wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic GMP-AMP synthase-like receptor 1 (cGLR1) (EC 2.7.7.-) (B3NQ14)
Organism: Drosophila erecta (Fruit fly)
Function: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG (By similarity). Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',2'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the antiviral immune response via activation of the NF-kappa-B transcription factor Rel (Relish) (By similarity).
Interaction partners:
Sequence:
MVRNLEDFCNEANAKHIRIEDRERYTGHFNALKDMVYSYWKKSKGLDKLVKGTTLCGGYGDNLKVSKPDEYDLLIHLVFPENDKIIVKADASNPGNVLLDMTKVMEIIAKQEHNKPVFDLLQKIVNNKKQLLEDKLQSFLHGIMTQTLNKMGNRIEVQGEISHLSYKKCGPAHNILVKGPCEYSVDFVPAIKLSAAQLVLAPEQRKHFGGTLYWDAVPKPMKPAKPDNPSFRTSFYEAERSLLHGKQNLKSAIRMIKHIRNEKNKANLKSYHIKTVFLWQVMEKDASYWEKPKKEILIEMLGKLADLLALTPRKGRLPYFWDPKLDMFADLTDDQRTDMFNCFRKCEYVFRKADGNLNDDNENSVHSSFKGSGRNGQKMEKTSTESEQKKPTETKPNAKVESTPVKPNPKPSVQEKQAKPNLADQKKCTKNANGTKSKTTTPKPS
Protein: Casein kinase II subunit beta (CK II beta) (A0A0D9R898)
Organism: Chlorocebus sabaeus (Green monkey) (Simia sabaea)
Interaction partners:
- Casein kinase II subunit alpha
- Casein kinase II subunit alpha
- Ribosomal RNA-processing protein 7 homolog A
- Nucleolar protein 6
- FACT complex subunit SSRP1
- WD repeat domain 36
- FACT complex subunit
- FUN14 domain containing 1
- Dishevelled segment polarity protein 3
- Dishevelled segment polarity protein 2
Sequence:
MSSSEEVSWISWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPHYRQALDMILDLEPDEELEDNPNQSDLIEQAAEMLYGLIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPMLPIGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPANQFVPSSCSRHPDLPLLPLRRPFCRMHFRLREVYHQQLIPMHGDHHLL
Protein: Protein TOC75-4, chloroplastic (75 kDa translocon at the outer-envelope-membrane of chloroplasts 4) (AtTOC75-IV) (Q5IZC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the insertion of proteins targeted to the outer membrane of chloroplasts. Required for the import of protein precursors into chloroplasts. Forms the voltage-dependent preprotein translocation channels (hydrophilic beta barrel) of the TOC complex in the chloroplastic outer membrane (By similarity). Required for etioplast formation and/or etioplast-chloroplast transition during deetiolation.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:15908591}; Multi-pass membrane protein {ECO:0000269|PubMed:15908591}.
Interaction partners:
- Translocase of chloroplast 34, chloroplastic
- Translocase of chloroplast 159, chloroplastic
- Translocase of chloroplast 33, chloroplastic
- Translocase of chloroplast 132, chloroplastic
- Translocase of chloroplast 120, chloroplastic
- Translocase of chloroplast 90, chloroplastic
- Protein TIC 20-I, chloroplastic
- Protein TIC 22, chloroplastic
- Protein TIC 20-IV, chloroplastic
- Chloroplast processing peptidase
Sequence:
MEAVKEAVRKIKSLVIPHADEKDNGIVFEIKLNETDQRVEKWGLDPSLDFFEVTGNCNLGRPNSEGSNQSLMGSVTIRNIFNPKLDDLLSKIEYVRFLEAVKKPRNRTFKTSFFNSRKLSPVFTGGPGYEDLVPPMFVGRDCLKATITENLTRQRELTYGVMFEEIITRDENRRISENGLLLSPDGGISINGPPTTLSGTGIDHIATLQANITRDNTKLVNGAVVGEKNIFQVDQGLGIGNNFPLFNRHQLSLTSFIQLKQVEEGSDKPQPPVLVLHGRYGGCIGDLPSYDVFALGGPNSVRGYSMGELGAAKNILELGAEIRIPVKNTHVYAFAEHGNDLGSSKDVKGNPTGLYRKMGHGSSYGLGVKLGMVRAEYTVRHNRGTGALFLRFGERY
Protein: A-type potassium channel modulatory protein KCNIP1 (Kv channel-interacting protein 1) (KChIP1) (Potassium channel-interacting protein 1) (Q9JJ57)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Regulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. Modulates KCND2/Kv4.2 currents. In vitro, modulates KCND1/Kv4.1 currents (By similarity). Increases the presence of KCND2 at the cell surface.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14572458}; Peripheral membrane protein {ECO:0000269|PubMed:14572458}. Cytoplasm {ECO:0000269|PubMed:14572458}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8R426}.
Interaction partners:
- A-type voltage-gated potassium channel KCND2
- A-type voltage-gated potassium channel KCND3
- A-type potassium channel modulatory protein DPP6
- Voltage-gated potassium channel KCNC1
- A-type voltage-gated potassium channel KCND1
- Kv channel-interacting protein 4
- Potassium voltage-gated channel subfamily A member 4
- Inactive dipeptidyl peptidase 10
Sequence:
MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQRDKIEDELEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM
Protein: Proto-oncogene serine/threonine-protein kinase mos (EC 2.7.11.1) (Oocyte maturation factor mos) (Proto-oncogene c-Mos) (P00536)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00540}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 1
- Dual specificity mitogen-activated protein kinase kinase 2
- Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- GTPase HRas
- GTPase KRas
- GTPase NRas
- Ras-related protein R-Ras2
- Bone morphogenetic protein 15
Sequence:
MPSPLSLCRYLPRELSPSVDSRSCSIPLVAPRKAGKLFLGTTPPRAPGLPRRLAWFSIDWEQVCLMHRLGSGGFGSVYKATYHGVPVAIKQVNKCTKDLRASQRSFWAELNIARLRHDNIVRVVAASTRTPEDSNSLGTIIMEFGGNVTLHQVIYGATRSPEPLSCREQLSLGKCLKYSLDVVNGLLFLHSQSILHLDLKPANILISEQDVCKISDFGCSQKLQDLRCRQASPHHIGGTYTHQAPEILKGEIATPKADIYSFGITLWQMTTREVPYSGEPQYVQYAVVAYNLRPSLAGAVFTASLTGKTLQNIIQSCWEARALQRPGAELLQRDLKAFRGALG
Protein: Mushroom body defect, isoform K (M9PJN0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDTRSWRKVLLQWIGECHFIESNYITLEQSDLDSFFSVFIQKIQETENVKGKNELQDQPTEQSPLVQEFLAHNYPEFIAQQDDKEVDLPLDCLYVYTLLLHYSCVKKPSLFFHNICNKLPELTQTCIASFFRETVDRLLTREYLSQAIANVAVVYRQGVSTSVSPCLPSSSLSPDPRSDDAPCPSTPSSSSSQPSSSTPQLRNHREQLRLNGCEMPPPSTPKTELLEQRTKELRGIRTQLEVVRYEKALLEEQQMEKDELIKVLNKEKMMAKMELEKLRNVKLTEEHHDNESHHIMPYEFEHMKGCLLKEIGLKESLIAEITDKLHDLRVENSELSEKLNLAGKRLLEYTDRIRFLESRVDDLTRIVSSRDVMISSLESDKQELDKCLKEARDDLHNRIEVLNASSDLLDCSLSPNTTPENLASSVIDKQLREKEHENAELKEKLLNLNNSQRELCQALSSFLQKHNIDHEFPVEWTSSSLLSTISAIESKFVNTLEKSTQMKKECDVQSVCVEKLLEKCKLLSVSLGCQPKELDGFEATIPEAMESGFESSRECETILSCCHMKVVDIASKNNDLELDNERLNDKCAELKSIIDRGDQHLADINLQLIEKEKQIKDVGAEIQELRKRNINLENMLSQIADKEASAASHAQHLKQCGELLRAKYEVCRNELIAKNAAQDELVRMMMVPDGETLNGRVRQLIDLEMMHDEHNKMYAQMLKQLNELSAKHDNMTHSHLDFVKRTEIELETKNAQIMAFDEHNNHFDRFLTRIFTLLRSRNCPKSTTMGSATNFLESMHIEKRFENIEMLIEGQLLSADDLKRELDDLRSKNEELAKQNINGIIKRNKFITSLEVNTEKVKQYITDLEEEAFKRKQKVVQLENTLSKEQSNAKEMAQRLDIAQQEIKDYHVEAIRFINTIRDRLQQDFNGVNTPQQLGTCMTEFLKMYDQMEVRYEESSSLVEKLTESQAKLEMQVAELQVELENKDTNQHSGALIKQLNDTIQNLEKVNAKLSEDNTVSHTVHSKLNESLLKAQKELDLRAKIIENLEASERNLSMKLCELKDLKNKLKSSDEKIAQIKETYEEQIKALQAKCDMEAKKNEHLERNQNQSLTQLKEDALENCVLMSTKLEELQAKLQEGQQLVDSQKLELDMNRKELALVKSAYEAQTKLSDDLQRQKESGQQLVDNLKVELEKERKELAHVNSAIGAQTKLSDDLECQKESGQQLVDNLKVELEKERKELAQVKSVIEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAKVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKMELDKERKELAQVKSAIGAQTKLSDDLECQKESVQQLVDNLKVELEKERKELAKVNSAFEAQTKLSDDLKLQKEDAQREVFLVKERLVKEKREFEVKLATLEDIIETLEMRCTQMEEERATAYEQINKLENRCQEKDNVKSSQLQVETFKVECLHHQLKSEMATHNSLVEDLNRKLAEKVSKLDFVQSRLMTEIAEHNQVKDQLAQITDIPKVVELQHRLEAETAEREEAQNKLAVVTGRLDEITRELDNARLEHGAQILRMEETAREVGNKNAELCELIEFYRNRVEALERLLLASNQELEELNSIQSNQAEGVRDLGDTYSAAEGRQTESDQDKERYQKLALDCKILQAKYRDAKDEIKRCEKKIKDQRLEMEGKLEKMKNKMGSRRRRWPQLMLLFIGLIILIVFFLYYILYISGINVIFKSRSPIVY
Protein: Aspartyl protease 25 (EC 3.4.23.-) (Protein RICE ANTHER DOWN-REGULATED BY CHILLING 1) (Q6F4N5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Anther-specific aspartic protease involved in tapetal programmed cell death (PCD). Directly regulated by the transcription factor EAT1/DTD in anthers during tapetum PCD and degeneration.
Interaction partners:
Sequence:
MAATTTIPLLLLLLAATVAAAAAELSVYHNVHPSSPSPLESIIALARDDDARLLFLSSKAATAGVSSAPVASGQAPPSYVVRAGLGSPSQQLLLALDTSADATWAHCSPCGTCPSSSLFAPANSSSYASLPCSSSWCPLFQGQACPAPQGGGDAAPPPATLPTCAFSKPFADASFQAALASDTLRLGKDAIPNYTFGCVSSVTGPTTNMPRQGLLGLGRGPMALLSQAGSLYNGVFSYCLPSYRSYYFSGSLRLGAGGGQPRSVRYTPMLRNPHRSSLYYVNVTGLSVGHAWVKVPAGSFAFDAATGAGTVVDSGTVITRWTAPVYAALREEFRRQVAAPSGYTSLGAFDTCFNTDEVAAGGAPAVTVHMDGGVDLALPMENTLIHSSATPLACLAMAEAPQNVNSVVNVIANLQQQNIRVVFDVANSRVGFAKESCN
Protein: Uncharacterized protein (Q57WZ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTYCPITRKELERYLPNFDPLLDPQIGEWVLVTPERRFAILGPLLQFVQEHAIKPIYPFLDNSEPSSAPVTTFNFCKEDSPKTLGDPSKVFPTLSEVWRRYRRRRFHISGMDEDGIGEEEENDDTILYLNPRALLLTPCAPAVFGGSDFIEGLDREGERVVFVNWKTGETRTDSGVLKPAPIPAWAEDVAEKAAMEWESWKKCVIPPSSTRE
Protein: Na(+)-translocating NADH-quinone reductase subunit F (Na(+)-NQR subunit F) (Na(+)-translocating NQR subunit F) (EC 7.2.1.1) (NQR complex subunit F) (NQR-1 subunit F) (Q56584)
Organism: Vibrio alginolyticus
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00430}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- NADH:ubiquinone reductase
- FAD:protein FMN transferase
- 
- Quinone oxidoreductase
- NADP-dependent oxidoreductase
Sequence:
MDIILGVVMFTLIVLALVLVILFAKSKLVPTGDITISVNDDPSLAIVTQPGGKLLSALAGAGVFVSSACGGGGSCGQCRVKVKSGGGDILPTELDHITKGEAREGERLACQVAMKTDMDIELPEEIFGVKKWECTVISNDNKATFIKELKLQIPDGESVPFRAGGYIQIEAPAHHVKYADYDIPEEYREDWEKFNLFRYESKVNEETIRAYSMANYPEEHGIIMLNVRIATPPPNNPDVPPGIMSSYIWSLKEGDKCTISGPFGEFFAKDTDAEMVFVGGGAGMAPMRSHIFDQLKRLHSKRKMSFWYGARSKREMFYVEDFDMLQAENDNFVWHCALSDPLPEDNWDGYTGFIHNVLYENYLRDHEAPEDCEYYMCGPPMMNAAVIGMLKDLGVEDENILLDDFGG
Protein: Leucine-rich repeat-containing protein 2 (Q8VDB8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGHKVVVFDISVVRALWETRVKKHKAWQKKEAERLEKSALEKIKEEWDFVAQCRRKGVPQAEYCKNGFVDTSTRLLEKIERNSVSRQSARVKDRDKRRSPFVFELSGTQWKELPDSLKEQTHLKEWYIHSTLIQIIPTYIELFQAMKILDLPKNQITCLPAEIGRLKNLKELNVSFNHLKSIPPELGDCEHLERLDCSGNLDLMDLPFELSNLKQVTFVDISANKFSSVPICVLRMCRLQWLDISSNNLSDLPQDIDRLEELQGFLLYKNKLTYLPQAMLNLKKLTLLVVSGDHLVEVPTALCDASTPLKFVSLVDNPIDKTGCQDTEDTVESERDRQHFDKEFMKAYIEDLKEREAVPSYTTKVSFSLQL
Protein: TRAF-interacting protein with FHA domain-containing protein A (Q2MHQ9)
Organism: Xenopus laevis (African clawed frog)
Function: Adapter molecule that plays a key role in the activation of pro-inflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs) (By similarity). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96CG3}.
Interaction partners:
Sequence:
MDKELIDVDTEQTISCLTLTLYHPNHQDQKLFRGINFSRKEEIKADAVVAFGRDYNVCRYPLLSNRVSRIQFNLQLFKHFNCSTSTFEIKNLSKKNKLYVDNLELDYLNKIELPKKCMIRFGDFQILAEIDEGDSDEKFEICCEKSHVSLVQDSFIPTMQPIPECGTLNAVEIDENEC
Protein: GDP-mannose transporter (GMT) (Q4WTQ6)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Nucleotide-sugar transporter, putative
- Nucleotide-sugar transporter, putative
- Nucleotide-sugar transporter, putative
- 60S ribosomal protein L9, putative
Sequence:
MADDKKTNEYTIEMDKLDHGNKDFEAPAPAVRPRGPPVAQLANNPILPVLAYCGSSILMTVMNKYVLSGRDFNLNFFLLCVQSIVCIVAIQTCKVSKLITYRDFNSDEAKKWFPITLLLIGMIYTGSKALQYLSIPVYTIFKNLTIILIAYGEVLWFGGSVTGLTLFSFGLMVLSSIIAAWADIKHAVESSGDATAKVSTLNAGYIWMLINCLCTSSYVLGMRKRIKLTNFKDFDTMFYNNLLSIPVLLVLTFLMEDWSSANIARNFPSTDRNGILFAMILSGLSSVFISYTSAWCVRVTSSTTYSMVGALNKLPIALSGLIFFDAPVTFPSVSAIVVGFISGIVYAVAKIKQSAKPKTGVLPMSNPPVSASSQSMRDSLRS
Protein: Prefoldin subunit 1 (Genes involved in microtubule biogenesis protein 6) (Gim complex subunit 6) (GimC subunit 6) (P46988)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Prefoldin subunit 2
- Prefoldin subunit 6
- Prefoldin subunit 4
- Prefoldin subunit 3
- Prefoldin subunit 5
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
Sequence:
MSQIAQEMTVSLRNARTQLDMVNQQLAYLDRQEKLAELTKKELESYPTDKVWRSCGKSFILQDKSKYVNDLSHDETVLLDQRKTLKIKKNYLETTVEKTIDNLKALMKN
Protein: Copper-containing nitrite reductase (EC 1.7.2.1) (Q2UDH5)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MNTAFSSLCRTKSRYASVTTIRGARRLPPRLLSSPCSPLRGPFLARQISTESRKGTSGFQIKYVLLLSTAATLSWLLYARQHGAVWLDSDKSYFTHPDPLAPNNGIHQQKTTNEIQDSQKETFKSLEAEDLPTEKAILTTAPNVPPPITRDYPVILDVDLTAVAKLEQLTNQYKYEKWTFNNSVPGPFIRARVGDIVNLKITNHDESGMPHNIDCHAFLGPGGGSALTTVNEGETKTARFRLQNPGLYIYHCAVGPVGVHIANGMYGLLYVQPEQDLPPVDKEYYVMQSEFYHEPPEPDDNGQMSSTVEFSWPHALREAADVVVFNGSEAALTEKPLKATLDDTVRIFFGNGGPNLTSSFHVIGTCFNKVYRDSDVLSPPGQCVQTVSVPPGGSTIVDMKMVVPGTYTIVDHAIFRLEKGAKGFLNVSGEPRPMLYYSTLPPQPCEGFNLKYKCLPNEVQQFVNLLNDISHIGTFFIGELNKSSTSQFTISIIVIPGQILELWTKYLSKRSTHNFPGLWHISTDSSFVNTTLIHLSLSCVLAEQHVFQFYLWGSVAQGQ
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (DNA polymerase alpha holoenzyme-associated protein P1) (P1-MCM3) (RLF subunit beta) (p102) (P25205)
Organism: Homo sapiens (Human)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division (Probable).
Subcellular location: Nucleus {ECO:0000305|PubMed:35585232}. Chromosome {ECO:0000305|PubMed:35585232}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000305|PubMed:35585232}.
Interaction partners:
- DNA replication licensing factor MCM5
- DNA polymerase epsilon subunit 2
- DNA replication complex GINS protein SLD5
- Protein MCM10 homolog
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM6
- DNA replication factor Cdt1
- Cell division control protein 45 homolog
- DNA replication complex GINS protein PSF3
Sequence:
MAGTVVLDDVELREAQRDYLDFLDDEEDQGIYQSKVRELISDNQYRLIVNVNDLRRKNEKRANRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYVGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKAKPGDRVQVVGTYRCLPGKKGGYTSGTFRTVLIACNVKQMSKDAQPSFSAEDIAKIKKFSKTRSKDIFDQLAKSLAPSIHGHDYVKKAILCLLLGGVERDLENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHRYRAPGEQDGDAMPLGSAVDILATDDPNFSQEDQQDTQIYEKHDNLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPVLTQESATYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKRSEDESETEDEEEKSQEDQEQKRKRRKTRQPDAKDGDSYDPYDFSDTEEEMPQVHTPKTADSQETKESQKVELSESRLKAFKVALLDVFREAHAQSIGMNRLTESINRDSEEPFSSVEIQAALSKMQDDNQVMVSEGIIFLI
Protein: Aldehyde-alcohol dehydrogenase (Q9ANR5)
Organism: Clostridium acetobutylicum
Interaction partners:
Sequence:
MKVTNQKELKQKLNELREAQKKFATYTQEQVDKIFKQCAIAAAKERINLAKLAVEETGIGLVEDKIIKNHFAAEYIYNKYKNEKTCGIIDHDDSLGITKVAEPIGIVAAIVPTTNPTSTAIFKSLISLKTRNAIFFSPHPRAKKSTIAAAKLILDAAVKAGAPKNIIGWIDEPSIELSQDLMSEADIILATGGPSMVKAAYSSGKPAIGVGAGNTPAIIDESADIDMAVSSIILSKTYDNGVICASEQSILVMNSIYEKVKEEFVKRGSYILNQNEIAKIKETMFKNGAINADIVGKSAYIIAKMAGIEVPQTTKILIGEVQSVEKSELFSHEKLSPVLAMYKVKDFDEALKKAQRLIELGGSGHTSSLYIDSQNNKDKVKEFGLAMKTSRTFINMPSSQGASGDLYNFAIAPSFTLGCGTWGGNSVSQNVEPKHLLNIKSVAERRENMLWFKVPQKIYFKYGCLRFALKELKDMNKKRAFIVTDKDLFKLGYVNKITKVLDEIDIKYSIFTDIKSDPTIDSVKKGAKEMLNFEPDTIISIGGGSPMDAAKVMHLLYEYPEAEIENLAINFMDIRKRICNFPKLGTKAISVAIPTTAGTGSEATPFAVITNDETGMKYPLTSYELTPNMAIIDTELMLNMPRKLTAATGIDALVHAIEAYVSVMATDYTDELALRAIKMIFKYLPRAYKNGTNDIEAREKMAHASNIAGMAFANAFLGVCHSMAHKLGAMHHVPHGIACAVLIEEVIKYNATDCPTKQTAFPQYKSPNAKRKYAEIAEYLNLKGTSDTEKVTALIEAISKLKIDLSIPQNISAAGINKKDFYNTLDKMSELAFDDQCTTANPRYPLISELKDIYIKSF
Protein: Bacterial general secretion pathway protein H (Q2YRC8)
Organism: Brucella abortus (strain 2308)
Interaction partners:
Sequence:
MVPQGRDTRIDVFRALALLTIFINHVPGTIYEHFTHKNLGFSDSAEAFVLISGMAVALAYGSKFVSGNRLVLSLKMWRRASVLYITHIMTTMATIAIFAAAAIFLKRSELLTQINIAPLIKKPVEGLFGLVTLGHQLGYNNILSMYAVMLILTPILLFLARISLPLMLGVSGVVWFLSGLYHVAPVNYPTEGVWFINPLSWQFLFAIGIAGVMHVRGGGQLPKHPLLIGLAVGYLVLALAWVRIPLWSINISMGLPMVITGFDKTFLSAPRLLHVLAMAYLIAVVPTLNSIARTAPEHPLAVLGKHSLPVFVAGTLLAMVAQVMKLVNPGGLPYDTLLIATGIVMQFALAYYLEWLPTIGWGKKGAVQAKPAPAAEPVVIQVSANPEPAMQRY
Protein: Rap guanine nucleotide exchange factor 4 (Exchange factor directly activated by cAMP 2) (Exchange protein directly activated by cAMP 2) (EPAC 2) (cAMP-regulated guanine nucleotide exchange factor II) (cAMP-GEFII) (Q8WZA2)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2 (By similarity).
Subcellular location: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Ras-related protein Rap-1b
- Regulating synaptic membrane exocytosis protein 2
- Ras-related protein Rap-1A
- ATP-binding cassette sub-family C member 8
- Protein piccolo
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- Adenylate cyclase type 8
- Adenylate cyclase type 6
Sequence:
MVAAHAAHSSSSAEWIACLDKRPLERSSEDVDIIFTRLKEVKAFEKFHPNLLHQICLCGYYENLEKGITLFRQGDIGTNWYAVLAGSLDVKVSETSSHQDAVTICTLGIGTAFGESILDNTPRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLLAPPYGVMETGSNNDRIPDKENTPLIEPHVPLRPANTITKVPSEKILRAGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTELVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRFLDDEHEDAPLPTEEEKKECDEELQDTMLLLSQMGPDAHMRMILRKPPGQRTVDDLEIIYEELLHIKALSHLSTTVKRELAGVLIFESHAKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDDFGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKVPAGNRASNQGNSQPQQKYTVMSGTPEKILEHFLETIRLEATLNEATDSVLNDFIMMHCVFMPNTQLCPALVAHYHAQPSQGTEQEKMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVSMAFLEEFYVSVSDDARMIAALKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQKRQPIRGSDEVLFKVYCMDHTYTTIRVPVATSVKEVISAVADKLGSGEGLIIVKMSSGGEKVVLKPNDVSVFTTLTINGRLFACPREQFDSLTPLPEQEGPTVGTVGTFELMSSKDLAYQMTIYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKRVQLLKKFIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTVAKLEPPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTARTVRYYRSQPFNPDAAQANKNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP
Protein: Potassium channel subfamily U member 1 (Calcium-activated potassium channel subunit alpha-3) (Calcium-activated potassium channel, subfamily M subunit alpha-3) (KCa5) (Slowpoke homolog 3) (A8MYU2)
Organism: Homo sapiens (Human)
Function: Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). May represent the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O54982}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:24670955, ECO:0000269|PubMed:38267364}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium-activated potassium channel subunit beta-4
- Small conductance calcium-activated potassium channel protein 1
- Intermediate conductance calcium-activated potassium channel protein 4
- Calcium-activated potassium channel subunit beta-1
- Small conductance calcium-activated potassium channel protein 2
- Small conductance calcium-activated potassium channel protein 3
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Calcium-activated potassium channel subunit beta-3
Sequence:
MFQTKLRNETWEDLPKMSCTTEIQAAFILSSFVTFFSGLIILLIFRLIWRSVKKWQIIKGTGIILELFTSGTIARSHVRSLHFQGQFRDHIEMLLSAQTFVGQVLVILVFVLSIGSLIIYFINSADPVGSCSSYEDKTIPIDLVFNAFFSFYFGLRFMAADDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPQILQILRAIKTSNSVKFSKLLSIILSTWFTAAGFIHLVENSGDPWLKGRNSQNISYFESIYLVMATTSTVGFGDVVAKTSLGRTFIMFFTLGSLILFANYIPEMVELFANKRKYTSSYEALKGKKFIVVCGNITVDSVTAFLRNFLRDKSGEINTEIVFLGETPPSLELETIFKCYLAYTTFISGSAMKWEDLRRVAVESAEACLIIANPLCSDSHAEDISNIMRVLSIKNYDSTTRIIIQILQSHNKVYLPKIPSWNWDTGDNIICFAELKLGFIAQGCLVPGLCTFLTSLFVEQNKKVMPKQTWKKHFLNSMKNKILTQRLSDDFAGMSFPEVARLCFLKMHLLLIAIEYKSLFTDGFCGLILNPPPQVRIRKNTLGFFIAETPKDVRRALFYCSVCHDDVFIPELITNCGCKSRSRQHITVPSVKRMKKCLKGISSRISGQDSPPRVSASTSSISNFTTRTLQHDVEQDSDQLDSSGMFHWCKPTSLDKVTLKRTGKSKYKFRNHIVACVFGDAHSAPMGLRNFVMPLRASNYTRKELKDIVFIGSLDYLQREWRFLWNFPQIYILPGCALYSGDLHAANIEQCSMCAVLSPPPQPSSNQTLVDTEAIMATLTIGSLQIDSSSDPSPSVSEETPGYTNGHNEKSNCRKVPILTELKNPSNIHFIEQLGGLEGSLQETNLHLSTAFSTGTVFSGSFLDSLLATAFYNYHVLELLQMLVTGGVSSQLEQHLDKDKVYGVADSCTSLLSGRNRCKLGLLSLHETILSDVNPRNTFGQLFCGSLDLFGILCVGLYRIIDEEELNPENKRFVITRPANEFKLLPSDLVFCAIPFSTACYKRNEEFSLQKSYEIVNKASQTTETHSDTNCPPTIDSVTETLYSPVYSYQPRTNSLSFPKQIAWNQSRTNSIISSQIPLGDNAKENERKTSDEVYDEDPFAYSEPL
Protein: Type 2A encapsulin shell protein (35 kDa antigen) (Major membrane protein 1) (Major membrane protein I) (MMP-I) (Q48899)
Organism: Mycobacterium avium
Function: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers. Probably encapsulates at least cysteine desulfurase (CyD) and allows passage of cysteine into its interior, probably involved in sulfur metabolism.
Subcellular location: Encapsulin nanocompartment {ECO:0000250|UniProtKB:Q55032}.
Interaction partners:
Sequence:
MTSAQNESQALGDLAARQLANATKTVPQLSTITPRWLLHLLNWVPVEAGIYRVNRVVNPEQVAIKAEAGAGSEEPVPQTYVDYETSPREYTLRSISTLVDIHTRVSDLYSSPHDQIAQQLRLTIETIKERQELELINSPEYGLLAQATGRQTIQTLAGAPTPDDLDALITKVWKTPSFFLTHPLGIAAFGREATYRGVPPPVVSLFGPTQFITWHGIRLPSDKVPVEDGKTKFILVRTGEERQGVVGLFQPGLVGEQAPGLSVRFTGINQSAIATYLVTLYTSLAVLTDDALAVLDDVAVDQFHEYK