wanglab/gogpt-training-data huggingface dataset:
Protein: Cytohesin-2 (ARF nucleotide-binding site opener) (Protein ARNO) (PH, SEC7 and coiled-coil domain-containing protein 2) (CLM2) (SEC7 homolog B) (P63035)
Organism: Rattus norvegicus (Rat)
Function: Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane (By similarity). Involved in neurite growth (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q99418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99418}. Cytoplasm {ECO:0000250|UniProtKB:P63034}. Cell projection {ECO:0000250|UniProtKB:P63034}. Cell projection, growth cone {ECO:0000250|UniProtKB:P63034}. Cell junction, tight junction {ECO:0000250|UniProtKB:P63034}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P63034}. Note=Recruited to the cell membrane through its association with ARL4A, ARL4C and ARL4D. Also requires interaction with phosphoinositides for targeting to plasma membrane (By similarity). In differentiating neuroblastoma cells, colocalizes with CCDC120 in both neurite shaft and growth cone areas (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63034}.
Interaction partners:
- ADP-ribosylation factor 6
- ADP-ribosylation factor 1
- ADP-ribosylation factor 2
- General receptor for phosphoinositides 1-associated scaffold protein
- FERM domain containing 4A
- Coiled-coil domain containing 120
- Interactor protein for cytohesin exchange factors 1
- FERM domain containing 4B
Sequence:
MEDGVYEPPDLTPEERMELENIRRRKQELLVEIQRLREELSEAMSEVEGLEANEGSKTLQRNRKMAMGRKKFNMDPKKGIQFLVEHELLQNTPEEIARFLYKGEGLNKTAIGDYLGEREELNLSVLHAFVDLHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCLCNPGVFQSTDTCYVLSFAVIMLNTSLHNPNVRDKPGLERFVAMNRGINEGGDLPEDLLRNLYDSIRNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVDDPRKPNCFELYIPNNKGQLIKACKTEADGRVVEGNHMVYRISAPTQEEKDEWIKSIQAAVSVDPFYEMLAARKKRISVKKKQEQP
Protein: Peptidyl-prolyl cis-trans isomerase C (PPIase C) (EC 5.2.1.8) (Cyclophilin C) (Rotamase C) (P45877)
Organism: Homo sapiens (Human)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30412}.
Interaction partners:
Sequence:
MGPGPRLLLPLVLCVGLGALVFSSGAEGFRKRGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSIINSGKIDVKTPFVVEIADW
Protein: Rho GTPase-activating protein 20 (Rho-type GTPase-activating protein 20) (Q9P2F6)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Interaction partners:
- Transforming protein RhoA
- Bromodomain and WD repeat-containing protein 3
Sequence:
MEAMSPQQETLGGQPGRSSSLTGVSRLAGGSCTKKKMKTLAERRRSAPSLILDKALQKRPTTRDSPSASVDTCTFLSSLVCSNRTLLIDGRAELKRGLQRQERHLFLFNDLFVVAKIKYNNNFKIKNKIKLTDMWTASCVDEVGEGNTNAMKSFVLGWPTVNFVATFSSPEQKDKWLSLLQRYINLEKEKDYPKSIPLKIFAKDIGNCAYSKTITVMNSDTANEVINMSLPMLGITGSERDYQLWVNSGKEEAPYPLIGHEYPYGIKMSHLRDSALLTPGSKDSTTPFNLQEPFLMEQLPREMQCQFILKPSRLAAAQQLSDSGHKTFKRRRSIINWAFWRGSSTHLDNLPSSPTSPMPGQLFGISLPNICENDNLPKPVLDMLFFLNQKGPLTKGIFRQSANVKSCRELKEKLNSGVEVHLDCESIFVIASVLKDFLRNIPGSIFSSDLYDHWVSVMDQGNDEEKINTVQRLLDQLPRANVVLLRYLFGVLHNIEQHSSSNQMTAFNLAVCVAPSILWPPASSSPELENEFTKKVSLLIQFLIENCLRIFGEEITSLFREVSVRCDTRENASDISCFQLNDSSYDSLENELNEDVDAPCSDLVKKLGQGSRSMDSVLTLSDYDLDQPEVEGLLTLSDFDLAHSKDEDVQMKRPLESKPVNILVYTKIPLRDHARAPSAMCTPSYLSTAAANAAKSLRRHRRCSEPSIDYLDSKLSYLREFYQKKLRKSSCDAILSQKDEDYLKQNQPLQEEGKTCFKQSLVTGTDVSKKNATTQNTKKKSLSGSEGNHVKLFPKSKPVAISVASYSPMSSQDHSKNQPFDVNTSGYSPPHTADALKGPRTHRRCSEPNIEDQNRKLTYLRGIYSKKQHKTSCEAGLLHGEEDYLKRHKSLQMEGQKLINQSLVMGIEVGKSSATNQNTEKVLPPRLNLCPRTSYSSLSSPGTSPSGSSVSSQDSAFSQISEHSVFTPTETSSPIDCTFQAQRKREDLSPDFSNASHVSGMPGPSSGQACSRPAYTKKDTMEWHSQMHSVTLHPSTWLRNGVASLKNWSLKKKAKAARPEEEKIASPKGPLEPPPHASGVPEANSLQEEQKDLPLRAAEGLSPVQSAQRCSSSPFQDSERHCSSPFSLVESRLKLCMKSHEEIEPGSQSSSGSLPWERASASSWTLEDATSPDSGPTVVCDIEDRYLTKDI
Protein: PDI-like 5-4 (F4JIR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVSTSKIKSVDFYSDPEVVGFASRVCALSLSFDLSDIELFRCYFLGFKMIVSHFDFGIVAKRVASKKIPRDLTEASLSGAGLSIIAALSMIFLFGMELNNYLAVSTSTSVIVDRSADGDFLRLDFNISFPSLSCEFASVDVSDVLGTNRLNVTKTIRKFSIDSNMRPTGSEFHAGEVLSLINHGDETGEEIVEDSVPLTGRNFDTFTHQFPILVVNFYAPWCYWCNLLKPSWEKAAKQIKERYDPEMDGRVILAKVDCTQEGDLCRRNHIQGYPSIRIFRKGSDLKDDNAHHDHESYYGDRDTESLVKMVVSLVEPIHLEPHNLALEDKSDNSSRTLKKAPSTGGCRVEGYMRVKKVPGNLMVSARSGSHSFDSSQMNMSHVVNHLSFGRRIMPQKFSEFKRLSPYLGLSHDRLDGRSFINQRDLGPNVTIEHYLQIVKTEVVKSNGQALVEAYEYTAHSSVAHSYYLPVAKFHFELSPMQVLITENSKSFSHFITNVCAIIGGVFTVAGILDSILHHSMTLMKKIELGKNF
Protein: Phosphomethylpyrimidine synthase (EC 4.1.99.17) (Hydroxymethylpyrimidine phosphate synthase) (HMP-P synthase) (HMP-phosphate synthase) (HMPP synthase) (Thiamine biosynthesis protein ThiC) (P30136)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
Interaction partners:
- Thiamine-phosphate synthase
- Thiazole synthase
- Sulfur carrier protein ThiS adenylyltransferase
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
- 2-iminoacetate synthase
- Sulfur carrier protein ThiS
- Hydroxyethylthiazole kinase
- Thiamine-monophosphate kinase
- tRNA sulfurtransferase
- Phosphoribosylformylglycinamidine cyclo-ligase
Sequence:
MSATKLTRREQRARAQHFIDTLEGTAFPNSKRIYITGTHPGVRVPMREIQLSPTLIGGSKEQPQYEENEAIPVYDTSGPYGDPQIAINVQQGLAKLRQPWIDARGDTEELTVRSSDYTKARLADDGLDELRFSGVLTPKRAKAGRRVTQLHYARQGIITPEMEFIAIRENMGRERIRSEVLRHQHPGMSFGAHLPENITAEFVRDEVAAGRAIIPANINHPESEPMIIGRNFLVKVNANIGNSAVTSSIEEEVEKLVWSTRWGADTVMDLSTGRYIHETREWILRNSPVPIGTVPIYQALEKVNGIAEDLTWEAFRDTLLEQAEQGVDYFTIHAGVLLRYVPMTAKRLTGIVSRGGSIMAKWCLSHHQENFLYQHFREICEICAAYDVSLSLGDGLRPGSIQDANDEAQFAELHTLGELTKIAWEYDVQVMIEGPGHVPMQMIRRNMTEELEHCHEAPFYTLGPLTTDIAPGYDHFTSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKEDVKQGLITYKIAAHAADLAKGHPGAQIRDNAMSKARFEFRWEDQFNLALDPFTARAYHDETLPQESGKVAHFCSMCGPKFCSMKISQEVRDYAATQTIEMGMADMSENFRARGGEIYLRKEEA
Protein: Leucine repeat adapter protein 25 (Mammary tumor virus receptor 2) (Q566R4)
Organism: Rattus norvegicus (Rat)
Function: Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta. Acts as an adapter that mediates the specific recognition of LIMK1 by CDC42BPA and CDC42BPB in the lamellipodia. LRAP25-mediated CDC42BPA/CDC42BPB targeting to LIMK1 and the lamellipodium results in LIMK1 activation and the subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9QUI1}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9QUI1}. Note=Co-localizes with CDC42BPA, CDC42BPB and LIMK1 in the lamellipodium. {ECO:0000250|UniProtKB:Q9QUI1}.
Interaction partners:
- Cell division cycle 16
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 27 homolog
- Cell division cycle protein 23 homolog
- Ubiquitin-conjugating enzyme E2 C
- Solute carrier family 66 member 2
- Solute carrier family 25 member 45
Sequence:
MNGLPSTEAPGGAGCALAGLPPLPRGLSGLLNASGGSWRELERVYSQRSRIHDELSRAARAPDGPRHAAGSANLGSAAGPRRPVNLDSALAALRKEMVGLRQLDMSLLCQLWGLYESIQDYKHLCQDLSLCQDLSSSLHSDSSYPPDAGLSDDDEPPDASLPPDPPPLTVPQTHNARDQWLQDAFQISL
Protein: Uncharacterized HTH-type transcriptional regulator Rv1828 (P9WME7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Transcriptional regulator that binds to its own promoter and thus may play a role in the regulation of the cotranscribed genes Rv1827 and Rv1828. Can also bind several promoter regions of genes that are essential, including ftsZ. Binds to the imperfect everted repeat sequence CTCAA through its winged-HTH motif.
Interaction partners:
- Glycogen accumulation regulator GarA
- Uncharacterized protein Rv1829
- Probable cell division protein WhiA
- Uncharacterized HTH-type transcriptional regulator Rv0472c
- HTH-type transcriptional regulator Rv1816
- Oxidative stress regulator AosR
- Uncharacterized HTH-type transcriptional regulator Rv1830
- Glycine cleavage system H protein
Sequence:
MSAPDSPALAGMSIGAVLDLLRPDFPDVTISKIRFLEAEGLVTPRRASSGYRRFTAYDCARLRFILTAQRDHYLPLKVIRAQLDAQPDGELPPFGSPYVLPRLVPVAGDSAGGVGSDTASVSLTGIRLSREDLLERSEVADELLTALLKAGVITTGPGGFFDEHAVVILQCARALAEYGVEPRHLRAFRSAADRQSDLIAQIAGPLVKAGKAGARDRADDLAREVAALAITLHTSLIKSAVRDVLHR
Protein: Nuclear migration protein unc-83 (Uncoordinated protein 83) (Q23064)
Organism: Caenorhabditis elegans
Function: Cargo-specific adapter that is involved in nuclear migration during development and thereafter. Component of the unc-83-unc-84 LINC (LInker of Nucleoskeleton and Cytoskeleton) complex where it interacts with unc-84 to form a bridge connecting the nuclear envelope to the cytoskeleton which allows for nuclear transport along microtubules. Within the complex, connects the nuclear envelope to the microtubule cytoskeleton through the kinesin-1 light chain protein klc-2 (most likely within the Kinesin 1 motor complex) to regulate nuclear migrations. Moreover, within the complex, also recruits the large microtubule-associated bicd-1-dlc-1-egal-1 and lis-1-nud-2 complexes to the nuclear envelope to regulate both the bidirectional migration of nuclei and the extent of nuclear migrations. Not required for centrosome attachment to the nucleus.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:11748140, ECO:0000269|PubMed:19605495, ECO:0000269|PubMed:20005871, ECO:0000269|PubMed:27697906, ECO:0000305|PubMed:21411627}; Single-pass type IV membrane protein {ECO:0000305}. Nucleus outer membrane {ECO:0000269|PubMed:16481402}; Single-pass type IV membrane protein {ECO:0000305}. Note=The transmembrane domain associates with the nuclear envelope (PubMed:11748140). Co-localizes with unc-84 and lmn-1 at the nuclear envelope (PubMed:11748140). {ECO:0000269|PubMed:11748140}.
Interaction partners:
- Nuclear migration and anchoring protein unc-84
- Nuclear anchorage protein 1
- Sun domain-containing protein 1
- Kinesin light chain
- Protein nud-2
- KASH
- Zygote defective protein 12
- Protein bicaudal D homolog
- Kinesin heavy chain
- Kinesin light chain
Sequence:
MDVMDSFSEVEMPNDISSEDHLLKVIESSAEEVDIFLENCSSLYNLILDSLHNLTSKTISCECLDEMTSTLEKSAKKILAERPEAENSVLLRLNTICCAMDQLRVQHNSRMMSGADSDTASSARSSTSSSTGEMRLWLHEVERRLEINEKRIRVEPNLQLLLSDQQALQLEIQHEGQLLVNRLNKQIKDDHDSDSSEEEKRKTCVDAIRKRWHTIYLNSLSLVCRIEELINHQQASEDSESDPDLVGPPIKRARIRTVGHLTASDTEESEADEEDRHSQTETVVTEDDNVLPFAENEYESIMDGRVTVDSCTSSSEDQMVEQSTNKKWESVLQDVGYSSGENSIHEALNTCADHLVPETSDMRRKRIECSPVKAFYRTVQLEDMSDLEVTKAINHDVEEEPNLSDSMYVNHDSTFLATQNLPEYDEVMALMDDDDLPMDMSMTESFNTKWREIHGQKKPLRRASRPSREQMNLIAKSSCDASSEDSSEGENQTNLEDDPEMMSVSFNSAQFDTSSPLKRQRSARGLKNASFLYDSLEMDGSFCSTRSEMLPPCKTRSLARRKLRVRRMPRSMSDGEQLGVVSSKPEGMMTPMIRVSPPSTPVRRLLRKLDEQIRNRDSDTAPEHSDAAQAYEWDEYNPPQKDDSISDRHIQTMTDISDQLMNIDDDFAEHFGTSSAIRLIEESKSHLRVVLKALEESDSNIPQLSNFELIARSNLRQVDEALKIQSGNQPSFLETSTLQDLRSEWANLYESIRSPFARIMHQVKKFAATLQEVSSMASLGDVDIRSKEDVAKTLDAVTAIERRLSSERQELRDLLASSSFRDVAKDLSCEFESVSEGYDDAVDKIGKMAHSLSQVKGEWDAWNSRQNDIRNAMVRIESHLKEGQMDNKMIADEMELCQERMNSLETMCNYLTASLGSIQNESNSKNLPDFKAELSIYSNALARLKDRFNDMIRVPTPPTVQFHPPEPLPSLARSMTTQTAEMESETENEPLTIAEAISSSRLIKFTFALSLLAALAAIFYYHVFGKPFGPHVTYVNGPPPV
Protein: L-proline 4-hydroxylase (O06499)
Organism: Dactylosporangium sp
Interaction partners:
Sequence:
MLTPTELKQYREAGYLLIEDGLGPREVDCLRRAAAALYAQDSPDRTLEKDGRTVRAVHGCHRRDPVCRDLVRHPRLLGPAMQILSGDVYVHQFKINAKAPMTGDVWPWHQDYIFWAREDGMDRPHVVNVAVLLDEATHLNGPLLFVPGTHELGLIDVERRAPAGDGDAQWLPQLSADLDYAIDADLLARLTAGRGIESATGPAGSILLFDSRIVHGSGTNMSPHPRGVVLVTYNRTDNALPAQAAPRPEFLAARDATPLVPLPAGFALAQPV
Protein: Protein VP3 [Includes: 2',5'-phosphodiesterase (EC 3.1.4.-); mRNA guanylyltransferase (EC 2.7.7.50); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56)] (A2T3S5)
Organism: Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Function: Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04128}. Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04128}.
Interaction partners:
Sequence:
MKVLALRHSVAQVYADTQVYVHDDTKDSYENAFLISNLTTHNILYLNYSIKTLEILNKSGIAAIALQSLEELFTLIRCNFTYDYELDIIYLHDYSYYTNNEIRTDQHWITKTNIEEYLLPGWKLTYVGYNGSETRGHYNFSFKCQNAATDDDLIIEYIYSEALDFQNFMLKKIKERMTTSLPIARLSNRVFRDKLFPSLLKEHKNVVNVGPRNESMFTFLNYPTIKQFSNGAYLVKDTIKLKQERWLGKRISQFDIGQYKNMLNVLTAIYYYYNLYKSKPIIYMIGSAPSYWIYDVRHYSDFFFETWDPLDTPYSSIHHKELFFINDVKKLKDNSILYIDIRTDRGNADWKKWRKTVEEQTINNLDIAYEYLRTGKAKVCCVKMTAMDLELPISAKLLHHPTTEIRSEFYLLLDTWDLTNIRRFIPKGVLYSFINNIITENVFIQQPFKVKVLNDSYIVALYALSNDFNNRSEVIKLINNQKQSLITVRINNTFKDEPKVGFKNIYDWTFLPTDFDTKEAIITSYDGCLGLFGLSISLASKPTGNNHLFILSGTDKYYKLDQFANHTSISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNIENSVSGHVYNALIYYRYNYSFDLKRWIYLHSIDKVDIEGGKYYELAPIELIYACRSAKEFATLQDDLTVLRYSNEIENYINTVYSITYADDPNYFIGIQFRNIPYKYDVKIPHLTFGVLHISDNMVPDVIDILKIMKNELFKMDITTSYTYMLSDGIYVANVSGVLSTYFKIYNVFYKNQITFGQSRMFIPHITLSFNNMRTVRIETTKLQIKSIYLRKIKGDTVFDMVE
Protein: chitin synthase (EC 2.4.1.16) (Q961Q5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDEAASEIHQTTIRLRPPKKYPTPYGGRLVWTLPGKTKFITHLKDKDRIRHRKRWSQVMYMYYLLGHRLMELPISVDRKDAIAENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLFRGKALMDDNVMKKYTTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPSTIANIMDLLADAKRTIKINDNISLLYIFYQMMLMGGTILGPGTIFLMLVGAFVAAFRIDNWTSFHYNIVPILAFMFICFTCKSNIQLFVAQVLSTAYALIMMAVIVGTALQLGEDGIGSPSAIFLISMVGSFFIAACLHPQEFWCITCGLIYLLSIPSMYLLLILYSIINLNVVSWGTREVVAKKTKKELEAEKKAAEEAKKRVKQKSMLSFLQSGIGDNGDEEGSVEFSLAGLFRCIFCTHGKTSDEKQQLTSIAESLDTIKHRMDTIESAVDPHGHHASRHGRRRTTSSGSKDHHLLTSVAEKSGDESDESDSDTSAEPKQERDFLTNPYWIEDPDVRKGEVDFLSSTEIQFWKDLIDQYLYPIDNDPVEQARIAKDLKELRDSSVFAFFMINALFVLIVFLLQLNKDNIHVKWPFGVRTNITYDESTQEVHISKEYLQLEPIGLVFVFFFALILIIQFTAMLFHRFGTISHILASTELNFCKKKSEDLTQDQLIDKHAVEIVKNLQRLQGIDGDYDNDSGSGPDRIARRKTIQNLEKARQPRRQIGTLDVAFKKRFLKLTADAENNPATPILTRRLTMRAETIRALEVRKNSVMAERRKSAMQTLGAKNEYGITTGAPINNNGALPNQRSGRVSNAGISIKDVFNVNGGGAEQIYGSNGGGTINQGYEHVIDEDGDGNSLRLTTRNPHPHPHHQVSWGQNTNGGGGNGTGRL
Protein: Magnetosome protein MamR (Q6NE51)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: May play a role in controlling magnetite number and size (Probable). Coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis.
Subcellular location: Magnetosome {ECO:0000269|PubMed:14766587}.
Interaction partners:
- Magnetosome protein MamQ
- Magnetosome protein MamB
- Magnetosome protein MamS
- Magnetosome protein MamT
- Multi-heme protein MamP
- Probable membrane transporter protein MamO
- Magnetosome protein MamM
- Magnetosome protein MamN
- Putative lipid kinase MamU
- Magnetosome protein MamL
Sequence:
MIWTAVIKGSALMTFVQGAMALVDKVFGEEILPHRIYSSGEAAQLLGMERLQVLEMVRAGTIKAKKVGDNYRILGSNLVEYMNR
Protein: Recoverin family protein DDB_G0272130 (Q86JE1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco11
Sequence:
MGSGESKNFGNIAQQSRLDHADLTVLLKQFNAISKNGEIKKDDLKKIIEKKYGSDSSLTAILYNLFDRDGDKTINFTEFALAYGFLVNKTLDDVVDTSFHCMDLNGDGNISKGELRAVVMMNKKMEKYIQNDKKVPLDKLTLLPIEVSKINQEADDLFLQLDVNKDGGVSKQEFIQLASSSPELKKKLTSYLVRDEALDFFGTTK
Protein: RNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48) (Polymerase basic protein 1) (PB1) (RNA-directed RNA polymerase subunit P1) (Q9Q0V0)
Organism: Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd)
Function: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065}.
Interaction partners:
Sequence:
MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCLETMEVVQQTRVDKLTQGRQTYDWTLKRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMDKGEMEIITHFQRKRRVRDNMTKKMVTQRTIGKKKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLASIDLKYFNESTRKKIEKIRPLLIDGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIEAGVDRFYRTCKLVGINMTKKKSYINRTGTCEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMMDNDLGPATAQMALQLFIKDYRYPYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLVSDGGPNPYNIRNLHIPEAGLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDEQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAMVSRARIDARIDFESGRIKKEEFAEIMKICSTIEELGRQK
Protein: Protein phosphatase 2C 51 (OsPP2C51) (EC 3.1.3.16) (Q65XK7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Protein phosphatase that acts as positive regulator of seed germination. Involved in the positive regulation of alpha-amylase gene expression. Acts as negative regulator of abscisic acid-mediated responses. May function directly by dephosphorylating ABI5 and suppressing its activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:26362328, ECO:0000269|PubMed:28000033}.
Interaction partners:
- Serine/threonine-protein kinase SAPK3
- Serine/threonine-protein kinase SAPK1
- Serine/threonine-protein kinase SAPK2
- Serine/threonine-protein kinase SAPK8
- Serine/threonine-protein kinase SAPK9
- Abscisic acid receptor PYL10
- Serine/threonine-protein kinase SAPK10
- Os03g0297600 protein
- Serine/threonine-protein kinase SAPK6
- Abscisic acid receptor PYL9
Sequence:
MRETGATDEGHACEVVVAGGDGKAAAARRRRRLELRRLGLAAEDDAAAKRIRSVKDGSSSDDSSTEVVPRSWPACVSHGSVSVIGRRREMEDAVAIERTFMASTGDGAGAIRGGGEGEEDFFAVYDGHGGSRVAEACRKRMHVVLAEEVSLRRLRGQSASGGDVRWKEAMLASFARMDGEVVGSVAAAAPRVDGTEPSGFRTVGSTAVVAVVGRRRIVVANCGDSRAVLSRGGVALPLSTDHKPDRPDELERVEAAGGRVINWNGYRVLGVLATSRSIGDYYLKPFVSAEPEVRVVERTDKDEFLILASDGLWDVVSNEVACKIARNCLNGRAASMFPESVSGSSAADAAALLAELAVSRGSRDNISVVVVELRRLKSRAA
Protein: N-acetyltransferase domain-containing protein (Q38AU6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLLSDEHLALLAKYYATVEFTGEQKDALIEKYWEANEAERKAIARAYASLFANDADFIQRLLAHYDMHVSPHVSQGASSCNENGEPCKSEAELSAGAPAEQDGNGSNNGSLPARPAKPSKGPSGQQLTYSQLVLRTAIQDQYSKLSGDGPFPMAFGLVLSEEERREVIDLYSLQFQYPDQPELQRLVILPQTHSTRTRRRAKGSYTWYLRSLNTNEMVCAVTIMAHHYETHHFVEVPLFATGVGYKKHGFGRLMNAALLQWCVETGFEFVMISADVKAIPFWSHLGYKTMEKSELTRIVFYYEHNCYKFKGAEVMIRYCRTWPTDGVKEALARVQKVIVSGHVGLMDA
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 1 (G5ECH5)
Organism: Caenorhabditis elegans
Function: Probable regulatory subunit of serine/threonine-protein phosphatase PP4 which may play a role in meiosis and embryonic mitosis. Probably in association with catalytic subunit pph-4.1, regulates microtubule severing during oocyte meiosis II by dephosphorylating and likely activating mei-1, a component of the katanin microtubule severing complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23918937}. Note=Localizes to the cytoplasm during meiosis and mitosis. {ECO:0000269|PubMed:23918937}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 catalytic subunit 1
- Protein Phosphatase Four Regulatory subunit
- Serine/threonine-protein phosphatase 4 catalytic subunit 2
- Serine/threonine-protein phosphatase 4 regulatory subunit ppfr-4
- Serine/threonine-protein phosphatase 2A catalytic subunit
- Serine/threonine-protein phosphatase 2A regulatory subunit sur-6
- Serine/threonine-protein phosphatase 2A activator
- Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2
- Serine/threonine-protein phosphatase 4 regulatory subunit 4
- Protein kup-1
Sequence:
MIKSQFATLIRVLIDFQKFWVFLSIFCTFLVVFKFDNLMFQKVRRVFQQNRKNSESIQPKLSTVSGSNSGEGMDKRNTGFSNLQQLGGAIFIDDAEDEPPRVKSSEDSRPAPHWLDSPRDSTTLPDIIASTYSDFIDEAEYATKQMLAILETLNPIEEYIELFESSFKAIEVRLPFDVILNDEKKPDWDAIRRKLIMGSLTVNTTSEKPGITTNQMTAIFDAIPFLFDAVACNPELYEYQNTLSMIVMIAMTGNSMIRRQSINAVQALMERNMLDQDFMRDGVVPGLFNIYQSGVGAFQSNDLRMECVQALCQVISYDAIHDRRWLFDNFLPRFSQMLKDPTMHVRKSALHIFGNLGNMFGQKFTEVFLVPHLITLSCDMTWAVRKVACEIFVKVAECASNQVRIDILSPNFVRLLNDPNKWVSFIAYQQLGPFISLFANPDITGLELRNGQVVVRDPVVLEPSVTEQEDPSNSTFSEDTSDDFRTLPKDTWLPEVDFNDDFEYQLGSIDNTQNQKELTTVTTALVKTPKRGERVMDSVLSGINKMFGSLERSSPKSKEVEKIAATFSSPSKRSPLSLHSAVSLIDKFSKRSNPNNPQRFPVFDSANSDSTLSSNSSNNNSSEQQNSTGIAAKCSSTDDLTKLGLEDDDSPDAAEDSDDFTSETRTTSPRGRRIATNAWSKLDIRQKIFLRRLGALPPSFPKKKATHSSSSSPRKSPTRSPLLSSRKKGLLFDFAAPIEIKSSSSDHSETIPVRTANQQQEKADDDKLNTDERQQYMENSGPKFNTDEDSTNDSDSDDEDNDFEKSFVADEDDGEQDDSPLSIEIKSSSSSDFESVSAATPTSQEPVSNEFSLTYWSSNYAISSIEDELKPFGSSSSFTNSPTSNSYLESRFDVMKVNLSPRARSVSFGTNGSPISTSPRRKANSTSEPSPPNTGNLKSDDSIVMLNTEEKEKLGILDFDEMNMSISSNSSIHGEAAMTEDSDISLTSIEQAALQHVPVDLVESYMRVMGPIGGSGSGGGGNGSSTTIATGDPSLCAETYRHCAHNFPAVCYTLGRAAWPRLKLVFRKLAMDEQARVRQSISHSIHEIANMLGQEITDEDLLPVFYDLRNDQNPDVRNGILIHLYDFVKFLSPEKRDEMILSLPQFFPIGAQPGNQAQNGDWRSRFELISQLSKLCSLYSIQDVNFHMSGIALTLADDRVAEVRREAVMLVSTIVGALVTAEWDNIKGVRDIENGHVDVKKKSNKTDFLSEQFVDDIVSSFAKTQKWTRRQTFCFICAQILRDKQCDGIQFRYFFATPLQQLAQDKVPNVRLASCEALSVWRKTLIAARAQERRGQSPISSPASEPSAIRRDINLVSDMMVKLSNDSDIDAAFIAKKCQGLTDDHQPVDVASRTTRMREREEQFFGDIILSYSPGCNARVSGKEIKQLIRHDQGAVQKAAPLQSMEDFGDEILAHAADSVNIQTPPEVVATVQRVSITNEQFEDNTEAVDMEIEEDEDENSTEKKENTEKTAEEESENVKNTEDELDIPMDPAPTLPPPVTSKNQSSSPITASSSDNNETSA
Protein: Alpha-N-acetylglucosaminidase (Q54DW5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Transmembrane protein
- Lysosomal beta glucosidase
Sequence:
MLKINKSKFGFLIFLTFLVINFSKSIQFNNQINFNDNGNEILNNIEDQRFNNVLLDLHMERDYKDGNKQISTVYGLIERLFNFEMTLFFKLKIEESEWMTGEYYEISTESVENEDSSKNITFVTIRADSGVNLAMGLQYYLKYYCFCSYTWSGDQCSITSYSQLPAVTEGSVSIPVISAYRYYMNVCTFGYSTTWWNWSRWEREIDWMALNGYNLPLAFVGQEYIWYRVFSELGLSFDQISTWLTGPAFLPWNRMGNVNGWGGPITLDWLEKQRDLQIKILERMRQYGMKPVLPGFAGHIPGAIQQLFPQANISVLSTWCNFNGTFYLESTDPLFAKITTMFIGELIDVFGTDHFYNFDPFNELEPPSNDTDYLRQTSQSMYENVLLADPKAVWVLQGWFIVDAPEFWQAKQTEAWFSGVPIGGVLVLDLWSDVIPGWTTTNYYYGHYWVWCMLHNFGGRSGMYGRLPWISSNPITARGLSPNMVGIGLTPEAIEQNVVVYDMMSEMSWRSVQPNLTEWVTQYTHRRYGKLVPEIVDVWISLVNTVFNATAATARANMGAPESFIALRPQLTFGNNSFYNPNILYNAWNVFSMVDDEYVISTETFEFDISEFTMQSLSNYFMDQYFLLIEAFNASDVQTLSTISIELLDIINYMDEIASTQSSLQLGLWTYRARLWAYPTNDIPTLQNSSNSNTAPYEFNARNVLTLWGPSNSVLHDYAFKLWSGLVSDFYSPRWQLFLKSLVQSVENRKPFNKESFNRMVENLEEQWVVQQTIYPTVPVGQAYNTSKYIQTHLKINF