wanglab/gogpt-training-data huggingface dataset:
Protein: High-affinity gluconate transporter (Gluconate permease 3) (Gnt-III system) (P0AC94)
Organism: Escherichia coli (strain K12)
Function: High-affinity gluconate transporter with fairly broad specificity, including low affinity for glucuronate, several disaccharides, and some hexoses, but not glucose.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Mannonate dehydratase
Sequence:
MHVLNILWVVFGIGLMLVLNLKFKINSMVALLVAALSVGMLAGMDLMSLLHTMKAGFGNTLGELAIIVVFGAVIGKLMVDSGAAHQIAHTLLARLGLRYVQLSVIIIGLIFGLAMFYEVAFIMLAPLVIVIAAEAKIPFLKLAIPAVAAATTAHSLFPPQPGPVALVNAYGADMGMVYIYGVLVTIPSVICAGLILPKFLGNLERPTPSFLKADQPVDMNNLPSFGVSILVPLIPAIIMISTTIANIWLVKDTPAWEVVNFIGSSPIAMFIAMVVAFVLFGTARGHDMQWVMNAFESAVKSIAMVILIIGAGGVLKQTIIDTGIGDTIGMLMSHGNISPYIMAWLITVLIRLATGQGVVSAMTAAGIISAAILDPATGQLVGVNPALLVLATAAGSNTLTHINDASFWLFKGYFDLSVKDTLKTWGLLELVNSVVGLIIVLIISMVA
Protein: poly(A)-specific ribonuclease (EC 3.1.13.4) (H0YBT3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKMFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEANKQS
Protein: Short coiled-coil protein homolog (A7LPF8)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
- UNC-76
- ADP-ribosylation factor-like protein 1
- ADP-ribosylation factor-related protein 1
Sequence:
MSQKTEQDDIPLADDDDTVTIISGGKTPRAAQPLPKEEPPEDPEEKARMITQVLELQNTLDDLSQRVESVKEESLKLRSENQVLGQYIQNLMSSSSVFQSSQPSRPKHSRRRFWRVRILEIRPIVNRRCPYHSLSFVSRAQFAQQKFSYRVQPAYFIFFTFSVRFFITFLCLCEYI
Protein: Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 isoform X1 (ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 3) (A0A140LH27)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MHTMATIGPCSDAEDLLASIHLERYLDHFRQAGFLLARDFCHVDNAALNRVGVAATGHRKRILKLVEHIQLICQHQSKEPSLDRCNSESAIHDVTPVKAKPLSPSKPPGTTFQALRNSSAPNLCAQVKRSFSERSTSVVKPVPKPRTVFHKLRGDKFSLATQHEHRKSSQDPVVIDSSSLSSSTDTVKTATESKKGHLEPSLSCTALSPESEGPLPPVPPRLNRGIPPSTFRRMSGQERLSTPPLCTPPDSPSSYQCSPFTNTPGSPPSPPCSGLEMVSNEIYCGTLPDTPHVFWSRSVPVPPPRQEPSPSTENHSTLEKSNSSESSKRTSASAEEDDDMINPYCETVFHSKRQYQHSEVERSESKEKTSNKEDKLRDHGHHNHSWLKRLDSPGYCTVGESSHSFSLPHNLCSSEADEDIISPYASFTSLSERAAPILSGWLDKLSPQGNYVFQKRYVKFDGKNLMYFGSEKDAYPKGVIPLAAIQMARLAKDNKFEIVTSHRTFVFRADNDVQRSKWCSTLQERVKEQLVFGRPRFGPGSHCQKSGFLELKGTKSKIYTAIIMEQIWLYKSEQCFKNGIGITVIEARGATIRDGKGKSFDLITPYKTFSFTAETDREKRDWMEALQESIAETLSDYEVAEKIWSNRSNKICADCKAINPDWASINLCVVICKNCAGQHRGLGTMVSKVQSLKLDTSVWSNEIVQLFIMLGNDRANEFWAARLPVSEELDCDATPEQRREFISHKYKEGRYRHPHPSFSSQEELLKALCTAVTEQNLLKTVTQIFAEAEAARLADANGNDKRVSPHYSYTQSADSCVYDEIMQPILYSGFLYKSGSLNKGTLSRRTRDADFQKYWCSVEKSILFYESDRCHEPSMKIDVKDIICLGVSRPDSSNNSGFIDKFRYTFELYLMSDKLVQFGLETPDALHSWARAIGKATTPLSCHCLLAREFERVGVLRYKAMLDPQQWKEGFFVLQKSNLFICPGNDGAAEDIINLKRLQELSIASEMENHEKKDILVLVEKGRTLHLQGTGRTDFSLWYADIQKAAGGKGNTLKDQQLSRNDIPIIVDSCIAFITQYGLGHEGIYRKNGAKSRIKLLMEEFRKDARNVKLRIGDNFIEDVTDVLKRFFREIDDPIFMADLHPFWKEAAKIPLKTQRLDRYKELIRGLPRVNRTTLAALISHLYRVQKCADLNQMCTKNLSLLFAPSLFQTDGKGEHEVKIIEDLIDNYLYIFDVDEEHQTQIDLEISLITTWRDTQLSQAGDLIIEVYLEEKIPDCCITLKVSPTMCAEELTNQVLYMRNIPAGEKDVWMTFEAIEDGELERPLHPKEKVLEQALQWCKMADPSSAYLVVKKVPRGEAIDIFTAYKSEIVKSGVLKCREEPPKLLQGNKFQERSFQIKDHKLLLMKDKKSNKPEKEWQLKTLKIYMGIRKKLKPPTKWGLTVLLDKQQLYLSCSCETELWDWMTNLLKAQNDDLRPPVMRRHSSSDISKQKFGTMPLVPIRGEESNTNSTMLSANQTLRKLHTRRALSMFFPMKIQQQDSFEERIEIPEPLYEEVGDFGLQVLKSLETSFLSSGHAETQEVPMRPISLGQRKTTSLDRMLGSRPFVSSGESLDALSHDGSSDSLPIPGRHRAHRSCSPQQELLLQELSTMFCKKPESDEPESLT
Protein: Serine/threonine-protein kinase cst-1 (EC 2.7.11.1) (STE20-like kinase 1) (STE20-like kinase MST) (cMST) [Cleaved into: Serine/threonine-protein kinase cst-1 37kDa subunit; Serine/threonine-protein kinase cst-1 18kDa subunit] (Q9NB31)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which extends lifespan and delays tissue aging, probably by activating daf-16.
Interaction partners:
- Mob1/phocein
- Protein salvador homolog 1
- Serine/threonine-protein kinase WARTS homolog
- Serine/threonine-protein kinase cst-1
- Yes-associated protein homolog 1
- Ras association domain-containing protein 1 homolog
- Forkhead box protein O
- Mps one binder kinase activator-like 2
Sequence:
MPPSTDSSRRNSEEGSSDGFKLDSSALNKPPEEVFDIVGKLGEGSYGSVHKAIHRESGHVLAIKKVPVDTDLQEIIKEISIMQQCKSKYVVKYYGSYFKHSDLWIVMEYCGAGSISDIMRARRKPLSEQEISAVLRDTLKGLQYLHDLKKIHRDIKAGNILLNTDGIAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIEEIGYDTKADIWSLGITAIEMAEGRPPYSDIHPMRAIFMIPTKPPPTFKKPEEWSSEFNDFIRSCLIKKPEERKTALRLCEHTFIKNAPGCDIMQLMIQDAQEKAILGQAPMAASSGNDATLLSEGMSTMIDGGESTLVQHKDNYVTAQSLRSQMESLRIGGEIPKSAYIPGSSKNGNSPRVQPPGHTASASDPSKNQPFAQDGTGPNFQLGTSESSYKDASYNMMNTEAEYENRFQRAVVDGDFEFLRNITLDELIRRKESLDSEMEEEIRELQRRYKTKRQPILDVIEIKKRLQ
Protein: Transcription factor Atoh8 (Helix-loop-helix protein mATH-6) (mATH6) (Okadin) (Protein atonal homolog 8) (Q99NA2)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (By similarity). Regulates endothelial cell proliferation, migration and tube-like structures formation (By similarity). Modulates endothelial cell differentiation through NOS3 (By similarity). May be implicated in specification and differentiation of neuronal cell lineages in the brain. May participate in kidney development and may be involved in podocyte differentiation. During early embryonic development is involved in tissue-specific differentiation processes that are dependent on class II bHLH factors and namely modulates the differentiation program initiated by the pro-endocrine factor NEUROG3. During myogenesis, may play a role during the transition of myoblasts from the proliferative phase to the differentiation phase. Positively regulates HAMP transcription in two ways, firstly by acting directly on the HAMP promoter via E-boxes binding and indirectly through increased phosphorylation of SMAD protein complex (By similarity). Repress NEUROG3-dependent gene activation in a gene-specific manner through at least two mechanisms; requires only either the sequestering of a general partner such as TCF3 through heterodimerization, either also requires binding of the bHLH domain to DNA via a basic motif.
Subcellular location: Nucleus {ECO:0000269|PubMed:24186058}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SQ7}. Cytoplasm {ECO:0000269|PubMed:24186058}.
Interaction partners:
Sequence:
MKHIPVLEDGPWKTVCVKELNGLKKLKRKGKEPVRRANGYKTFRLDLEAPELGATVSTTAATNGLRDRTQPFPIATPVPASVAPAVPPGGGTDTAREFRGIRAPEVSDARKRGFALGTVGPGLPTPPPPPASQSLAPGDPEAHSFREQALRPRILLCAPPARPTQSAPLAPPAAPQESPVRPAPPTRPGESSYSSISHVIYNNHPDSSASPRKRPGEATAASTEIKALQQTRRLLANARERTRVHTISAAFEALRKQVPCYSYGQKLSKLAILRIACNYILSLARLADLDYSADHSNLSFSECVQRCTRTLQAEGRAKKRKE
Protein: Transmembrane protein (F4J4F8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDRSSVLTLLLLILFISNASSFDRFRELVDEETQKDNSNSTTKQESPLINPQPIGDGKSNVTSSEPTLPTSNSTNTNPKEPDSMSPPPPLIPVNEKNDTKVLNTTEPMSPPPPPANLTDSQDSGKLPANMAPPPKSLESGKNETEPGKESPPLAKDPAKGKDDKGSSESASVDTCVGKSNICRTENSLVACTLSIDKGYETFLDIIVIPQQFARSLLCAANWLILVQNEGETSLKAKIVLPVNALQELTLPKHQSQKVNISISGDTNKIILDTGKGQCALHMYPSEESTLPFHFPSYEKLVTPINGAYFLIVSVIIFGGIWAFCLCRKNRRAGSGVPYRELELSGGPGLENESGVHDVETADWDEGWDDDWDENNAVKSPGSAAKSVSISANGLTARAPNRDGWDHDWDD
Protein: Tegument protein UL26 (F5HGG3)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Plays a role in the inhibition of host NF-kappa-B. This inhibition affects both the canonical and the non-canonical pathways. Blocks the induction of host IKK phosphorylation. May also influence the normal phosphorylation state of several tegument proteins including pp28 in virions.
Subcellular location: Virion tegument {ECO:0000250|UniProtKB:P16762}. Host nucleus {ECO:0000269|PubMed:16537622}. Note=Also found in dense bodies.
Interaction partners:
Sequence:
MYAVFGLTRSEVTPHEAAAARYKHRGVIDRRGAAMTSRRAPDGGLNLDDFMRRQRGRHLDLPYPRGYTLFVCDVEETILTPRDVEYWKLLVVTQGQLRVIGTIGLANLFSWDRSVAGVAADGSVLCYEISRENFVVRAADSLPQLLERGLLHSYFEDVERAAQGRLRHGNRSGLRRDADGQVIRESACYVSRALLRHRVTPGKQEITDAMFEAGNVPSALLP
Protein: Separin (EC 3.4.22.49) (Cell untimely torn protein 1) (Separase) (P18296)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the rad21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/cut2 protein. It is also required for pointed nuclear formation.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Securin
- Structural maintenance of chromosomes protein 3
- Meiotic recombination protein rec8
- Cohesin subunit rad21
- Structural maintenance of chromosomes protein 1
- Serine/threonine-protein kinase plo1
- Cohesin subunit psc3
- Tyrosine-protein phosphatase CDC14 homolog
- Sister chromatid cohesion protein pds5
- Protein phosphatase PP2A regulatory subunit B
Sequence:
MSTRSIVTSKVSWTPEKFISALSYPEHCSITLVKRLKASVKLKDLKQNISRDAPSWTFEHLFVAFKCAVSNLAKQWAELSTTDKEKTRRMFCTPSRLNTAHRPEVFYLLECCTYILEQMQVVTKNTSHLYDCIRSGVSICNRLLDMEIFEPAISLLMKTHKNLIILLTYRDHDAIPTATLLNPTLDVSEIQLESCLFVPMVPASYFLNIGTIVVTFQLNVLRCLSLSQINGLSLNTINNLQSEDGPFQWIERSFPSQVQLANSRREILARLLTRFSMIQNNALQSFKLLILSIALWLNILSSQRADDKEFDVNQLETRILQLFSKVVQLCKSEDIEGSILNKDMTQLHHLLENLSKESRLHILLQLSQLYYKYNDFQLSAAYVIRGYSLSFEDISFKLKFLLFSFRLSIHDNSICFPFNLIQELSSLQQLFVENALPYSEALHLLDSIERSFRLFNDSTVFDDTVFALNISEILSWILSSVVRDILVEDELLNLQLKIRKFLMFTFHIIRSFSELTKFQSSLEGCLNLAAYYEDAEFPQKLSNHLYNLCVKSSNVNYARECISLSIKIAVSHKLTNDETYLLKILKNFQLRYHDSLQLQEKCDVLHTTFNQLDLYVGTTSVGKSSVLDNILKRIFNSLTSINDSNIEKLLESISYSLLKLFFKCANEGSRYNASAALSFKLSLMLHEKEEVLLLKTNVSCVLANHGYNDIKFEEMVLCVIKGDQNLLEHNSNNNAKLALNESLLCSWENLLCYRRAEDDSRILTIIESWTIFISRFSSVISRCSFTDFEINSILNFFFCFLHTVEPSGKLTFELAFLEIFYELFNCLLHLQFSKYLVIIGTLLSDKYMTLGFSGKAHLFYTKCYSYLRQCKSSPFINFWNVSYGKYLILTGNTDKGILQLKKYSLSSEEDFNSNGLSRTVSLNLLLYERIQLSDALFQLGYTTVSLGFIMQNLKVIKGLFSKSSKEHFNGGKYITWRLFAVSAHSNVCAARIYEHMGQAREAEFFYRQACSISEKMPFSCFSATFQLRLCSLLTRAGKLEKGEKILFDLTEAMKSTDTYHKLLWNYGAAEVCATKSELDGAICHYSECVKLLEIIKSEYYLFFNRNREKSLTKGIKRLSLSSQPTFVTESNTTEFDDWSILQNTAANLLRLISMFELKRGNLEIAKALMTDSTKCSIASFFNIVSANILKSKLIVCEADSTLFGDPVLRTLPDSVISLPGISHKFQKNQSKTKALGENTGFRKGSKRLDYLRERLKINLQNVRLSCEIIFSNAYERSSVCVCREVNELISYSTIMQSALTTIGETTDVDSSSASFFLEIPKALGFHRRREAQKFRNQHKELHFSSLEQILNSRLSIPDVRTFQDNFIDSLPSIWNVVSITINNSGEDLFISKIRKGHSPLIFRLPLQRHNSRDADEEILVFTKAQTELFRIISKSNQMAQNGKHYTRREDKETWWKERRHLDQCLQQLLENIEISWLGGFKGIFNPHKIDTSLFAKFSSQFQNIIAKNFNMDKKTPVPTLSPEILELFITLGKPGYEGYEQLLEDLIYFILDIFQFRGLHFAYDEIDTDQLSMDLQDALNAYFNNYVSEENRSHTVLVLDKSVHQFPWESLPCLNRQSVSRVPSLSILRDILSQSFVVNGEYVEVRKEAGSYILNPSLDLKHTQEMFEHKLVEGGWKGLIASQPSNRDFIKMLSGNDFFLYFGHGGGEQYTTSYDLATLKRCAVTILMGCSSGALYECGSFEPWGTPLDYLSAGCPTLVANLWDVTDKDIDRFSLKMLESWGLFENKAPFVNSTSICTAVSESRSCCHLRYLNGAAPVIYGIPAYIIP
Protein: Transient receptor potential channel pyrexia (Q9W0T5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor-activated non-selective cation channel involved in protection or tolerance from high temperature stress. Activated by temperatures above 40 degrees Celsius. More permeable to K(+) than to Na(+). May act in stress protection allow flies to survive in natural environments.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Inactive
- Transient receptor potential-gamma protein
Sequence:
MENVRFSIIENDLKWNSESDPTADVDLLLDKRSISSEANSAGVFSDEAHEIFARQQQNQILWDLDEVKETLTESPGGKHVVDMVQSGCFLELMTDSADCNLALICCSVFGSVENTLFLLKHYNADPNVADSRGRTPLHFACCRANAPIAKVLLDFGADPNRWDARKEVTSLHCAASSKSVECILLLLRRKASINIGIEKRSALHYAIDVNAVDCVEILLKYGADPNTPQVYTETPLHTASAAGFAKCVQLLLSHNADVRSQFGEGKVTALHLAAENDYVECARLLLEHRAEVDCRNASHQTPLHLACLSQSIGTVDLLISYGANVNAVYRDGRTALHAAIVKQSRSLDCCNALLKAGADVNKADNYGYTPLHIAALNEFSSCVYTFIEHGADITARTDGRVSALSFIVRRTPEIIPKLMQKLDSSIKANDQEIGDVDCQIKLDFRLLVPSSSMDRGETELLLSLIEVGQKRILMHPLCETFLFLKWRRIRKFFLMSLAYHTLFVILFTFYVIWVYVRCCKKEELCVAPGYVSTIGYLVIILNLILLGKEVFQMAHGLRGYAKYWENWLQWTIGTGVLLCVTPETVRTDDLTAVPVWQHHVAAIVILLVWLELMMLVGRFPIFGVYVQMFTKVAVNFAKFLLAYICLLVAFGLSFAVLFNDYPAFENITWSFLKSITMMSGELEFEDIFYGDYAVKFPVTAHIIFLSFVLLVTVILTNLMVGLAVSDIQGLQVSATLDRLVRQAELVSRLESLFFSRLLRSAPTNLIQLCKRSALLRTSRDKLQFTIRPNDPRDNQLPEDIKLNVYKLVAERRDRNQSLRRRQFENNYNIFSRSLQRQQQPLHTDFLKPEPATGTTKKTPQNLFHMHELLRPRSATNVPQQFRQEAEGTVQMKNQANVLSAVLAEVQAIKTQLVDLVAKFERFSENATRKLNYSTDELCRLRQQGQSVASSHIRRHR
Protein: Zinc finger CCCH domain-containing protein 42 (AtC3H42) (Q9SD61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g31870
- At2g32600/T26B15.16
- AT3G18790 protein
- Nuclear protein-like
- FHA domain-containing protein DDL
- SMAD/FHA domain protein
- Cell division cycle 5-like protein
- Uncharacterized protein At3g23325
- Pre-mRNA-processing-splicing factor 8A
- PHD finger-like domain-containing protein 5A
Sequence:
MNPLTQVKNLQKINARESDLGISDEASWHAKYKNSAYVYVGGIPFDLTEGDLLAVFSQYGEIVDVNLIRDKGTGKSKGFAFLAYEDQRSTILAVDNLNGALVLGRTIKVDHCGAYKKHEEEDEETRRQNREARGVCRAFQRGECTRGDSCKFSHDEKRAANTGWGHEEDRSSKWDHDKNREGRGVCRAFQRGECTRGDSCKFSHDEKRAATTGWGHEEDRSSKWDQDKLNGAKKGGTSFGNRGDFKPDVEEKSYRGRGDGDASYGRPKERERVDREDMGPRSRDAYDMKEQKRSGRYDNAYSRRHNDEIDYVREDKGSRAQDWEKRKAESRRDRNDREEKDRDSLRREDRRR
Protein: Cullin-2 (CUL-2) (Q9D4H8)
Organism: Mus musculus (Mouse)
Function: Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. CUL2 may serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase.
Subcellular location: Nucleus {ECO:0000305|PubMed:33590678}.
Interaction partners:
- von Hippel-Lindau disease tumor suppressor
- Elongin-B
- Elongin-C
- E3 ubiquitin-protein ligase RBX1
- RING-box protein 2
- Hypoxia-inducible factor 1-alpha
- COMM domain-containing protein 1
- Ubiquitin-like protein NEDD8
- Leucine-rich repeat protein 1
- Protein zer-1 homolog
Sequence:
MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYAETKIFLESHVRHLYKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQYIKKNKLTEADIQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQNILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQGIFVSPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHSECHSIIQQERKNDMANMYVLLRAVSSGLPHMIEELQKHIHDEGLRATSNLTQEHMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDKLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIRNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMSFSSKRTKFKITTSMQKDTPQELEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA
Protein: CRISPR-associated exonuclease Csa1 (Q97YD4)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). A ssDNA exonuclease that has both 5' to 3' and 3' to 5' activity, yielding 5'-OH and 3'-phosphate groups. Has Mn(2+)-dependent endonuclease activity on circular ssDNA. Can unwind dsDNA; unwinding does not require ATP.
Interaction partners:
- CRISPR-associated exonuclease Cas4
- CRISPR-associated exonuclease Cas4
- CRISPR-associated exonuclease Cas4
- CRISPR-associated endoribonuclease Cas2 2
- CRISPR-associated endoribonuclease Cas2 1
Sequence:
MFFTHSDMLLLSKRIKKLPKNVDEELRGWNWSEPPVYTRSLSQVSISEMVYCSTLRNVYLKVKGFRGEIGRQILQGSLIHTIYAIGIEAIKRFIYSRESIDGSTLRTLMGDEFYSLLKDLREEEGIYAKVLWDHITNIYSAELDRVRSKFTNLTRDSLVSQVVPFYVEFPVDGSLLGLTNLRVDAFIPHLPLIAEMKTGKYRYTHELSLAGYALAIESQYEIPIDFGYLCYVTVTEKEVKNNCKLIPISDSLRSEFLDMRDKAQDIMDKGVDPGIAKDCESDCMFYKVCHP
Protein: Phosducin (PHD) (33 kDa phototransducing protein) (Protein MEKA) (P20941)
Organism: Homo sapiens (Human)
Function: May participate in the regulation of visual phototransduction or in the integration of photoreceptor metabolism. Inhibits the transcriptional activation activity of the cone-rod homeobox CRX.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10866677}. Nucleus {ECO:0000269|PubMed:10866677}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P19632}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P19632}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:10866677}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Rhodopsin
- S-arrestin
- Perilipin-2
Sequence:
MEEAKSQSLEEDFEGQATHTGPKGVINDWRKFKLESQDSDSIPPSKKEILRQMSSPQSRNGKDSKERVSRKMSIQEYELIHKEKEDENCLRKYRRQCMQDMHQKLSFGPRYGFVYELETGKQFLETIEKELKITTIVVHIYEDGIKGCDALNSSLTCLAAEYPIVKFCKIKASNTGAGDRFSLDVLPTLLIYKGGELISNFISVAEQFAEEFFAGDVESFLNEYGLLPEREVHVLEHTKIEEEDVE
Protein: Corticosteroid-binding globulin (CBG) (Serpin A6) (Transcortin) (P08185)
Organism: Homo sapiens (Human)
Function: Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species.
Subcellular location: Secreted.
Interaction partners:
- Sex hormone-binding globulin
- Albumin
- Glucocorticoid receptor
- Pro-opiomelanocortin
- Transient receptor potential cation channel subfamily V member 1
- G-protein coupled receptor 55
Sequence:
MPLLLYTCLLWLPTSGLWTVQAMDPNAAYVNMSNHHRGLASANVDFAFSLYKHLVALSPKKNIFISPVSISMALAMLSLGTCGHTRAQLLQGLGFNLTERSETEIHQGFQHLHQLFAKSDTSLEMTMGNALFLDGSLELLESFSADIKHYYESEVLAMNFQDWATASRQINSYVKNKTQGKIVDLFSGLDSPAILVLVNYIFFKGTWTQPFDLASTREENFYVDETTVVKVPMMLQSSTISYLHDSELPCQLVQMNYVGNGTVFFILPDKGKMNTVIAALSRDTINRWSAGLTSSQVDLYIPKVTISGVYDLGDVLEEMGIADLFTNQANFSRITQDAQLKSSKVVHKAVLQLNEEGVDTAGSTGVTLNLTSKPIILRFNQPFIIMIFDHFTWSSLFLARVMNPV
Protein: ELMO domain-containing protein 1 (Q8N336)
Organism: Homo sapiens (Human)
Function: Acts as a GTPase-activating protein (GAP) toward guanine nucleotide exchange factors like ARL2, ARL3, ARF1 and ARF6, but not for GTPases outside the Arf family.
Interaction partners:
- ELMO domain-containing protein 3
Sequence:
MKHFLRMLIQVCLYFYCKFLWRCLKFVMRKLTGRCELQRICYNTKPGASRTMKIETSLRDSKSKLLQTSVSVHPDAIEKTIEDIMELKKINPDVNPQLGISLQACLLQIVGYRNLIADVEKLRREAYDSDNPQHEEMLLKLWKFLKPNTPLESRISKQWCEIGFQGDDPKTDFRGMGLLGLYNLQYFAERDATAAQQVLSDSLHPKCRDITKEEISKFSKAEWEKKRMDKAIGYSFAIVGINITDLAYNLLVSGALKTHFYNIAPEAPTLSHFQQTFCYLMHEFHKFWIEEDPMDIMEFNRVREKFRKRIIKQLQNPDMALCPHFAASEGLINM
Protein: Sterile alpha motif domain containing 4B (M0QY61)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMFRDQVGILAGWFKGWNECEQTVALLSLLKRVTRTQARFLQLCLEHSLADCNDIHLLESEANSAAIVSQWQQESKEKVVSLLLSHLPLLQPGNTEAKSEYMRLLQKVLAYSIESNAFIEESRQLLSYALIHPATTLEDRNALALWLSHLEERLASGFRSRPEPSYHSRQGSDEWGGPAELGPGEAGPGWQDKPPRENGHVPFHPSSSVPPAINSIGSN
Protein: RB binding protein 7, chromatin remodeling factor (E9PC52)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTTSELEGQGS
Protein: D(1A) dopamine receptor (Dopamine D1 receptor) (Q61616)
Organism: Mus musculus (Mouse)
Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P18901}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18901}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P18901}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18901}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:P21728}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:25865831}. Cell projection, dendritic spine {ECO:0000269|PubMed:25865831}. Note=Transport from the endoplasmic reticulum to the cell surface is regulated by interaction with DNAJC14. {ECO:0000250|UniProtKB:P18901}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Neuron-specific vesicular protein calcyon
- VIP peptides
- Pituitary adenylate cyclase-activating polypeptide
- Pro-glucagon
- Natriuretic peptides A
- Gastric inhibitory polypeptide
Sequence:
MAPNTSTMDETGLPVERDFSFRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFQYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTWPLDGNFTSLEDAEDDNCDTRLSRTYAISSSLISFYIPVAIMIVTYTSIYRIAQKQIRRISALERAAVHAKNCQTTTGNGNPVECSQSESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFISNCMVPFCGSEETQPFCIDSITFDVFVWFGWANSSLNPIIYAFNADFQKAFSTLLGCYRLCPTTNNAIETVSINNNGAVMFSSHHEPRGSISKDCNLVYLIPHAVGSSEDLKREEAGGIPKPLEKLSPALSVILDYDTDVSLEKIQPVTHSGQHST
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10 (P50151)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Interacts with beta-1 and beta-2, but not with beta-3.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-4
- 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
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 7
- Guanine nucleotide-binding protein G
Sequence:
MSSGASASALQRLVEQLKLEAGVERIKVSQAAAELQQYCMQNACKDALLVGVPAGSNPFREPRSCALL