wanglab/gogpt-training-data huggingface dataset:
Protein: Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p14ARF) (Q8N726)
Organism: Homo sapiens (Human)
Function: Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Plays a role in inhibiting ribosome biogenesis, perhaps by binding to the nucleolar localization sequence of transcription termination factor TTF1, and thereby preventing nucleolar localization of TTF1 (By similarity). Interacts with COMMD1 and promotes its 'Lys63'-linked polyubiquitination. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16173922, ECO:0000269|PubMed:18305112, ECO:0000269|PubMed:22094112, ECO:0000269|PubMed:27323397}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18305112, ECO:0000269|PubMed:27323397}.; SUBCELLULAR LOCATION: [Isoform smARF]: Mitochondrion {ECO:0000269|PubMed:16713577}.
Interaction partners:
Sequence:
MVRRFLVTLRIRRACGPPRVRVFVVHIPRLTGEWAAPGAPAAVALVLMLLRSQRLGQQPLPRRPGHDDGQRPSGGAAAAPRRGAQLRRPRHSHPTRARRCPGGLPGHAGGAAPGRGAAGRARCLGPSARGPG
Protein: L-rhamnose isomerase (RhamIso) (EC 5.3.1.14) (P32170)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the interconversion of L-rhamnose and L-rhamnulose. Can also catalyze the isomerization of L-lyxose to L-xylulose.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00541, ECO:0000305}.
Interaction partners:
- L-Rhamnulokinase
- L-rhamnose mutarotase
- Rhamnulose-1-phosphate aldolase
- HTH-type transcriptional activator RhaR
- L-rhamnose-proton symporter
- L-fucose isomerase
- HTH-type transcriptional activator RhaS
- L-rhamnonate dehydratase
- L-arabinose isomerase
- L-fuculokinase
Sequence:
MTTQLEQAWELAKQRFAAVGIDVEEALRQLDRLPVSMHCWQGDDVSGFENPEGSLTGGIQATGNYPGKARNASELRADLEQAMRLIPGPKRLNLHAIYLESDTPVSRDQIKPEHFKNWVEWAKANQLGLDFNPSCFSHPLSADGFTLSHADDSIRQFWIDHCKASRRVSAYFGEQLGTPSVMNIWIPDGMKDITVDRLAPRQRLLAALDEVISEKLNPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYVPQLLLHVSRPVRWDSDHVVLLDDETQAIASEIVRHDLFDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALLEPTAELRKLEAAGDYTARLALLEEQKSLPWQAVWEMYCQRHDTPAGSEWLESVRAYEKEILSRRG
Protein: RNA polymerase III subunit Rpc25 domain-containing protein (Q382L2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase III subunit RPC3
- DNA-dependent RNA polymerases, putative
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase II, putative
Sequence:
MSLFHSYAMRDVVEVEPVYLPDGEVKRQRNTTGEGSPDAQAYQCTVDDILMHRLTERYVGRIVPSLGLCVAIHEVAHYTSGIVRGSSASAWFTVQFRVCVFSPTPGARVRATIGAQTREGIFLSLDFFQFVFFVPGDQLIAPSFFDEGNQCWMLRVDDGTDEDAVNPYEKGDEVVVRVDRVIVRDPVDLHRAEGARGSTSNAMGNADGTRSATGGLKDSGREPQVEKWPMEVYGSFVGTGLGPVVWF
Protein: Bud emergence protein 1 (Suppressor of RHO3 protein 1) (P29366)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Serine/threonine-protein kinase STE20
- Cell division control protein 24
- Cell division control protein 42
- Serine/threonine-protein kinase CLA4
- Ras-related protein RSR1
- BEM1-interacting protein 1
- BEM1-interacting protein 2
- Protein STE5
- Exocyst complex component SEC15
- Exocyst complex component EXO70
Sequence:
MLKNFKLSKRDSNGSKGRITSADISTPSHDNGSVIKHIKTVPVRYLSSSSTPVKSQRDSSPKNRHNSKDITSPEKVIKAKYSYQAQTSKELSFMEGEFFYVSGDEKDWYKASNPSTGKEGVVPKTYFEVFDRTKPSSVNGSNSSSRKVTNDSLNMGSLYAIVLYDFKAEKADELTTYVGENLFICAHHNCEWFIAKPIGRLGGPGLVPVGFVSIIDIATGYATGNDVIEDIKSVNLPTVQEWKSNIARYKASNISLGSVEQQQQQSITKPQNKSAKLVDGELLVKASVESFGLEDEKYWFLVCCELSNGKTRQLKRYYQDFYDLQVQLLDAFPAEAGKLRDAGGQWSKRIMPYIPGPVPYVTNSITKKRKEDLNIYVADLVNLPDYISRSEMVHSLFVVLNNGFDREFERDENQNNIKTLQENDTATFATASQTSNFASTNQDNTLTGEDLKLNKKLSDLSLSGSKQAPAQSTSGLKTTKIKFYYKDDIFALMLKGDTTYKELRSKIAPRIDTDNFKLQTKLFDGSGEEIKTDSQVSNIIQAKLKISVHDI
Protein: Ovomucoid (Allergen Gal d I) (allergen Gal d 1) (P01005)
Organism: Gallus gallus (Chicken)
Function: Serine protease inhibitor. Inhibits trypsin.
Subcellular location: Secreted.
Interaction partners:
- Ovotransferrin
- Ovotransferrin
- Ovalbumin
- Ovotransferrin
- Uncharacterized protein.
- Ovostatin
- Ovalbumin-related protein X
- chymotrypsin
- Albumin
- Lysozyme C
Sequence:
MAMAGVFVLFSFVLCGFLPDAAFGAEVDCSRFPNATDKEGKDVLVCNKDLRPICGTDGVTYTNDCLLCAYSIEFGTNISKEHDGECKETVPMNCSSYANTTSEDGKVMVLCNRAFNPVCGTDGVTYDNECLLCAHKVEQGASVDKRHDGGCRKELAAVSVDCSEYPKPDCTAEDRPLCGSDNKTYGNKCNFCNAVVESNGTLTLSHFGKC
Protein: Berberine bridge enzyme-like 3 (AtBBE-like 3) (EC 1.1.1.-) (FAD-linked oxidoreductase) (EC 1.-.-.-) (Flavin-dependent oxidoreductase FOX1) (Q9FZC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavin-dependent oxidoreductase involved in the biosynthetic pathway to 4-hydroxyindole-3-carbonyl nitrile (4-OH-ICN), a cyanogenic metabolite required for inducible pathogen defense. Converts indole cyanohydrin into indole-3-carbonyl nitrile (ICN).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:21443605}. Cell membrane {ECO:0000269|PubMed:21443605}. Secreted, cell wall {ECO:0000250|UniProtKB:O64743}.
Interaction partners:
- Thioredoxin superfamily protein
- Cytochrome P450 71A12
- Xanthotoxin 5-hydroxylase CYP82C2
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Peroxidase 62
- Bifunctional dihydrocamalexate synthase/camalexin synthase
- Indoleacetaldoxime dehydratase
- Protein S40-4
Sequence:
MKEALFGLYLVLLVSGLEAAVTKPNSGNFIECLRYQASPENPITDAIFTVDNTTTFLSSYVSYTKNTRFSNPNNKNLLAIVVAKDVSHVQATVVCAKSNGIQIRIRSGGHDNEGLSYVSSVPFVILDMHKLRDITVDVSSKKAWVQAGATLGELYVKIDEASQTLAFPAGICATVGAGGHISGGGYGNLMRKFGTTVDHVIDAELVDVNGKLLNRSTMGEDLFWAIRGGGGASFGVILSWKINLVEVPKIFTVFQVNKTLEQGGTDVVYKWQLVANKFPDNLFLRAMPQVVNGTKHGERTIAIVFWAQFLGRTDELMEIMNQSFPELGLRREDCQEMSWLNTTLFWAMLPAGTPKTVLLGRPTDPVFFKSKSDYVKKPIPKEGLEKIWKTMLKFNNIVWLHFNPYGGMMDRIPSNATAFPHRKGNLFKVQYYTTWLDPNATESNLSIMKELYEVAEPYVSSNPREAFFNYRDIDIGSNPSGETDVDEAKIYGYKYFLGNLKRLMDVKAKSDPENFFKNEQSIPPLLSRVRRDDEL
Protein: Prolactin-releasing peptide C-RFamide (Q4U0U9)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MNNLARGKLSTDPPQQATYVYVPCRPSTMTPETTAGCPVTVRECVLGSRWLMAALTILLLLATKVTCVHSTTVEHDFHIVHNVDNRSPEIDPFWYVGRGVRPIGRFGKRQSGGGGSGGLRHPGAVVSTLEILLDIIRNQENIGKTLRGEDADWLP
Protein: Calcium/calmodulin-dependent protein kinase type II subunit beta (CaM kinase II subunit beta) (CaMK-II subunit beta) (EC 2.7.11.17) (P28652)
Organism: Mus musculus (Mouse)
Function: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Also regulates the migration of developing neurons. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity). Phosphorylates reticulophagy regulator RETREG1 at 'Thr-134' under endoplasmic reticulum stress conditions which enhances RETREG1 oligomerization and its membrane scission and reticulophagy activity (By similarity).
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Sarcoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Synapse {ECO:0000250|UniProtKB:P08413}.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Calmodulin-1
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
- 55 kDa erythrocyte membrane protein
- Disks large homolog 4
- Glutamate receptor 3
- Calcium/calmodulin-dependent protein kinase type 1G
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor 1
Sequence:
MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTKNSSAITSPKGSLPPAALEPQTTVIHNPVDGIKESSDSTNTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAPVAPLQ
Protein: Carboxynorspermidine/carboxyspermidine decarboxylase (CANS DC/CAS DC) (CANSDC/CASDC) (EC 4.1.1.96) (A8FNH9)
Organism: Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
Function: Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine in vitro. In vivo, responsible for synthesizing spermidine, but not sym-norspermidine.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MFYEKIQTPAYILEEDKLRKNCELLASVGEKSGAKVLLALKGFAFSGAMKIVGEYLKGCTCSGLWEAKFAKEYMDKEIHTYSPAFKEDEIGEIASLSHHIVFNSLAQFHKFQSKTQKNSLGLRCNVEFSLAPKELYNPCGRYSRLGIRAKDFENVDLNAIEGLHFHALCEESADALEAVLKVFKEKFGKWIGQMKWVNFGGGHHITKKGYDVEKLIALCKNFSDKYGVQVYLEPGEAVGWQTGNLVASVVDIIENEKQIAILDTSSEAHMPDTIIMPYTSEVLNARILATRENEKISDLKENEFAYLLTGNTCLAGDVMGEYAFDKKLKIGDKIVFLDQIHYTIVKNTTFNGIRLPNLMLLDHKNELQMIREFSYKDYSLRN
Protein: TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L (TAF5L) (PCAF-associated factor 65 beta) (PAF65-beta) (Q91WQ5)
Organism: Mus musculus (Mouse)
Function: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (By similarity). With TAF6L, acts as an epigenetic regulator essential for somatic reprogramming. Regulates target genes through H3K9ac deposition and MYC recruitment which trigger MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state.
Subcellular location: Nucleus {ECO:0000269|PubMed:31005419}.
Interaction partners:
- TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- Transcriptional adapter 3
- STAGA complex 65 subunit gamma
- Transcription factor SPT20 homolog
- SPT3, SAGA and STAGA complex component
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 6
- Transformation/transcription domain-associated protein
Sequence:
MKRVRTEQVQVAVSCYLKRRQYVDSEGPLKQGLRLSQTPEEMAANLTVQSESGCANAVSAAPCQAEPQQYEVQFGRLRSFLTDSDSQYSREVMPLLYPLFVYLHLNLVQSGPKSTVESFYSRFHGMFLQNASQKDVIEQLQTTQTIQDILSNFQLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLAVHIHLDVQPAKRTDYQLYASGGSSRTENSSLEPPEVPSPILQNEAALEVLQESIKRVKDGPPSLTTICFYAFYNTEQLLNTAEISSDSKLLAAGFDNSCIKLWSLRSKKLKSEPHHVDTSRIRLACDTLEEEENEEDNTGTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDVDISPFSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLSFSPNGKYLASAGEDQRLKLWDLASGTLFKELRGHTDSITSLAFSPDSGLIASASMDNSVRVWDIRSTCCNTPADGSSGELVGVYTGQMSNVLSVQFMACNLLLVTGITQENQEH
Protein: ATP synthase subunit a (ATP synthase F0 sector subunit a) (F-ATPase subunit 6) (P0AB98)
Organism: Escherichia coli (strain K12)
Function: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01393, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393, ECO:0000269|PubMed:15919996}.
Interaction partners:
- ATP synthase epsilon chain
- ATP synthase subunit c
- ATP synthase subunit beta
- ATP synthase subunit alpha
- ATP synthase gamma chain
- ATP synthase subunit delta
- ATP synthase subunit b
- ATP synthase protein I
- Cytochrome bo
- Inorganic pyrophosphatase
Sequence:
MASENMTPQDYIGHHLNNLQLDLRTFSLVDPQNPPATFWTINIDSMFFSVVLGLLFLVLFRSVAKKATSGVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPYIAEHVLGLPALRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH
Protein: Kinase D-interacting substrate 220 (A0A1Y7VNF8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGQQIEPLFQFSWLIVFLILLLCGGLGLVFAFTVDTNLAIAVSLSFLALLYIFFIVIYFGGRQEGESWNWAWALSTRLARHIGYLELLFKLMFVNPPELPEQTTKALPVRFLFTDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDSQGKKKWKKTCCLPSFIIFLFIVGCIIAGITLLAIFRVDPKHLTVNAILISIASIVGLAFVLNCRTWWQVLDSLLNSQRKRLHSAASKLHKLKSEGFMKVLKCEVELMARMAKTIDSFTQNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLRDSNINGHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDISCSEATGVQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQMQRTITRQMSFDLTKLLVTEDWFSDISPQTMRRLLNIVSVTGRLLRANQITFNWDRLASWINLTEQWPYRTSWLILYLGETEGIPDQMTLKTIYERISKNIPTTKDVEPLLEIDGDIRNFEVFLSSRTPVLVARDVKTFLPCTVNLDPKLREIIADVRAAREQINIGGLAYPPLPLHEAPPRPPSGYSQPASVCSSSASFNGPFPGGVVSPQPHSSYYSGLSGPQHPFYNRPFFAPYLYTPRYYPGGSQHLISRSSVKTSLPRDQNNGLASVPATGTSLLLSSMTVDIVCEKLRQIEGLDQGMLPQYCTTIKKANINGRVLAQCNIDELKKEMAMNFGDWHLFRSMVLEMRSVENQVVPEDPRFLNENSSAPVAHGESARRTSHSELPHTELSSQTPYTLNFSFEELNTLGLDEGAPRHSNLSWQEENAAPVLDRQRFRRSSLN
Protein: Twinfilin-1 (Protein A6) (Q91YR1)
Organism: Mus musculus (Mouse)
Function: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10669753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10669753}. Note=Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts.
Interaction partners:
- F-actin-capping protein subunit beta
- WD repeat-containing protein 82
- Plastin-1
- F-actin-capping protein subunit alpha-1
- Profilin-4
- Unconventional myosin-VIIa
- Glutaredoxin domain-containing cysteine-rich protein 2
- Radixin
- Fascin-2
- Unconventional myosin-Ic
Sequence:
MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVVGSCSPPSDSWEQDYDSFVLPLLEDKQPCYVLFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVSVDTKHQTLQGVAFPISRDAFQALEKLSKKQLNYVQLEIDIKNETIILANTENTELRDLPKRIPKDSARYHFFLYKHSHEGDYLESVVFIYSMPGYTCSIRERMLYSSCKSPLLEIVERQLQMDVIRKIEIDNGDELTADFLYDEVHPKQHAHKQSFAKPKGPAGKRGIRRLIRGPAEAEATTD
Protein: Transient receptor potential cation channel subfamily M member 8 (U3JD03)
Organism: Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLDSSNLLLAFAVVYCSSISSSTTLFQVSMGSMRHRRNGNFESSRLLYSSMSRSIDVACSDADLANFIQENFKKRECVFFTKDTKSMGNLCKCGYPENQHIEGTQVNTTEKWNYKKHTKELPTDAFGDIQFENLGKRGKYIRLSCDTDSETLYDLMTQHWHLKTPNLVISVTGGAKNFALKPRMRKIFSRLIYIAQSKGAWIFTGGTHYGLMKYIGEVVRDNTISRSSEENVVAIGIAAWGMISNRETLIRTADSDGSYLAHYIMDDLKRDPLYCLDNNHTHLLLVDNGTHGHPTIEAKVRTQLEKYISERVIPESNYGGKIPIVCFAQGGGKETLKSINVAIKSKIPCVVVEGSGRIADVIASLVEAEGTLASSCVKESLLRFLPRTISRLSEEETESWIKWIKEVLESPHLLTVIKIEEAGDEIVSNAISFALYKAFSTNEHDRDNWNGQLKLLLEWNQLDLASDEIFTNDRNWESADLQDVMFTALVKDRPKFVRLFLENGLNLRKFLTTEVLRELYTNNFSSLVFKNLQIAKNSYNDALLTFVWKMVEDFRRGFKRYYKNSKDEMEIELSEECPITRHPLQALFIWSVLQNKKELSKVIWEQTRGCTLAALGASKLLKSMAKVKNDINAAGESEELANEYETRAVELFTECYSNDEDLAEQLLTYSCEAWGGSNCLELAVEARDQQFIAQPGVQNFLSKQWYGEISRDTKNWKIILCLFFFPLIGCGFISFRKKPVEKTKKLFLYYVSFFTSPFVVFSWNVIFYIAFLLLFAYVLLMDFQKEPTALEIILYVLVFILLCDEVRQWYMNGSKYFSDLWNVMDTLAIFYFIAGIVFRLHSDESSWYSGRVIFCLDYIVFTLRLIHIFTVSRNLGPKIIMLQRMMIDVFFFLFLFAVWMVAFGVARQGILRKNEHRWEWIFRSVIYEPYLAMFGQYPDDIDGTTYNFDHCTFSGNESKPLCVELDANNQPRFPEWITIPLVCIYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQRFFLVQEYCSRLTIPFPFVIFAYIFMVMRKCFKCCCKKESKEPSVCCSRNEDNEILAWEAVMKENYLVKINTKASDSSEDQTNTKNISLVLEAKVS
Protein: Multimerin-1 (EMILIN-4) (Elastin microfibril interface located protein 4) (Elastin microfibril interfacer 4) (Endothelial cell multimerin) [Cleaved into: Platelet glycoprotein Ia*; 155 kDa platelet multimerin (p-155) (p155)] (Q13201)
Organism: Homo sapiens (Human)
Function: Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein.
Subcellular location: Secreted {ECO:0000269|PubMed:38237698, ECO:0000269|PubMed:39775168}. Note=O-fucosylation of Thr-216 and Thr-1055 is important for protein secretion. {ECO:0000269|PubMed:38237698, ECO:0000269|PubMed:39775168}.
Interaction partners:
- Coagulation factor V
- Vitronectin
- von Willebrand factor
Sequence:
MKGARLFVLLSSLWSGGIGLNNSKHSWTIPEDGNSQKTMPSASVPPNKIQSLQILPTTRVMSAEIATTPEARTSEDSLLKSTLPPSETSAPAEGVRNQTLTSTEKAEGVVKLQNLTLPTNASIKFNPGAESVVLSNSTLKFLQSFARKSNEQATSLNTVGGTGGIGGVGGTGGVGNRAPRETYLSRGDSSSSQRTDYQKSNFETTRGKNWCAYVHTRLSPTVILDNQVTYVPGGKGPCGWTGGSCPQRSQKISNPVYRMQHKIVTSLDWRCCPGYSGPKCQLRAQEQQSLIHTNQAESHTAVGRGVAEQQQQQGCGDPEVMQKMTDQVNYQAMKLTLLQKKIDNISLTVNDVRNTYSSLEGKVSEDKSREFQSLLKGLKSKSINVLIRDIVREQFKIFQNDMQETVAQLFKTVSSLSEDLESTRQIIQKVNESVVSIAAQQKFVLVQENRPTLTDIVELRNHIVNVRQEMTLTCEKPIKELEVKQTHLEGALEQEHSRSILYYESLNKTLSKLKEVHEQLLSTEQVSDQKNAPAAESVSNNVTEYMSTLHENIKKQSLMMLQMFEDLHIQESKINNLTVSLEMEKESLRGECEDMLSKCRNDFKFQLKDTEENLHVLNQTLAEVLFPMDNKMDKMSEQLNDLTYDMEILQPLLEQGASLRQTMTYEQPKEAIVIRKKIENLTSAVNSLNFIIKELTKRHNLLRNEVQGRDDALERRINEYALEMEDGLNKTMTIINNAIDFIQDNYALKETLSTIKDNSEIHHKCTSDMETILTFIPQFHRLNDSIQTLVNDNQRYNFVLQVAKTLAGIPRDEKLNQSNFQKMYQMFNETTSQVRKYQQNMSHLEEKLLLTTKISKNFETRLQDIESKVTQTLIPYYISVKKGSVVTNERDQALQLQVLNSRFKALEAKSIHLSINFFSLNKTLHEVLTMCHNASTSVSELNATIPKWIKHSLPDIQLLQKGLTEFVEPIIQIKTQAALSNLTCCIDRSLPGSLANVVKSQKQVKSLPKKINALKKPTVNLTTVLIGRTQRNTDNIIYPEEYSSCSRHPCQNGGTCINGRTSFTCACRHPFTGDNCTIKLVEENALAPDFSKGSYRYAPMVAFFASHTYGMTIPGPILFNNLDVNYGASYTPRTGKFRIPYLGVYVFKYTIESFSAHISGFLVVDGIDKLAFESENINSEIHCDRVLTGDALLELNYGQEVWLRLAKGTIPAKFPPVTTFSGYLLYRT
Protein: Glucan endo-1,3-beta-D-glucosidase (EC 3.2.1.39) (Major pollen allergen Ole e 9) (allergen Ole e 9) (Q94G86)
Organism: Olea europaea (Common olive)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAANVQTSSLLFLVFLLLQNFYSANSQSFLGVNYGQLSDNLPSLQATVNLLKSTTIQKVRLFGAEPAVIKAFANTGVEIVIGFDNGDIPTLASNPNVASQFVKSNVMSFYPASNIIAITVGNEVLTSGDQKLISQLLPAMQNVQNALNAASLGGKVKVSTVHAMAVLSQSYPPSSGVFNPGLGDTMKALLQFQSANDAPFMISPYPYFAYKNQPTPDTLAFCLFQPNAGQVDSGNGHKYTNMFDAQVDAVHSALNAMGFKDIEIVVAETGWPHGGDSNEVGPSLDNAKAYVGNLINHLKSKVGTPLMPGKSIDTYLFSLYDEDKKTGASSEKYFGLFKPDGSTTYDVGLLKNTQNPTTPATPTPTPKAAGSWCVPKPGVSDDQLTGNINYACGQGIDCGPIQPGGACFEPNTVKAHAAYVMNLYYQSAGRNSWNCDFSQTATLTNTNPSYGACNFPSGSN
Protein: Serglycin (Chondroitin sulfate proteoglycan core protein) (Cytolytic granule proteoglycan core protein) (PG19 core protein) (Proteoglycan 10K core protein) (Secretory granule proteoglycan core protein) (P04917)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization (By similarity).
Subcellular location: Cytoplasmic granule {ECO:0000250|UniProtKB:P10124}. Cytolytic granule {ECO:0000250|UniProtKB:P10124}. Secreted, extracellular space {ECO:0000250|UniProtKB:P10124}. Golgi apparatus {ECO:0000250|UniProtKB:P10124}. Note=Found in mast cell granules and in cytoplasmic granules of cytolytic T-lymphocytes from where it is secreted upon cell activation. Secreted constitutively by endothelial cells and macrophages. Located to Golgi apparatus during neutrophil differentiation (By similarity). {ECO:0000250|UniProtKB:P10124, ECO:0000250|UniProtKB:P13609}.
Interaction partners:
- CD44 antigen
- Perforin-1
- Mast cell carboxypeptidase A
Sequence:
MRQVPVGTRLVLALAFVLVWGSSVQGYPARRARYQWVRCKPDGIFANCIEEKGPRFDLIAEESNVGPPMTDPVLMRGFPNDFFPISDDYSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSGSLADMEWEYQPTDENNIVYFNYGPFDRMLTEQNQEQPGDFII
Protein: At2g46100 (Nuclear transport factor 2 (NTF2) family protein) (Q6ID84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVASLSFHSIATVNPIFSGDGGRSIFRTNRRFEATGVSCRGQNPTDEPQTSKGPEPDNVLLKIAWYGSELLGIAASVFRSPETSPIVTGFEVPVDCSGRAVRVAVVDSIKQDFKRSYFVTGNLTPEVYEEKCEFADPAGSFKGLARFKRNCTNFGSLIEKSNMKLMKWENFEDKGIGHWKFSCVMSFPWKPILSATGYTEYYFDTESGKICRHVEHWNVPKIALFKQLLRPSRGLVGTQN