQTLNVLREFNKMGMQSFSLKKLCRNSDRKQAAAKFYTLLILKKHRAIELSQSVPYADIIATVGPMFYKM
Protein: NMDA receptor synaptonuclear signaling and neuronal migration factor (Nasal embryonic luteinizing hormone-releasing hormone factor) (Nasal embryonic LHRH factor) (Q6X4W1)
Organism: Homo sapiens (Human)
Function: Couples NMDA-sensitive glutamate receptor signaling to the nucleus and triggers long-lasting changes in the cytoarchitecture of dendrites and spine synapse processes. Part of the cAMP response element-binding protein (CREB) shut-off signaling pathway. Stimulates outgrowth of olfactory axons and migration of gonadotropin-releasing hormone (GnRH) and luteinizing-hormone-releasing hormone (LHRH) neuronal cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:20025934}. Nucleus envelope {ECO:0000250}. Nucleus membrane {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:20025934}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:20025934}; Peripheral membrane protein {ECO:0000269|PubMed:20025934}. Cell projection, dendrite {ECO:0000250}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density {ECO:0000250}. Membrane {ECO:0000250}. Note=Found on the outside of the luteinizing-hormone-releasing hormone (LHRH) cell membrane and axons projecting from the olfactory pit and epithelium. Associates with transcriptionally active chromatin regions. Detected at the nuclear membranes of CA1 neurons. Cortical cytoskeleton. Localized in proximal apical dendrites. Colocalizes with CABP1 in dendrites and dendritic spines. Myristoylation is a prerequisite for extranuclear localization. Translocates from dendrites to the nucleus during NMDA receptor-dependent long-term potentiation (LTP) induction of synaptic transmission at Schaffer collateral/CA1 synapses of hippocampal primary neurons and in a importin-dependent manner (By similarity). {ECO:0000250}.
Interaction partners:
- Neuromedin-K receptor
- KiSS-1 receptor
- Prokineticin-2
- Tachykinin-3
- Chromodomain-helicase-DNA-binding protein 7
- Gonadotropin-releasing hormone receptor
- Fibroblast growth factor receptor 1
- Progonadoliberin-1
- Prokineticin receptor 2
- Heparan-sulfate 6-O-sulfotransferase 1
Sequence:
MGAAASRRRALRSEAMSSVAAKVRAARAFGEYLSQSHPENRNGADHLLADAYSGHDGSPEMQPAPQNKRRLSLVSNGCYEGSLSEEPSIRKPAGEGPQPRVYTISGEPALLPSPEAEAIELAVVKGRRQRHPHHHSQPLRASPGGSREDVSRPCQSWAGSRQGSKECPGCAQLAPGPTPRAFGLDQPPLPETSGRRKKLERMYSVDRVSDDIPIRTWFPKENLFSFQTATTTMQAISVFRGYAERKRRKRENDSASVIQRNFRKHLRMVGSRRVKAQTFAERRERSFSRSWSDPTPMKADTSHDSRDSSDLQSSHCTLDEAFEDLDWDTEKGLEAVACDTEGFVPPKVMLISSKVPKAEYIPTIIRRDDPSIIPILYDHEHATFEDILEEIERKLNVYHKGAKIWKMLIFCQGGPGHLYLLKNKVATFAKVEKEEDMIHFWKRLSRLMSKVNPEPNVIHIMGCYILGNPNGEKLFQNLRTLMTPYRVTFESPLELSAQGKQMIETYFDFRLYRLWKSRQHSKLLDFDDVL