wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein uL4 (60S ribosomal protein L4) (Q9D8E6)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein eS21
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein eL8
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL10
Sequence:
MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALAASALPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVQLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRNIPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDELYGTWRKAASLKSNYNLPMHKMMNTDLSRILKSPEIQRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQARNHKLRVKKLEAAATALATKSEKVVPEKGTADKKPAVGKKGKKVDAKKQKPAGKKVVAKKPAEKKPTTEEKKPAA
Protein: Erythrocyte membrane protein 3 (O96124)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Knob-associated histidine-rich protein
- Ring-infected erythrocyte surface antigen
- Ring-infected erythrocyte surface antigen
Sequence:
MATIKKYHIRGRKNILIFLLKIFLFSPLIWILIYSEYFTVVKNYNKIDNVYNIFEIRLKRSLAQVLGNTRLSSRGVRDPRTKEALKEKQFRDHKRKEALKQKTEKNEKARNALKEKKLKEQKKNDAQKAKDLTKKESQDSSSEKSLKEKVNGEALKEKENKETLKKKELENQKEKEEKNKIKDNNDEALKNKGNDKDDKKIVPKKPESVEKDLKEMELKEKEFIKQHLKDYEERKEKRRNWILRSLRRDKLREIEQLEKLNAQLESAINELKERRASRRPMMVKMQRGMKDEVDEWIKKYDDEQAEKNGTKDEEIKDKGDGYEEIVETKFYGMRENALGELDEYEERYEKKRYYLKEDGEGDLKDVEEKLEETGYGFREKFPTTRILVKRKRNKEQKKLKEDKEKKLIAAEEPDDEKKIKLKDSDDKVVVPVNKNKSSFPDKFRAPDKKRTMFYRLSELFPIVPRKDNELAVSGDCMDSKVNGKKLKSTFNPFKRRRNKLKERKMQELHKFKKNYKKYQKLLEREKRENPDGEPLNTPEIHVIRPSDLMDKGENKSAGHPFKYQPTKGLKEYEESHVAKDYQLEHEPPTKLPEYEKGHVSREYQLDNEVRDELPEYEKGHVSREYQLDNEVRDELPEYEKGHVSREYQLDNEGPSTLKEYDQTELAKGKDITNKPHESVDEYDQSELAKGKDITNKPHESVDEYDQTELAKGKEVTNKPHENLEEYNETDLAKGKEVTNKPHESVDEYDQSELAKGKDITNKPHESVDEYDQTELAKGKEVTNKPHENLEEYNETDLAKGKEVTNKAHENLEEYNETDLAKGKEVTNKAHENLEEYNETDLAKGKEVTNKAHENLEEYNETDLAKGKEVTNKARENLEEYNETDLAKGKEVTNKARENLEEYNETDLAKGKEVTNKAHENLEEYNETDLAKGKEVTNKAHENLEEYNETDLAKGKEVTNKAHENLEEYNETDLAKGKEVTNKARENLEEYNETDLAKGKEVTNKARENLEEYNETDLAKGKEVTNKARENLEEYNETDLAKGKEVTNKARENLEEYEEKDYMKNNELQNKGSDGLKENAELKNKELRNKGSDGLKENAELKNKELRNKGSDGLKENAELKNKELQNKGSEGLKENAELKNKELQNKGSEGLKENAELKNKELRNKGSEGLKENAELKNKELQNKGSEGLKENAELKNKELQNKGSEGLKENAELKNKELQNKGSEGLKENAELKNKELRNKGSEGLKENVYTNNDLKNNDIQNKDLSNKDMKNKELLNKDISNKDMKNKELLNKDLSNEDMKNKELLNKDIRNKDLKSIGNMEQQNTGLKNTPSKGQQNTGLKNTPNERQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPNERQQNTGLKNTPSEGQQNTGLKNTPIEGQQNTGLKNTPSEGQQNTGLKNTPNERQQNTGLKNAANKGQQNTGLKNTPSKGQQNTGLKNTPNERQQNTGLKNTPNERQQNTGLKNTPSEGQQNNDLKNTPNERQQNTGLKNTASKGQQNTGLKNAPNERQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPNERQQNTGLKNTASKGQQNTGLKNAPNERQQNTGLKNTPSEGQQNTGLKNSASKGQQNTGLKNTPSEGQQNNDLKNAPNERQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPSGGQQNTGLKNTPNERQQNTGLKNTPSEGQQNTGLKNTPNERQQNTGLKNAANKGQQNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPNERQQNTGLKNAANKGQQNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNAANKGQQNTGLKNTPSGGQQNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPNERQQNTGLKNTPSEGQQNTGLKNTPSEGQPNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNAANKGQQNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNAANKGQQNTGLKNTPNERQQNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNTPSEGQPNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNAANKGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNAANKGQQNTGLKNTPSEGQQNTGLKNTPSEGQQNTGLKNAANKGQQNTGLKNTPSEGQPNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNTPNEGQQNTGLKNTPSEGQQNTGLKNTPNEGQQNNDLKNKASKGQQNNDLENDGLKHKPNQGQKHTELNNKNLKNKPTDGLKNVKDDELSDNESSDNEKSKKNLRGKKN
Protein: Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (PGD2 synthase) (PGDS) (PGDS2) (Q9XSM0)
Organism: Ovis aries (Sheep)
Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity).
Subcellular location: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
Interaction partners:
Sequence:
MATPNRPWMGLLLLGVLGVLQTPAPTEAALQPNFEEDKFLGRWFTSGLASNSSWFLEKRKVLSMCKSEVAPAADGGLNVTSTFLRKDQCETRTLLLRPAGPPGCYSYTSPHWSSTHEVSVAETDYETYALLYTESVRGPGPDSLMATLYSRTQTPRAEVKEKFTTFARSLGFTEEGIVFLPKTDKCMEVRT
Protein: Rhino (Q49BL2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRNHQRPNLGLVDAPPNDHVEEYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESEVFRLHRKAAAKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMNQKKGKNIKKTAGKIKDIENYPKTQMPSTSQVSTDSTEVFDGNPSATTTNMIKSPRIHSLFSDLNLIEPTKDKDVGDTSLKTPPKSRRLIEFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPRRKRKKTYPNWKFPEITKPFGVNRGLDLDEILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK
Protein: COMPASS component SWD2 (Complex proteins associated with SET1 protein SWD2) (Set1C component SWD2) (P36104)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819204}. Chromosome, telomere {ECO:0000269|PubMed:12819204}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-2
- COMPASS component SPP1
- mRNA 3'-end-processing protein YTH1
- COMPASS component SDC1
- COMPASS component BRE2
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Protein SYC1
- COMPASS component SWD3
- Pre-mRNA polyadenylation factor FIP1
- COMPASS component SHG1
Sequence:
MTTVSINKPNLLKFKHVKSFQPQEKDCGPVTSLNFDDNGQFLLTSSSNDTMQLYSATNCKFLDTIASKKYGCHSAIFTHAQNECIYSSTMKNFDIKYLNLETNQYLRYFSGHGALVNDLKMNPVNDTFLSSSYDESVRLWDLKISKPQVIIPSLVPNCIAYDPSGLVFALGNPENFEIGLYNLKKIQEGPFLIIKINDATFSQWNKLEFSNNGKYLLVGSSIGKHLIFDAFTGQQLFELIGTRAFPMREFLDSGSACFTPDGEFVLGTDYDGRIAIWNHSDSISNKVLRPQGFIPCVSHETCPRSIAFNPKYSMFVTADETVDFYVYDE
Protein: Sorting nexin (B5DEY8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Sorting nexin-1
- Sorting nexin-2
- Sorting nexin-5
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26A
- Sorting nexin
- VPS26 retromer complex component B
- Sorting nexin-3
- TBC1 domain family member 5
Sequence:
MMEGLDDGPDFLSEEDRGLKSINVDLQSDAALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYNQDLSVRGKNKKEKLEDFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICKFFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNGDT
Protein: 2'-5'olygoadenylate synthetase 1E, 45kD isoform (Q8K3L5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MARELFRTPIWRLDNFIEDQLLPDTTFLTELRADIDSISAFLKERCFQGATHPMRVSRVVMGGSYDEHNALKGRSEANMVVFFNDLTSFEDQLKWQQVFIEEIRKHLLQLQQEKPCKLKFEVQSSEEPNTRSLTFKLCSPERQQEVEFDVQPAYDALYEGGYCKSFESINYNKVYAQLIHECTTLEKEGEFSICFTDLHQSFLRYRAPKLWNLIRLVKHWYQLCKEKLRGPLPPQYALELLTVYVWEFGVQDSFGLHAAQCFRTVLELVTKYKCLLIYWTWFYDFRPEISDYLHGQIKKARPLILDPADPTRNVAGSDLQAWDLLAKEAQTWIHSNFFRNCDMSLVNGWEVSLPTVFSGSQAVMDREERKLDFHLSTCWEVLSNSG
Protein: Attractin (Protein zitter) (Q99J86)
Organism: Rattus norvegicus (Rat)
Function: Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines (By similarity). May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti (By similarity). Has a critical role in normal myelination in the central nervous system.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:O75882}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O75882}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000250|UniProtKB:O75882}.
Interaction partners:
- E3 ubiquitin-protein ligase MGRN1
- Agouti-signaling protein
- PC-esterase domain containing 1A
- SLX4 interacting protein
Sequence:
MVAAAAAAEATEARLRGYTTATAAPAGWKERQHRPCAATGAWRPWPRAGLCLPRVLSRALSPPPLLPLLPLLFSLLLLPLPREAEAAAVAAAVSGSAAAEAKECDRPCVNGGRCNPGTGQCVCPTGWVGEQCQHCGGRFRLTGSSGFVTDGPGNYKYKTKCTWLIEGQPNKIMRLRFNHFATECSWDHLYVYDGDSIYAPLIAAFSGLIVPERDGNETAPEVTVTSGYALLHFFSDAAYNLTGFNITYNFDMCPNNCSGRGECKSSNSSSTVECECSENWKGESCDIPHCTDNCGFPHRGICNASDTRGCSCFPHWQGPGCSIPVPANQSFWTREEYSDLKLPRASHKAVVNGNIMWVVGGYMFNHSDYSMVLAYDLASREWLSLNHSVNSVVVRYGHSLALHKDKIYMYGGKIDSTGNVTNELRVFHIHNESWVLLTPKAKDQYAVVGHSAHIVTLSSGRVVMLVIFGHCPLYGYISVVQEYDLEKNTWSILQTQGALVQGGYGHSSVYDHRTKALYVHGGYKAFSANKYRLADDLYRYHVDTQMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTSMSHGAKCFSSDFMAYDIACDRWSVLPRPELHHDVNRFGHSAVLHNSTMYVFGGFNSLLLSDVLVFTSEQCDAHRSEAACVAAGPGIRCLWDTQSSRCTSWELATEEQAEKLKSECFSKRTLDHDRCDQHTDCYSCTANTNDCHWCNDHCVPVNHSCTEGQISIAKYDNCPKDNPMYYCNKKTSCRSCALDQNCQWEPRNQECIALPENICGIGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQSSQSTSKLTLTPWVGLRKINVSYWCWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCERPANHSAKQCRTPCALRTACGECTSSSSECMWCSNMKQCVDSNAYVASFPFGQCMEWYTMSSCPPENCSGYCTCSHCLEQPGCGWCTDPSNTGKGKCIEGSYKGPVKMPSHASTGNVYPQPLLNSSMCLEDSRYNWSFIHCPACQCNGHSKCINQSICEKCEDLTTGKHCETCISGFYGDPTNGGKCQPCKCNGHASLCNTNTGKCFCTTKGVKGEECQLCEVENRYQGNPLKGTCYYTLLIDYQFTFSLSQEDDRYYTAINFVATPDEQNRDLDMFINASKNFNLNITWATSFPAGTQTGEEVPVVSKTNIKEYKDSFSNEKFDFRNHPNITFFVYVSNFTWPIKIQIAFSQHSNFMDLVQFFVTFFSCFLSLLLVAAVVWKIKQSCWASRRREQLLREMQQMASRPFASVNVALETDEEPPDLIGGSIKTVPKPIALEPCFGNKAAVLSVFVRLPRGLGGIPPPGQSGLAVASALVDISQQMPIVYKEKSGAVRNRKQQPPAQPGTCI
Protein: Protein tyrosine phosphatase type IVA 3 (EC 3.1.3.48) (PRL-R) (Protein-tyrosine phosphatase 4a3) (Protein-tyrosine phosphatase of regenerating liver 3) (PRL-3) (O75365)
Organism: Homo sapiens (Human)
Function: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12782572}. Early endosome {ECO:0000269|PubMed:12782572}.
Interaction partners:
- Metal transporter CNNM3
- Breast cancer anti-estrogen resistance protein 1
Sequence:
MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEKDGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALIESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM
Protein: Trimethylguanosine synthase (Cap-specific guanine-N(2) methyltransferase) (Q9VEA4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein modigliani
- Probable small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein G
- Uncharacterized protein
- Small nuclear ribonucleoprotein-associated protein B
- Gem-associated protein 2
- RNA helicase
- LP09875p
- Probable small nuclear ribonucleoprotein E
Sequence:
MNTHHLTTSRTNPQFYIFSQLFGNDFDWNNCNWGGIQNVTWKEFWQREGHELLEQKWHKRFPEYKDLIEVVSSEEQGLWQELWEKHASDYSEKFWYIFSCAFENYQHDLAKSFGLDVAENSEDVEEDLQNLSLTNKPIKSKQQRVTEKEEDESYLTANDDPEDCDEEQQLRLLGLPTSFASKADIINYRKERKTQYELSSSDSEDDHDLLTMENNENEALHGVQSGSVKKKKRRQRQIKKLKARMPECMQEDNNKMVKYWVKRFSLFSRFDQGIRLDRESWFSVTPEKIAKQTARRLACDVIVDAFCGCGGNAIQFANTCGRVIAVDIDAEKLAMAKHNAGIYGVAHKIEFIHADFLQFAASTKLRPNVVFLSPPWGGPDYQKQATFDIETGLLPVGASQLMQLSRSLASDVAFFLPRNANMKQVVALSGVGQQCEVEHNYLDTRMVALTAYYGKGIIKGSVGEDE
Protein: Yop proteins translocation protein K (Low calcium response locus protein KB) (P69974)
Organism: Yersinia pestis
Function: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function.
Interaction partners:
Sequence:
MMENYITSFQLRFCPAAYLHLEQLPSLWRSILPYLPQWRDSAHLNAALLDEFSLDTDYEEPHGLGALPLQPQSQLELLLCRLGLVLHGEAIRRCVLASPLQQLLTLVNQETLRQIIVQHELLIGPWPTHWQRPLPTEIESRTMIQSGLAFWLAAMEPQPQAWCKRLSLRLPLATPSEPWLVAESQRPLAQTLCHKLVKQVTPTCSHLFK
Protein: Histone-lysine N-methyltransferase ATX5 (EC 2.1.1.-) (Protein SET DOMAIN GROUP 29) (Trithorax-homolog protein 5) (TRX-homolog protein 5) (Q8GZ42)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein TRAUCO
- Protein RBL
- Histone-lysine N-methyltransferase ATX2
- Histone H3-lysine
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- Lysine-specific demethylase JMJ26
- Methyl-CpG-binding domain-containing protein 9
- Histone-lysine N-methyltransferase ATX3
- SWR1 complex subunit 6
- SWR1 complex subunit 2
Sequence:
MIIKRKLKTLKRCNSTNEEDDIVRKKRKVNLNGGGSGGDYYYPLNLLGEIGAGIVPGKNGFSVSLCKQVSCSPKVEVVEEEEEEEEIKSTRLVSRPPLVKTSRGRVQVLPSRFNDSVIENWRKDNKSSGEEREEEIEEEACRKEKVKVSSNHSLKIKQQETKFTPRNYKYSSSSALCGEIDDEDKCEEIVRYGNSFEMKKQRYVDDEPRPKKEGVYGPEDFYSGDLVWGKSGRNEPFWPAIVIDPMTQAPELVLRSCIPDAACVMFFGHSGTENERDYAWVRRGMIFPFVDYVERLQEQSELRGCNPRDFQMALEEALLADQGFTEKLMQDIHMAAGNQTFDDSVYRWVEEAAGSSQYLDHVAPSQDMKKYRNPRACVGCGMVLSFKMAQKMKALIPGDQLLCQPCSKLTKPKHVCGICKRIWNHLDSQSWVRCDGCKVWIHSACDQISHKHFKDLGETDYYCPTCRTKFDFELSDSEKPDSKSKLGKNNAPMVLPDKVIVVCSGVEGIYFPSLHLVVCKCGSCGPERKALSEWERHTGSKAKNWRTSVKVKSSKLPLEEWMMKLAEFHANATAAKPPKRPSIKQRKQRLLSFLREKYEPVNVKWTTERCAVCRWVEDWDYNKIIICNRCQIAVHQECYGTRNVRDFTSWVCKACETPEIKRECCLCPVKGGALKPTDVETLWVHVTCAWFQPEVCFASEEKMEPALGILSIPSSNFVKICVICKQIHGSCTQCCKCSTYYHAMCASRAGYRMELHCLEKNGRQITKMVSYCSYHRAPNPDTVLIIQTPSGVFSAKSLVQNKKKSGTRLILANREEIEESAAEDTIPIDPFSSARCRLYKRTVNSKKRTKEEGIPHYTGGLRHHPSAAIQTLNAFRHVAEEPKSFSSFRERLHHLQRTEMERVCFGRSGIHGWGLFARRNIQEGEMVLEYRGEQVRGIIADLREARYRREGKDCYLFKISEEVVVDATEKGNIARLINHSCMPNCYARIMSVGDDESRIVLIAKTTVASCEELTYDYLFDPDEPDEFKVPCLCKSPNCRKFMN
Protein: Ubiquitin carboxyl-terminal hydrolase 45 (EC 3.4.19.12) (Ubiquitin specific peptidase 45) (E9QG68)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the deubiquitination of SPDL1 (By similarity). Plays a role in the repair of UV-induced DNA damage via deubiquitination of ERCC1, promoting its recruitment to DNA damage sites (By similarity). May be involved in the maintenance of photoreceptor function. May play a role in normal retinal development.
Subcellular location: Photoreceptor inner segment {ECO:0000269|PubMed:30573563}. Cytoplasm {ECO:0000250|UniProtKB:Q70EL2}. Nucleus {ECO:0000250|UniProtKB:Q70EL2}.
Interaction partners:
- Kelch-like family member 7.
- Topoisomerase I-binding, arginine/serine-rich a.
- A-type voltage-gated potassium channel KCND1
Sequence:
MRLKDPFSLKTADMTKRSNKPKKPRDEDSSDEVGGLTCQHVSRAVDLSSVKKAVTGSLWSVCSDCLKERNVLEGETAGAHDILVCLKCGFQGCNQAEVQHSTKHQQAHHSDSHCITISLTTWKAWCFECKEELSTHCNKKALAQTLDFLQKQSAKATSGTSSKLIKLREEPAEYVDTQRGKSPVNSTLIPVKGINNLGNTCFFNAVMQNLSQTHMLNDLIQDVKEKGHKMKISPSTETNLGSLTVTLPSPEPLTSAMFLFLQSMKESGKGPVSPKILFNQLCQKAPRFKGYQQQDSQELLHYLLDSMRVEETKRIKAGILKAFNNPTEKTADEETKRQVKAYGKEGVKLNFVDRIFVGELTSTIMCEECEHISTVKEAFIDISLPIIEERISKPTNPARLGKSGREQDSLTSHDDSLAAHSQANRNSRRLSGQKLQSRHSSTSHDDRGPDTVSSRQEEDLCVAGRGLSSYRTDTMGSQSDCSEKESNLQDSSNDADSEASESEWSPRIPSVSSHSSTSDKTSITTTLSTTTHNPSLKSNPSSTPLPSIRPQQGGAVEQLVSAVSKLGLVHTSTDTLPISHSQEELSETRDRDRQHHQGAFQVLCHSYTPSSKECSVQSCLHQFTSIELLMGNNKLLCENCTDRRQRQMKRSDKKAEKVYTSARKQMLISALPPVVTLHLKRFHQAGMNLRKVNRHVDFPLLLDLAPFCSATCKNLGSGERVLYSLYGIVEHSGSMRGGHYAAYVKVRTPQRKPEQRRNQSGSREACSAPQGQWVYVSDTTVQTVPESRVLNSQAYLLFYEELL
Protein: Esterase/lipase/thioesterase family protein (Putative LEA protein) (Q9SVL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cysteine-rich repeat secretory protein 54
- Cysteine-rich repeat secretory protein 42
- At1g77670
- Cysteine-rich repeat secretory protein 41
- Riboflavin biosynthesis protein PYRD
- Protein REVEILLE 7-like
- At4g38410
- Uncharacterized protein At3g50800
- Quinoprotein amine dehydrogenase, beta chain-like RIC1-like guanyl-nucleotide exchange factor
- Dehydrin family protein
Sequence:
MARVAFATSSPPLISSVRTLRRHFSVFAAANPEMSRPSHHSSLEVIGGGSDRFLPSLKDSLAKPYNAFPLIGFNRHVETIYASFFRSVPFVRLRRECLRTKDNGSVALDWVAGEDRHFPPDSPILILLPGLTGGSQDSYVRHMLLRAQSKKWRCVVFNSRGCGDSPVTTPQFYSASFLGDIGEVIDHVVDKFPKANLYAAGWSLGGNILVNYLGQESHNCPLTAAVSLCNPFDLVIADEDFHKGFNNVYDKALSKSLRRIFSKHSLLFEDIGGEFNIPLAANAETVRDFDDGLTRVSFGFKSVDEYYSKSSSSKAIKHVRIPLLCIQAANDPIAPERGIPRDDIKANPNCVLIVTPRGGHLGWVAGEEAPNGAPWTDQVVMEFLQHVENRETINGERSFEDVHDQIQV
Protein: Glycine-rich protein (Q9C9N4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGSTNKLWSRKPDVKTGKSEFPVTRFLRTQIDNIKTTTVGPGIGGGIGCGAGIGIGLSGGLGIGASEGLDHSNVVLGFGIGCGIGFGFGYGFGVGGGYSFDDIKERFDL
Protein: Phospholipase A1 (EC 3.1.1.32) (EC 3.1.1.4) (Detergent-resistant phospholipase A) (DR-phospholipase A) (Outer membrane phospholipase A) (OM PLA) (OMPLA) (Phosphatidylcholine 1-acylhydrolase) (P0A921)
Organism: Escherichia coli (strain K12)
Function: Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:6397463}; Multi-pass membrane protein {ECO:0000269|PubMed:6397463}. Note=One of the very few enzymes located there.
Interaction partners:
- Lysophospholipase L2
- Outer membrane protein assembly factor BamA
- Bifunctional protein Aas--phospholipid O-acyltransferase); Acyl-[acyl-carrier-protein] synthetase
- Phosphatidylserine decarboxylase proenzyme
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- Lipid A palmitoyltransferase PagP
- Outer membrane protein assembly factor BamC
- Outer membrane protein assembly factor BamD
- Outer membrane protein assembly factor BamE
- Outer membrane protein assembly factor BamB
Sequence:
MRTLQGWLLPVFMLPMAVYAQEATVKEVHDAPAVRGSIIANMLQEHDNPFTLYPYDTNYLIYTQTSDLNKEAIASYDWAENARKDEVKFQLSLAFPLWRGILGPNSVLGASYTQKSWWQLSNSEESSPFRETNYEPQLFLGFATDYRFAGWTLRDVEMGYNHDSNGRSDPTSRSWNRLYTRLMAENGNWLVEVKPWYVVGNTDDNPDITKYMGYYQLKIGYHLGDAVLSAKGQYNWNTGYGGAELGLSYPITKHVRLYTQVYSGYGESLIDYNFNQTRVGVGVMLNDLF
Protein: Multicopper oxidase LPR2 (EC 1.-.-.-) (Protein LOW PHOSPHATE ROOT 2) (Q949X9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Multicopper oxidase that may be involved in copper homeostasis and oxidative stress response, and that is necessary for root growth inhibition by low phosphate conditions. Functions together with LPR1 and PDR2 in a common pathway that adjusts root meristem activity to phosphate availability.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:19666499}; Peripheral membrane protein {ECO:0000305|PubMed:19666499}. Note=Associates with PDR2 at the ER membrane. {ECO:0000305|PubMed:19666499}.
Interaction partners:
- Probable manganese-transporting ATPase PDR2
- Aluminum-activated malate transporter 1
- Protein SENSITIVE TO PROTON RHIZOTOXICITY 1
- CLAVATA3/ESR
- Protein ALUMINUM SENSITIVE 3
- Phospholipase D zeta 1
- Inorganic phosphate transporter 1-1
- Protein PHOSPHATE STARVATION RESPONSE 1
- E3 SUMO-protein ligase SIZ1
Sequence:
MEPSRRRMTRDMLLLIVTMAWLVTGDEGGIKQEERLFNLGKLEMFVDKLPHIPTLHGYHFVNGFLKPKSLHIGMFFKKWKFHRDLPATPVFAYGTSKRSATVPGPTIEAVYGVDTYVTWRNHLPLHHILPWDPTISPAIPKHGGIPTVVHLHGGIHEPTSDGNADSWFTAGFKETGSKWTKKTTHYVNKQQPGNMWYHDHAAGLTRVNLLAGLLGSYILRHSSVESPLRLPTGREFDRPLVIFDRSFRKDGSIYMNATGNNPTIHPQWQPEYFGDAIIVNGKAWPRLTVRRRKYRFRITNASNARFFRFFFSNGLDFIVVGSDSAYLAKPVSTKSVLLAPSEIVDVLVDFSKSTSKTAILANNAPYPYPSGDPVTEENSKVMKFIINYKSEVDTSIIPKKLIEYPPAHVSTSTRTRYIAMFEYVSSIDEPTHLYINGLPYNAPVTETPKIGTSEVWEVINLTEDNHPLHIHLGLFKVLEQTALVKSEEFIECMTKRNDAVKCEISKYARGNKTAVTVHERGWKNVFKMMPGHVTKILVRFSYIHSNESYSFDATQEPGYVYHCHILDHEDNMMMRPFAMVL
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA) (E5KS60)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03220}.
Interaction partners:
Sequence:
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Protein: X-linked lymphocyte-regulated 4A (A2BI40)
Organism: Mus musculus (Mouse)
Interaction partners:
- X-linked lymphocyte regulated gene 4
- X-linked lymphocyte-regulated 4C
Sequence:
MASKIKGRPPKQPKVTPALPSDDSQQLHENNPGNNLALETCGESSSSHGTGGPKPGPSKKTLNERKRKYGVSVNKTVQNIEWNVDHFLKVQHERRQELYKDYSHQFLTLVMMWNIDVDQIKKQAGKLSDILDEQQKLFQQFQSIHMQKIEEFKELCDRHLKNLQAIKCCRRKAIIEEARKLMDYLEKTVTEETVHVNKQEAKDGVQSSLLSLLIS
Protein: Coronin-like protein (Q06440)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Actin
- Cofilin
- Proline-rich protein LAS17
- Actin-binding protein
- Fimbrin
- Actin-related protein 2
- Actin-interacting protein 1
- Twinfilin-1
- Riboflavin synthase
- F-actin-capping protein subunit beta
Sequence:
MSGKFVRASKYRHVFGQAAKKELQYEKLKVTNNAWDSNLLKTNGKFIAVNWNASGGGAFAVIPIEEVGKAPDQVPLFRGHTAQVLDTDFDPFNDHRIASGSDDSKIGIWDIPENYKFHDHVDEDGEPIDIKPVKFLTGHARKVGHVLYHPVAENVLASSSGDYTVKLWNVETGKDMITLKHPDMVTSMSFSYDGNYLATVARDKKLRVWNIREEKIVSEGPAHTGAKNQRVVWLGNSDRLATTGFSKLSDRQIGIWDAFNIEKGDLGGFYTVDQSSGILMPFYDEGNKILYLVGKGDGNIRYYEFQNDELFELSEFQSTEAQRGFAVAPKRMVNVKENEVLKGFKTVVDQRIEPVSFFVPRRSEEFQEDIYPDAPSNKPALTAEEWFSGKSVEGPILVSMRSIYDGSAPSFHEAKRPQQPTTQETALEEKKEQPKVEKPISESEKEVKQEAPKSPSPLKSASSSSTINHVLKEDNSINKLLKKSSDIDQVNNAEDPSRDTSGWEEADDEPAPIKIETPVTPTETKKDRTPKVEPSKELKPEPVSIATDRKQEQSLPQEEKSSEKTKSPEQEKSATPPSSITAAKTAITASSKEEPSAARTSPKSLGLKKSVEKLSTLVLQLEDVVDKLTKANLDKDERLLKLEQKIGELSK
Protein: Uncharacterized protein, isoform F (Q8IR33)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEALVNYSSEDDQEDAGFQIRAPQQQQQLRHLPHAKSPKTTTDSLLKQKNNNNYGSGNSPRGKEREREREREREKTKPMSQQQSHRSSSRGRIDESKTKNENKPDRR