wanglab/gogpt-training-data huggingface dataset:
Protein: Proton myo-inositol cotransporter (H(+)-myo-inositol cotransporter) (Hmit) (H(+)-myo-inositol symporter) (Solute carrier family 2 member 13) (Q3UHK1)
Organism: Mus musculus (Mouse)
Function: H(+)-myo-inositol cotransporter. Can also transport related stereoisomers.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96QE2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96QE2}.
Interaction partners:
- Sodium/myo-inositol cotransporter
Sequence:
MSRKASEDVEYTLRSLSSLMGERRRRQPEPGAPGGERSLLAAESAASLQGAELERAARRQFQRDETPAFVYAAAAFSALGGFLFGYDTGVVSGAMLLLRRQMRLGAMWQELLVSGAVGAAAVAALAGGALNGALGRRSAILLASALCTVGSAVLAAAANKETLLAGRLVVGLGIGIASMTVPVYIAEVSPPNLRGRLVTINTLFITGGQFFASVVDGAFSYLQKDGWRYMLGLAAIPAVIQFLGFLFLPESPRWLIQKGQTQKARRILSQMRGNQTIDEEYDSIRNSIEEEEKEATAAGPIICRMLSYPPTRRALVVGCGLQMFQQLSGINTIMYYSATILQMSGVEDDRLAIWLASITAFTNFIFTLVGVWLVEKVGRRKLTFGSLAGTTVALIILALGFLLSAQVSPRVTFRPTTPSDQNTTCTGYSYCNECMLDPDCGFCYKINGSAVIDSSCVPVNKASTTEAAWGRCDNETKFKAEGAHWAYSFCPTPYSWTALVGLVLYLVFFAPGMGPMPWTVNSEIYPLWARSTGNACSAGINWIFNVLVSLTFLHTAEYLTYYGAFFLYAGFAAVGLLFVYGCLPETKGKKLEEIESLFDHRLCSCGAADSDEGRYIEYIRVKGSNYHLSDNDASDVE
Protein: Zinc finger protein 644a (A2BIH4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Low density lipoprotein receptor-related protein-associated protein 1.
- Euchromatic histone-lysine N-methyltransferase 2.
- procollagen-proline 3-dioxygenase
- Solute carrier family 39 member 5.
- DDE_Tnp_1_7 domain-containing protein.
- Si:dkeyp-53e4.4.
- Coiled-coil domain-containing 24.
- Protein SCO2 homolog
Sequence:
MSALKESAKVEENDISMSSISQDLLSNQSFSVEGTTSGPSVHCLHETMELLSDQGDLLSSVSFIDSICSDGPAKAAYVNGSTSPHISDEILLDISKNVPGFLPKSLHAQNSVTTNVHFEGADPLRKEGEITIRQTLTAEDVENRGIWGFDNESPEASLDNYDDANDLGWNPQREFMKFLWDDDNGLDIEEKLSPVPSPINQKRRVPSPIVHKRRRRKEKLVLKVDPSEDPFSDLNLDSKQDHPGEGSPIEFGPVKKTRSPRKPSKLQSPIVKNTKYFNGTAEAVKHLFPKPAKKPLSKTQKIGLIRETLSSDSEGPTFFQQNNDFKEKSLGQNQITCNKDTTSSKPFVCKECGQCYYDRSSLLNHISVHQDKGKKLNQFHQIKDEGKDAKLQCPQCNFGTNCPNTFVQHAKTHEKDKRYYSCNKCDFVEMNEDDLRRHLYHKHGVIGADHTVWKSDGFQERKVNKSPCLNSYSPSFERKTKNSVGNHVEEEQVNSHSLDSGDEEPPTTEQSFSACNVLTSCAKPKARSPRLLVKFGAPDEENNLSNDKCGLLRKKKRVGESKLDKSIHTLLSRKKRRDKSGSEIDTHQEPAKSSTKEFLDRSLNCETTFSETSSPPSKYLKRSAHSKEGNTKRTSKFDVNVTCSEDAGKTHLGLEKQTLKKSPSKRKMSTPFHNMQGQDILLDFPKCRQKFKKPQATRRRKVLINNSDILSVSSDALGPEECEMDKNANARLVKRRSSSSKASLGASASHFERNHSSPRVLSVKDEYKDEEISESITAVKLEPSSDVETDLKGCPYCPAVFESGISLSNHIRGHLHRVGLKVRRAPVKSAVKVASDKVPPVRRQALSQVKTEEDTSQTDHPAELPTDCQQTELICPLCREWFDNRTGLSNHVRGHLKRLGKPTSTASKSPVIILKELMRDKKQFQLKLQVLEKKCRTTNTFYPVRLGNGLTFASTVKRQKDDKEEKKRLEINKGSPPSDLIGILKKRRAHEEAKAKHQSLTAKKALSLTSGKDCGLEIHTCKAVPSSPGEKGDNKRNVCVHCNASFHSGISLSNHLRGYSQRKRKALQDGATLDCKQRKQRARPWSKKKAFSLMHNPEEIYRLTCRFCDLVFQGPLSVQEDWIKHLQRHIMNTAVPHTGAGMVEVTSFPKDYCPITVPHAQSSVMQTSS
Protein: Kinesin family member 13B (E9Q4K7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- ArfGAP with dual PH domains 1
- Disks large homolog 4
- Disks large homolog 1
- Guanylate kinase
Sequence:
MGDSKVKVAVRVRPMNRREIDLHTKCVVDVEANKVILNPVNTNLSKGDARGQPKIFAYDHCFWSMDESVREKYAGQEDVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQGAGKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNEDPNARIIRDLREEVEKLREQLTKAEAMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQTSGIKVGDDKCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHGIIDITPEGQVVLTPQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKKKAEREDEDREASLKNDSSSEQLDADGDSSSEVSSEINFNFEYAQMEVTMKALGSNDPMQSILSSLEQQHEEEKRSALERQRLMYEHELEQLRRRLSPERQNCRGVDRLSFHSPSAQQRLKQWAEEREATLNNSLMRLREQIVKANLLVREASYIAEELDKRTEYKVTLQIPTSSLDANRKRGSLLSEPAIQVRRKGKGKQIWSLEKLENRLLDMRDLYQEWKECEEDSPVSRSYFKRADPFYDEQENHSLIGVANVFLETLFYDVKLQYAVPIINQKGEVAGRLHVEVMRLSGAIGERIAGGDDPTEVSSEKEAQENRLVCMVKILQATGLPQHLCHFVFCKYDFWDQQEPVTVAPEVDTSSSPTSKQPQCMVVFDHCSEFSVNITEDFIEYLSEGALAIEVYGHKMNDPRKNPALWDLGIIQAKTRSLRDRWSEVTRKLEFWVQILEQNENGDYCPVEVIAAKDVPTGGIFQLRQGQSRRVQVEVKSVQESGTLPLMEECILSVGIGCVKVRPLRSPKIHENVHEEEEDMDSYQDRDLERLRRKWLNALTKRQEYLDQQLQKLVSKHDKTEDDADREAQLLEMRLTLTEERNAVMVPSAGSGIPGAPAEWTPVPGMETHIPVIFLDLNADDFSSQDNLDDPEAGWDATLTGEEEEEFFELQIVKQHDGEVKAEASWDSAVHSCPQLSKGTPADERVFLILRVTVQLSHPADMQLVLRKRICVHVHGRQGFAQSLLKKMSHRSSIPGCGVTFEIVSNIPEDAQGVEEREALARMAANVENPASADSEAYIEKYLRSVLAVENLLTLDRLRQEVAVKEQLTGKGKLSRRSISSPSMNRLSGSRQELSPSHSLGSNKGRWESQQDVSQTLVSRGIAPGPPALSVSPQNNQSPDPGLGGVAASYLNPVKSLVPQMPKLLKSLFPVRDDRRGRHSSPLAHQPVPRILVQPTFSDTWATRTEEVSHQVGAAPLAEVMAAPAVKICDKPVKVSSPPSPMVVTQPPEGQDGPPSPLSEASSGYFSHSVSSATLSETLTLGLDTTGLGSQTPGSPPALCQVTPEPELAFLSCTQSHPPAPEEAHVPAAPTQSTELEVPRAPLLSEPASAVPTSPFRIRKVRTSELKSFTGMLGGASSGAEEDPLASEDPSNARGQTLGRLEVTSDSEDASEVPEWLREGEYVVVGTNKTGIVRYIGPTDFQEGTWIGVELDLPAGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRAVGTGRRRSSGLQPQGAPEVRRSATISGSATNLASLTAALAKGDRSYKNPENRKSWAS
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad-1 (Oligosaccharyl transferase subunit dad-1) (Defender against cell death 1) (Protein dad-1) (P52872)
Organism: Caenorhabditis elegans
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Possesses cell death-inhibiting activity. Suppresses some programmed cell death in C.elegans.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Translocon Sec61/SecY plug domain-containing protein
- Protein transport protein Sec61 subunit beta
- Dol-P-Glc:Glc
- Translocon-associated protein subunit beta
Sequence:
MAAQVVPVLSKLFDDYQKTTSSKLKIIDAYMTYILFTGIFQFIYCLLVGTFPFNSFLSGFISTVTSFVLASCLRMQVNQENRSEFTAVSTERAFADFIFANLILHLVVVNFLG
Protein: Syntaxin VAM3 (Vacuolar morphogenesis protein 3) (Q12241)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vacuolar assembly. Provides the t-SNARE function in a late step of the vacuolar assembly. Required for homotypic vacuole membrane fusion, autophagy and fusion of biosynthetic transport vesicles with the vacuole. Required for the delivery of alpha-factor receptor-ligand complexes to the vacuole.
Subcellular location: Vacuole membrane; Single-pass type IV membrane protein.
Interaction partners:
- t-SNARE VTI1
- Vacuolar v-SNARE NYV1
- Vacuolar protein sorting-associated protein 16
- Vacuolar protein sorting-associated protein 33
- Synaptobrevin homolog YKT6
- Synaptobrevin homolog 2
- Vacuolar membrane protein PEP3
- Vacuolar protein sorting-associated protein 41
- Protein transport protein SFT1
- E3 ubiquitin-protein ligase PEP5
Sequence:
MSFFDIEAQSSKGNSQQEPQFSTNQKTKELSNLIETFAEQSRVLEKECTKIGSKRDSKELRYKIETELIPNCTSVRDKIESNILIHQNGKLSADFKNLKTKYQSLQQSYNQRKSLFPLKTPISPGTSKERKDIHPRTEAVRQDPESSYISIKVNEQSPLLHNEGQHQLQLQEEQEQQQQGLSQEELDFQTIIHQERSQQIGRIHTAVQEVNAIFHQLGSLVKEQGEQVTTIDENISHLHDNMQNANKQLTRADQHQRDRNKCGKVTLIIIIVVCMVVLLAVLS
Protein: Protocadherin alpha-1 (PCDH-alpha-1) (Q9Y5I3)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Protocadherin alpha-3
- Protocadherin alpha-11
Sequence:
MVFSRRGGLGARDLLLWLLLLAAWEVGSGQLHYSIPEEAKHGTFVGRVAQDLGLELAELVPRLFRVASKTHRDLLEVNLQNGILFVNSRIDREELCQWSAECSIHLELIADRPLQVFHVEVKVKDINDNPPVFRGREQIIFIPESRLLNSRFPIEGAADADIGANALLTYTLSPSDYFSLDVEASDELSKSLWLELRKYLDREETPELHLLLTATDGGKPELQGTVELLITVLDVNDNAPLFDQAVYRVHLLETTANGTLVTTLNASDADEGVNGEVVFSFDSGISRDIQEKFKVDSSSGEIRLIDKLDYEETKSYEIQVKAVDKGSPPMSNHCKVLVKVLDVNDNAPELAVTSLYLPIREDAPLSTVIALITVSDRDSGANGQVTCSLMPHVPFKLVSTFKNYYSLVLDSALDRESLSVYELVVTARDGGSPSLWATARVSVEVADVNDNAPAFAQPEYTVFVKENNPPGCHIFTVSARDADAQENALVSYSLVERRVGERALSNYVSVHAESGKVYALQPLDHEELELLQFQVSARDAGVPPLGSNVTLQVFVLDENDNAPALLAPRVGGTIGAVSELVPRLVGAGHVVAKVRAVDADSGYNAWLSYELQPAAGGARIPFRVGLYTGEISTTRVLDEADLSRYRLLVLVKDHGEPALTATATVLVSLVESGQAPKASSRASVGVAGPEAALVDVNVYLIIAICAVSSLLVLTLLLYTALRCSVPPTEGAYVPGKPTLVCSSALGSWSNSQQRRQRVCSSEGPPKTDLMAFSPGLSPSLNTSERNEQPEANLDLSGNPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPTNSQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
Protein: Phenolphthiocerol/phthiocerol polyketide synthase subunit E (EC 2.3.1.292) ((Phenol)carboxyphthiodiolenone synthase subunit E) (Beta-ketoacyl-acyl-carrier-protein synthase I) (Phthiocerol synthesis polyketide synthase type I PpsE) (Q7TXL6)
Organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Function: Part of the PpsABCDE complex involved in the biosynthesis of the lipid core common to phthiocerols and phenolphthiocerols by successive additions of malonyl-CoA or methylmalonyl-CoA extender units. PpsA can accept as substrate the activated forms of either icosanoyl (C20), docosanoyl (C22) or lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-hydroxyphenyl)-C19 fatty acyl from FadD29 (By similarity). PpsA initiates the biosynthesis and extends its substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins add the second and third malonyl-CoA extender units. PpsD adds an (R)-methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product (By similarity).
Interaction partners:
Sequence:
MSIPENAIAVVGMAGRFPGAKDVSAFWSNLRRGKESIVTLSEQELRDAGVSDKTLADPAYVRRAPLLDGIDEFDAGFFGFPPLAAQVLDPQHRLFLQCAWHALEDAGADPARFDGSIGVYGTSSPSGYLLHNLLSHRDPNAVLAEGLNFDQFSLFLQNDKDFLATRISHAFNLRGPSIAVQTACSSSLVAVHLACLSLLSGECDMALAGGSSLCIPHRVGYFTSPGSMVSAVGHCRPFDVRADGTVFGSGVGLVVLKPLAAAIDAGDRIHAVIRGSAINNDGSAKMGYAAPNPAAQADVIAEAHAVSGIDSSTVSYVECHGTGTPLGDPIEIQGLRAAFEVSQTSRSAPCVLGSVKSNIGHLEVAAGIAGLIKTILCLKNKALPATLHYTSPNPELRLDQSPFVVQSKYGPWECDGVRRAGVSSFGVGGTNAHVVLEEAPAEASEVSAHAEPAGPQVILLSAQTAAALGESRTALAAALETQDGPRLSDVAYTLARRRKHNVTMAAVVHDREHAATVLRAAEHDNVFVGEAAHDGEHGDRADAAPTSDRVVFLFPGQGAQHVGMAKGLYDTEPVFAQHFDTCAAGFRDETGIDLHAEVFDGTATDLERIDRSQPALFTVEYALAKLVDTFGVRAGAYIGYSTGEYIAATLAGVFDLQTAIKTVSLRARLMHESPPGAMVAVALGPDDVTQYLPPEVELSAVNDPGNCVVAGPKDQIRALRQRLTEAGIPVRRVRATHAFHTSAMDPMLGQFQEFLSRQQLRPPRTPLLSNLTGSWMSDQQVVDPASWTRQISSPIRFADELDVVLAAPSRILVEVGPGGSLTGSAMRHPKWSTTHRTVRLMRHPLQDVDDRDTFLRALGELWSAGVEVDWTPRRPAVPHLVSLPGYPFARQRHWVEPNHTVWAQAPGANNGSPAGTADGSTAATVDAARNGESQTEVTLQRIWSQCLGVSSVDRNANFFDLGGDSLMAISIAMAAANEGLTITPQDLYEYPTLASLTAAVDASFASSGLAKPPEAQANPAVPPNVTYFLDRGLRDTGRCRVPLILRLDPKIGLPDIRAVLTAVVNHHDALRLHLVGNDGIWEQHIAAPAEFTGLSNRSVPDGVAAGSPEERAAVLGILAELLEDQTDPNAPLAAVHIAAAHGGPHYLCLAIHAMVTDDSSRQILATDIVTAFGQRLAGEEITLEPVSTGWREWSLRCAALATHPAALDTRSYWIENSTKATLWLADALPNAHTAHPPRADELTKLSSTLSVEQTSELDDGRRRFRRSIQTILLAALGRTIAQTVGEGVVAVELEGEGRSVLRPDVDLRRTVGWFTTYYPVPLACATGLGALAQLDAVHNTLKSVPHYGIGYGLLRYVYAPTGRVLGAQRTPDIHFRYAGVIPELPSGDAPVQFDSDMTLPVREPIPGMGHAIELRVYRFGGSLHLDWWYDTRRIPAATAEALERTFPLALSALIQEAIAAEHTEHDDSEIVGEPEAGALVDLSSMDAG
Protein: DNA gyrase subunit A (EC 5.6.2.2) (Q59556)
Organism: Mycolicibacterium smegmatis (Mycobacterium smegmatis)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state; also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. At comparable concentrations has a stronger decatenation activity than E.coli, which is inhibited by ciprofloxacin and novobiocin. Cleaves dsDNA at the sequence 5'-AT/GGCC-3', leaving a 4 base overhang. Relaxes negatively supercoiled DNA in an ATP-independent manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:12000834}.
Interaction partners:
Sequence:
MTDTTLPPEGEAHDRIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMYDSASSDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSRGIAVGMATNNPPHNLGELAEAVYWCLENYEADEEATCEAVMERVKGPDFPTSGLIVGTQGIEDTYKTGRGSIKMRGVVEIEEDSRGRTSIVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVVELKRDAVAKVVLNNLYKHTQLQTSFGANMLSIVDGVPRTLRLDQLIRLYVDHQLDVIVRRTRYRLRKANERAHILRGLVKALDALDEVIALIRASQTVDIARAGLIELLDIDDIQAQAILDMQLRRLAALERQKIVDDLAKIEAEIADLEDILAKPERQRGIVRDELKEIVDKHGDARRTRIVPADGQVSDEDLIAREDVVVTITETGYAKRTKTDLYHSQKRGGKGVQGAGLKQDDMVNHFFVCSTHDWILFFTTQGRVYRAKAYELPEASRTARGQHVANLLAFQPEERIAQVIQIKSYEDAPYLVLATRNGLVKKSKLSDFDSNRSGGIVAINLREGDELVGAVLCSAEDDLLLVSANRQSIRFSATDEALRPMGRATSGVQGMRFNEDDRLLSLNVVRPDTYLLVATSGGYAKRTSIDEYSVQGRGGKGILTIQYDRKRGSLVGALIVDDDTELYAITSTGGVIRTAARQVRKAGRQTKGVRLMNLAEGDTLIAIARNGRGRGGRVDQRIRRGHRRVTRGVMETLRSRKVLGPS
Protein: Mitochondrial RNA binding complex 1 subunit (Q389W5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRCKLWLQGKGLTTLISAVSSCRVALASEDVYKICALLKAKEDTLHLQTNQSFIHGLHVQYKKLDPEEVTPFQKSFIDGTFAAFPLSPDLLVASSQTGKNEGSDITNIQAGETSISPVVASGTVVEKCPHAGLGSGGETEVEERLAAVWDIVQECQKSNFVGTDGIQKIQVHCKALERHLRRMRPFEIVSLVRALATINYQDYALTNLLARRSCEVASKLSSSEVCRTYFNLSKLQSHDSMVAFVNQIEIQMDNLHRDQVQFVAMALERQPQIASAPARMVPKLLARAVTLLHEVNDAAYHRSLLVVAARYNLRRHPAVPKIIANVTKHLGSVSDRDLLTMLQSAVDLEISAGTTGMSELLERTETAVDTVEVRSLDTLVDILSVLPVDTGKIMERLLNRLTVDAGKLSIPQLALTLDLLSGYPAARGHPCIAALAFAASMRADSFDGEALEQLLLNLGQLGQFSDDFYALVQVLQNVKGGFRSAEKLFELMRCCTRDVVSDVRGQDMITRGILGLAPGMNDENLSEARKLLVQLGVDDKNVHQIIFRRAKQIQRESGSRWGRRGYDVSGDTM
Protein: Syndecan-3 (SYND3) (Q64519)
Organism: Mus musculus (Mouse)
Function: Cell surface proteoglycan that may bear heparan sulfate. May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Pleiotrophin
- Tenascin
- Glial cell line-derived neurotrophic factor
- Proto-oncogene tyrosine-protein kinase Src
- Neurturin
- Artemin
- Src substrate cortactin
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Glypican-4
- Versican core protein
Sequence:
MKPGPPRRGTAQGQRVDTATHAPGARGLLLPPLLLLLLAGRAAGAQRWRNENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGLETAMRFIPDMALAAPTAPAMLPTTVIQPVDTPFEELLSEHPSPEPVTSPPLVTEVTEVVEESSQKATTISTTTSTTAATTTGAPTMATAPATAATTAPSTPEAPPATATVADVRTTGIQGMLPLPLTTAATAKITTPAAPSPPTTVATLDTEAPTPRLVNTATSRPRALPRPVTTQEPDVAERSTLPLGTTAPGPTEMAQTPTPESLLTTIQDEPEVPVSGGPSGDFELQEETTQPDTANEVVAVEGAAAKPSPPLGTLPKGARPGPGLHDNAIDSGSSAAQLPQKSILERKEVLVAVIVGGVVGALFAAFLVTLLIYRMKKKDEGSYTLEEPKQASVTYQKPDKQEEFYA
Protein: Beta-galactosidase 7 (Lactase 7) (EC 3.2.1.23) (Q9SCV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- RING-type E3 ubiquitin transferase
- La-related protein 6C
Sequence:
MKMKHFTRLLSLFFILITSLSLAKSTIVSHDERAITINGKRRILLSGSIHYPRSTADMWPDLINKAKDGGLDAIETYVFWNAHEPKRREYDFSGNLDVVRFIKTIQDAGLYSVLRIGPYVCAEWNYGGFPVWLHNMPNMKFRTVNPSFMNEMQNFTTKIVKMMKEEKLFASQGGPIILAQIENEYGNVISSYGAEGKAYIDWCANMANSLDIGVPWLMCQQPNAPQPMLETCNGFYCDQYEPTNPSTPKMWTENWTGWFKNWGGKHPYRTAEDLAFSVARFFQTGGTFQNYYMYHGGTNFGRVAGGPYITTSYDYHAPLDEFGNLNQPKWGHLKQLHTVLKSMEKSLTYGNISRIDLGNSIKATIYTTKEGSSCFIGNVNATADALVNFKGKDYHVPAWSVSVLPDCDKEAYNTAKVNTQTSIMTEDSSKPERLEWTWRPESAQKMILKGSGDLIAKGLVDQKDVTNDASDYLWYMTRLHLDKKDPLWSRNMTLRVHSNAHVLHAYVNGKYVGNQFVKDGKFDYRFERKVNHLVHGTNHISLLSVSVGLQNYGPFFESGPTGINGPVSLVGYKGEETIEKDLSQHQWDYKIGLNGYNDKLFSIKSVGHQKWANEKLPTGRMLTWYKAKFKAPLGKEPVIVDLNGLGKGEAWINGQSIGRYWPSFNSSDDGCKDECDYRGAYGSDKCAFMCGKPTQRWYHVPRSFLNASGHNTITLFEEMGGNPSMVNFKTVVVGTVCARAHEHNKVELSCHNRPISAVKFASFGNPLGHCGSFAVGTCQGDKDAAKTVAKECVGKLNCTVNVSSDTFGSTLDCGDSPKKLAVELEC
Protein: Serine/threonine-protein kinase H1 (EC 2.7.11.1) (Protein serine kinase H1) (PSK-H1) (Q91YA2)
Organism: Mus musculus (Mouse)
Function: May be a SFC-associated serine kinase (splicing factor compartment-associated serine kinase) with a role in intranuclear SR protein (non-snRNP splicing factors containing a serine/arginine-rich domain) trafficking and pre-mRNA processing.
Subcellular location: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus speckle {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized in the brefeldin A- sensitive Golgi compartment, at centrosomes, in the nucleus with a somewhat speckle-like presence, membrane-associated to the endoplasmic reticulum (ER) and the plasma membrane (PM), and more diffusely in the cytoplasm. Found to concentrate in splicing factor compartments (SFCs) within the nucleus of interphase cells. The acylation-negative form may be only cytoplasmic and nuclear. Acylation seems to allow the sequestering to the intracellular membranes. Myristoylation may mediate targeting to the intracellular non-Golgi membranes and palmitoylation may mediate the targeting to the Golgi membranes. Dual acylation is required to stabilize the interaction with Golgi membranes (By similarity). {ECO:0000250}.
Interaction partners:
- Neuronal migration protein doublecortin
Sequence:
MGCGTSKVLPEPPKDVQLDLVKKVEPFSGTKNDVYKHFITEVDSVGPLKAGFPATSQYAPPCPGVPNTGHTAPPSEPPRRARVAKYRAKFDPRVTAKYDIKALIGRGSFSRVVRVEHRATRQPYAIKMIETKYREGREVCESELRVLRRVRHANIIQLVEVFETQERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVRYLHALGITHRDLKPENLLYYHPGTDSKIIITDFGLASARKKGDDCLMKTTCGTPEYIAPEVLVRKPYTNSVDMWALGVIAYILLSGTMPFEDDNRTRLYRQILRGKYSYLGEPWPSVSNLAKDFIDRLLTVDPGARMTALQALRHPWVVSMAASSSMKNLHRSISQNLLKRASSRCQSTKSSQSTRSSRSTRSNKSRRVRERELRELNLRYQQQYNG
Protein: dual-specificity kinase (EC 2.7.12.1) (D1L3Y5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- DDB1- and CUL4-associated factor 7
- E3 ubiquitin-protein ligase RNF169
Sequence:
MSSQHSHPSFSNIHSMADQQQVLSDMTILQRRIPPSFRDPASAPLRKLSVDLIKTYKHINEVYYTKKKRRAQQVPPEDSSTKKERKVYNDGYDDDNYDYIVKNGEKWLDRYEIDSLIGKGSFGQVVKAYDHHEQEWVAIKIIKNKKAFLNQAQIELRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGSNEVDQMNKIVEVLGVPPNHMLDQAPKARKYFDKLSDGLWTVKKNKDIKKEYKPPATRRLHEILGVETGGPGGRRAGEQGHAPCDYLKFKDLILRMLDYDPKTRITPFYALQHNFFKKTTDEGTNTSSSTSTSPAMDHSHSTSTTSSVSSSGGSSGSSNDNRNYRYSNRYYNSAVTHTDYEMQSPQAPSQQQLRIWPGGDSSMGQLSNSGSDSSYPQLLLHKPAATQHSRHFLGNIGGMMEPHHPHPIYGSHHSNGRQLRQQQQQQNQPQGQASQGQQGTALMPVSSPQMQDSIELSLTHHHHLGQSSIMQPPPSSLDSSQYGSSNLHLGLSAFRTRTVMAPQQPPSASQQQLPQAPASQDSMVAASGLGYIPPCYAGSNNNNNPPQGSVGVGAMLTGGPPPRGVGGAGGRPDSEESSMMAVCGSGSGSGQSAANS
Protein: NFKB inhibitor epsilon (NFKBIE protein) (cDNA FLJ61640, highly similar to NF-kappa-B inhibitor epsilon) (Q7LC14)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEARKGPDEAEESQYDSGIESLRSLRSLPESTSAPASGPSDGSPQPCTHPPGPVKEPQEKEDADGERADSTYGSSSLTYTLSLLGGPEAEDPAPRLPLPHVGALSPQQLEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRPEPGRGTSHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDDLKISGKLLLCTD
Protein: Regulator of hypoxia-inducible factor 1 (Q9XVW1)
Organism: Caenorhabditis elegans
Function: Involved in the response to variation in environmental oxygen levels by inhibiting hif-1-mediated gene transcription in a vhl-1-independent manner. Plays a role in susceptibility to killing mediated by P.aeruginosa and by pore-forming toxins produced by B.thuringiensis. Probably by preventing hif-1 transcriptional activity, regulates behavioral responses, such as locomotion speed following acute reoxygenation. Plays a role in normal egg-laying probably by regulating spermatogenesis and in body morphogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16980385}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase
- Hypoxia-inducible factor prolyl hydroxylase
- von Hippel-Lindau tumor suppressor homolog
- Cysteine synthase 1
- HIG1 domain-containing protein
- Nuclear hormone receptor family member nhr-57
Sequence:
MSSSPHTHTLIIMERLSEVRLYSSPMTSVLNSNLSSCLTNAFIPDTVRMASSPLLAWMTLVVIGTLAPVSVFSCLSLKRSVKELLTERSSKLDVLDIFRFVAILWVMLNHTGSEGRIDILDRLPSADAFKSAMHDHPIFGALMGNSALGVEIFLVLSGLLAARSWLRKADEPFFQHWKSFIARRLLRLAPSMFIFVYIAAGPIMNALLPRYSSSMVSACGFWGILSHVTFTSNWQSTPTCMGYLWYLGLDMQLYMVAPIFLNLLHKFPKRGMALTITTIIASMVIRAGYCTAYGTCNQSDVDIPFISYPGQDAETLKSIYAGLWDMYSRPYTKCGPFLIGLLLGYITVSSKYIMVSTTSKTLFRSSLIVAIATIYAILPEYWNPNAGNTLYNTVYTAVFRSVFAMAISGMIAALYFRQEYRPTNPIFAMLAKLTYNAYLLHMPVVYIFNWLPFLQAATSPIHLLLVLPFVAILSFIAALIFYLFIEAPIGHLTSQYATRLGL
Protein: Magnetosome formation protease MamE (EC 3.4.21.-) (Magnetochrome MamE) (Magnetosome serine protease MamE) (Q2W8Q8)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Acts at 2 distinct steps of magnetosome formation; required for correct localization of proteins to the magnetosome while the protease activity is required for maturation of small magnetite crystals into larger, functional ones. The 2 functions are separable by mutation. Probably cleaves at least itself, MamO and MamP; cleavage requires the putative transport domain of MamO (Probable). Involved in localization of some proteins (at least MamA, MamC, MamF, MamI and MamJ) to the magnetosome.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:20161777, ECO:0000305|PubMed:21414040}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Magnetosome protein MamH
- Magnetosome protein MamI
- Actin-like protein MamK
- Magnetosome-associated protein MamJ
- Magnetosome protein MamM
- Magnetosome protein MamN
- Trypsin-like serine protease
- Magnetosome protein MamL
- Magnetosome protein MamB
- Multi-heme protein MamP
Sequence:
MAMFNGDVEDGGRGDASCGKDLKRYLMLMGVVALVVLFGAFIYRQSSGGLRLGAMLEQMGRGTGPAVNVPVQQGGPSAAVNPAMSVPAGARVAPPSAAGAIATMPPMVDFGPAPIGAGGPFSSVVTLLRNSVVAVTASSANGQAMPDPLGLANPDGLPHFANPATRSVENIGTGVIVRNDGFIVTNYHVVRGANSVFVTVQDDVGSTRYSAEIIKMDEALDLALLKVAPKTPLTAAVLGDSDGVQVADEVIAIGTPFGLDMTVSRGIISAKRKSMVIEGVTHSNLLQTDAAINQGNSGGPLVISNGTVVGINTAIYTPNGAFAGIGFAVPSNQARLFILDEVGWLPTSTAEGASMGLVAMQRPMGGGVGAAGPAIFAGTRAPHTDGRQNMDCTTCHDLIPAGNGRPAPMMPIAAPIPPPPIPMGAVSPHTDGRQNMNCANCHQMLGGAAPIAAPGLGGGAYRFAQPPGSLAINIQGPRGGQSTAAGTGRVTLLGAALTPMSQRLGAQTGVPVGRGVFISGVTPNTPAATAGLRPGDVLLKVDGRPVRLPEEVSAIMVEMHAGRSVRLGVLRDGDVRNMTLVAGPAGLAAAAVQAPAIADMAQPPMGGMAPTAPGMVAVPGGPAVMPKPPTEFNWLGMEIETFQAPRPITGVPGAVPVPGAKGAQVAEVLVGSRAAVAGLQANDLILEVNNRPVAGPARLDAAIKGATNAGQQILLKVNRNGQEFWIVL