wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS14 (40S ribosomal protein S29) (Q6FWE3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL43
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS28
- 40S ribosomal protein S27
- YL17
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Large ribosomal subunit protein eL39
Sequence:
MAHENVWFSHPRRFGKGSRQCRVCSSHTGLIRKYDLNICRQCFRERASDIGFNKYR
Protein: Nucleoporin nup40 (Nuclear pore protein nup40) (O13838)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm).
Subcellular location: Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
Interaction partners:
- Nucleoporin nup44
- Nucleoporin nsp1
- Meiotically up-regulated gene 87 protein
- Nucleoporin nup186
- Uncharacterized WD repeat-containing protein C4F10.18
- Probable nucleoporin C890.06
- Nuclear envelope protein ndc1
- Nucleoporin nup61
- Nucleoporin nup211
- Nucleoporin nup120
Sequence:
MSFGGSGSITNRSTLKPLSVDDLRSPSPQKEYRGFRTSVSNIPQEKKFVPSHLSHFGSSQQRRFAPEVSSPLAEPYESSSSFRLSLSSPPSSKFGGPSFGTPKPFLHTNRLGTGSLIEDAPPTQSIYDFSSSRQINALNVGQSSSPFSPVSEKVYDPSFTMSGAPQDSNTSVIVFGFPPELTNQVIAEFSRFGTIISENSLTASSAGFTPSKGPISGNWLQLTYAEPSSAAKAVLSNGMLINDSFMVGCIYSPAEAKEHVPKTLRNSNKDLEMTDASSSETSMSIPVHADAHFQSQSGLGKKVIVQHKNDIFKSSQKHQPRNWLFHYLFGFGSTEPIDEEEKSKTASDNTSLQTSLFGKIVQVVLHTLFGF
Protein: Elongation factor 1-alpha 1 (EF-1-alpha 1) (eEF-1A1) (P0DH99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Probable elongation factor 1-gamma 2
- GTP-binding nuclear protein Ran-2
- GTP-binding nuclear protein Ran-3
- GTP-binding nuclear protein Ran-1
- GTP-binding nuclear protein Ran-4
- Elongation factor 1-delta 2
- Glyceraldehyde-3-phosphate dehydrogenase GAPC2, cytosolic
- Glyceraldehyde-3-phosphate dehydrogenase GAPC1, cytosolic
- Elongation factor 1-beta 1
- Glyceraldehyde-3-phosphate dehydrogenase GAPCP1, chloroplastic
Sequence:
MGKEKFHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIIKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGMIKPGMVVTFAPTGLTTEVKSVEMHHESLLEALPGDNVGFNVKNVAVKDLKRGYVASNSKDDPAKGAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSEILTKIDRRSGKEIEKEPKFLKNGDAGMVKMTPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVDKKDPTGAKVTKAAVKKGAK
Protein: Large ribosomal subunit protein uL24c (50S ribosomal protein L24, chloroplastic) (CL24) (Protein SUPPRESSOR OF VARIEGATION 8) (P92959)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (By similarity). Required for optimal plastid performance in terms of photosynthesis and growth. Required for the translation of plastid mRNAs. Plays a critical role in biosynthesis of thylakoid membrane proteins encoded by chloroplast genes.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21923745}.
Interaction partners:
- Large ribosomal subunit protein bL27c
- Large ribosomal subunit protein bL9c
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18z
- Small ribosomal subunit protein uS9c
- Large ribosomal subunit protein uL4c
- Large ribosomal subunit protein bL17c
- Large ribosomal subunit protein eL24y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL6c
Sequence:
MATMSALQSSFTSLSLSPSSSFLGQRLISPISLSVTSPVKPAENPCLVLAKLKRWERKECKPNSLPILHKMHVKFGDTVKVISGRDKGKIGEVTKIFTHNSTIVIKDVNLKTKHMKSREEGEPGQIVKIEAPIHSSNVMLYSKEKDVVSRVGHKVLEDGQKVRYLIKTGELIDTIEKWKLLKEAKDKETTQVAVTSAS
Protein: Cell division protein ZipA (FtsZ interacting protein A) (P77173)
Organism: Escherichia coli (strain K12)
Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL and FtsN. ZipA overproduction protects FtsZ from degradation by ClpP by preventing recognition by ClpX. Does not affect the GTPase activity of FtsZ.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:9008158}; Single-pass type I membrane protein {ECO:0000269|PubMed:9008158}. Note=Localizes to the Z ring in an FtsZ-dependent manner (PubMed:10209756, PubMed:9008158, PubMed:9864327). Localization does not depend upon FtsA or FtsI (PubMed:10209756, PubMed:9864327). {ECO:0000269|PubMed:10209756, ECO:0000269|PubMed:9008158, ECO:0000269|PubMed:9864327}.
Interaction partners:
- Cell division protein FtsA
- Cell division protein FtsZ
- Cell division protein FtsQ
- Cell division protein FtsN
- Cell division protein FtsL
- Cell division ATP-binding protein FtsE
- Probable peptidoglycan glycosyltransferase FtsW
- DNA translocase FtsK
- Peptidoglycan D,D-transpeptidase FtsI
- Cell division protein ZapA
Sequence:
MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA
Protein: D-allose import ATP-binding protein AlsA (EC 7.5.2.8) (P32721)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex AlsBAC involved in D-allose import. Probably responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- D-allose transport system permease protein AlsC
- D-allose-binding periplasmic protein
- D-allulose-6-phosphate 3-epimerase
- D-allose kinase
- Ribose import permease protein RbsC
- Probable ABC transporter permease protein YphD
- Autoinducer 2 import system permease protein LsrC
- L-arabinose transport system permease protein AraH
- Autoinducer 2 import system permease protein LsrD
- Galactose/methyl galactoside import permease protein MglC
Sequence:
MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNISYNKLDHKLAAQLGIGIIYQELSVIDELTVLENLYIGRHLTKKICGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGIVSDVSNDDIVRLMVGRELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALPQE
Protein: Probable dipeptidyl peptidase 4 (EC 3.4.14.5) (Dipeptidyl peptidase IV) (DPP IV) (DppIV) (Q4WPH9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Dipeptidyl-peptidase 5
- Leucine aminopeptidase 1
- Extracellular metalloproteinase mep
- Tripeptidyl-peptidase sed4
- Tripeptidyl-peptidase sed3
- Neutral protease 2 homolog AFUB_070680
- Neutral protease 2 homolog AFUA_4G13750
- Neutral protease 2
- Tripeptidyl-peptidase sed2
Sequence:
MKWSILLLVGCAAAIDVPRQPYAPTGSGKKRLTFNETVVKRAISPSAISVEWISTSEDGDYVYQDQDGSLKIQSIVTNHTQTLVPADKVPEDAYSYWIHPNLSSVLWATNYTKQYRHSYFADYFIQDVQSMKLRPLAPDQSGDIQYAQWTPTGDAIAFVRDNNVFVWTNASTSQITNDGGPDLFNGVPDWIYEEEILGDRFALWFSPDGAYLAFLRFNETGVPTFTVPYYMDNEEIAPPYPRELELRYPKVSQTNPTVELNLLELRTGERTPVPIDAFDAKELIIGEVAWLTGKHDVVAVKAFNRVQDRQKVVAVDVASLRSKTISERDGTDGWLDNLLSMAYIGPIGESKEEYYIDISDQSGWAHLWLFPVAGGEPIALTKGEWEVTNILSIDKPRQLVYFLSTKHHSTERHLYSVSWKTKEITPLVDDTVPAVWSASFSSQGGYYILSYRGPDVPYQDLYAINSTAPLRTITSNAAVLNALKEYTLPNITYFELALPSGETLNVMQRLPVKFSPKKKYPVLFTPYGGPGAQEVSKAWQALDFKAYIASDPELEYITWTVDNRGTGYKGRAFRCQVASRLGELEAADQVFAAQQAAKLPYVDAQHIAIWGWSYGGYLTGKVIETDSGAFSLGVQTAPVSDWRFYDSMYTERYMKTLESNAAGYNASAIRKVAGYKNVRGGVLIQHGTGDDNVHFQNAAALVDTLVGAGVTPEKLQVQWFTDSDHGIRYHGGNVFLYRQLSKRLYEEKKRKEKGEAHQWSKKSVL
Protein: Citrate transport protein (Q7KSQ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
- Large ribosomal subunit protein mL40
- Citrate synthase
- Probable citrate synthase, mitochondrial
- Transport and Golgi organization protein 2
- ATP-citrate synthase
- DNA polymerase epsilon subunit 2
- ADP,ATP carrier protein
- Guanylate binding protein 128up
- STING ER exit protein
- RE68649p
Sequence:
MDRSAFASLVSPYRRRPWMTEHGAAAADSGQVGLKGIVAGGITGGIEICITYPTEYVKTQLQLDEKGAAKKYNGIFDCVKKTVGERGFLGLYRGLSVLVYGSIPKSAARFGAFEFLKSNAVDSRGQLSNSGKLLCGLGAGVCEAIVAVTPMETIKVKFINDQRSGNPKFRGFAHGVGQIIKSEGISGIYKGLTPTILKQGSNQAIRFFVLESLKDLYKGDDHTKPVPKLVVGVFGAIAGAASVFGNTPLDVVKTRMQGLEASKYKNTAHCAVEILKNEGPAAFYKGTVPRLGRVCLDVAITFMIYDSFMDLFNKVWV
Protein: Lysozyme 1 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase) (Q27650)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Has antibacterial activity against Gram-positive bacteria. No activity against S.aureus. Does not appear to have chitinase activity.
Subcellular location: Cytoplasmic granule {ECO:0000269|PubMed:7649184}.
Interaction partners:
Sequence:
MFALFLCIALASAKLGIDVSQPTSTSSFTCLRNKGFTTMVIVRAWKSTGSFDTNAPQTLKNANAAGFSIENSDVYYYPCISCGNMAGQVRTFWQKVGQYSLKVKRVWFDIEGTWTSSVSTNQNYLMQMMNEARAIGIVHGIYGSKYYWGNLFGSSYKYAYASSTPLWYPHYDNSPSFSDFSSFGGWTSPSMKQYRGDVSVCSAGVDYNYKP
Protein: Classical arabinogalactan protein 6 (Q9LY91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death (By similarity). Plays an important role during the formation of the nexine layer of the pollen wall.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Arabinogalactan protein 23
- Arabinogalactan protein 40
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II, IV and V subunit 11
- Fasciclin-like arabinogalactan protein 3
- Transcription initiation factor IIF subunit alpha
- FACT complex subunit SSRP1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH subunit TFB4
Sequence:
MARQFVVLVLLTLTIATAFAADAPSASPKKSPSPTAAPTKAPTATTKAPSAPTKAPAAAPKSSSASSPKASSPAAEGPVPEDDYSASSPSDSAEAPTVSSPPAPTPDSTSAADGPSDGPTAESPKSGAVTTAKFSVVGTVATVGFFFFSF
Protein: Class V chitinase CHIT5b (MtCHIT5b) (EC 3.2.1.14) (A0A072UR65)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5. Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules. Has the capacity to reduce hyphal growth of the fungus Trichoderma viride in an agar-plate bioassay.
Interaction partners:
- Beta-hexosaminidase
- Beta-hexosaminidase
- Beta-hexosaminidase
Sequence:
MANILNLKHLLTLALILLALATKSSTSSSSSITRVKGIYWLENPFFPPTTVDTSLFTHIFYSFLTPNNITYKLEISSSQILSLNTFTKTFKTKSPPAATLFSIGGAGSNSSLLAFIASDPPACAAFINSTIDVARTFGFDGIDLDWEFPKNTKEMNDLGEMLFQWRKAISDEGATTGRPPLLLTAAVYFAVNFSIYGEPRMYPVNSINENLDWVNVMSYELRGPRSNKTGAPSGTFDPKSNVSVVSGLLSWIHSGVVPEKLVMGMPLYGKSWKLRDPNVHGIGAPSVGSGPGVNGLMAYFQVLDFNRQKSAKVEYDVDTASVYSYSGSTWIGYDNPFTVSIKVGFAQALKLRGYFFWVAGLDTLDWKIATQASKAWKLV
Protein: Receptor-like protein 9DC2 (P0DO06)
Organism: Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium)
Function: Involved in plant defense. Confers resistance to the fungal pathogen C.fulvum through recognition of the AVR9 elicitor protein.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGCVKLVFFMLYVFLFQLVSSSSLPHLCPEDQALALLQFKNMFTVNPNAFHYCPDITGREIQSYPRTLSWNKSTSCCSWDGVHCDETTGQVIALDLRCSQLQGKFHSNSSLFQLSNLKRLDLSNNNFIGSLISPKFGEFSDLTHLDLSDSSFTGVIPSEISHLSKLHVLLIGDQYGLSIVPHNFEPLLKNLTQLRELNLYEVNLSSTVPSNFSSHLTTLQLSGTGLRGLLPERVFHLSDLEFLDLSYNSQLMVRFPTTKWNSSASLMKLYVHSVNIADRIPESFSHLTSLHELDMGYTNLSGPIPKPLWNLTNIESLDLRYNHLEGPIPQLPIFEKLKKLSLFRNDNLDGGLEFLSFNTQLERLDLSSNSLTGPIPSNISGLQNLECLYLSSNHLNGSIPSWIFSLPSLVELDLSNNTFSGKIQEFKSKTLSAVTLKQNKLKGRIPNSLLNQKNLQLLLLSHNNISGHISSAICNLKTLILLDLGSNNLEGTIPQCVVERNEYLSHLDLSKNRLSGTINTTFSVGNILRVISLHGNKLTGKVPRSMINCKYLTLLDLGNNMLNDTFPNWLGYLFQLKILSLRSNKLHGPIKSSGNTNLFMGLQILDLSSNGFSGNLPERILGNLQTMKEIDESTGFPEYISDPYDIYYNYLTTISTKGQDYDSVRILDSNMIINLSKNRFEGHIPSIIGDLVGLRTLNLSHNVLEGHIPASFQNLSVLESLDLSSNKISGEIPQQLASLTFLEVLNLSHNHLVGCIPKGKQFDSFGNTSYQGNDGLRGFPLSKLCGGEDQVTTPAELDQEEEEEDSPMISWQGVLVGYGCGLVIGLSVIYIMWSTQYPAWFSRMDLKLEHIITTKMKKHKKRY
Protein: Dual specificity protein kinase zakA (EC 2.7.12.1) (Zaphod K Kinase 1) (Zaphod kinase 1) (Zaphod kinase A) (Q75JK0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Positive regulator of gsk3/gskA activity required for cell pattern formation and a downstream effector of carC. The kinases, gsk3/gskA, zakA and zak2, form part of a signaling pathway that responds to extracellular cyclic AMP. The pathway has a role in transcriptional regulation; required to direct prespore/spore fates during development. ZakA negatively regulates prestalk differentiation by regulating expression of ecmB. Phosphorylates Y-214 of gsk3/gskA, in vitro.
Interaction partners:
- Cyclic AMP receptor 3
Sequence:
MHYHNKDDWEEISFIGEGQYGRVIKCRKKNGFILNEQVDYVAIKIISKDKFKRNETDILEKIRLFNIPRYYSHAEDDNFIYIYMEYIEGENLANILKTKKQGRFKESRIISMIADLVETLSFLHKHHVIHRDIKTANLVLDKNKNLKLIDFGASTIQNKKQFEQYLNETTNNNNNPNNNNNNNNNNNNNNNNNNNNNNNNNNINNINNNNDLNGSGSGISTYLNEQYKQSSFAIIGTFNYMAPEVKRNYRATRKSDVWSLGCTIIEMAGGDLSQKLNGIPIIPDHLSDTLKDFLNHCLVIDPKKRSYMEELLSHKLIVHIIGPNKSKNYGVEPKFKDDDDFEEIENEKDNYLSSRFPAKFAPQYEKPKWEIEFEELEFDKDDSEGGAGNFGDVKKGLLNETEVAIKFVKKAHCEAITVCDTFYHEVLILSNLRHPNIVQFMAACIKYGEKETNHCIVSEWMSGGNLTQFLMNNHKVLENNPHLRVKLLTDIAKGILYLHKQHIIHRDLTSNNVLLDFKREILPNQLYGSNEFTAKVCDFGLSSNQSESKKLRGGSIHYMAPENLNGSPINEKSDIYSFGLLVWQMFSYAPPNTIYSPKEMASMVSDPKQNYRPQIPFNVPLKFKELITQCWDRNPLNRPKDFSIIIEKLKEIGLTYNRSSSNVSPINSPLINNNNNNYNNNHLNSLSSSLNSSPTYYAKTFGDSNSNIDVYHSADSITPIVSSPPIIKIDLTQDDWDSKLKQLDLEHENKSLISISINDNNNNNINNNNTNNNNVNDLGYC
Protein: Delta(14)-sterol reductase TM7SF2 (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (Sterol C14-reductase) (Transmembrane 7 superfamily member 2) (E9PLL1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Microsome membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}.
Interaction partners:
Sequence:
MAPTQGPRAPLEFGGPLGAAALLLLLPATMFHLLLAARSGPARLLGPPASLPGLEVLWSPRALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAGLPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSELNPRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGS
Protein: Lymphocyte antigen 96 (Ly-96) (ESOP-1) (Protein MD-2) (Q9Y6Y9)
Organism: Homo sapiens (Human)
Function: Binds bacterial lipopolysaccharide (LPS). Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both LY96 and TLR4, but not TLR4 alone, respond to LPS.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11593030, ECO:0000305|PubMed:11274165}. Secreted {ECO:0000269|PubMed:11593030}. Note=Retained in the extracellular space at the cell surface by interaction with TLR4 (PubMed:10359581). {ECO:0000269|PubMed:10359581, ECO:0000269|PubMed:11593030}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 4
- Toll-like receptor 2
- Lymphocyte antigen 86
- Toll/interleukin-1 receptor domain-containing adapter protein
- Lipopolysaccharide-binding protein
- Monocyte differentiation antigen CD14
- High mobility group protein B1
- CD44 antigen
- Toll-like receptor 1
Sequence:
MLPFLFFSTLFSSIFTEAQKQYWVCNSSDASISYTYCDKMQYPISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDDYSFCRALKGETVNTTISFSFKGIKFSKGKYKCVVEAISGSPEEMLFCLEFVILHQPNSN
Protein: SEC24 homolog C, COPII coat complex component (A0A286YD08)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
VRLLCEELKSLLDYLPREGGAEESAIRVGFVTYNKVLHFYNVKSSLAQPQMMVVSDVADMFVPLLDGFLVNVSESRAVITSLLDQIPEMFADTRETETVFAPVIQAGMEALKAAECAGKLFLFHTSLPIAEAPGKLKNRDDRKLINTDKEKTLFQPQTAHWRLCLQICLLPGGK
Protein: Cytochrome c (P53698)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular location: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex catalytic subunit, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 7, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit Va
- Cytochrome c oxidase subunit 1
- Elongation factor Tu
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 9, mitochondrial
Sequence:
MPAPFEKGSEKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGVFGRKSGLAEGYSYTDANKKKGVEWTEQTMSDYLENPKKYIPGTKMAFGGLKKPKDRNDLVTYLKKATS
Protein: SNF2 domain-containing protein CLASSY 3 (EC 3.6.4.-) (Protein CHROMATIN REMODELING 31) (AtCHR31) (F4I8S3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable chromatin remodeling factor.
Subcellular location: Nucleus {ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- DNA-directed RNA polymerase IV subunit 1
- Protein SAWADEE HOMEODOMAIN HOMOLOG 1
- DNA-directed RNA polymerase V subunit 1
- Hydroxyproline-rich glycoprotein family protein
- Uncharacterized protein
- Uncharacterized protein
- Chromatin structure-remodeling complex protein SYD
- Proline-rich family protein
- Zinc knuckle
- Zinc finger
Sequence:
MECIGKRVKSRSWQRLQAVNKRKKMETVAPVTSPPKKRRQKKPKNYDSDIEDITPTCNDSVPPPQVSNMYSVPNNSVKESFSRIMRDLNVEKKSGPSSSRLTDGSEQNPCLKERSFRVSDLGVEKKCSPEITDLDVGIPVPRFSKLKDVSEQKNTCLMQKSSPEIADLDLVISVPSSSVLKDVSEEIRFLKDKCSPEIRGLVLEKSVPGEIEILSDSESETEARRRASAKKKLFEESSRIVESISDGEDSSSETDEEEEENQDSEDNNTKDNVTVESLSSEDPSSSSSSSSSSSSSSSSSSSDDESYVKEVVGDNRDDDDLRKASSPIKRVSLVERKALVRYKRSGSSLTKPRERDNKIQKLNHREEEKKERQREVVRVVTKQPSNVVYTCAHCGKENTGNPESHSSFIRPHSIRDEIEDVNNFASTNVSKYEDSVSINSGKTTGAPSRPEVENPETGKELNTPEKPSISRPEIFTTEKAIDVQVPEEPSRPEIYSSEKAKEVQAPEMPSRPEVFSSEKAKEIQVPEMPSIPEIQNSEKAKEVQANNRMGLTTPAVAEGLNKSVVTNEHIEDDSDSSISSGDGYESDPTLKDKEVKINNHSDWRILNGNNKEVDLFRLLVNSVWEKGQLGEEDEADELVSSAEDQSQEQAREDHRKYDDAGLLIIRPPPLIEKFGVEEPQSPPVVSEIDSEEDRLWEELAFFTKSNDIGGNELFSNVEKNISANETPAAQCKKGKHDLCIDLEVGLKCMHCGFVEREIRSMDVSEWGEKTTRERRKFDRFEEEEGSSFIGKLGFDAPNNSLNEGCVSSEGTVWDKIPGVKSQMYPHQQEGFEFIWKNLAGTIMLNELKDFENSDETGGCIMSHAPGTGKTRLTIIFLQAYLQCFPDCKPVIIAPASLLLTWAEEFKKWNISIPFHNLSSLDFTGKENSAALGLLMQKNATARSNNEIRMVKIYSWIKSKSILGISYNLYEKLAGVKDEDKKTKMVREVKPDKELDDIREILMGRPGLLVLDEAHTPRNQRSCIWKTLSKVETQKRILLSGTPFQNNFLELCNVLGLARPKYLERLTSTLKKSGMTVTKRGKKNLGNEINNRGIEELKAVMLPFVHVHKGSILQSSLPGLRECVVVLNPPELQRRVLESIEVTHNRKTKNVFETEHKLSLVSVHPSLVSRCKISEKERLSIDEALLAQLKKVRLDPNQSVKTRFLMEFVELCEVIKEKVLVFSQYIDPLKLIMKHLVSRFKWNPGEEVLYMHGKLEQKQRQTLINEFNDPKSKAKVFLASTKACSEGISLVGASRVILLDVVWNPAVERQAISRAYRIGQKRIVYTYHLVAKGTPEGPKYCKQAQKDRISELVFACSSRHDKGKEKIAEAVTEDKVLDTMVEHSKLGDMFDNLIVQPKEADLVEGFSILMP
Protein: DNA (cytosine-5)-methyltransferase DRM1 (EC 2.1.1.37) (Protein DOMAINS REARRANGED METHYLASE 1) (Q9LXE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in de novo DNA methylation. Controls asymmetric and CpNpG methylation. Required for FWA gene silencing but not for the maintenance of SUP gene silencing. Functionally redundant to CMT3 to maintain non-CpG methylation. Involved in RNA-directed DNA methylation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA
- DNA
- DNA
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4
- DNA glycosylase/AP lyase ROS1
- DNA-directed RNA polymerase V subunit 1
- Protein CHROMATIN REMODELING 35
- DNA-directed RNA polymerase IV subunit 1
- Endoribonuclease Dicer homolog 3
- DEMETER-like protein 2
Sequence:
MVMSHIFLISQIQEVEHGDSDDVNWNTDDDELAIDNFQFSPSPVHISATSPNSIQNRISDETVASFVEMGFSTQMIARAIEETAGANMEPMMILETLFNYSASTEASSSKSKVINHFIAMGFPEEHVIKAMQEHGDEDVGEITNALLTYAEVDKLRESEDMNININDDDDDNLYSLSSDDEEDELNNSSNEDRILQALIKMGYLREDAAIAIERCGEDASMEEVVDFICAAQMARQFDEIYAEPDKKELMNNNKKRRTYTETPRKPNTDQLISLPKEMIGFGVPNHPGLMMHRPVPIPDIARGPPFFYYENVAMTPKGVWAKISSHLYDIVPEFVDSKHFCAAARKRGYIHNLPIQNRFQIQPPQHNTIQEAFPLTKRWWPSWDGRTKLNCLLTCIASSRLTEKIREALERYDGETPLDVQKWVMYECKKWNLVWVGKNKLAPLDADEMEKLLGFPRDHTRGGGISTTDRYKSLGNSFQVDTVAYHLSVLKPLFPNGINVLSLFTGIGGGEVALHRLQIKMNVVVSVEISDANRNILRSFWEQTNQKGILREFKDVQKLDDNTIERLMDEYGGFDLVIGGSPCNNLAGGNRHHRVGLGGEHSSLFFDYCRILEAVRRKARHMRR
Protein: Fe2+/Zn2+ uptake regulation proteins (Q8NNC4)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- DNA-directed RNA polymerase subunit alpha
- ABC-type transporter, permease components
- Predicted transcriptional regulators
- ABC-type transporter, ATPase component
- ABC-type transporter, permease components
- ABC-type transporter, periplasmic component
- ABC-type transporter, periplasmic component
- GTPases
- Diphtheria toxin repressor
- DNA-directed RNA polymerase subunit omega
Sequence:
MGINRISQGSAPKLGVRSTRQRKAVIDVLEEIDNFASAKEIHHELSTREHNVGLTTVYRTLQSLADIGAVDVLTVTGGETLYRQCHDEGHHHHLVCTNCGRTVEIDGGPVETWAQEIATKNGFALSSHEAEIFGLCADCKEKVT
Protein: Trypsin inhibitor 1 (SFTI-1) (Q4GWU5)
Organism: Helianthus annuus (Common sunflower)
Function: Inhibits trypsin, cathepsin G, elastase, chymotrypsin and thrombin. Does not inhibit factor Xa.
Interaction partners:
Sequence:
MATTMAKLITLVVLAILAFVEVSVSGYKTSISTITIEDNGRCTKSIPPICFPDGRP