wanglab/gogpt-training-data huggingface dataset:
Protein: Crumbs cell polarity complex component 1 (A0A8I6A4M0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLKKTAYLLALYLSSSLLICVKNSFCNKNNTRCLSNSCQNNSTCKRFPQDSSCCLDTANDLDTDCEDLKDPCLSSPCQGTATCVNIPGERSFLCQCPPGYSGLTCDTATNSCGGNLCQHGGTCHKDPEHPVCICPPGYAGRFCETDHNECDSSPCHNGAVCQDRINGYSCFCVPGYQGRHCDLEVDECVSDPCMNEAVCLNEIGRYTCVCPQEYSGVNCELEIDECGSQPCLHGATCRDALGGYFCDCAPGFLGDHCELNFNECESQPCLHGGLCVDGRNSYHCDCTGSGFRGIHCESLIPLCWSKPCHNDATCEDTVDSYICHCWPGRHCEEDIDECLPNPCLNGGTCQNLPGNYTCHCPFDDTSRTFYGGEDCSEILLGCTHHQCLNNGKCIPHFQNGQHEFTCQCPSGYAGPLCETVTTLSFESNGFLWVTSGSHTSMGSECNISLKFQTVQPNALLLVRGNKDMSVKLELLDGCVHLSIEVWNQSKVLLYISHNTSDGEWHLVEVTFAETITLALNGSSCKEKCTTKSSVSIENHQSICALQNSFLGGLPMGTASDSMSVLNIYNVPSTPSFVGCLQDIRFDLNHITLESISSGLSSNVKAGCLRKDWCESQPCQNRGRCINLWQGYRCECDRPYAGSNCLKEYVAGRFGQDDSTGYAAFKVNDNFGQNFNLSMFVRTRQPLGFLLTLGNSTYQYVCVWLEHGSLALKTPGSPKLVANFFLSDGNAHLISLRIKPNEIELYQSSQNLGFMSVPAWTIQRGDVIFIGGLPDREKTEAYGGFLKGCIQDVRLNSQNLEFFPNSTNSAQHDPVLVNVTQGCPGDNVCKSNPCHNGGVCHSLWDDFSCSCPTNTSGRACDEVQWCQLSPCPPIAECQLVPQGFECIANAAFSGLSSEILFRSNGNITRELTNITFGFRTQDTNAVILHAEKEPEFLNISIQDSRLLFQLRSGNSFYTLHLTGSQLVNDGAWHRVTFSMIDPRAQTSLWQMEVDDQTPFVISAVATGNLNFLKDNTDIYVGDQAVDNQKGLQGCLSTVQIGGLYLSYFESLHGFTSKPQEEQFLKVSTNVALTGCLPLSACHSSPCLHGGICEDSYSSYRCACLPGWSGAHCEINVDECSSSPCVHGNCSDGVAAYHCRCEPGYTGGNCEAEVDTCKSHQCANGATCVSGAQGYSCLCLGNFTGRFCRHSRLPSTVCGNEKTNFTCYNGGSCSVFQEDWKCVCRPGFTGEWCEENINECASDPCINGGLCRDLVNRFQCICDVAFAGERCELDVSGLSFYVSLLLWQNLFQLLSYLILRMNDEPEVEWGAQENY
Protein: Na(+)/citrate cotransporter (NaCT) (Sodium-coupled citrate transporter) (Sodium-dependent citrate transporter) (Solute carrier family 13 member 5) (Q8CJ44)
Organism: Rattus norvegicus (Rat)
Function: High-affinity sodium/citrate cotransporter that mediates citrate entry into cells, which is a critical participant of biochemical pathways. May function in various metabolic processes in which citrate has a critical role such as energy production (Krebs cycle), fatty acid synthesis, cholesterol synthesis, glycolysis, and gluconeogenesis (By similarity). Transports citrate into the cell in a Na(+)-dependent manner, recognizing the trivalent form of citrate (physiological pH) rather than the divalent form. Can recognize succinate as a substrate, but its affinity for succinate is several fold lower than for citrate. The stoichiometry is probably 4 Na(+) for each carboxylate, irrespective of whether the translocated substrate is divalent or trivalent, rendering the process electrogenic. Involved in the regulation of citrate levels in the brain (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q86YT5}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASAKTYVTKFKSFVILFFAPILLLPLIILVPDKFARCAYVIILMAIYWCTDVIPVAITSLLPVLLFPLLKVLDSKQVCVQYMTDTNMLFLGSLIVATAVERWELHKRIALRMLLFVGTKPSRLMLGFMFVTAFLSMWISNTATTAMMIPIVEAMLEQMVATNVAVDASQRTMELLDKNKASELPGSQVVFEDPSVQKQEDEETKNMYKAMNLCVCYAASIGGTATLTGTGPNVVLLGQMQELFPDSKDVMNFASWFAFALPNMLLMLVMAWLWLLCFYMRPNLKKTCICCGRKKKDTEKIASKVLYEEYRKLGPLSYAECNVLFCFGLLIILWFSRDPGFMPGWLSIAWIEGNTKHVTDATVAIFVAILLFIVPSQKPKFNFSRQTEEERKTPFYPPPLLNWKVTQEKVPWGIVLLLGGGFAMAKGCETSGLSEWMARQMEPLSSVRPAIITLILSCIVAMTTECTSNVATTTLFLPIFASMARSIGIHPLYVMIPCTLSASLAFMLPVATPPNAIVFAYGHLKVIDMVKTGLVMNILGIASVFLSVNTWGRAVFNLDKFPDWANLTHINT
Protein: Remodeling and spacing factor 1 (H7C306)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XAAAAAAVMAPPGCPGSCPNFAVVCSFLERYGPLLDLPELPFPELERVLQAPPPDVGNGEVPKELVELHLKLMRKIGKSVTADRWEKYLIKYLCECQFDDNLKFKNIINEEDADTMRLQPIGRDKDGLMYWYQLDQDHNVRMYIEEQDDQDGSSWKCIVRNRNELAETLALLKAQIDPVLLKNSSQQDNSSRESPSLEDEET
Protein: Uncharacterized protein C824.03c, mitochondrial (Q9UT40)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MWILKSGFNRCRNFSFMNRGLLGLRNLSVTHNNLVSYLEHLSVQKPSTSNTVAQGTLFEYLVQYVLKQHSFQLERCGGKGDGGVDLVGQFSIKNVLFEPTKVVVSCKSNKGSIGPRFVRELEGSLSSYPTDTLGILACLGSFTSSSLKTLSISNRPLALCRIYVDGFHSYMFQFVWNHQALAIFPDLSVRQIYKLPSPTANIVPLSQEFSQVNYVSLFELLQPLSRTEERPVPLVLVYKNQKISLNC
Protein: CLAVATA3/ESR (CLE)-related protein 5 [Cleaved into: CLE5p] (Q8S8N2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate.
Subcellular location: [CLE5p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MATLILKQTLIILLIIFSLQTLSSQARILRSYRAVSMGNMDSQVLLHELGFDLSKFKGHNERRFLVSSDRVSPGGPDPQHH
Protein: Neuronal regeneration-related protein (Neuronal protein 3.1) (Protein p311) (Q16612)
Organism: Homo sapiens (Human)
Function: May have roles in neural function. Ectopic expression augments motility of gliomas. Promotes also axonal regeneration (By similarity). May also have functions in cellular differentiation (By similarity). Induces differentiation of fibroblast into myofibroblast and myofibroblast ameboid migration. Increases retinoic-acid regulation of lipid-droplet biogenesis (By similarity). Down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3 (By similarity). May play a role in the regulation of alveolar generation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11358844}.
Interaction partners:
Sequence:
MVYYPELFVWVSQEPFPNKDMEGRLPKGRLPVPKEVNRKKNDETNAASLTPLGSSELRSPRISYLHFF
Protein: Cell death abnormality protein 1 (Q9XWD6)
Organism: Caenorhabditis elegans
Function: Involved in programmed cell death, also called apoptosis, in both somatic and germ cells. Acts by recruiting ced-6 to phagosomes which enables actin-dependent cytoskeletal reorganization and subsequent engulfment of the apoptotic cell corpse. Has a role in the association of ppk-3 and rab-7 with the phagosomal surface which is necessary for the incorporation of lysosomes to phagosomes during phagosome maturation. Activates the expression of unfolded protein response genes, which are involved in the immune response to live bacteria.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11163239, ECO:0000269|PubMed:35929733}; Single-pass type I membrane protein {ECO:0000269|PubMed:11163239}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:11163239, ECO:0000269|PubMed:35929733}; Single-pass type I membrane protein {ECO:0000269|PubMed:11163239}. Note=Colocalizes with ced-6 and actin halos around early apoptotic cells. Temporally colocalizes with dyn-1 during engulfment of cell corpses. {ECO:0000255, ECO:0000269|PubMed:11163239}.
Interaction partners:
- Cell death protein 6
- Transthyretin-like protein 52
- Cell death abnormality protein 2
- ABC transporter ced-7
- Cell death abnormality protein 12
- CED-5
- Cell death protein 3
- Ras-related protein ced-10
- Bifunctional arginine demethylase and lysyl-hydroxylase psr-1
- Cell death protein 4
Sequence:
MRLILLVLLATWQVVVDTRAPTFPDKLTQQLQQQGTTEPQGDHVCTVKTIVDDYELKKVIHTVVYNDTEQCLNPLTGFQCTVEKRGQKASYQRQLVKKEKYVKQCCDGYYQTKDHFCLPDCNPPCKKGKCIEPGKCECDPGYGGKYCASSCSVGTWGLGCSKSCDCENGANCDPELGTCICTSGFQGERCEKPCPDNKWGPNCVKSCPCQNGGKCNKEGKCVCSDGWGGEFCLNKCEEGKFGAECKFECNCQNGATCDNTNGKCICKSGYHGALCENECSVGFFGSGCTQKCDCLNNQNCDSSSGECKCIGWTGKHCDIGCSRGRFGLQCKQNCTCPGLEFSDSNASCDAKTGQCQCESGYKGPKCDERKCDAEQYGADCSKTCTCVRENTLMCAPNTGFCRCKPGFYGDNCELACSKDSYGPNCEKQAMCDWNHASECNPETGSCVCKPGRTGKNCSEPCPLDFYGPNCAHQCQCNQRGVGCDGADGKCQCDRGWTGHRCEHHCPADTFGANCEKRCKCPKGIGCDPITGECTCPAGLQGANCDIGCPEGSYGPGCKLHCKCVNGKCDKETGECTCQPGFFGSDCSTTCSKGKYGESCELSCPCSDASCSKQTGKCLCPLGTKGVSCDQKCDPNTFGFLCQETVTPSPCASTDPKNGVCLSCPPGSSGIHCEHNCPAGSYGDGCQQVCSCADGHGCDPTTGECICEPGYHGKTCSEKCPDGKYGYGCALDCPKCASGSTCDHINGLCICPAGLEGALCTRPCSAGFWGNGCRQVCRCTSEYKQCNAQTGECSCPAGFQGDRCDKPCEDGYYGPDCIKKCKCQGTATSSCNRVSGACHCHPGFTGEFCHALCPESTFGLKCSKECPKDGCGDGYECDAAIGCCHVDQMSCGKAKQEFEALNGAGRSTGLTWFFVLLIVALCGGLGLIALFYRNKYQKEKDPDMPTVSFHKAPNNDEGREFQNPLYSRQSVFPDSDAFSSENNGNHQGGPPNGLLTLEEEELENKKIHGRSAAGRGNNDYASLDEVAGEGSSSSASASASRRGLNSSEQSRRPLLEEHDEEEFDEPHENSISPAHAVTTSNHNENPYADISSPDPVTQNSANKKRAQDNLYT
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (A0A1B0GU54)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTPTDPGAMPHPGPSPGPGPSPGPILGPSPGPGPSPGSVHSMMGPSPGPPSVSHPMPTMGSTDFPQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPMSGGGPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQGKRTLPGLQQQQQQQQQQQQQQQQQQQQQQQPQQQPPQPQTQQQQQPALVNYNRPSALNAGNSNLKTPADSVSGEGLLPDS
Protein: GH10876p (Q7JYM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
QLEGCTMRSLCFVLLFVWFFYQNEAKSKVSCKDEAGNDVDWWHLYKLPKHYQHNDLGKDTSGLKYLYVTSQNYDTWQMSGKFISDPLSLPAQTLNPLNDDPSHTLLAAYNDQQPNGTVFSSGGHAKGVVASDGETAIWIVHSVPKFPTIPDYSYPTSGEQYAQSMLCVTLKGEDLEKVGQILVYNEPHFYYQRNPLATRSDELFPSLERALHGQWRTESPFQKDLEVRSLDGKKFRLFGKSGRANVELYADVVAPTLDVSLFVEAWRDGAGNLPNSCDKSDKVLNVESISNPELSVDFKTTQDHSKWAVSRPTGILIYHWRVGGGDWICVGDINRQEGQLHRGGGTVCHKSARVSNLYRQLVTNYDKCAQQE
Protein: CRISPR system Cmr subunit Cmr3 (CRISPR type III-B/RAMP module-associated protein Cmr3) (Q8U1S7)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA. Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19945378}.
Interaction partners:
- CRISPR system Cmr subunit Cmr2
- CRISPR system Cmr subunit Cmr6
- CRISPR system Cmr endoribonuclease Cmr4
- CRISPR system Cmr subunit Cmr5
- CRISPR system Cmr subunit Cmr1-1
- TIGR01897 family CRISPR-associated protein
- CRISPR-associated endoribonuclease Cas6
- CRISPR-associated endonuclease Cas1
- CRISPR system Cmr subunit Cmr1-2
- CRISPR-associated helicase Cas3
Sequence:
MIEVTFTPYDVLLFRESRPFDAGSESVARSIIPLPQTVAGAIRTLLFYKGLKNCVGVGEEEPEFTLVGIAIGTEKGRIYPLPFNIIKSEKFYKVVNPGRFLGKLILPPKGKYKSGYVTESILEKYLKGELKEVEENKVIRIEKEKRIGIKLSREKKVVEEGMLYTVEFLRIEKIYAWIEDPGCGIKDILSSYEFLTLGGESRVAFVEVDDKTPDIFNRELGSTKKALFYFSTPTIGKVGEIVQELEKRLNAKIDDYLLVSSRPTAISGWDMHEKKPKGTKFAIPPGSVLFVEFKEEVEVPPYIKLGKLKKLGYGLALGGIWE
Protein: HLA class II histocompatibility antigen, DO beta chain (MHC class II antigen DOB) (P13765)
Organism: Homo sapiens (Human)
Function: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. Modifies peptide exchange activity of HLA-DM.
Subcellular location: Endosome membrane; Single-pass type I membrane protein. Lysosome membrane; Single-pass type I membrane protein. Note=Complexes with HLA-DM molecule during intracellular transport and in endosomal/lysosomal compartments. Heterotetramerization is necessary to exit the ER.
Interaction partners:
- HLA class II histocompatibility antigen, DM beta chain
- HLA class II histocompatibility antigen, DM alpha chain
- MHC class II beta chain N-terminal domain-containing protein
- HLA class II histocompatibility antigen, DR alpha chain
- HLA class II histocompatibility antigen, DO alpha chain
- HLA class II histocompatibility antigen gamma chain
- HLA class I histocompatibility antigen, B alpha chain
- HLA class I histocompatibility antigen, C alpha chain
- HLA class II histocompatibility antigen, DP alpha 1 chain
- HLA class II histocompatibility antigen, DRB1 beta chain
Sequence:
MGSGWVPWVVALLVNLTRLDSSMTQGTDSPEDFVIQAKADCYFTNGTEKVQFVVRFIFNLEEYVRFDSDVGMFVALTKLGQPDAEQWNSRLDLLERSRQAVDGVCRHNYRLGAPFTVGRKVQPEVTVYPERTPLLHQHNLLHCSVTGFYPGDIKIKWFLNGQEERAGVMSTGPIRNGDWTFQTVVMLEMTPELGHVYTCLVDHSSLLSPVSVEWRAQSEYSWRKMLSGIAAFLLGLIFLLVGIVIQLRAQKGYVRTQMSGNEVSRAVLLPQSC
Protein: L-2,3-diaminopropanoate--citrate ligase (EC 6.3.2.54) (Staphyloferrin B biosynthesis protein SbnE) (Q2G1M9)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Catalyzes the synthesis of citryl-L-2,3-diaminopropionic acid from L-2,3-diaminopropionic acid (L-Dap) and citrate, the first step in staphyloferrin B biosynthesis.
Interaction partners:
- 2-[
- N-
- 2-[
- Staphyloferrin B synthase
- ATP-dependent L-serine kinase SbnI
- Staphyloferrin B transporter
- N-
- HpcH/HpaI aldolase/citrate lyase domain-containing protein
Sequence:
MQNKELIQHAAYAAIERILNEYFREENLYQVPPQNHQWSIQLSELETLTGEFRYWSAMGHHMYHPEVWLIDGKSKKITTYKEAIARILQHMAQSADNQTAVQQHMAQIMSDIDNSIHRTARYLQSNTIDYVEDRYIVSEQSLYLGHPFHPTPKSASGFSEADLEKYAPECHTSFQLHYLAVHQDVLLTRYVEGKEDQVEKVLYQLADIDISEIPKDFILLPTHPYQINVLRQHPQYMQYSEQGLIKDLGVSGDSVYPTSSVRTVFSKALNIYLKLPIHVKITNFIRTNDLEQIERTIDAAQVIASVKDEVETPHFKLMFEEGYRALLPNPLGQTVEPEMDLLTNSAMIVREGIPNYHADKDIHVLASLFETMPDSPMSKLSQVIEQSGLAPEAWLECYLNRTLLPILKLFSNTGISLEAHVQNTLIELKDGIPDVCFVRDLEGICLSRTIATEKQLVPNVVAASSPVVYAHDEAWHRLKYYVVVNHLGHLVSTIGKATRNEVVLWQLVAHRLMTWKKEYANNAVFVDCVEDLYQTPTIAAKANLMSKLNDCGANPIYTHIPNPICHNKEVSYCESNNS
Protein: Uncharacterized acyltransferase C1718.04 (EC 2.3.-.-) (Q9P7P0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Lysophospholipid acyltransferase
- Uncharacterized acyltransferase C1851.02
- Putative lysophosphatidic acid:oleoyl-CoA acyltransferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase [NAD
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Triacylglycerol lipase ptl3
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Nuclear elongation and deformation protein 1
- Probable proteasome subunit beta type-5
Sequence:
MQHTFIYDTCLWILSILIDFFFREVKTRGSFRVPRKGPLILVAAPHANQFVDPLILMLQLRREVGRRTSILVAAKSYRQRFIGLMSRAFGAIPVERAQDLAIRGEGKIFVVAEGDKTAIHGKDTLFTKHSVGDTLLLPNNYGSSHIASIKSDTLLYVKREFRGEDAERVLLSPEGSSYKVAPEIDQTYVYNEVRRRLVKGACIALFPEGGSHDRPEMLPLKAGVAIMALETLSQHPDCGLQLLPCGMNYFHPHRFRSRAVLEFGSPLSIPTEYVELYKAKKRREAIQGVLDMIYDALLSVTVQAPDYETLMVIQACRRLYKPAHIQFALPKVVDLNRKLIVGYNHFKHDPRVIRLHDKILLYNRQLYRLGLRDHQVQSLQYSRFMILYKLVYRCCKLFLLALGALPGAILFSPVFIAAHRISVKKAAAALKASSVKIQGRDILATWKLLVALGMTPILYSFYALLCCYYIYSYKLIPHSSIFVYTVPIISTFLFPMVTYAALRFGEVAVDIYKSIRPLFLALIPSKANAVYILKDERKQLVAEVTDLINKLGPELFPDFDPDRITTTIEKPERPSRFARRLSSSVASDVDNLSQLHDTDLNSEVSAPAPLQNVYLYSPNPSALPPSDEEEKDINDKAKLIRNALRQRMGQRMTEIRSRDTPPEEVFSESDEELSD
Protein: RNA polymerase-binding transcription factor DksA (G3XD14)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00926}.
Interaction partners:
- DNA-directed RNA polymerase subunit omega
- RNA polymerase sigma factor RpoD
- RNA polymerase sigma factor RpoS
- GTP pyrophosphokinase
- Transcription elongation factor GreB
- Sugar fermentation stimulation protein homolog
- RNA-binding protein Hfq
- Transcription elongation factor GreA
- Translational regulator CsrA
- Putative Fis-like DNA-binding protein
Sequence:
MSTKAKQQSSQQMTRGFEPYQETKGEEYMSERMRAHFTAILNKWKQELMEEVDRTVHHMQDEAANFPDPADRASQEEEFSLELRARDRERKLIKKIDETLQLIEDEEYGWCDSCGVEIGIRRLEARPTATLCIDCKTLAEIREKQLGS
Protein: Cell division cycle associated 7 like (C9IZR6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MELATRYQQDVRFHSKYFTEELRRIFIEDTDSETEDFAGFTQSDLNGKTNPEVMVVESDLSDDGKASLVSEEEEDEEEDKATPRRSRSRRSSIGLRVAFQFPTKKLANKPDKNSSSEQLFSSARLQNEKKTILERKKDCRQVIQREDSTSESEDDS
Protein: Radical S-adenosyl methionine domain-containing protein 1, mitochondrial (Putative heme chaperone) (Q5SUV1)
Organism: Mus musculus (Mouse)
Function: May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen-III oxidase activity (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS19
Sequence:
MVPSGVRTGRWVAAARAAQRRPRVDSLGQPPSPESASTRAALYVHWPYCEKRCSYCNFNKYIPRGVEEGTVRNCLVTEARTLLRLSGVQRVESVFFGGGTPSLASPHTVAAVLEAVAQEVYLPADSEVTLEANPTSAPGPRLAAFGAAGVNRLSIGLQSLDDAELQLLGRTHSASDALRTLAEARLLFPGRVSVDLMLGLPAQKVEPWLQQLQKLLYHCDDHLSLYQLTLERGTSLFAQVQQGTLPAPDPDLAAEMYQEGRTVLRDAGFRQYEVSNFARNGALSTHNWTYWQCGQYLGIGPGAHGRFVPQGTGGHTREARIQTLEPDNWMKEVTLFGHGTRKCVRLGKLELLEEVLAMGLRTDVGVTHQHWQQFEPQLTLWDVFGASKEVEELLAQGLLLLDYRGLRCSWEGLAVLDSLLLTLLPQLQEAWQHRPSSPVSGG
Protein: FMRF-Like Peptide (Q8WQF5)
Organism: Caenorhabditis elegans
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLSGVLFSIFVLAISANASCDVSALTTENEKELGLRICHLEAEMQVVQRALQEVMQQTDVTLYDQEVPVMNKRKNEFIRFGKRSDGMEKRKNEFIRFGKRKNEFIRFGRSDKGLGLDDNDVSMEKRKNEFIRFG
Protein: Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) (C5A1D5)
Organism: Escherichia coli (strain K12 / MC4100 / BW2952)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
Interaction partners:
Sequence:
MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGMGGMGGMM
Protein: 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein (F4INZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cysteine/Histidine-rich C1 domain family protein
- Putative glucuronosyltransferase PGSIP8
- Transcription factor bHLH149
- Adenine/guanine permease AZG2
- Protein SHORT ROOT IN SALT MEDIUM 1
- Zinc finger CCCH domain-containing protein 17
- Protein PHLOEM PROTEIN 2-LIKE A5
- Transcription factor bHLH147
Sequence:
MSPSMIAPVMEEENKKYQKGVKHLCENGLTKVPTKYIWPEPDRPILTKSDKLIKPNKNLKLPLIDFAELLGPNRPHVLRTIAEACKTYGFFQVVNHGMEGDVSKNMIDVCKRFFELPYEERSKYMSSDMSAPVRYGTSFNQIKDNVFCWRDFLKLYAHPLPDYLPHWPSSPSDFRSSAATYAKETKEMFEMMVKAILESLEIDGSDEAAKELEEGSQVVVVNCYPPCPEPELTLGMPPHSDYGFLTLLLQDEVEGLQILYRDEWVTVDPIPGSFVVNVGDHLEIFSNGRYKSVLHRVLVNSTKPRISVASLHSFPLTSVVKPSPKLVDKHNPSQYMDTDFTTFLQYITSREPKWKNFLESRKIHHV
Protein: Serine-threonine kinase receptor-associated protein (Q9LW17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- La-related protein 6C
- Serine-threonine kinase receptor-associated protein
- Serine-threonine kinase receptor-associated protein
- La-related protein 6A
- La-related protein 6B
- La-related protein 1A
Sequence:
MEKKKVATPLVCHGHSRPVVDLFYSPITPDGFFLISASKDSQPMLRNGETGDWIGTFEGHKGAVWSSCLDNNALRAASASADFSAKLWDALTGDVLHSFEHKHIVRACAFSQDTKYLITGGFEKILRVFDLNRLDAPPTEIDKSPGSIRTLTWLHGDQTILSSCTDIGGVRLWDVRSGKIVQTLETKSPVTSAEVSQDGRYITTADGSTVKFWDANHFGLVKSYDMPCNIESASLEPKSGNKFVAGGEDMWVRLFDFHTGKEIGCNKGHHGPVHCVRFAPTGESYASGSEDGTIRIWQTGPVNPEEISESKPKQSVDEVARKIEGFHINKEGKTAEKPSDA
Protein: Exodeoxyribonuclease 1 (EC 3.1.-.-) (Exodeoxyribonuclease I) (EXO I) (Exonuclease I) (P53695)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: 5'->3' double-stranded DNA exonuclease that could act in a pathway that corrects mismatched base pairs.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Double-strand break repair protein rad32
- Putative MutL protein homolog 1
- DNA replication ATP-dependent helicase/nuclease dna2
- DNA mismatch repair protein msh2
- DNA repair protein rhp51
- DNA mismatch repair protein msh6
- DNA mismatch repair protein pms1
- ATP-dependent DNA helicase hus2/rqh1
- ATP-dependent DNA helicase II subunit 2
- ATP-dependent DNA helicase II subunit 1
Sequence:
MGIKGLLGLLKPMQKSSHVEEFSGKTLGVDGYVWLHKAVFTCAHELAFNKETDKYLKYAIHQALMLQYYGVKPLIVFDGGPLPCKASTEQKRKERRQEAFELGKKLWDEGKKSQAIMQFSRCVDVTPEMAWKLIIALREHGIESIVAPYEADAQLVYLEKENIIDGIITEDSDMLVFGAQTVLFKMDGFGNCITIRRNDIANAQDLNLRLPIEKLRHMAIFSGCDYTDGVAGMGLKTALRYLQKYPEPRAAIRAMRLDKSLKVPVSFEKEFALADLAFRHQRVYCPKDKTLVHLSPPERELSVHEDAFIGSFFDNQLAIDIAEGRSNPITKCAFDIKDSSMQSFTKTTITISKRKGISKTDISNFFMKSIPPSKRPTKSTSLIDVTNVKVQRTHLANDISSEKQSIKSANEKAYVTPKSNSLKPGFGKSLSDISNSATKNENVPFLPPRTGVSKYFKLQKNTEKEIDEQVPSQSNNTTPTSAKSDSASPQNWFSSFSYQTPNSASPPFSSLSHTLPISALAKIGHDALNRKNHASLPSRRIVYKPPSSPSTPISMNPRPKGILSLQQYKFR
Protein: Histidinol-phosphatase (HolPase) (EC 3.1.3.15) (Histidinol-phosphate phosphatase) (Q8NS80)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Catalyzes the dephosphorylation of histidinol-phosphate to histidinol, the direct precursor of histidine.
Interaction partners:
- Histidinol dehydrogenase
- Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family
- Histidinol-phosphate aminotransferase
- Aromatic amino acid aminotransferase
- ATP phosphoribosyltransferase
- Imidazoleglycerol-phosphate dehydratase
- Phosphoribosyl-ATP pyrophosphatase
- 1-
- Fructose-1,6-bisphosphatase class 2
- Imidazole glycerol phosphate synthase subunit HisF
Sequence:
MSKYADDLALALELAELADSITLDRFEASDLEVSSKPDMTPVSDADLATEEALREKIATARPADSILGEEFGGDVEFSGRQWIIDPIDGTKNYVRGVPVWATLIALLDNGKPVAGVISAPALARRWWASEGAGAWRTFNGSSPRKLSVSQVSKLDDASLSFSSLSGWAERDLRDQFVSLTDTTWRLRGYGDFFSYCLVAEGAVDIAAEPEVSLWDLAPLSILVTEAGGKFTSLAGVDGPHGGDAVATNGILHDETLDRLK
Protein: Protein lin-56 (Abnormal cell lineage protein 56) (Q09377)
Organism: Caenorhabditis elegans
Function: Required for translation, stability and/or localization of lin-15a.
Subcellular location: Nucleus {ECO:0000269|PubMed:21196525}.
Interaction partners:
- Protein lin-15A
- Protein lin-8
- C2H2-type domain-containing protein
- Myb_DNA-bind_3 domain-containing protein
Sequence:
MDHHAMYRTAEFNKTTVRLLAEFIEKTGQNATIVNMDSFLEFFAYLNPTAPIPTVPEIEKQLLLKSPIRCIVCGMETESDSAVTLSIDNASIILTATVIGYCRDPSDAVNQIRKESLRACTKHFNSIFHVIFEGLQIENTYCAHHAKYSLANRWCKVYTMIRSSLGEQFTKFDVRNFKSILQSFLDTFGEIDDDKKDKESSHFDECFEEMDSENVEIKMESPQEEAAEKSKFSENLVEVKLEPIETHELDKTISDFSSSDIIDSSQKLQQNGFPEKVEQMDKYSNKLKDEASDKKYEKPGKKDYVEEEGYWAPITDSEDDEA
Protein: Aquaporin PIP1-3/PIP1-4 (Plasma membrane intrinsic protein 1-3) (Plasma membrane intrinsic protein 1-4) (ZmPIP1-3) (ZmPIP1-4) (ZmPIP1;3) (ZmPIP1;4) (Q9AQU5)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Aquaporin SIP2-1
Sequence:
MEGKEEDVRLGANKFSERQPIGTAAQGAGAGDDDKDYKEPPPAPLFEPGELKSWSFYRAGIAEFVATFLFLYITVLTVMGVSKSTSKCATVGIQGIAWSFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRAIFYIIMQCLGAICGAGVVKGFQQGLYMGNGGGANVVAPGYTKGDGLGAEIVGTFILVYTVFSATDAKRNARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNRDHAWSDHWIFWVGPFIGAALAAIYHQVIIRAIPFKSRS