wanglab/gogpt-training-data huggingface dataset:
Protein: Protein Vhl (Q9V3C1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in development of tracheal vasculature. Probably involved in halting cell migration at the end of vascular tube outgrowth. Possesses E3 ubiquitin ligase activity when in complex with Elongin BC complex, Cul2 and Rox1a/Rbx1, and can target sima/Hif1a for ubiquitination. May play a critical role in promoting microtubule stabilization when tubulins are correctly folded by the prefoldin complex. If tubulin is incorrectly folded, may promote its degradation.
Interaction partners:
- Elongin-C
- Elongin-B
- Cullin-2
- Protein similar
- RING-box protein 1A
- COP9 signalosome complex subunit 5
- Ubiquitin-like protein NEDD8
- RING-box protein 1B
- hypoxia-inducible factor-proline dioxygenase
- LD27256p
Sequence:
MALQIAQNNRDGQQLVGADQGKVEVYVLFANTTYRTLDLYWVCERERENMYLTLKPFEEVRVNTFTTHSWLFRDYYTGERMHVRSQRIFQPIRVRVPKSQQSPDQLVDVRSEVLIHFPMRSLRENCLWLVARWLIRTSNAPRRIIHGYHIPSTLKQQLLSLLTCIESYSRVAGTRRRR
Protein: POU domain, class 4, transcription factor 1 (Brain-specific homeobox/POU domain protein 3A) (Brain-3A) (Brn-3A) (Brn-3.0) (P17208)
Organism: Mus musculus (Mouse)
Function: Multifunctional transcription factor with different regions mediating its different effects. Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes. Regulates the expression of specific genes involved in differentiation and survival within a subset of neuronal lineages. It has been shown that activation of some of these genes requires its N-terminal domain, maybe through a neuronal-specific cofactor. Ativates BCL2 expression and protects neuronal cells from apoptosis (via the N-terminal domain). Induces neuronal process outgrowth and the coordinate expression of genes encoding synaptic proteins. Exerts its major developmental effects in somatosensory neurons and in brainstem nuclei involved in motor control. Stimulates the binding affinity of the nuclear estrogene receptor ESR1 to DNA estrogen response element (ERE), and hence modulates ESR1-induced transcriptional activity. May positively regulate POU4F2 and POU4F3. Regulates dorsal root ganglion sensory neuron specification and axonal projection into the spinal cord. Plays a role in TNFSF11-mediated terminal osteoclast differentiation. Negatively regulates its own expression interacting directly with a highly conserved autoregulatory domain surrounding the transcription initiation site.
Subcellular location: Nucleus {ECO:0000269|PubMed:17668438}. Cytoplasm {ECO:0000269|PubMed:17668438}.
Interaction partners:
- Visual system homeobox 2
- Neurogenin-1
- Insulin gene enhancer protein ISL-1
- Cellular tumor antigen p53
- RNA-binding protein with multiple splicing
- Transcription factor Atoh7
- Tubulin beta-3 chain
- Melanopsin
- Paired box protein Pax-6
- Recoverin
Sequence:
MMSMNSKQPHFAMHPTLPEHKYPSLHSSSEAIRRACLPTPPLQSNLFASLDETLLARAEALAAVDIAVSQGKSHPFKPDATYHTMNSVPCTSTSTVPLAHHHHHHHHHQALEPGDLLDHISSPSLALMAGAGGAGAAGGGGGAHDGPGGGGGPGGGGGPGGGGPGGGGGGGGPGGGGGGPGGGLLGGSAHPHPHMHGLGHLSHPAAAAAMNMPSGLPHPGLVAAAAHHGAAAAAAAAAAGQVAAASAAAAVVGAAGLASICDSDTDPRELEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEGAQREKMNKPELFNGGEKKRKRTSIAAPEKRSLEAYFAVQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKFSATY
Protein: Asperous, isoform A (LP13770p) (Q9W5X1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE47447p
- Rho GTPase activating protein at 5A, isoform A
Sequence:
MQQLLVVALVAVAIASLPQLAAGKKLGKRCVNCTYRTYYTYGDGRSLQRVVYRDPVYTRAQSYASGCSGSPCGVNAVCQEASGGRPVCSCPPGFSGNPLTHCNRGECLDNVDCRDNLQCKDNRCVNPCVGACGIGSNCDARNHVAVCSCPAGYNGDPYHACHLNDPEEQCHPSPCGVNTKCEIINGVPTCSCVHGYVGNPLSGCRHECDHDGDCSSRDMCSSNFKCVPACGQCGTGATCRTVSNHRAVCECPKGYIGSPYTECRPECYGDADCPAGRPACFYGICKNTCEGACGIGADCNLRGLTPVCSCPRDMTGDPFVRCRPFTKEDLCDPNPCGTNAICVPGHDNTGRERPVCNCLPGHTGNPLSHCTRGECLSNNECPDHRACINYQCIDPCIGKCATGASCEPKAHLAVCRCPQGQSGDALVSCRQTRTFPVAKYH
Protein: Gap junction alpha-8 protein (Connexin-50) (Cx50) (Lens fiber protein MP70) (P48165)
Organism: Homo sapiens (Human)
Function: Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16397066, ECO:0000269|PubMed:18006672, ECO:0000269|PubMed:19756179, ECO:0000269|PubMed:26004348}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55917}. Cell junction, gap junction {ECO:0000269|PubMed:18006672, ECO:0000269|PubMed:19756179}.
Interaction partners:
- Gap junction alpha-3 protein
- Lens fiber major intrinsic protein
- Gap junction beta-2 protein
- Phakinin
- Gamma-crystallin D
- Beta-crystallin B2
- Beta-crystallin B1
- Gamma-crystallin S
- Gap junction alpha-1 protein
- Gap junction delta-3 protein
Sequence:
MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLMYVGHAVHYVRMEEKRKSREAEELGQQAGTNGGPDQGSVKKSSGSKGTKKFRLEGTLLRTYICHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNVMELGHLGLKGIRSALKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVETSPLPAKPFNQFEEKISTGPLGDLSRGYQETLPSYAQVGAQEVEGEGPPAEEGAEPEVGEKKEEAERLTTEEQEKVAVPEGEKVETPGVDKEGEKEEPQSEKVSKQGLPAEKTPSLCPELTTDDARPLSRLSKASSRARSDDLTV
Protein: Zinc finger protein 606 (F8W1C8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAINPWASWGALTDQSWGMTAVDPWASWALCPQYPAWHVEGSLEEGRRATGLPAAQVQEPVTFKDVAVDFTQEEWGQLDLVQRTLYRDVMLETYGHLLSVGNQIAKPEVISLLEQGEEPWSVEQACPQRTCPEWVRNLESKALIPAQSIFEEEQSHGMKLERYIWDDPWFSRLEVLGCKDQLEMYHMNQSTAMRQMVFMQKQVLSQRSSEFCGLGAEFSQNLNFVPSQRVSQIEHFYKPDTHAQSWRCDSAIMYADKVTCENNDYDKTVYQSIQPIYPARIQTGDNLFKCTDAVKSFNHIIHFGDHKGIHTGEKLYEYKECHQIFNQSPSFNEHPRLHVGENQYNYKEYENIFYFSSFMEHQKIGTVEKAYKYNEWEKVFGYDSFLTQHTSTYTAEKPYDYNECGTSFIWSSYLIQHKKTHTGEKPYECDKCGKVFRNRSALTKHERTHTGIKPYECNKCGKAFSWNSHLIVHKRIHTGEKPYVCNECGKSFNWNSHLIGHQRTHTG
Protein: Nck-associated protein 1-like (Hematopoietic protein 1) (Q8K1X4)
Organism: Mus musculus (Mouse)
Function: Essential hematopoietic-specific regulator of the actin cytoskeleton. Controls lymphocyte development, activation, proliferation and homeostasis, erythrocyte membrane stability, as well as phagocytosis and migration by neutrophils and macrophages. Component of the WAVE2 complex which signals downstream of RAC to stimulate F-actin polymerization. Required for stabilization and/or translation of the WAVE2 complex proteins in hematopoietic cells. Within the WAVE2 complex, enables the cortical actin network to restrain excessive degranulation and granule release by T-cells. Required for efficient T-lymphocyte and neutrophil migration (By similarity). Exhibits complex cycles of activation and inhibition to generate waves of propagating the assembly with actin. Also involved in mechanisms WAVE independent to regulate myosin and actin polymerization during neutrophil chemotaxis (By similarity). In T-cells, required for proper mechanistic target of rapamycin complex 2 (mTORC2)-dependent AKT phosphorylation, cell proliferation and cytokine secretion, including that of IL2 and TNF (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P55160}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P55160}. Note=Localizes to the leading edge of polarized neutrophils. {ECO:0000250|UniProtKB:P55160}.
Interaction partners:
- Cytoplasmic FMR1-interacting protein 1
- Cytoplasmic FMR1-interacting protein 2
- Abl interactor 1
- Actin-binding protein WASF2
- Actin-binding protein WASF1
- Abl interactor 2
- Protein BRICK1
- Actin-binding protein WASF3
- ABI gene family member 3
- Ras-related C3 botulinum toxin substrate 2
Sequence:
MSLTSAYQLKLAEKLTILNDRGQGVLIRMYNIKKTCSDSKSKPPFLLEKSMESCLKYINKKFPNIDVRNSTQHLGPVHREKAEIIRFLTNYYQSFVDVMEFRDHVYELLNTIDACQCHFDINLNFDFTRSYLDLIVTYTSVILLLSRIEDRRILIGMYNCAHEMLHGHSDPSFARLGQMVLEYDHPLKKLTEEFGPHTKAVSGALLSLHFLFVRRNQGAEQWRSAQLLSLISSPPAMINPANSDTMACEYLSVEVMERWIIIGFLLCHGCLNSNSQCQKLWKLCLEGSLYITLIREDVLQVHKVTEDLFSSLKGYSKRVADIKESKEHAITNSGQFHCQRRQFLRTAVKELETVLNDEPGLLGPKALFAFMALSFIRDEVTWLVRHTENVTKTKTPEDYADSSIAELLFLLEEIRALVRRHIKVIQQYHLQYLARFDVLVLSDIIQNLSVCPEEESVIMSSFVSILSSLNLKQVDNEEKFDFSGLRLDWFRLQAYTSVSKAPLHLHENPDLAKVMNLIIFHSQMLDSVEKMLVETSDLSTFCFHLRTFEKMFATTLEEPTMLRYTIAFPLICAHFVHCVHEMCPEEYPHLKNHGLHHCNSFLEDLAKQTSNCVLEICAEQRNLNEQLLPKHCATTISKAKNKKSMKQRQAPRKGEPERDKPGAESHRKNRSLVTNMDKLHLNLTELALAMNHVHSFSVFEHTIFPSEYLSSHLEARLNRAIVTLAGYNATTQEILRPSELLAGVKAYISFIQSLAQFLGADASRIVRNALLQQTQPLDSSGEQTVTTLYTNWYLESLLRQASSGAIVLSPAMQAFISLPRDGEQNFSAEEFSDISEMRALAEILGPYGMKFLSENLMWHVTSQIVELKKLVVENMDILVQIRSNFSKPELMASLLPQLTGAENVLKRMTIIGVILSFRAMAQEGLQEVFSAHCPFLMGPIECLKEFVTPDTDIKVTLSVFELACAAGVSCDIDPALVAAIANLKADNSSPEEEYKVACLLLIFLAVSLPLLATDPSSFFSIEKDGYNNNIHCLTKAIIQVSAALFTLYNKNIETHLKEFLVVASVSLLQLGQETDKLKTRNRESISLLMRLVVEESPFLTLDMLESCFPYVLLRNAYREVSRAFYLNRLPASSH
Protein: G protein alpha subunit, putative (C4M483)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Interaction partners:
- RGS domain-containing protein
- Guanine nucleotide exchange factor, putative
- Guanine nucleotide-binding protein subunit beta, putative
- Glycylpeptide N-tetradecanoyltransferase
- Methionine aminopeptidase 2
- Glycerophosphoryl diester phosphodiesterase, putative
- Mitogen-activated protein kinase
- Protein kinase domain containing protein
- Protein kinase domain containing protein
- DNA-directed DNA polymerase
Sequence:
MGCGQSKDNSIDKQIVEMAKSKPITVMLLGSGESGKSTIAKQLKILFGGGFPEQERATHKSSICSNVVTCMRTLIEQSAILNHPMKYQPKSKEFTTEDPVTLPFSPELVGDVEALWADEGIQATYEESAKFQLPDCAKYLFENVKRIAMEDYVPTEEDLIHNRTKTTGIHEYDFVVKDIPFHLIDVGGQRSERKKWVSFFSDVDCAIFVTSLAEYDMKLYEDGNTSRLTESIAVFKDIMTNEFLKGAVKLIFLNKMDLFEEKLTKVPLNTIFPEYTGGDNAVMGAQYIQQLFTGKLQTEEMNISGADGTANIEGAVNEKVYTNPTNATDGSNIKRVFMLAVDVIMKNMAANGKMRPTK
Protein: SNF2 N-terminal domain-containing protein (G1K104)
Organism: Caenorhabditis elegans
Interaction partners:
- Nuclear hormone receptor family member nhr-115
- F-box domain-containing protein
- Uncharacterized protein T25D10.1
- F-box domain-containing protein
- CUB_2 domain-containing protein
- ShKT domain-containing protein
- ATP-dependent DNA helicase
- ATP-dependent DNA helicase
- ATP-dependent DNA helicase
- ATP-dependent DNA helicase
Sequence:
MGFDLDEKQKNMMNSMAKYESGDNCGGIITIATATNDRIEEVLMSHIIEQNKTLENGSKPNKTLMVGSPSWTNKLQKLPSKCKKVPEVSEVPEECSENSQNDALSFYKLKRKTKSQDFVEEDIVLANYGLLETIQELKVTWERIIFHDFSLETKNNYHQFETVCKLNATFRWYITENHKQDRLEEYLVADDGKRMHVKGDIDTFLDQANLYLPSAEPKSRNLKTPLDGRQKDFKSNLAQREKEPVRGGIITTLIRDILIKETIIEFLLDQKNTSEEYGHSMGKTLLVVPPDMIESWKKLLEKLLEKDDLVIHYFYRNEDKKPDDSHEVVITTYDMLKNIENRNILWKRIIFEDNYSASEKDRQQYQLLFSFLCQLHAEYRWCLTENPTQQKLARFMNRKEYGESHNLIKSISLGNAKDDEEKSTAKLVKNIEGFLKQVTLRFPRSSNDYEKHITNAKKEKKENEPNIRKFCNNLLAAIISYTEEFYIKHFNISTESDEDIEEMYDSFCAGLQDPSHVGLIVKVWVDAHWNFSKSEQDRSFIVKAMKNIIENFEKAIEIIEKATQTSIEESYNQMRAARQQRTANREN
Protein: UPAR/Ly6 domain-containing protein bou (Protein boudin) (Q9W3T7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000269|PubMed:19502482}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19502482}; Extracellular side {ECO:0000269|PubMed:19502482}. Cell junction, septate junction {ECO:0000269|PubMed:19502482}. Cytoplasm, cell cortex {ECO:0000269|PubMed:19502482}. Secreted {ECO:0000269|PubMed:19502482}. Apicolateral cell membrane {ECO:0000269|PubMed:28977027}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19502482}; Extracellular side {ECO:0000269|PubMed:19502482}. Note=Accumulates in the apical cell cortex, possibly associated with secretory vesicles (PubMed:19502482). Cell membrane localization includes, but is not restricted to, the septate junction region (PubMed:19502482, PubMed:28977027). The secreted form, potentially associated with extracellular vesicles called 'boudosomes' via its GPI-anchor, diffuses through the extracellular space and is endocytosed by distant cells and incorporated into their cell membrane, where it co-localizes with septate junctions (PubMed:19502482, PubMed:28977027). {ECO:0000269|PubMed:19502482, ECO:0000269|PubMed:28977027}.
Interaction partners:
- UPAR/Ly6 domain-containing protein cold
- UPAR/Ly6 domain-containing protein crok
- UPAR/Ly6 domain-containing protein crim
- Uncharacterized protein, isoform B
- UPAR/Ly6 domain-containing protein rtv
Sequence:
MWPPKHAHIGWLSSLALVVLLMSLQMVMVSGIECYVCDTSDTEHPFQCGEWFERYDIPDIQPQNCSSVHGAQFCVKHVGRFEGGIGAKRFCSSKDMGNYCDYVRNKGDRMDYRSCIYTCDTDGCNAAGRLELEWGVAAALLTLTWLLRH
Protein: Apolipophorin-3 (Apolipophorin-III) (ApoLp-III) (P80703)
Organism: Galleria mellonella (Greater wax moth)
Function: Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects. Has antibacterial activity against the Gram-positive bacteria L.monocytogenes (MIC=6.5 uM). Lacks antibacterial activity against the Gram-positive bacteria B.circulans, M.luteus, S.aureus, and S.lutea, and the Gram-negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Lacks antifungal activity against S.cerevisiae, P.pastoris, Z.marxianus, C.albicans, C.wickerhamii, A.niger, F.oxysporum, and T.harizianum.
Subcellular location: Secreted {ECO:0000269|PubMed:17194500, ECO:0000269|PubMed:29289504}. Note=Secreted into hemolymph. {ECO:0000269|PubMed:29289504}.
Interaction partners:
Sequence:
MAAKYVFVVAACSALAQAGIVRRDASTPLQDLEKHAAEFQKTFSEQLNAFTNSKDTKEFNTALKEGSDSVLQQLNALASSLQKALNDANGKAKEALEQTRTNLERTAEELRRAHPDVERQAGALRDRLQTAVQATVQETQKLAKTVGANLEETNKKLAPQIKSAYDDFVKQAQEVQKKLHEAASKQ
Protein: Zcf1p (A0A1D8PJJ7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein
Sequence:
MSSALLPISCISCRKRKIKCNRIKPCDQCIKRHLPCEFPEKFRNIKIQEDEIKPELDGEPKLEPEDDMNSIYDYTRKPSENSSISTSGSASILSSAPSKSTDSTDSIPTSTDSATNSDSREKCMVTKNHSTGKISHSSPSAIPITVGSLNNSIISSSKNLIDSDAPNQDSDNLTLLRDDYDIMKAANTQLLSSNRLLKRQLEELQQSTLSHFRRSDMRNCHDNAHKNGSCSCNKTTKTIDNGNHNRGDANANLLPNLPRSGDKRANTSDSFSDESPNKKEKVGVFGYSKSSFPKDSASQNQGIYSNNQFNEDNSSSPPKETSTTSTDSSSSGGEIGQTLTFQPLSKEQRELLNGRKVHRVKRNRGQGFYEHQVSSQPPVNKNGLPNRSVNHNHNWEQDAETYQDQESIKSSIQIQKSLKKKTLPILPSYLLKYDDPGISVDSTTYQDISRLNFEVVVKLVEKFFENNSYYRTFISSVHVFDFLNGYNSINDRDWENDDDLLLVYMILCLSIERLSPQDFVELNLLPDGSLNICTKYRKFLTRQVLYKSFERLKENLVDESMITIQTYILCSEWLFLQQNYEECWQMMFHACSISFSIGLHIMNQFRATNTKENKPFKNVVDATMGESDSSSEKKDTMELEEDKKNEDEELNAQQYRLWYALKYSTSVICSIFGRPNPISVKVGMIDSTPLNQIDQKLHVLLKSESSESLRLSNLMLIENYMIDISFENVMTLKLKFDTDILTLEDSYDSIHGKITCSLIGGSEQQNKSNDNANKWIGYDDYTKGSLTTKELDVLSDTIILHINSVKLLEPFVKKYETQKGKDTLSEKQIDSIGXFYNY
Protein: Homeobox protein DLX-3 (Q64205)
Organism: Mus musculus (Mouse)
Function: Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:35922041}. Cytoplasm {ECO:0000269|PubMed:35922041}.
Interaction partners:
- Enamelin
Sequence:
MSGSFDRKLSSILTDISSSLSCHAGSKDSPTLPESTVTDLGYYSAPQHDYYSGQPYGQTVNPYTYHHQFNLNGLAGTGAYSPKSEYTYGGSYRQYGAYREQPLPAQDPVSVKEEPEAEVRMVNGKPKKVRKPRTIYSSYQLAALQRRFQKAQYLALPERAELAAQLGLTQTQVKIWFQNRRSKFKKLYKNGEVPLEHSPNNSDSMACNSPPSPALWDTSSHSTPAPARNPLPPPLPYSASPNYLDDPTNSWYHTQNLSGPHLQQQPPQPATLHHASPGPPPNPGAVY
Protein: Phosphate import ATP-binding protein PstB 1 (EC 7.3.2.1) (ABC phosphate transporter 1) (Phosphate-transporting ATPase 1) (P9WQL1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ABC transporter complex PstSACB involved in phosphate import (Probable). Responsible for energy coupling to the transport system.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01702}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01702}.
Interaction partners:
- Phosphate transport system permease protein PstA 1
- Phosphate transport system permease protein PstC 2
- Phosphate transport system permease protein PstA 2
- Phosphate transport system permease protein PstC 1
- Phosphate-binding protein PstS 3
- Phosphate-binding protein PstS 2
- Phosphate-binding protein PstS 1
- Phosphate-specific transport system accessory protein PhoU homolog 2
- Phosphate-specific transport system accessory protein PhoU homolog 1
- Phosphate import ATP-binding protein PstB 2
Sequence:
MAKRLDLTDVNIYYGSFHAVADVSLAILPRSVTAFIGPSGCGKTTVLRTLNRMHEVIPGARVEGAVLLDDQDIYAPGIDPVGVRRAIGMVFQRPNPFPAMSIRNNVVAGLKLQGVRNRKVLDDTAESSLRGANLWDEVKDRLDKPGGGLSGGQQQRLCIARAIAVQPDVLLMDEPCSSLDPISTMAIEDLISELKQQYTIVIVTHNMQQAARVSDQTAFFNLEAVGKPGRLVEIASTEKIFSNPNQKATEDYISGRFG
Protein: Probable insulin-like peptide beta-type 1 (Q09626)
Organism: Caenorhabditis elegans
Function: Probable insulin-like peptide which negatively regulates synapse development at the neuromuscular junctions. Probably acts as a daf-2/InsR agonist ligand to prevent dauer formation under optimal environmental conditions.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Probable insulin-like peptide beta-type 3
- Ceinsulin-1
- Insulin-like receptor
- Insulin-like peptide 17
- INSulin related
- INSulin related
- INSulin related
- INSulin related
- INSulin related
- Probable insulin-like peptide gamma-type 1
Sequence:
MFSFFTYFLLSALLLSASCRQPSMDTSKADRILREIEMETELENQLSRARRVPAGEVRACGRRLLLFVWSTCGEPCTPQEDMDIATVCCTTQCTPSYIKQACCPEK
Protein: Recombination protein RecR (Q9ZNA2)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Interaction partners:
- DNA repair protein RecO
- Nucleoid-associated protein DR_0199
- DNA replication and repair protein RecF
- Protein RecA
- Thymidylate kinase
- DNA polymerase III subunit gamma/tau
- N-acetyltransferase domain-containing protein
Sequence:
MKYPPSLVSLIRELSRLPGIGPKSAQRLAFHLFEQPREDIERLASALLEAKRDLHVCPICFNITDAEKCDVCADPSRDQRTICVVEEPGDVIALERSGEYRGLYHVLHGVLSPMNGVGPDKLHIKPLLPRVGQGMEVILATGTTVEGDATALYLQRLLEPLGAAISRIAYGVPVGGSLEYTDEVTLGRALTGRQTVSKPQPPQRPGDEDGADGAAVPASR
Protein: Protein fuzzy homolog isoform X1 (A0A1L8FNF3)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Uncharacterized protein.
- Uncharacterized protein.
- Protein inturned
- Ciliogenesis and planar polarity effector 2
- MGC81434 protein
- t-SNARE coiled-coil homology domain-containing protein.
Sequence:
MEDSSVFLLCLATSSGVPLYCRSKGSSRQLTFSVIGSLNGVHMFASNQDVLLTSTCTDNTRVAWRAFHDSITLIVMSSESGASDLSLNRLLENVFNAMVLVIGLDDLVNIKNVERLKKDLRACYRLIDSFLLETEKIGDLTQCVDCVIAYDVPILQECLDGFTQAAESNFGCLMAGGKVVVATEKWWRLSSQEVMLLCWLVSSLAPHSSRDYPVYLPQGSPTVPHRLLTFQLVPGVDVCVLCGPKPSLQKVETELVERFWKPVHDPLKSCLRVQMRSFPASVPLHHGILGLLLINRDMNKSLYTVQAHPMEEMQKTDLKLTLEQRRATLHSFYTLAMSRYFPSERTEGKNTLPSDESFQCGFSHNAHQCYTVSSSCKCYGMKTDLHLLFLLFKPEVPTFSMRSIANKTIAAFTKDFPF
Protein: Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3) (E7EUD1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364110}. Nucleus {ECO:0000256|RuleBase:RU364110}.
Interaction partners:
Sequence:
MVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCK
Protein: Lipophorin receptor 2, isoform H (A0A0B4KH38)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGPICRILGCSFLLLIAGLVPHHASRVVGLESTCSQEQFRCGNGKCIPRRWVCDRENDCADGSDESTSQCRSHTCSPEEFACKSGEGECIPLSWMCDQNKDCRDGSDEAQCNRTCRSDEFTCGNGRCIQNRFKCDDDDDCGDGSDEKNCGEKAKCGSNFFACKSGPCIPNQWVCDGDSDCRNGEDEMQNCTVSLLNFCQAGEFQCSDRITCLHKSWVCDGEADCPDGEDESQSNCLKVSCRPDQFQCNDQSCIAGHLTCNGKRDCADGSDEIMCDISATPRTCNATTEFDCGGGLCIPNAKVCNRRKDCPNGEDEPAGKCGINECSSKNGGCMHQCVNLEVGYRCECHDGYKLGADQHTCVDIDECETPGICSQVCVNEIGAFKCECEAGYMRLLKNHTRCKASEGHASLLLARRHDIRKIALDRPEMTSIVNSTKAATALDFVFRTGMIFWSDVATQSIYKAPIDEGNDRTVVLTKSSVTSDGLAVDWIYNHVYFTDTHKCTIELTNFEGSMGKVLVKDSLDIPRSIALDPIEGWMYWSDWGASPRIERAGMDGTHRTAIITYDVKWPNGITLDLVQKRLYWVDGKLNTISSSNYDGSQRHQVLYSGEYLRHPFSITTFEDYVYWTDWDKQAVFKANKFNGMDVEPVTATHMLEHPMVVHVYHPYRQPDGVNHCQSVNGHCSHLCLPAPRINERSPRISCACPTGLKLMPDGLMCVEDLGIPTVRPTAPMHRTIEQSSNSTTKLPQDGYSETPVETKTGNNRTDTSNQVHKSDAESENDYVEIALHVIASLAGTALVASVIYVVYRRCTRAVNSMNFENPVYHKTTEDHFSLEKNGTPHIYAAANDEEAVNPLFKSGTECV
Protein: Cerebellin-1 (Brain protein D3) (Precerebellin) [Cleaved into: Cerebellin (CER); [des-Ser1]-cerebellin (des-Ser1-cerebellin)] (Q9R171)
Organism: Mus musculus (Mouse)
Function: Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components. On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles. Required for CBLN3 export from the endoplasmic reticulum and secretion. NRXN1-CBLN1-GRID2 complex mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity). Essential for long-term maintenance but not establishment of excitatory synapses. Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells.
Subcellular location: Secreted {ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:29782851}. Postsynaptic cell membrane {ECO:0000269|PubMed:19200061}. Note=Interaction with CBLN3 may cause partial retention in the endoplasmic reticulum. {ECO:0000269|PubMed:17331201}.
Interaction partners:
- Neurexin-1
- Glutamate receptor ionotropic, delta-2
- Neurexin-2
- Neurexin-3
- Glutamate dehydrogenase 1, mitochondrial
- Leucine-rich repeat transmembrane neuronal protein 2
Sequence:
MLGVVELLLLGTAWLAGPARGQNETEPIVLEGKCLVVCDSNPTSDPTGTALGISVRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLNGWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL
Protein: HTH cro/C1-type domain-containing protein (Q8E7C5)
Organism: Streptococcus agalactiae serotype III (strain NEM316)
Interaction partners:
Sequence:
MFIYGPIFREFRLNRQFSLKQVASNELSVSQLSRFERGESDLSLTKFLGALEAIDLSISEFMYRVNKYQKSDQISLMSQMAQYHYQRDVAGLEKMISVEEGKLKKDSSDIRCRLNIVLFRGMICECDSSRKMSEEDLCFLSDYLFQKDSWEISDYILIGNLYRYYNTRYICQLVKEVINQKEYYRDIYTNRNVVEATLLNVVETLIERRALEEATFFVEKVEALLNNERNAYHRIILLYEKGFLAYAKGDSRGIQSMKQAIFCFQAIGSKHHVENFQEHFNRVTRL
Protein: Homeobox protein NANOG (Homeobox transcription factor Nanog) (cNanog) (A7Y7W3)
Organism: Gallus gallus (Chicken)
Function: Transcription factor required for the maintenance of pluripotency and self-renewal of embryonic stem cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:25846318}.
Interaction partners:
- POU domain, class 5, transcription factor 3
- Transcription factor SOX-2
- Protein lin-28 homolog A
Sequence:
MSAHLAMPSYGSVRCGHYYWPSPGSMDSASAAEAPAADLSLTTEQKTPCHPDASPASSSSGTLIQYTPDSATSPTADHPSHRPTFQKVKDKGESGTRKAKSRTAFSQEQLQTLHQRFQSQKYLSPHQIRELAAALGLTYKQVKTWFQNQRMKFKRCQKESQWVDKGIYLPQNGFHQAAYLDMTPTFHQGFPVVTNRNLQAVTSAHQAYSSGQTYGNGQGLYPFMAVEDEGFFGKGGTSCNTQQAMGLLSQQMNFYHGYSTNVDYDSLQAEDTYSFQSTSDSITQFSSSPVRHQYQAPWHTLGTQNGYET