wanglab/gogpt-training-data huggingface dataset:
Protein: Sonic hedgehog protein (SHH) (EC 3.1.-.-) (Shh unprocessed N-terminal signaling and C-terminal autoprocessing domains) (ShhNC) [Cleaved into: Sonic hedgehog protein N-product (ShhN) (Shh N-terminal processed signaling domains) (ShhNp)] (Q91035)
Organism: Gallus gallus (Chicken)
Function: The C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Once cleaved, ShhC is degraded in the endoplasmic reticulum (By similarity).
Subcellular location: [Sonic hedgehog protein]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15465}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15465}. Note=Co-localizes with HHAT in the ER and Golgi membrane. {ECO:0000250|UniProtKB:Q15465}.; SUBCELLULAR LOCATION: [Sonic hedgehog protein N-product]: Cell membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}. Note=The dual-lipidated sonic hedgehog protein N-product (ShhNp) is firmly tethered to the cell membrane where it forms multimers (By similarity). Further solubilization and release from the cell surface seem to be achieved through different mechanisms, including the interaction with DISP1 and SCUBE2, movement by lipoprotein particles, transport by cellular extensions called cytonemes or by the proteolytic removal of both terminal lipidated peptides. {ECO:0000250|UniProtKB:Q62226}.
Interaction partners:
- Protein patched homolog 1
- Patched 2.
- Hedgehog-interacting protein
- Cell adhesion associated, oncogene regulated.
- Protein smoothened
- Growth arrest specific 1.
- Zinc finger protein GLI1
- BOC cell adhesion associated, oncogene regulated.
- Zinc finger protein GLI2
- Fibroblast growth factor 8
Sequence:
MVEMLLLTRILLVGFICALLVSSGLTCGPGRGIGKRRHPKKLTPLAYKQFIPNVAEKTLGASGRYEGKITRNSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDKLNALAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRSKYGMLARLAVEAGFDWVYYESKAHIHCSVKAENSVAAKSGGCFPGSATVHLEHGGTKLVKDLSPGDRVLAADADGRLLYSDFLTFLDRMDSSRKLFYVIETRQPRARLLLTAAHLLFVAPQHNQSEATGSTSGQALFASNVKPGQRVYVLGEGGQQLLPASVHSVSLREEASGAYAPLTAQGTILINRVLASCYAVIEEHSWAHWAFAPFRLAQGLLAALCPDGAIPTAATTTTGIHWYSRLLYRIGSWVLDGDALHPLGMVAPAS
Protein: Serine/arginine-rich splicing factor RSZ22 (RS-containing zinc finger protein 22) (At-RSZ22) (At-RSZp22) (AtRSZ22) (O81126)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific RNA-binding protein probably involved in pre-mRNA splicing. In vitro, can complement efficiently splicing-deficient mammalian SRSF7-depleted HeLa cell extract.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:17114353, ECO:0000269|PubMed:18674533, ECO:0000305|PubMed:12176998}. Nucleus, nucleolus {ECO:0000269|PubMed:15133128, ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:17114353, ECO:0000269|PubMed:20237019}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:17114353}. Cytoplasm {ECO:0000269|PubMed:17114353, ECO:0000269|PubMed:20237019}. Note=Shuttling between nucleolus, nucleoplasm and cytoplasm surrounding the nucleus. Nucleolus localization is dependent on phosphorylation state. {ECO:0000269|PubMed:15686520, ECO:0000269|PubMed:17114353, ECO:0000269|PubMed:20237019}.
Interaction partners:
- Serine/arginine-rich splicing factor RS2Z33
- Serine/arginine-rich splicing factor RSZ21
- Serine/arginine-rich splicing factor SC35
- U1 small nuclear ribonucleoprotein 70 kDa
- Serine/arginine-rich SC35-like splicing factor SCL30A
- Serine/arginine-rich splicing factor RS31
- Serine/threonine-protein kinase AFC2
- Serine/arginine-rich SC35-like splicing factor SCL33
- RNA-binding protein Y14
- Serine/arginine-rich splicing factor SR45
Sequence:
MSRVYVGNLDPRVTERELEDEFRAFGVVRSVWVARRPPGYAFLDFEDPRDARDAIRALDGKNGWRVEQSHNRGERGGGGRGGDRGGGGGGRGGRGGSDLKCYECGETGHFARECRNRGGTGRRRSKSRSRTPPRYRRSPSYGRRSYSPRARSPPPPRRRSPSPPPARGRSYSRSPPPYRAREEVPYANGNGLKERRRSRS
Protein: Serine/threonine-protein phosphatase 2B catalytic subunit 2 (EC 3.1.3.16) (Calmodulin-dependent calcineurin A2 subunit) (Q27889)
Organism: Drosophila melanogaster (Fruit fly)
Function: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.
Interaction partners:
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
- Serine/threonine-protein phosphatase 2B catalytic subunit 1
- Protein sarah
- Serine/threonine-protein phosphatase 2B catalytic subunit 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase classes I and II
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Calcium and integrin-binding family member 2
Sequence:
MSSNNQSSSVAQAATSARTVSAGSAEATDANSTASNNNNNSSSTAAAGNNSDNSSPTTGTGTGASTGKLHGGHTAVNTKERVVDSVPFPPSHKLTLAEVFDQRTGKPNHELLKQHFILEGRIEEAPALKIIQDGAALLRQEKTMIDIEAPVTVCGDIHGQFYDLMKLFEVGGSPASTKYLFLGDYVDRGYFSIECVLYLWSLKITYPQTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEIHELEDIRRLDRFKEPPAFGPMCDLLWSDPLEDFGNEKNSDFYTHNSVRGCSYFYSYAACCDFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELMTEESEEPLSDDEAALRKEVIRNKIRAIGKMARVFSVLREESESVLQLKGLTPTGALPLGALSGGKQSLKNAMQGFSPNHKITSFAEAKGLDAVNERMPPRRDQPPTPSEDPNQHSQQGGKNGAGHG
Protein: Keratin, type II cytoskeletal 8 (Cytokeratin endo A) (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8) (P11679)
Organism: Mus musculus (Mouse)
Function: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix {ECO:0000250|UniProtKB:Q10758}.
Interaction partners:
- Keratin, type I cytoskeletal 18
- Keratin, type I cytoskeletal 19
- Sequestosome-1
- Epithelial cell adhesion molecule
- Cadherin-1
- Dystrophin
- Keratin, type II cytoskeletal 7
- Predicted gene 20431
- Ubiquitin-conjugating enzyme E2 variant 1
- Utrophin
Sequence:
MSIRVTQKSYKMSTSGPRAFSSRSFTSGPGARISSSSFSRVGSSSSSFRGSMGTGVGLGGFGGAGVGGITAVTVNQSLLSPLKLEVDPNIQAVRTQEKEQIKSLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTSRSNMDNMFESYINNLRRQLEALGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRELQSQISDTSVVLSMDNSRSLDMDGIIAEVRAQYEDIANRSRAEAETMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRNINRLQAEIEALKGQRASLEAAIADAEQRGEMAIKDAQTKLAELEAALQRAKQDMARQLREYQELMNVKLALDIEITTYRKLLEGEESRLESGMQNMSIHTKTTSGYSGGLSSSYGGLTSPGFSYGMSSFQPGFGSAGGSNTFSRTTKAVVVKKIETRDGKLVSESSDVVSK
Protein: Pantoate--beta-alanine ligase (EC 6.3.2.1) (Pantoate-activating enzyme) (Pantothenate synthetase) (Q9FKB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the condensation of pantoate with beta-alanine to form pantothenate. Essential for panthotenate biosynthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16042590}.
Interaction partners:
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 1, mitochondrial
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 2, mitochondrial
- Pantothenate kinase 2
- Pantothenate kinase 1
- Glutamate decarboxylase 3
- Glutamate decarboxylase 4
- Glutamate decarboxylase 2
- Glutamate decarboxylase 5
- Glutamate decarboxylase 1
- Beta-ureidopropionase
Sequence:
MEPEVIRDKDSMRKWSRAMRSQGKTIGLVPTMGYLHEGHLSLVRQSLALTDVTVVSIYVNPGQFSPTEDLSTYPSDFSGDLTKLAALSGGKVVVFNPKNLYDYGGETKKINDGGGNGGRVVSCVEEGGLGHETWIRVERLEKGFCGKSRPVFFRGVATIVTKLFNIVEPDVALFGKKDYQQWRIIQRMVRDLNFGIEIVGSDIAREKDGLAMSSRNVRLSDEERQRALSISRSLAMAKASVAEGKTNCAELKDMIIQQVVGSAGRVDYVEIVDQETLEGVEEIKSGVVICVAAWFGTVRLIDNIEINVSL
Protein: Uncharacterized protein (Q387Q4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calcineurin B subunit, putative
- 1-phosphatidylinositol 4-kinase
- Epsilon tubulin
Sequence:
MSYLTEEEEKERQREQQRRMSRQQIIEHVKKNLLYTAFDVKWVPHSACLAIVGQYPNNQGALSFMQLNKGELTVRHEIRTKLPLKCCTFAHNSRQMSSAALTIAAGDFAGGLSLWDVERLSSSSGDNGKFDENEALFKAPRAHENIINAVDGAQFTGPPEIASCGRDGCVKVWDVRQAAKPVVVLSPADPARARDCWTVRLGNSSDPDERVVVAGYDNGDVKLFDLRTQKMLHEFNVGNGVCDVEFDRPDIPMNKLIVSLLEGRVRVYDVRTLHPTLGYAYVEERVSSGTVWCSRALPQNREVFACGGGGEVTLCRYRYPPERTLRDSDGVAKGIAGCVEELNKAKVGDQPIHTMDWNRSKEGLLACASFDQSIRVMLVTKLSLVQ
Protein: GH15549p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform C) (Uncharacterized protein, isoform D) (Q9I7R7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 9
- AT02348p
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 5A, mitochondrial
Sequence:
MSAARLPYYQRDQEDGHQRRAARGHQRGYYERGSGSGSSRREHSRYSRSRSRSRSRSRSAERFGQRRRHQKRQSSRYHRDRDSRDRSRDRSRDRSRDRERDRDRDHSRRSSHYRRSESPSSSDIGHGSNNSQRRGHHASSSSKSELSAVQKAAAAAAAATNQVQLAGKSSAASAVGAYYNLDTDEPFDKERIHREMEQKLREALAREGKVYPPPKPEPPSHPVFANDGSFMELFKKMQEGQKQQATSQLMQPSVKEVLQQQLVPPEAASTGPALPAIALGAASSAAAPYIAAAAAGKLAPPPPIVGRRRGGKVLKTGVVAKVKTPNESDVDPKDFWSLYLAEVNKYKSNACDTDNGKRPLVK
Protein: Septin-5 (Cell division control-related protein 1) (CDCrel-1) (Peanut-like protein 1) (Q99719)
Organism: Homo sapiens (Human)
Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=In platelets, found in areas surrounding alpha-granules.
Interaction partners:
- Septin-11
- Septin-6
- Septin-7
- E3 ubiquitin-protein ligase parkin
- Septin-8
- Neuronal-specific septin-3
- Septin-12
- Uncharacterized protein C17orf47
- Septin-10
- Septin-2
Sequence:
MSTGLRYKSKLATPEDKQDIDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLSAEERISQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNTECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPSEIRKLKERIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQRMKQQMQDQ
Protein: Alpha-(1,3)-fucosyltransferase 7 (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase) (Selectin ligand synthase) (Q11130)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization. In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc. Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium. May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi.
Interaction partners:
- Type 2 lactosamine alpha-2,3-sialyltransferase
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Alpha-
- P-selectin
- E-selectin
- Headcase protein homolog
- P-selectin glycoprotein ligand 1
- Zinc finger and BTB domain-containing protein 32
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Galactoside alpha-
Sequence:
MNNAGHGPTRRLRGLGVLAGVALLAALWLLWLLGSAPRGTPAPQPTITILVWHWPFTDQPPELPSDTCTRYGIARCHLSANRSLLASADAVVFHHRELQTRRSHLPLAQRPRGQPWVWASMESPSHTHGLSHLRGIFNWVLSYRRDSDIFVPYGRLEPHWGPSPPLPAKSRVAAWVVSNFQERQLRARLYRQLAPHLRVDVFGRANGRPLCASCLVPTVAQYRFYLSFENSQHRDYITEKFWRNALVAGTVPVVLGPPRATYEAFVPADAFVHVDDFGSARELAAFLTGMNESRYQRFFAWRDRLRVRLFTDWRERFCAICDRYPHLPRSQVYEDLEGWFQA
Protein: BZIP domain-containing protein (F6WVZ0)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Interaction partners:
- Transcription factor protein
- BZIP domain-containing protein
- BTB domain-containing protein
Sequence:
MTDDKKEKYFSQQSKIQSGQSVIFSDEELLNLSVRDLNRHLRSLSPEESRRLKQRRRTLKNRGYAASCRIKRLTQKDELDIERIQLQNEVDRVTQENQRMKLELEAFQKKFHDLEQFAKSIGKGSSSYTGDGNVPTLLQVMRPPTTQQNGDSANTESNMIS
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (C8V7D1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Transcription factor steA
- MAP kinase kinase
- protein-tyrosine-phosphatase
- protein-tyrosine-phosphatase
- Cytokinesis protein sepA
- von Willebrand and RING finger domain protein
- mitogen-activated protein kinase kinase
- mitogen-activated protein kinase kinase kinase
- MADS-box domain-containing protein
- G-protein beta subunit
Sequence:
MVQQMPPQGGSRKISFNVSDQYEIQDVIGEGAYGVVCSAIHKPSGQKVAIKKITPFDHSMFCLRTLREMKLLRYFNHENIISILDIQRPRNYESFNEVYLIQELMETDMHRVIRTQDLSDDHCQYFIYQTLRALKAMHSANVLHRDLKPSNLLLNANCDLKVCDFGLARSAASTDDNSGFMTEYVATRWYRAPEIMLTFKEYTKAIDVWSVGCILAEMLSGKPLFPGKDYHHQLTLILDVLGTPTMEDYYGIKSRRAREYIRSLPFKKKIPFKALFPKSNDLALDLLEKLLAFNPTKRITVEEALRHPYLEPYHDPDDEPTAPPIPEGFFDFDKNKDALSKEQLKILIYEEIMR
Protein: Differentiation-associated protein 2 (DIA-2) (O96042)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Has an essential role in the initiation of differentiation. Also required for cAMP signaling.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:17825085}. Vacuole {ECO:0000269|PubMed:17825085}. Note=During late development it changes it's location from endoplasmic reticulum to pre-spore-specific vacuoles.
Interaction partners:
Sequence:
MKQIIRLITTLLLLSLIGITCAAVAKLHETDKKFKGVELPEKFLDDFNLEVGKLQYANLFRSKKDDITHSAGEIRIDQQGSFSRGEKKKKFKVYNLQAQTNGKSSKTVAHVEVFDTIDAKTKAEQNEVLALAKEAFTKSKDSGKLYQVIPN
Protein: Ribosome-recycling factor (O96173)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MIFQHFLSLHNEKKISMFFYTFLILYISHVRIFYDCLNLKNEKNYNVLLKNGNNNSPSYYFLNSNYRNNNNFLRRKENYQRVLLLYNPKFNDGAKRNSYILYAHSKKNKNKNKINHNINITKRETVSRRDRDDEDDNYDDDDENYDDDDDNYDDDENYEDDENYDDDDENYDDGENYEDDENYNDDENYDDDENYDDEYDDDDYPFNNDDIDIGDKDTPYETQKSKIRSKDENVAHQNKGGNTLSLENYKIKKNANSDLETDKKNKVKKKQDEEMDETNKNNKNETNEKDEKDEKEEKDDNINDNNDDIMEDEYEEDYITEEHIKDLHKICSEKMNKVYEFLKKESYRFNLNNVSNDMFENEKVKINERIYTVKHICHIKKKENLFTITPYDPYFVNFLYQHFIKEFDELKFYVKDKSLYAIIPPISENLKNEIKMKIKRKIEDSKVTLRTVRKQMMDKLEKFKNKIGKDIYFKQKNYIQSIHDQTKKNIEKLFADTK
Protein: Uncharacterized protein (G5EAY1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Cytokinesis protein sepA
- Kinesin-like protein
- Dis1/XMAP215 protein AlpA
- SH3 domain-containing protein
- Clip 170 homolog
- Aspergillus nidulans myosin V homolog
- Phospholipid-transporting ATPase
- TeaA receptor TeaR
- GTP-binding protein ypt1
Sequence:
MAFLFKSKKNQQTSGLPPATRNVHTSEGAPAGSGATLNGSKDGVVTSQTPTPSGSYNNSLNSVTSTNSPEQQRMRQRAESESQAQRPQQSTSPVSSPGSSLYPWSQRRLNFSSPQANPFPRYGAAINAVASKEGDIYMMGGLIDGSTVKGDLWMLESSSGNLSCFPIATVSEGPGPRVGHASLLVGNAFIVFGGDTKVDENDTLDDTLYLLNTSSRQWSRSIPPGPRPTGRYGHTLNILGSRLYVFGGQVEGYFFNDLVAFDLNQLQNPGNKWEFLIQNSHEGGPPPGQIPPARTNHTIVSFNDKLYLFGGTNGLQWFNDVWSYDPRTNSWTQLDCVGFIPTPREGHAAALVNDVMYVFGGRTDEGIDLGDLAAFRISTRRWYSFQNMGPAPSPRSGHSMTAFGRQIIVLAGEPSSAPRDPVELSMAYMLDTSKIRYPTENPNGEKAMFPGPTKTGAGEKPPSGRVSREAQNQPSDQFRRAQGPRESVVSPTGRPTELGPGPGSRLPRASIANAPAGPPPPGQAPTPGPRGNPPRDGNNFRSKTPTKQERGYGGPPIDTTRAIAGDREREPAPRDSPKDPRFAQESTGQRTPTQQSQRMSARAMEAGEAAPLVAPARQRSLRQRQRSSMDSADESILGRHASIDGSVDSRTHRNSRTGDEPRSPRLTAHQEALFKELEALKSRNAWYASELALAKKAGYTPNISANSALDERTSDAFTDEDRPLIEAFLAMRAELAKMQATVDRQAAIASKRVAEVEQQRDVAVNEAAYARAKLAAHGGSQQSTPSLDGQSHDLDKAASDRTTDLSRRLALALASQNELKSKLEALSTDLEQEKRGRELAEETSEATRRRLAELEMQNNPLETESLRAQLHQVEASFREESMLRSEAESSLKQLALDKEELSRKLEDSTNRLRDFGDNIGGLKQAVTASVEKASILEKKLDEERERREGLERKLLQLRSEHEERTAELENATRRLRDAEELAESHAREAEAHKNAFILGLERASSFDSETSIRSLVDQRVATSEAQVERANKLARASQAAADEAAEKLRRAEERIAGLEAYQEQASREGLQLRRQLQAALKDCQTYTAENRELKAQIENHQREAGALAVQHAALKDLLGERGYTDSRRSPRGESPGSRFGTPEQNRLRELEQQLSASLKAHDELKASFETREQETDRAYKEKLEQLENDYQSAVHYVKGTEKMLKRMKDELTRYKMQNAKIQSELEAAQSREGSVAPSGWEAERSQLQQSLTDLQQDTSRSITNLEEQITSLKESLASAEAEKEKSVAEYETMRQELLAVSEKTSSELEQLKHENSLLEARAMDAEQKVSMLLDQVEASVGHYRRQSQHGQGVNGISRTHSNASSGTIGAGTRRSRANSAVSQDDTFLDNRGSMALDSLANELEALRSHWESTNSNYRLSTQSDFDRTPTKDSGLSDSLAEWRRRLDEEEARAGSPEKGKPRTAAEGQAAANMI
Protein: Thymosin beta-4 (T beta 4) [Cleaved into: Hematopoietic system regulatory peptide (Seraspenide)] (P62329)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Scaffold protein ILK
- Profilin-4
- MK1
- Profilin-2
- Profilin-3
Sequence:
MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES
Protein: EG:BACR7C10.7 protein (Q9U1K9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MFAITVGIIIGCMICIAVFAGFQHEDVKFKTMLVSIVIVLIFQFLIGDPIKFVILSIDRALWPPRIYIPPRCDKDEMDEKEERRDFLKQRLINKRANLMLTSRYRNYKLNDQYKMIAHDLFIYGPYFLCLMCLVLVTRDQTLYHNTRIITDLFMYNHTDYTGLQEVYFLNQLFDFIESTLVLAFNSNSTESGSPGWAHAEQSVLLGVMRLRHVRVSNPQVGLGPPKFSDTYYMPDWQLPYRKLHYSDKYWRIYEPWIPIKMGFEFLDALLMNFDHVGSLNSYPELAGYVSLLARSAANSMKVIDYLSENHWLTLNTSAVFIDFTLYNVDKTPFGGIVPDVQVDSAKLLENVDQMPYTGLLALLIYVLVFIQFAQTLAVKLWYEPHLLKSVWNKLDLFIFMVNVLVVVLVVLRESLVASMMKKVEGASKMEFIDFRRPSRMHQLTTITIGFLICITTLRLWRVLQFASVFKLFTRTLYLAWSAVASTAIAIVIFLIGFCFAVVTINGNYSSNFNKLVKSMVMCMCYSFGFSAQVKPSELFHGGKWLGILCYGVLAFVIIVLLINVFVSLINDYFTVAKTIRDSERENRITFFEFLVVEFSGVLGRFRKLPCWRRNYVRNGRTVAENVSRKLDSMDRQRLMRRRLRQGRHHVSRPVSAEDALLEYKDRGDKMVNVHYILNIQLTLIRMFLFDEYVEWPQEQQKQPEAQDPDPNLGPDGSPPQDKRQDEAEA
Protein: U3 small nucleolar RNA-associated protein 25 (U3 snoRNA-associated protein 25) (U three protein 25) (P40498)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DEAD-box RNA helicase-like protein required for pre-18S rRNA processing, specifically at sites A0, A1, and A2.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- U3 small nucleolar RNA-associated protein MPP10
- Something about silencing protein 10
- Pre-rRNA-processing protein ESF2
- U3 small nucleolar ribonucleoprotein protein IMP4
- rRNA biogenesis protein RRP36
- U3 small nucleolar RNA-associated protein 21
- U3 small nucleolar ribonucleoprotein protein LCP5
- Probable ATP-dependent RNA helicase DHR2
- U3 small nucleolar RNA-associated protein 22
- Ribosome biogenesis protein SLX9
Sequence:
MSDSSVREKNDNFRGYRKRGRQELRKIKRSSARTEGGSTETLEDVAEDIDHRSDEDEVSDVDSGDDFDIEDEEGKKEKVYDALLTILKSEHPEPKRRRREADESNKAPAEVGEDEHENTEHGPVDDQLEIENGLLGNHEDDNDDDSSGDEKDIDSEDEQDPFESHFNQVPEKFVDKLSNAFKTKSVKYKSVKGSLSDSESYIYAKPVVIGEEALVESPYRSSSIYSYFLKQRLKVQNGLLDKKTDPLTALQKKLVDPMFQYKDILYEYDSYEKDEDEYRDLYALHVLNHIYKTRDRILKNNQRLQDNPDTEHLDQGFTRPKVLIVVPTREVAYRVVDKIISKSGIDQVDKKGKFYDQFRDDSLPPKSKPKSFQHIFRGNTNDFFVVGLKFTRKAIKLYSNFYQSDIIVCSPLGIQMILENTDKKKRQDDFLSSIELMVIDQLHSIEYQNISHIFTIFDHLNKIPDQQHEADFSRIRMWYINEQAKLFRQTMVFTKYISPAANSLINGRCRNMAGRWKNHKVIGSENSSIGQSGLKIRQIFQRFDIIGNSIIEEPDYRFKFFTSVIIPGIVKSTGYEDGILIYIPDYTDFIRIRNYMKEKTTILFGDINEYSSQRQLNANRSLFQQGRLKVMLYTERLHHYRRYEIKGVKSVVFYKPPNNPEFYNEVVRFIGKNAFLGNTDLNISTVRCIYSKLDGLSLERIVGTKRAAVLSHAQKEIYEFK
Protein: Early growth response factor homolog 1 (Q18250)
Organism: Caenorhabditis elegans
Function: Sequence-specific DNA-binding transcription factor (By similarity). Plays a role in oocyte development, acting cell-autonomously in the somatic gonad. Involved in negative regulation of oocyte MAPK activation and inhibits oocyte maturation and ovulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:20736289}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20736289}. Note=Perinuclear localization only observed in sperm. {ECO:0000269|PubMed:20736289}.
Interaction partners:
- Lipase
- C2H2-type domain-containing protein
- Putative steroid dehydrogenase 4
Sequence:
MALHEPPSKLNRHSHSNLLKPPSLNKPILTFADNDCLKTPTMNDMLKTPTVNSPRHTPMNIDGTPKVNGFSGFTPQTDQKFFGEHEPLFNQMHTTTLMPAPSSSYKEPAYSSEQPSSSSDEAKPKELLGSNSFGVPRMTNGNSKQKPEELTLKDIEISSTGPGGVDSPGLSAAMFQFSPMVEHFLQNLTNKAGLPELVVDSKTAGLNHQEPSDLIKSVQVRRSSIEDQKFSDVLHVPTLPRKTSEPSHLGSSLQNEHPQSNSRPSTVIPRVQRTNTSASLTRSMDHSSMSPISAHDDPYSNSASYSSLSTHTSFSDSASLAHFEPKTEPMDDYSYNFSDNDFNSFEFSSTSEELKNIGCQKMKSSKMPLQDRPYKCPRDGCDRRFSRSDELTRHIRIHTGQKPFQCRICMRAFSRSDHLTTHVRTHTGEKPFSCDICGRKFARSDERKRHTKVHKTSRSGS
Protein: Missing-in-metastasis, isoform E (A0A0B4JD47)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLSLERDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRHKAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDGLQSLMDSHMQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLPQASEELIHDAKASINLYPESPGGGSGSQGGGCSNSLGSRKSSVCSISSMNSSGSSNSPGHHHYPRSLSQFVTPAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPHSQDGVDTLPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSSLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKELSAAHHAQQQQQQQNQQPQTPPTYVNMSELATMAALKQTNQQQKPSTPPLQQQSSIDSTSSQHSNDSTGSHQLLQQQQQHHQSQQNHHSATATRSHSISSTASSLHSHPSIDSTVACGSLVGQHNHSTSTNTNTTSPSSGSSTPQNHYSPLLTNSPTSTAAGTPSGSSLGPGSGLGFVYQVSSPTPPSSEVLKITEQAAAGQDQGPANSVADETDERSRASVLQKASMFEKAAAAAAVSPPAPMQIASGSPASGGGTRRSEAEQQEMGGAAGGGSTRIGRRSSINQSKPPPPVRRSSSVTPSPNASVGTFRTSSPAAGGGGGGGIYAQPKLVNSMSSFRTSSPSPNGHAHPLPPTQPKANPNLIAQLNARLSGKQQQHQQQQHIEGIYGNQQAPGGESIYMRSGLSMSQPQQQQHFDDYATSTNIEKTGSIRAKTKAEFLENLNAKLAKQGMSGRAFAVRNLINSKALPDPRICHESLMDQIKRGATLKRNQKINDRSAPKIH
Protein: Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (QAPRTase) (QPRTase) (Q5I0M2)
Organism: Rattus norvegicus (Rat)
Function: Involved in the catabolism of quinolinic acid (QA).
Interaction partners:
- Nicotinamide-nucleotide adenylyltransferase
- Nicotinate phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide riboside kinase 1
- 3-hydroxyanthranilate 3,4-dioxygenase
- Nicotinamide riboside kinase 2
- Glutamine-dependent NAD
- Kynureninase
- NAD-capped RNA hydrolase NUDT12
- Cytosolic purine 5'-nucleotidase
Sequence:
MDPEGLQFLLPPASLAALANSWLQEDCPGLNFASLVTGSAPAQAVLWAKSPGVLAGRPFFDAIFTQLNCQVSWLLPEGSKLVPVVKVAEVRGPAHHLLLGERVALNTLARCSGIASAAATAVEVATSTGWAGHVAGTRKTTPGFRLVEKYGLLVGGAECHRYDLGGLVMVKDNHVVAAGSMEKAVLKARQAAGFPLKVEVECSSLKEALQAAEAGADLVMLDNFKPEELHPTAATLKAKFPNVSVEASGGVTLDNLPQFCGTNIDVISLGMLTQAAPALDFSLKLYAEGDIPVPHARRS