wanglab/gogpt-training-data huggingface dataset:
Protein: CMRF35-like molecule 1 (CLM-1) (CD300 antigen-like family member F) (Immune receptor expressed on myeloid cells 1) (IREM-1) (Immunoglobulin superfamily member 13) (IgSF13) (NK inhibitory receptor) (CD antigen CD300f) (Q8TDQ1)
Organism: Homo sapiens (Human)
Function: Acts as an inhibitory receptor for myeloid cells and mast cells. Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells. Plays an important role in the maintenance of immune homeostasis, by promoting macrophage-mediated efferocytosis and by inhibiting dendritic cell-mediated efferocytosis (By similarity). Negatively regulates Fc epsilon receptor-dependent mast cell activation and allergic responses via binding to ceramide and sphingomyelin which act as ligands. May act as a coreceptor for interleukin 4 (IL-4). Associates with and regulates IL-4 receptor alpha-mediated responses by augmenting IL-4- and IL-13-induced signaling (By similarity). Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 and TRIF through activation of PTPN6/SHP-1 and PTPN11/SHP-2. Inhibits osteoclast formation. Induces macrophage cell death upon engagement (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- CMRF35-like molecule 7
- CMRF35-like molecule 6
- CMRF35-like molecule 8
- CMRF35-like molecule 5
- Triggering receptor expressed on myeloid cells 2
- Trem-like transcript 1 protein
Sequence:
MPLLTLYLLLFWLSGYSIVTQITGPTTVNGLERGSLTVQCVYRSGWETYLKWWCRGAIWRDCKILVKTSGSEQEVKRDRVSIKDNQKNRTFTVTMEDLMKTDADTYWCGIEKTGNDLGVTVQVTIDPAPVTQEETSSSPTLTGHHLDNRHKLLKLSVLLPLIFTILLLLLVAASLLAWRMMKYQQKAAGMSPEQVLQPLEGDLCYADLTLQLAGTSPQKATTKLSSAQVDQVEVEYVTMASLPKEDISYASLTLGAEDQEPTYCNMGHLSSHLPGRGPEEPTEYSTISRP
Protein: Mitochondrial processing peptidase, beta subunit, putative (EC 1.10.2.2) (Q57W51)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial processing peptidase alpha subunit, putative
- Cytochrome c1, heme protein, mitochondrial
- Reiske iron-sulfur protein, mitochondrial
- Mitochondrial processing peptidase alpha subunit, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Uncharacterized protein
- Electron transfer protein, putative
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
Sequence:
MSVSFSTLIQRSRPSSNHATTKLLSNVLAKIPPTTLSTVGSGVRVACEENPIASLATVGVWLDAGTRHEPAQYAGTARVLQKCGFLGTSNQTAAQIAAAVDELGGQLTANVGREHTHLYMRVAREDTERAVSLLADVVRNARLSDEDVEVAKQAVLRDQHDFEQRPDDICMDNLHRCAFDSTTHGPGTPLYGTEVGTTRLSNAQLREYRDKMLSAGRVVVVGSGAVNHTALERAATSAFGDLQKGTVTLAGVPEARFVGGEYKLWNLRYKTVHIGWAFETCGAACEDSLPLALACEVPGPFHRSQHELGQHAMHRVLKTFSSLDHSTPTNTHFNEKCIEIANPFLHQYKDTGLCGMYVVGRPAQAGPGDGTAMIEVFQYTIAEWCRICQKILHEQELAQAKVNLKSQLLFNMDGSSNSAEDIGRQVLHYGRRIPLEEMYARIDDVTPTNVQEVLQHYFYGRKPVYSYLGYCANIPGYDWTQHWSYKYWY
Protein: GH13165p (Radial spoke head protein 4a) (Q9W1D3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
- Radial spoke head protein 9 homolog
- AT19426p
- GH13213p
- Dynein, axonemal, intermediate chain 2, isoform C
- Uncharacterized protein, isoform B
- Zinc finger MYND domain-containing protein 10 homolog
- Spag1 axonemal dynein assembly factor
- Dynein axonemal assembly factor 5
- Dynein regulatory complex subunit 4
- AT09290p
Sequence:
MDRDSCQNFSLDSTSSSHFAPPPVCAPRRKKPEKPAAEEASPECSNVTSSSSSSTTTISIGAFDSQCNLHNARNPEAPNIGYELNVAKSILQKYSTLSGDNLFDHLSDIIKRVIDERPPNVIDFFEEFSRNVREQKFHLPERFPPSGVFDEVRSFRVAKKILQSMKLPYVVEGEDLMGEDLSVEDLRTNEDMRIVIDDSMRYFVTFNERVQQLQFYWTQCGFSISNDDIFQLASAMNRLQTHPSIMQCRFWGCINGLKASYYIVEASLTREEIASRLVMMEEEMRQKQIPFPMRKDREDKPPPAHIGPELTPGIYGWEEFPPEELEKMKPKAAPVPLVEEMELYDIPPEFIGKGCNRYSYFVVNSLFDDWIELPIVTPRQIVVSRQIKKFLTGDLEADVISYPCFPGKEKHYLRTLIGRITAGTYIAPVGYYRRMTKKEQRMFDGEEEEEGEEEEEEEEEEEFNEGEEEQIEDNDVMLLKNEKYEAEPLGSLATPVAWVHVRSNILNQQGRVVWYDEEKARKEREKALALYLKMQMLGEMEEEVEEEEDEEEGEEEGEEEGMIEGFNQPELGPSILSSCANDMNPEVPVSWLARMTSKYTNQKERMLVMQSNVWPGAYTFIFEKTCESIYLGWGHKYYARNIPFKHLPMVQEEFPHNPEDFVEANDPTVEEEEAYKAWLLRKQQKAEYVAEDIEDYDDDEFADQYDDD
Protein: GATA transcription factor 24 (Protein TIFY 2B) (ZIM-like 1 protein) (Q8GXL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein TIFY 8
- GATA transcription factor 15
- GATA transcription factor 14
- Protein TIFY 4A
- Alcohol dehydrogenase transcription factor Myb/SANT-like family protein
- Protein TIFY 4B
- Putative receptor-like protein kinase At2g30940
- GATA transcription factor 21
- GATA transcription factor 2
- F28K20.8 protein
Sequence:
MDDLHGRNGRMHIGVAQNPMHVQYEDHGLHHIDNENSMMDDHADGGMDEGVETDIPSHPGNSADNRGEVVDRGIENGDQLTLSFQGQVYVFDRVSPEKVQAVLLLLGGREVPHTLPTTLGSPHQNNRVLGLSGTPQRLSVPQRLASLLRFREKRKGRNFDKTIRYTVRKEVALRMQRKKGQFTSAKSSNDDSGSTGSDWGSNQSWAVEGTETQKPEVLCRHCGTSEKSTPMMRRGPDGPRTLCNACGLMWANKGTLRDLSKVPPPQTPQHLSLNKNEDANLEADQMMEVTGDISNTQ
Protein: DNA topoisomerase (EC 5.6.2.1) (Q384B1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RecQ mediated genome instability protein 1 OB-fold domain-containing protein
- DNA topoisomerase
- DNA 3'-5' helicase
- DNA 3'-5' helicase
- Crossover junction endonuclease MUS81
- DNA repair protein, putative
- DNA repair protein RAD50
- DNA topoisomerase 2
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Elongation factor 2
Sequence:
MVQTVLMVAEKPSIAESIAHHLSNGRTAKHSRALPVFEYDGYFQGAPAHFRVTSTTGHIFSCDFTPQYQSWDRTDEESLFGAPVVWREESGRVSRHLEHEAKGCATLVLWLDCDREGENICFEVMQVVSRSIHDIRCIWRAKFSAITREAITEAFVNLGKPNKNLSDAVSCRQELDLKVGVVFTRYQTKYFQGKYGNLDASVVSYGPCQTPTLAFCVQRHDEILNFKPENYWKLVPTCNRYGSPITFEWARGRVFDELIARLLHQRVSRSKVAKVVDVSVGADTRARPTALNTVELMKIASKFLGIGPHHAMQIAENLYISGYISYPRTESTAYPVSFDLKAALATQQGHPVWGEYVQELLKGRYTRPKAGKDAGDHPPITPMRAATAGELSSDSWRLYEYITRHFIATVSPDCKLSRTKLVLELSGELFTFTGKVVVDPGFTTILAHLAVKDDKVPTNIEVGSDFPINDVRLQAGQTQAPGYLTEADLIGLMEKNGIGTDASISQHVNNIVERGYCAVKPGRVMEPTKLGVVLIHGIKSIDPELVLPLVRSKVEEYVTCIAEGQARLDEVLSSVLDLFFGKFRYFKENIERFDALMGASFSPLTSSGKPITRCGNCMRYLKHLEARPQRLYCAYCEVTYALPQGGTIKQYSNYKCPLDNFELVICHVEGGKSFPICPNCYNNPPFPDARVQGGRQLMACDECKHPTCYHSLATNYVADCVDPRCDGCMAFVPRTSGKWKICCNHCTMMILLPPTAQRVYVSSEECPECGAMMVDLQFPEGKSPLPNRKDRIVSCVFCDPALSNNVSEVRGKLGNFSRRGGGGKGRGRGGRGRGRGRGYRN
Protein: SIGIRR protein (Single Ig IL-1-related receptor precursor) (Single immunoglobulin and toll-interleukin 1 receptor (TIR) domain) (cDNA, clone cssl:d0148) (A4JYJ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Plakophilin 3a
- Myeloid differentiation primary response protein MyD88
Sequence:
MWRCHFILFLTCLANSHSADSLCGSSPEFKHDRTQSVSSTLGHSVVLTCTASMGLNGTDLDCEDHPEWMKDGLQLTNLTIYPQNSKEWYTDDEGRMESSELTLTLRDRADFGVYYCIVRNSTAQFTVKEYKSPSHTGAVVASVVMLVVLALAAVVYSKCRLNFKLWYKNIYGEYEINDGKMYDAYISYVNNENDRKFVNFILKPHLENKYSHKLLLNDTNILPGAEPSAELLMNISRCRRLIVVLSQSYLEQEWCTTNFRQGLWHLIELSRKPIFIIFQSQQKQISQDISQQLRQHQPCITMITWGAHSMTPSSGFWKELALVMPRKVTFHRESAGDPQTLLQGDKAPMLTQQPDYLDCRLDPDPAGDLGLRLPIYKTLPTKAPVLPAAPGPTGEAKPSEIDVSDLGLRNYSARRDFYCLVTDDDL
Protein: Far upstream element-binding protein 2 (FUSE-binding protein 2) (KH type-splicing regulatory protein) (KSRP) (p75) (Q92945)
Organism: Homo sapiens (Human)
Function: Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:19198587}. Cytoplasm {ECO:0000269|PubMed:19198587}. Note=A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites. {ECO:0000250}.
Interaction partners:
- Ribonuclease 3
- Endoribonuclease Dicer
- Poly
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein F
- Heterogeneous nuclear ribonucleoprotein H
- 14-3-3 protein zeta/delta
- Heterogeneous nuclear ribonucleoprotein D0
- ELAV-like protein 1
- KH domain-containing, RNA-binding, signal transduction-associated protein 1
Sequence:
MSDYSTGGPPPGPPPPAGGGGGAGGAGGGPPPGPPGAGDRGGGGPGGGGPGGGSAGGPSQPPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNSTPDFGFGGQKRQLEDGDQPESKKLASQGDSISSQLGPIHPPPRTSMTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRIGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDGTGPEKIAHIMGPPDRCEHAARIINDLLQSLRSGPPGPPGGPGMPPGGRGRGRGQGNWGPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQLPPNGDPNFKLFIIRGSPQQIDHAKQLIEEKIEGPLCPVGPGPGGPGPAGPMGPFNPGPFNQGPPGAPPHAGGPPPHQYPPQGWGNTYPQWQPPAPHDPSKAAAAAADPNAAWAAYYSHYYQQPPGPVPGPAPAPAAPPAQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAQVATGGGPGAPPGSQPDYSAAWAEYYRQQAAYYGQTPGPGGPQPPPTQQGQQQAQ
Protein: 5,6-dimethylbenzimidazole synthase (DMB synthase) (EC 1.13.11.79) (Q2RNG5)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: Involved in the biosynthesis of cobalamin (vitamin B12). Catalyzes the oxidative fragmentation and contraction of the isoalloxazine heterocycle and the cleavage of the ribityl tail of FMNH(2) to form 5,6-dimethylbenzimidazole (DMB) and D-erythrose 4-phosphate (E4P). NAD(P)H is only required initially to reduce FMN and oxygen drives the oxidative fragmentation.
Interaction partners:
- Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
- Cobyrinate a,c-diamide synthase
- Bifunctional adenosylcobalamin biosynthesis protein
- Precorrin-6Y C5,15-methyltransferase
- threonine-phosphate decarboxylase
Sequence:
MRTGPLFDPSFRDGLDALFQWRRDVRHFRKDPIDEETVARLLACADLAPSVGNSQPWRFVRVDDGARRGVIIDDFTRCNAAARALQPEERQDAYARLKLEGLREAPLQLAVFCDEATDQGHGLGQATMPETRRYSVVMAIHTLWLAARARGLGVGWVSVLDPQTVTAALDVPAEWAFVAYLCIGWPREEHPIPELERLGWQSRRPHPVVRR
Protein: O-glucosyltransferase rumi (EC 2.4.1.-) (Q8T045)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein O-glucosyltransferase. Catalyzes the reaction that attaches glucose through an O-glycosidic linkage to a conserved serine residue found in the consensus sequence C-X-S-X-[PA]-C in epidermal growth factor-like repeats. Regulates Notch signaling by glucosylating Notch in the ER, glucosylation is required for the correct folding and cleavage of Notch.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:18243100}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 1
- FI12101p)
- Xyloside xylosyltransferase 1
Sequence:
MLINHLIVVLLISLVGTGGAEDDGLCSADQKSCAQSEPDQINEDEFSFKIRRQIEKANADYKPCSSDPQDSDCSCHANVLKRDLAPYKSTGVTRQMIESSARYGTKYKIYGHRLYRDANCMFPARCEGIEHFLLPLVATLPDMDLIINTRDYPQLNAAWGNAAGGPVFSFSKTKEYRDIMYPAWTFWAGGPATKLHPRGIGRWDQMREKLEKRAAAIPWSQKRSLGFFRGSRTSDERDSLILLSRRNPELVEAQYTKNQGWKSPKDTLDAPAADEVSFEDHCKYKYLFNFRGVAASFRLKHLFLCKSLVFHVGDEWQEFFYDQLKPWVHYVPLKSYPSQQEYEHILSFFKKNDALAQEIAQRGYDFIWEHLRMKDIKCYWRKLLKRYVKLLQYEVKPEDQLIYIGPKKDEL
Protein: Prominin-1 (Antigen AC133 homolog) (Prominin-like protein 1) (CD antigen CD133) (O54990)
Organism: Mus musculus (Mouse)
Function: May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner.
Subcellular location: Apical cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment. Endoplasmic reticulum {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine.
Interaction partners:
- CD44 antigen
- Signal transducer CD24
- Hematopoietic progenitor cell antigen CD34
- Epithelial cell adhesion molecule
- Transcription factor SOX-2
- POU domain, class 5, transcription factor 1
- Aldehyde dehydrogenase 1A1
- Homeobox protein NANOG
- Nestin
- Aldehyde dehydrogenase, dimeric NADP-preferring
Sequence:
MALVFSALLLLGLCGKISSEGQPAFHNTPGAMNYELPTTKYETQDTFNAGIVGPLYKMVHIFLSVVQPNDFPLDLIKKLIQNKKFDISVDSKEPEIIVLALKIALYEIGVLICAILGLLFIILMPLVGCFFCMCRCCNKCGGEMHQRQKQNAPCRRKCLGLSLLVICLLMSLGIIYGFVANQQTRTRIKGTQKLAKSNFRDFQTLLTETPKQIDYVVEQYTNTKNKAFSDLDGIGSVLGGRIKDQLKPKVTPVLEEIKAMATAIKQTKDALQNMSSSLKSLQDAATQLNTNLSSVRNSIENSLSSSDCTSDPASKICDSIRPSLSSLGSSLNSSQLPSVDRELNTVTEVDKTDLESLVKRGYTTIDEIPNTIQNQTVDVIKDVKNTLDSISSNIKDMSQSIPIEDMLLQVSHYLNNSNRYLNQELPKLEEYDSYWWLGGLIVCFLLTLIVTFFFLGLLCGVFGYDKHATPTRRGCVSNTGGIFLMAGVGFGFLFCWILMILVVLTFVVGANVEKLLCEPYENKKLLQVLDTPYLLKEQWQFYLSGMLFNNPDINMTFEQVYRDCKRGRGIYAAFQLENVVNVSDHFNIDQISENINTELENLNVNIDSIELLDNTGRKSLEDFAHSGIDTIDYSTYLKETEKSPTEVNLLTFASTLEAKANQLPEGKPKQAFLLDVQNIRAIHQHLLPPVQQSLNTLRQSVWTLQQTSNKLPEKVKKILASLDSVQHFLTNNVSLIVIGETKKFGKTILGYFEHYLHWVFYAITEKMTSCKPMATAMDSAVNGILCGYVADPLNLFWFGIGKATVLLLPAVIIAIKLAKYYRRMDSEDVYDDVETVPMKNLEIGSNGYHKDHLYGVHNPVMTSPSRY
Protein: Chemosensory protein A 98a (Q9VAT5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
Sequence:
MDAKIIILALVSLFYKANGAFYELSVADEEIFSSCPNPEPGTLDIHGLFDFSEFSTSLEADGLTVSGNQTLVWDIQRGDRVQLFIKLFYFDRGTWTSTAFSILSQDFCKTMYDKSNVLYEPWTGHVMNDVKDQCINAPGTKLILDTYFLSLSASVTVPLREGRYKTTIKFRAFDSKGTERPTSICCEVIGDVFKIRN
Protein: Acid sphingomyelinase-like phosphodiesterase 3b (ASM-like phosphodiesterase 3b) (EC 3.1.4.-) (Q92485)
Organism: Homo sapiens (Human)
Function: Lipid-modulating phosphodiesterase. Active on the surface of macrophages and dendritic cells and strongly influences macrophage lipid composition and membrane fluidity. Acts as a negative regulator of Toll-like receptor signaling (By similarity). Has in vitro phosphodiesterase activity, but the physiological substrate is unknown. Lacks activity with phosphocholine-containing lipids, but can cleave CDP-choline, and can release phosphate from ATP and ADP (in vitro) (By similarity).
Subcellular location: Secreted {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P58242}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P58242}.
Interaction partners:
Sequence:
MRLLAWLIFLANWGGARAEPGKFWHIADLHLDPDYKVSKDPFQVCPSAGSQPVPDAGPWGDYLCDSPWALINSSIYAMKEIEPEPDFILWTGDDTPHVPDEKLGEAAVLEIVERLTKLIREVFPDTKVYAALGNHDFHPKNQFPAGSNNIYNQIAELWKPWLSNESIALFKKGAFYCEKLPGPSGAGRIVVLNTNLYYTSNALTADMADPGQQFQWLEDVLTDASKAGDMVYIVGHVPPGFFEKTQNKAWFREGFNEKYLKVVRKHHRVIAGQFFGHHHTDSFRMLYDDAGVPISAMFITPGVTPWKTTLPGVVNGANNPAIRVFEYDRATLSLKDMVTYFMNLSQANAQGTPRWELEYQLTEAYGVPDASAHSMHTVLDRIAGDQSTLQRYYVYNSVSYSAGVCDEACSMQHVCAMRQVDIDAYTTCLYASGTTPVPQLPLLLMALLGLCTLVL
Protein: Heat shock protein beta-6 (HspB6) (Heat shock 20 kDa-like protein p20) (Hsp20) (P97541)
Organism: Rattus norvegicus (Rat)
Function: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (By similarity). Seems to have versatile functions in various biological processes (By similarity). Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility (By similarity). May regulate myocardial angiogenesis implicating KDR (By similarity). Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14558}. Nucleus {ECO:0000250|UniProtKB:O14558}. Secreted {ECO:0000250|UniProtKB:O14558}. Note=Translocates to nuclear foci during heat shock. {ECO:0000250|UniProtKB:O14558}.
Interaction partners:
- Bcl2-associated athanogene 3.
- Heat shock 70 kDa protein 4
- RAC-alpha serine/threonine-protein kinase
- Heat shock protein beta-8
Sequence:
MEIRVPVQPSWLRRASAPLPGFSTPGRLFDQRFGEGLLEAELASLCPAAIAPYYLRAPSVALPTAQVPTDPGYFSVLLDVKHFSPEEISVKVVGDHVEVHARHEERPDEHGFIAREFHRRYRLPPGVDPAAVTSALSPEGVLSIQATPASAQASLPSPPAAK
Protein: Disks large-associated protein 3 (DAP-3) (PSD-95/SAP90-binding protein 3) (SAP90/PSD-95-associated protein 3) (SAPAP3) (Q6PFD5)
Organism: Mus musculus (Mouse)
Function: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15024750}; Peripheral membrane protein {ECO:0000269|PubMed:15024750}. Postsynaptic density {ECO:0000269|PubMed:15024750}. Synapse {ECO:0000269|PubMed:15024750}. Note=Postsynaptic density of neuronal cells.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 3
- Disks large homolog 4
- Disks large-associated protein 2
- SLIT and NTRK-like protein 5
- Disks large homolog 2
- SH3 and multiple ankyrin repeat domains protein 1
- Disks large homolog 3
- Ras/Rap GTPase-activating protein SynGAP
- SH3 and multiple ankyrin repeat domains protein 2
- Excitatory amino acid transporter 3
Sequence:
MRGYHGDRGSHPRPARFADQQHMDVGPAARAPYLLGSREAFSTEPRFCAPRAGLGHLSPEGPLSLSEGPSSVGPEGGPGGVGAGGGSSTFPRMYPGQGPFDTCEDCVGHPQGKGATRLPPTLLDQFEKQLPVQQDGFHTLPYQRGPAGPGPGPGSGAAPEARSESPSRIRHLVHSVQKLFAKSHSLEAPGKRDYNGPKADGRGSSGGDSYSGPGSGGTPTSHHHHHHHHHHHHQSRHGKRSKSKDRKGDGRHQTKATGWWSSDDNLDSDSGFLGGRPPGEPGGPFCLDAPDGSYRDLSFKGRSGGSEGRCLACTGMSMSLDGQSVKRSAWHTMMVSQGRDGYPGAGPGKGLLGPETKAKARTYHYLQVPQDDWGGYPTGGKDGEIPCRRMRSGSYIKAMGDEESGDSDGSPKTSPKALARRFASRRSSSVDTARINCCVPPRIHPRSSIPGYSRSLTTGQLSEEFNQQLEAVCGSVFGELESQAVDALDLPGCFRMRSHSYLRAIQAGCSQDDDCLPLLAAPASVSGRPGSSFNFRKAPPPIPPGSQAPPRISITAQSSTDSAHESFTAAEGPARRCSSADGLDGPTMGARTLELAPVPPRASPKPPTLIIKTIPGREELRSLARQRKWRPSIGVQVETISDSDTENRSRREFHSIGVQVEEDKRRARFKRSNSVTAGVQADLELEGLAGLATVATEDKALQFGRSFQRHASEPQPGPRAPTYSVFRTVHTQGQWAYREGYPLPYEPPATDGSPGPTPVPAPGPGSGRRDSWMERGSRSLPDSGRTSPCPRDGEWFIKMLRAEVEKLEHWCQQMEREAEDYELPEEILEKIRSAVGSTQLLLSQKVQQFFRLCQQSLDPTAFPVPTFQDLAGFWDLLQLSIEDVTLKFLELQQLKANSWKLLEPKEEKKVPPPIPKKPSRGRGVPVKERSLDSVDRQRQEARKRLLAAKRAASFRHSSATESADSIEIYIPEAQTRL
Protein: Calcitonin/calcitonin-related polypeptide, alpha (F1QIK6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVMLKISAFLVAYALIICQMYSSNAAPARPALESSPDRTTLSDYEARRLLQAIVKEFMQMTAEDMEQQATEENSLGRAVSKRCSSLSTCVLGKLSQELHKLQTYPRTNVGAGTPGKKRSLEGSDGYGEALGRV
Protein: WIZ zinc finger (A0A669KBH9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASTAQCRVTKAESKAAAGPRAGGARERAPAGAPPPSPPSPGPAAPPAPPPPPPPPPPPPPPPPPPPPPRDGPKAEPEPGPGPASAPAPGLGSEENAMVAMDLGSPSLPKKSLPVPGALEQVASRLSSKVAAEVPHGSKQELQDLKAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTLDSDGGRELDCQLCGAWFETRKGLSSHARAHLRHLGVSDPDAKGSPIDVLHGLIRRDGVQIRLPPRRGALAHPGRPPPTSAALSLLPPPPPAKKAKLKAAGMASPWGKQDLSAAAAAGIFWASDVEPSPLNLSSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP
Protein: AE binding protein 2 (A0A669KBL4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASFASQGGLARHVPTHFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRPHDFFDAQTLDAIRHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEDSGKIKLLLHWMPEDILPDVWVNESERHQLKTKVVHLSKLPKDTALLLDPNIYRLEN
Protein: RNA helicase (EC 3.6.4.13) (I1GWP1)
Organism: Brachypodium distachyon (Purple false brome) (Trachynia distachya)
Interaction partners:
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor 4G
- MI domain-containing protein
- RNA helicase
- RNA helicase
- Eukaryotic translation initiation factor 3 subunit I
- Tr-type G domain-containing protein
- Tr-type G domain-containing protein
- Tr-type G domain-containing protein
- Protein mago nashi
Sequence:
MAGMAPEGSQFDAKNYDSKMQELLSQGETEEFFTSYDEVHESFDDMGLQENLLRGIYAYGFEKPSAIQQRGIVPFCKGLDVIQQAQSGTGKTATFCSGILQQLDYGLVECQALVLAPTRELAQQIEKVMRALGDYLGVKVHACVGGTSVREDQRILASGVHVVVGTPGRVFDMLRRQSLRPDHIKMFVLDEADEMLSRGFKDQIYDIFQLLPGKIQVGVFSATMPPEALEITRKFMNKPVRILVKRDELTLEGIKQFYVNVEKEEWKLDTLCDLYETLAITQSVIFVNTRRKVDWLTDKMRGRDHTVSATHGDMDQNTRDIIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTQPENYLHRIGRSGRFGRKGVAINFVTREDERMLFDIQKFYNVVIEELPANVADLL
Protein: Acyl-CoA synthetase family member 3 (F5H5A1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMPEFSPQQVWEKFLSSETPRINVFMAVPTIYTKLMEYYDRHFTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREACSYTIHAEGDERGTKVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHFHPS
Protein: Glycine-N-acyltransferase-like protein 3 (EC 2.3.1.13) (Acyl-CoA:glycine-N-acyltransferase-like protein 3) (E9Q5L8)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conjugation of long-chain fatty acyl-CoA thioester and glycine to produce long-chain N-(fatty acyl)glycine, an intermediate in the primary fatty acid amide biosynthetic pathway.
Interaction partners:
Sequence:
MLVLKCSTKLFILENMLKSHFPESLKVYGAVMNINRGNPFQKEVVLDSWPNFKVIITRREREAETDNLDHYTNAYAVFYKDIRAYQQLLEEHDVINWDQVFQIQGLQSELYAASKAVAKARLLDLDINLASFKAVHFSPVSSVPDHSFLTGPTPRLTYLSVSDADLLNRTWSRGGNQQCLRYLANLIACFPSVCVRDEKGNPVSWGITDQFATMCHGYTLPDHRRKGYSRLVALTLARKLQSRGFPSQGNVLDDNLASINLLKSVQAEFLPCRFHRLILTPAAFSRQAHL