wanglab/gogpt-training-data huggingface dataset:
Protein: Tcc1p (A0A1D8PKT0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Kinesin-like protein
- NADH-ubiquinone oxidoreductase chain 4
- Very long-chain fatty acid transport protein
Sequence:
MPISPVMAKSASTATTTTAPTAVNTTSFDTAATETWITCGECANTLGLIVSAIKSFESAVNRDPANATALVGLSSSLRLNDISVNETIGSQAAIEKLNKSLESFPSLSKEANIFKELCECYLLVGLNDQAYQAIQSAIQLAPQDASLWLLSAQTLIRAGARAHATGSLAHCLSLLPDGTFSSTDIETARAAHAELAAISAADGNIELSIKELRATLELPPPPLSRIDEYVALVCALASALERDNDIPGAIKVCEDGESVVGNSPRILMSHAYLLLSNNSSPNINGAAEQAINLLTKVVDVENESAVQEGSDFLPWYLLGKANSYLDPRAAYDCYQVALRCASNCSIIWLAVGKLYLELKQLKDALEAYSQALKLQLGDGSNGTATAWDGLSCVYERCEDQLMDASDACNRAAACFKAMGDIKSCQFFEDRAIALEKASKKEGPMLNLRDPPDVPTFLIRDIVALAPNERITFTKQQLQAQQQAQQRAQDQVQQQQAQQQQAQQQAQQQAQQQQAQQQAQQQQAQQQAQQQQAQQQQQQQQSHNQSPVQPHHQETARNSPQVPIQTPQQQLVQYQGPPAPPQLPPHQQYLYPMPKNSPRQPQVSTPQIQHAWSPQPQHLQQPQQSPHQNQHQPQQPQQQQQPGSHQPQQNQPPAPQLPPHQQQQFFYPPPPLGPGQPQPNGGPHRSPMNPPQMNPAGAXXMLWVQEVPTIVLSDITIMYSFSAVHKTCNIHHQIGEDRCNGNPKEWSTI
Protein: Peptidyl-prolyl cis-trans isomerase CYP21-2 (PPIase CYP21-2) (EC 5.2.1.8) (Cyclophilin of 21 kDa 2) (Cyclophilin-21-2) (Q8L8W5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- UPF0235 protein At5g63440
- Formyltetrahydrofolate deformylase 2, mitochondrial
- At1g09850
- Probable glucomannan 4-beta-mannosyltransferase 1
- Cysteine proteinase RD21A
- Probable cysteine protease RD21C
- Probable cysteine protease RD21B
- Protein QUA-QUINE STARCH
- Tetratricopeptide repeat
- CDGSH iron-sulfur domain-containing protein NEET
Sequence:
MAITATRLVSLTLLWIVVLFVTLALIQIKLTDVADPSVNEKILDAKLNQVGEDLEGVTHKVYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKGVGNMGKPLYFKGSSFHRIIPGFMIQGGDFTRGDGRGGESIYGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANVIIFASGEVSL
Protein: Transcription factor Sox-11-B (Transcription factor Sox-13) (xSox-13) (XLS13B) (P40650)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that binds to the DNA sequence 5'-AACAAT-3'. Acts as a transcriptional activator (By similarity). Plays a role together with nlk in neural induction during early embryogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MVQRADMDSSQHTEPDTEEGEFMACSPAALDESDPDWCKTATGHIKRPMNAFMVWSKIERRKIMEQSPDMHNAEISKRLGKRWKMLNDSEKIPFIREAERLRLKHMADYPDYKYRPRKKPKVDPTASKSPTLAQSPEKSPKSRSAGKKCPKLKPSHSGNSSKSLSIKSEYGVGGDYVFGSPKSSGKAAVMKCVFMDEDDEEEEEDEEEEEDELQIRIKQEEDDESLRLYNVAKVPASPTLSSSSAESVEGASMYEDIRNGTRLYYNFKNITKQSTIPQATITLAPRPLLATTSPAGSHELLFDLSLNFTQQNPQLPDPNSGNVSLSLVDKDLDSCSEGSLGSHFDFPDYCTPELSEMIAGDWLEANFSDLVFTY
Protein: Phosphoenolpyruvate carboxylase 3 (AtPPC3) (PEPC 3) (PEPCase 3) (EC 4.1.1.31) (Q84VW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pyruvate, phosphate dikinase 1, chloroplastic
- Malate dehydrogenase, chloroplastic
- phosphoenolpyruvate carboxykinase
- Phosphoenolpyruvate carboxykinase 1
- Phosphoglycerate kinase 3, cytosolic
- Citrate synthase 4, mitochondrial
- Citrate synthase 3, peroxisomal
- Citrate synthase 1, peroxisomal
- Citrate synthase 2, peroxisomal
- Citrate synthase 5, mitochondrial
Sequence:
MAGRNIEKMASIDAQLRQLVPAKVSEDDKLVEYDALLLDRFLDILQDLHGEDLRETVQELYELSAEYEGKREPSKLEELGSVLTSLDPGDSIVISKAFSHMLNLANLAEEVQIAHRRRIKKLKKGDFVDESSATTESDIEETFKRLVSDLGKSPEEIFDALKNQTVDLVLTAHPTQSVRRSLLQKHGRIRDCLAQLYAKDITPDDKQELDESLQREIQAAFRTDEIRRTPPTPQDEMRAGMSYFHETIWKGVPKFLRRVDTALKNIGIDERVPYNAPLIQFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAANLYYNQIENLMFELSMWRCTDEFRVRADELHRNSRKDAAKHYIEFWKTIPPTEPYRVILGDVRDKLYHTRERSRQLLSNGISDIPEEATFTNVEQFLEPLELCYRSLCSCGDSPIADGSLLDFLRQVSTFGLSLVRLDIRQESERHTDVLDAITKHLDIGSSYRDWSEEGRQEWLLAELSGKRPLFGPDLPKTEEISDVLDTFKVISELPSDCFGAYIISMATSPSDVLAVELLQRECHVKNPLRVVPLFEKLADLEAAPAAVARLFSIDWYKNRINGKQEVMIGYSDSGKDAGRLSAAWELYKAQEELVKVAKKYGVKLTMFHGRGGTVGRGGGPTHLAILSQPPDTVNGSLRVTVQGEVIEQSFGEAHLCFRTLQRFTAATLEHGMNPPISPKPEWRALLDEMAVVATEEYRSVVFQEPRFVEYFRLATPELEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGAAFRYAIKKDVRNLHMLQDMYKQWPFFRVTIDLIEMVFAKGDPGIAALYDKLLVSEDLWAFGEKLRANFDETKNLVLQTAGHKDLLEGDPYLKQRLRLRDSYITTLNVCQAYTLKRIRDANYNVTLRPHISKEIMQSSKSAQELVKLNPTSEYAPGLEDTLILTMKGIAAGLQNTG
Protein: Caspase-12 (CASP-12) (EC 3.4.22.-) (Q920D5)
Organism: Rattus norvegicus (Rat)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Apoptosis-associated speck-like protein containing a CARD
- DNA damage-inducible transcript 3 protein
- Gasdermin D
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Caspase-1
- TNF receptor-associated factor
- NLR family CARD domain-containing protein 4
- Apoptosis regulator Bcl-2
- X-box-binding protein 1
Sequence:
MAAKRTHERDPIYKIKGLAKDMLDGVFDDLMDKNVLNGDELLKIGEGASLILSKAENLVESFFEKTEMAGKIFAGHIANSDKQLSLQFPSDDEEDELQKMFTPSSASESRGKVEDEEMEVNVGVAHASHLMLTVPQGIQSTEVQDSLKLCSRDWFCTMKTERAEEIYPVMEKEGRTRLALIICNKKFDYLFDRDDAETDILNMKELLQNLGYSVVIKENLTAQEMETELMKFAGRPEHQSSDSTFLVFMSHGILEGICGVKHRNKKPDVLHDDTIFTIFNNSNCPSLRNKPKILIMQACRGRHTGTIWVSTSKGIATADTDEECVLSHRWNNSITKAHVETDFIAFKSSTPHNISWKVGKSGSLFISKLIDCFKKYCWCYHLEEIFRKVQYSFEVPGELTQMPTIERVSMTRYFYLFPGN
Protein: General transcription factor IIH subunit 4 (Basic transcription factor 2 52 kDa subunit) (BTF2 p52) (General transcription factor IIH polypeptide 4) (TFIIH basal transcription factor complex p52 subunit) (Q92759)
Organism: Homo sapiens (Human)
Function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription.
Subcellular location: Nucleus.
Interaction partners:
- CDK-activating kinase assembly factor MAT1
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIH subunit 2
- General transcription factor IIH subunit 1
- General transcription factor IIH subunit 3
- General transcription factor IIH subunit 5
- General transcription factor IIH subunit 2-like protein
- Cyclin-dependent kinase 7
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Cyclin-H
Sequence:
MESTPSRGLNRVHLQCRNLQEFLGGLSPGVLDRLYGHPATCLAVFRELPSLAKNWVMRMLFLEQPLPQAAVALWVKKEFSKAQEESTGLLSGLRIWHTQLLPGGLQGLILNPIFRQNLRIALLGGGKAWSDDTSQLGPDKHARDVPSLDKYAEERWEVVLHFMVGSPSAAVSQDLAQLLSQAGLMKSTEPGEPPCITSAGFQFLLLDTPAQLWYFMLQYLQTAQSRGMDLVEILSFLFQLSFSTLGKDYSVEGMSDSLLNFLQHLREFGLVFQRKRKSRRYYPTRLAINLSSGVSGAGGTVHQPGFIVVETNYRLYAYTESELQIALIALFSEMLYRFPNMVVAQVTRESVQQAIASGITAQQIIHFLRTRAHPVMLKQTPVLPPTITDQIRLWELERDRLRFTEGVLYNQFLSQVDFELLLAHARELGVLVFENSAKRLMVVTPAGHSDVKRFWKRQKHSS
Protein: AT01055p (Smooth, isoform I) (Q8IHH3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNNLNANASAFLWQVPPPQQLTPQSVQQQTVQSVQSMQSVQHSQLLQSAVVSQPRKFGGNKSNYNYMQNHAIMGPGGGPMGGIGGNPNIYRKRHSINTYNAGLYQTNGKSLFSIPENVVMLESQPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPPGLTEDQLIGIFNIKDVPATSVRLFPLKTERSSSGLIEFSNISQAVLAIMKCNHLPIEGKGTKFPFIMKLCFSSSKSMNGAWNNAASEGMIEKENEVDTKVDIYN
Protein: Blue copper protein (PhBcp) (A0A0M4FTF3)
Organism: Petunia hybrida (Petunia)
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAYSKILFCFMIGFVGFLPAITMATQYLVGDDRGWTLDFDYQTWAKNKTFKVGDTLAPPPSEGLTSGYDVITLTKPGKKWYICGVPTHCSDYNQKLVITVEDGAPAPAPASPAPQTEYWVGDDKGWTIDVDYQAWAKGKTFKVGDTLVFKYTKGHHNVFKVNQTGFQNCIAPPPSEGLTSGHDVITLAAPGKKWYICGFPTHCSEHKQKLAITVEGAPAQTPPVWAPAPAPGTPKKIDTGNSYKITSPYKMFVGGAVSIWTILTLV
Protein: Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase (LjCCaMK) (EC 2.7.11.17) (A0AAR7)
Organism: Lotus japonicus (Lotus corniculatus var. japonicus)
Function: Calcium- and calmodulin-dependent protein kinase necessary and sufficient for dedifferentiation of root cortical cells into nodule initials. Not required for calcium spiking. Acts as central regulator of the nodule organogenesis program. Required for root hair curling and infection thread (IT) formation upon rhizobial infection, and arbuscule formation during arbuscular mycorrhiza (AM) fungal infection. Phosphorylates the downstream target IPD3, a protein required for root infection by symbiotic rhizobia and AM fungi. Phosphorylates the downstream target CIP73, a protein required for root nodule organogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:19074278, ECO:0000269|PubMed:21209278}.
Interaction partners:
Sequence:
MGYDQTRKLSDEYEISEILGRGGFSVVRKGTKKSGNEKTQVAIKTLRRLGSSPSGTGGGQKSTATVMGFPSLRQVSVSDALLTNEILVMRRIVENVSPHPNVIDLYDVCEDSNGVHLVLELCSGGELFDRIVAQDKYAETEAAAVVRQIAAGLEAVHKADIVHRDLKPENCLFLDSRKDSPLKIMDFGLSSVEEFTDPVVGLFGSIDYVSPEALSQGKITAKSDMWSLGVILYILLSGYPPFIAQNNRQKQQMIINGNFSFYEKTWKGITQSAKQLISSLLTVDPSKRPSAQELLSHPWVRGDKAKDEQMDPEIVSRLQSFNARRKLRAAAIASVWSSTIFLRTKKLRSLVGTYDLKEEEIESLRIHFKKICGNGDNATLSEFVEVLKAMKMPSLIPLAPRIFDLFDNNRDGTIDMREILCGFSSLKNSKGDDALRLCFQMYDTDRSGCITKEEVASMLCALPEECLPADITEPGKLDEIFDLMDANSDGKVTFEEFKAAMQRDSSLQDMLLSSLRPS
Protein: RE59356p (Q8SYH4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGGYKKEAHNMGLLPPTYSVIPQPVSMWHAGQVATGSPVGLECNKPSELVPPPMYMSYSGGSIANSTEVDIAKEHNPAWREKALQMEKDYRRTACDRERTRMRDMNRAFDLLRSKLPISKPNGKKYSKIESLRIAINYINHLQAMLRESSVGQNGNGCCAWSGGSSSPYDNGNDHWGA
Protein: Protein Wnt (Q8AY89)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
Sequence:
MPECDGVGCASPARRDRQRARGGFLSRRERRGATQRIYLLFILLLLMFTPSVDSSWWYIGALGARVICDNIPGLVNKQRQLCQRHPDLMQSIGQGAKEWIRECQHQFRHHRWNCSTLERDHTVFGRVMLRSSREAAFVYAISSAGVVYAITRACSQGELKICSCDSQRRGRASDEDGDFDWGGCSDNINYGIKFAKAFVDARERMVKDARALMNLHNNRCGRMAVKRFMKTECKCHGVSGSCALRTCWLAMPDFRRTGDYLRKKYNAAVEVMMNQDGTGFMVADRDYKRTTKNDLVYIENSPDYCLMDRSAGSLGTSGRVCNKSSRGMDGCEIMCCGRGYDTTRVNRMTKCECKFKWCCAVECRDCEETVDVHTCKLHKKPDWLDLT
Protein: Transcription factor BTF3 (Q5XGK2)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MKETIMNQEKLAKLQAQVRIGGKGTARRKKKVVHRTATADDKKLQFSLKKLGVNNISGIEEVNMFTNQGTVIHFNNPKVQASLAANTFTITGHAETKQLTEMLPSILNQLGADSLTSLRRLAEALPKQSMDGNAPLASGEDEDDEVPDLVENFDEASKNESV
Protein: Primary amine oxidase 1 (AtAO1) (EC 1.4.3.21) (O23349)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Oxidizes preferentially the aliphatic diamine putrescine with production of the corresponding aldehyde, ammonia and hydrogen peroxide. May be involved in the regulation of developmental programmed cell death (PCD) in both vascular tissue and the root cap. Required for jasmonic acid-(MeJA) mediated early protoxylem differentiation associated with putrescine levels reduction and H(2)O(2) accumulation in roots.
Subcellular location: Secreted {ECO:0000250|UniProtKB:H2A0M3}.
Interaction partners:
- Tyrosine decarboxylase 2
- Polyamine oxidase 1
- Probable polyamine oxidase 5
- Phenylacetaldehyde synthase
- Precursor of CEP12
- Tyrosine aminotransferase
- Probable aminotransferase TAT2
- Probable aminotransferase TAT4
- Tyrosine transaminase family protein
- Probable aminotransferase TAT1
Sequence:
MNTSILAILFLIQCVFTLGLHFHPLDPLTPQEINKTSFIVKKSHLGNLKDLTFHYLDLEEPNKSHVLQWLSPNPSKKPPPPRRRSFVVVRAGGQTYELIIDLTTSKIASSRIYTGHGFPSFTFIELFKASKLPLTYPPFKKSILDRSLNISEVSCIPFTVGWYGETTTRRELKASCFYRDGSVNVFTRPIEGITVTIDVDSMQVIKYSDRFRKPIPDKEGNDFRTKHRPFPFFCNVSDTGFKILGNRVKWANWKFHVGFTARAGVTISTASVLDPRTKRFRRVMYRGHVSETFVPYMDPTYEWYYRTFMDIGEFGFGRSAVNLQPLIDCPQNAAFLDGHVAGPDGTAQKMTNVMCVFEKNGYGASFRHTEINVPGQVITSGEAEISLVVRMVATLGNYDYIVDWEFKKNGAIRVGVDLTGVLEVKATSYTSNDQITENVYGTLVAKNTIAVNHDHYLTYYLDLDVDGNGNSLVKAKLKTVRVTEVNKTSSRRKSYWTVVKETAKTEADGRVRLGSDPVELLIVNPNKKTKIGNTVGYRLIPEHLQATSLLTDDDYPELRAGYTKYPVWVTAYDRSERWAGGFYSDRSRGDDGLAVWSSRNREIENKDIVMWYNVGFHHIPYQEDFPVMPTLHGGFTLRPSNFFDNDPLIG
Protein: Putative alpha-xylosidase 2 (EC 3.2.1.177) (F4J6T7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000250}. Secreted, extracellular space, apoplast {ECO:0000250}.
Interaction partners:
- Beta-D-xylosidase 3
- Beta-D-xylosidase 4
- Endo-1,4-beta-xylanase 2
- Putative mannan endo-1,4-beta-mannosidase P
- Beta-glucosidase 44
- (R)-mandelonitrile lyase-like (Hydroxynitrile lyase-like) ((R)-oxynitrilase-like)
- Protein trichome birefringence-like 32
- Glucosidase 2 subunit beta
- Expressed protein
Sequence:
MASCLSLLVAIILCFSSLQCSNAIGKGYRLISMEKSPDDGSFIGYLQVKQSNKIYGSDITILRLFINYRTDHRLRVHITDAKKQRWEVPYNLLRREQPPNVIGKSRKSPVTVQEISGPELILIFTVDPFSFAVRRRSNGETIFNTSSSDESFGEMVFKDQYLEISTSLPKDASLYGFGENSQANGIKLVPNEPYTLFTEDVSAFNLNTDLYGSHPVYMDLRNVSGKAYAHSVLLLNSHGMDVFYRGDSLTYKVIGGVFDFYFFAGPSPLNVVDQYTSLIGRPAPMPYWSLGFHQCRWGYRNVSVVKDVVDNYQKAKIPLDVIWNDADYMDGYKDFTLDLVNFPHAKLLSFLDRIHKMGMKYVVIKDPGIGVNASYGVYQRGMASDVFIKYEGKPFLAQVWPGPVYFPDFLNPKTVSWWGDEIRRFHELVPIDGLWIDMNEINATGHKASLGFKTIPTSAYHYNGVREYDAHSIYGFSEAIATHKALLAVQGKRPFILSRSTFVGSGQYAAHWTGDNQGTWQSLQVSISTMLNFGIFGVPMVGSDICGFFPPTPEELCNRWIEVGAFYPFSRDHADYYAPRKELYQWGTVAESARNALGMRYKLLPFLYTLNYEAHMSGAPIARPLFFSFPEFTECYGLSKQFLLGSSLMISPVLEQGKTQVEALFPPGSWYHMFDMTQVVVSKNGRLFTLPAPFNVVNVHLYQNAILPMQQVVAFPAGASEGYASGKLFLDDDELPEMKLGNGKSTYIDFYASVGNESVKIWSQVKEGQFALSQGLVIEKVIVLGLKGTWKVSEILLNGSSISNETKTIEVSSKEQMYVVGSEDEGESKSFMVELKGLEMLVGKDFNISWKMASTNVLSMAGNEVIAR
Protein: Zinc finger FYVE domain protein, putative (DUF1666) (Q9S7U2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGIVTTKTKTYTTTNFDFSNKGFGVGGLKQFVYGNTFIVLDAFWVSFSNLFRVNPDKETSLVLFEKQNTKDSSVFGDHQDQNQICGTQDDDQMESSLVSISKRCEFYSDNKSIVGFVEEPKAFSFKFHEYSAITVQEEEKKKMVSFSDEKTSSMVLEKSESDGFMKEHVKEEMLVYEFMSCGVLKESLVHENLVGGEDNLFDDDDGFIELNPSLQISNFAYGEEEEEEFIHREEEMKMGFDEQEEVYDEFDDGSDSDDDEFEHSDVIEKLKTELRTARTGGLCTILEESETPLQELKPLKIEPKPDQHKDRIAEIHKVYKNYAVKMRKLDVIDSQTMHSISLLKLKDSSKPSRNTDKPPKSSLHQNIWPFKKHTLECDPSERLVKEASRDFETVYVGQVCLSWEMLRWQYDKVLEFDSQVTTYQYNLVAGEFQLFQVLLQRFVENEPFQNSSRVETYLKNRRHFQNFLQIPLVRDDRSSKKKCRYEGEFAVKTEMLREIIRESMSVFWEFLCADKDEFTSMMKVSHQTQVSPQDSLDLELLTDIRTHLQKKEKKLKEIQRSQSCIVKKLKKNESKSSIGVKDELLIAKIELRLVSRVMYMSKLTTEKLHWCQEKLEKISFNGRKIHMEPYFSLLPC
Protein: Cellulose/chitin binding protein Rv1987 (Carbohydrate binding protein) (CBP) (P9WLQ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Secreted {ECO:0000269|PubMed:37879252}. Secreted, cell wall {ECO:0000269|PubMed:33469941, ECO:0000269|PubMed:37879252}. Cell membrane {ECO:0000269|PubMed:33469941, ECO:0000269|PubMed:37879252}.
Interaction partners:
Sequence:
MAGLNIYVRRWRTALHATVSALIVAILGLAITPVASAATARATLSVTSTWQTGFIARFTITNSSTAPLTDWKLEFDLPAGESVLHTWNSTVARSGTHYVLSPANWNRIIAPGGSATGGLRGGLTGSYSPPSSCLLNGQYPCT
Protein: Vacuolar protein sorting-associated protein 9A (OsVPS9A) (Protein GLUTELIN PRECURSOR ACCUMULATION 2) (Q10NQ3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as guanine nucleotide exchange factor (GEF) for Rab small GTPases. Activates specifically RAB5A protein (Probable). Functions cooperatively with RAB5A to regulate post-Golgi dense vesicle-mediated transport of storage proteins to the type II protein bodies (PBII) protein storage vacuoles in developing endosperm.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24488962}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24488962}. Prevacuolar compartment {ECO:0000269|PubMed:24488962}. Note=Expressed in trans-Golgi network and prevacuolar compartment when recruited by GPA3. {ECO:0000269|PubMed:24488962}.
Interaction partners:
- Ras-related protein Rab5A
- Os03g0666500 protein
- Os06g0687100 protein
- Os03g0151900 protein
- Protein GLUTELIN PRECURSOR ACCUMULATION 3
- Os10g0441800 protein
- Ras-related protein Rab-21
- Os01g0314700 protein
- Vacuolar protein sorting-associated protein 29
- Kinesin-like protein KIN-14I
Sequence:
MDGGGGGDAFGSATAPLAWHDFLERMRQPSAADFVKSIKGFIVTFSNRAPDPEHDSAAVQEFLENMEGAFRAHTPWAGSSEEELESAGEGLEKYVMTKLFNRVFASVPEDVKSDEELFEKMSLLQQFIRPENLDIKPEYQSETSWLLAQKELQKINMYKAPRDKLACILNCCKVINNLLLNASIVSNENPPGADEFLPVLIYVTIKANPPQLHSNLLYIQRYRRQSRLVSEAQYFFTNILSAESFIWNIDGESLSMDERDFQKKMDLARERMLGLSASSENQDNQNNLDVREQKSQTLKASRDSDVNLSLKDNFQGPGLEMRRDSDASSNPVERVQSISDLEKKGAAELLKDDDLNKKIQEYPFLFARSGDLTVADVENLLNSYKQLVLKYVALSQGMGINLENPPVQSMQTVSDLVESEEPKNVKNAVNFSEGSSKTSDDIKNDTLYSEVDNTGTQQTAVDPSYQKAQQDEASDQPEHA
Protein: Protein male abnormal 21 (Q20054)
Organism: Caenorhabditis elegans
Function: Acts in a cell autonomous fashion to specify the properties of the sensory ray and non-autonomously in the choice of hypodermal versus neuroblast cell fate.
Interaction partners:
- Paired box protein 6 homolog
- Protein dbl-1
- Uncharacterized protein
- Putative neurobeachin homolog
- Uncharacterized protein W02B3.4
Sequence:
MLGHNQNVVYQVNNYFNEKVQHRKVRVTKTVQRIAKVVQEILKEVEAQEPRFINTLSETTTGRFDGIVVHSPSEYEAVLYLNQMGVFNFVDDGTIQGCAVLKLSDGRKRSMSLWVEFITASGYLSARKIRHRFQNIVAQVLQTPQFSDYCKLLQDNTDVRVRVDDKYTVQITCAFRCNGIWPRSASHWPIAGLPWPNAALANQTKAEGFDLTSRETAITQQNNPNKQASSMEADAWAMKMHGAENMLLTGGRRKTLSILKCLRDAHMDFPGTPVTNYILKTLVLYECEKHCSEYEWEDPNIGDRLVGILLQLVSCLQCRRCAHYFLPSLDLLRSKPVHSIEHSAQLAWHLVRKLMIDPNALQSL
Protein: Lysozyme C-2 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (Lysozyme C type M) (P08905)
Organism: Mus musculus (Mouse)
Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz2 is active against a range of Gram-positive and Gram-negative bacteria. More effective than Lyz1 in killing Gram-negative bacteria. Lyz1 and Lyz2 are equally effective in killing Gram-positive bacteria.
Subcellular location: Secreted.
Interaction partners:
- Lysozyme C-1
- Adhesion G protein-coupled receptor E1
- Macrophage colony-stimulating factor 1 receptor
- TYRO protein tyrosine kinase-binding protein
- Low affinity immunoglobulin gamma Fc region receptor III
- Receptor-type tyrosine-protein phosphatase C
- Integrin alpha-X
- Complement C1q subcomponent subunit A
- Integrin alpha-M
- C-C motif chemokine 6
Sequence:
MKTLLTLGLLLLSVTAQAKVYERCEFARTLKRNGMAGYYGVSLADWVCLAQHESNYNTRATNYNRGDQSTDYGIFQINSRYWCNDGKTPRAVNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLSQYIRNCGV
Protein: Histone-lysine N-methyltransferase, H3 lysine-36 specific (EC 2.1.1.359) (Lysine N-methyltransferase 3) (SET domain-containing protein 2) (O14026)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3 (By similarity). Involved in transcription elongation as well as in transcription repression.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit rpb1
- Histone H3.1/H3.2
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Chromatin modification-related protein eaf3
- Histone H4
- SET domain and MYND-type zinc finger protein 6
- Histone-lysine N-methyltransferase set9
- Transcription elongation factor spt6
- Histone-lysine N-methyltransferase, H3 lysine-9 specific
- DNA-directed RNA polymerase II subunit RPB3
Sequence:
MQTASSLSVLTPLNEENVDRKSSWSKDTIAVQAVGSSPSSSSSHDFESKEDAEGMNKDESAPSPSTSSPSSASSRSQSKYVRKEALPPQLFHHLDSAKDKALTTFEEIQECQYASANIGKPPENEAMICDCRPHWVDGVNVACGHGSNCINRMTSIECTDEDNVCGPSCQNQRFQRHEFAKVDVFLTEKKGFGLRADANLPKDTFVYEYIGEVIPEQKFRKRMRQYDSEGIKHFYFMMLQKGEYIDATKRGSLARFCNHSCRPNCYVDKWMVGDKLRMGIFCKRDIIRGEELTFDYNVDRYGAQAQPCYCGEPCCVGYIGGKTQTEAQSKLPENVREALGIEDEEDSWENITARRQRRKKGIDETSKIIEEVQPTPLTSESATKVIGVLLQTKDDLLTRKLMERIFLTSDPSVCRSIIALRGYNIFGLMLKKFSIDIEFILRSIKTMLSWPRLTRNKIQDSNIEPVVQEFCDHENEEVKDHAKTLLKEWESLEIAYRIPRRKPGQVAPQSTNAEPSNNQSNPPLRDQEPQRGDKGDIKSAINNSTEDLSKKHPALHSSRPSDSRSRSKFGNDYQSHSKHNLFRKNSFPKRRRLSNSDTPSETTTPNNEQEQVSNQANKVDLNKIISAAMESVNQKNVLKAQKEEEERIAQQKREEKRRLAYEESLKRHAKKLHEKKTKSSQDATIDHHLTSHSPESIAFKAVLAKFFANKTARYQEKLGKAEFKLRVKKMTEIILKKHIQLVLSKKEKALPDELSDSQQRKLRVWAFRYLDTVVSRSGTATTTPTDSPSIGESPKKAA
Protein: Insulin-degrading enzyme (EC 3.4.24.56) (Insulin protease) (Insulinase) (Insulysin) (Q9JHR7)
Organism: Mus musculus (Mouse)
Function: Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling. Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (By similarity). Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP. Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia. Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (By similarity). Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (By similarity). Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21576244, ECO:0000269|PubMed:9830016}. Cell membrane {ECO:0000269|PubMed:21576244}. Secreted {ECO:0000269|PubMed:21576244, ECO:0000269|PubMed:9830016}.
Interaction partners:
- Amyloid-beta precursor protein
- Insulin-2
- Islet amyloid polypeptide
- Insulin-1
- Membrane metallo-endopeptidase-like 1
- Pro-glucagon
- Neprilysin
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Natriuretic peptides A
Sequence:
MRNGLVWLLHPALPGTLRSILGARPPPAKRLCGFPKQTYSTMSNPAIQRIEDQIVKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIPGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLLDASCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVREELLKFHSTYYSSNLMAICVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLRQLYKIVPIKDIRNLYVTFPIPDLQQYYKSNPGYYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGKLHYYPLNGVLTAEYLLEEFRPDLIDMVLDKLRPENVRVAIVSKSFEGKTDRTEQWYGTQYKQEAIPEDVIQKWQNADLNGKFKLPTKNEFIPTNFEILSLEKDATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKRYNDKQPILLKKITEKMATFEIDKKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGVMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKAIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNYDRDNIEVAYLKTLTKDDIIRFYQEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPSQNDINLSEAPPLPQPEVIHNMTEFKRGLPLFPLVKPHINFMAAKL