wanglab/gogpt-training-data huggingface dataset:
Protein: TATA box binding protein (A0A8I6AFF5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPVQNTNSLSILEEQQRQQQQQQQQQQQQQQQAVATAAASVQQSTSQQPTQGASGQTPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT
Protein: Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (P41390)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Bifunctional purine biosynthetic protein ADE1
- Phosphoribosylformylglycinamidine synthase
- Phosphoribosylglycinamide formyltransferase
- Glutamine synthetase
- Carbamoyl phosphate synthase arginine-specific small chain
- Multifunctional protein ura1
- Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial
- Phosphoribosylaminoimidazole carboxylase
- Probable glutamine--fructose-6-phosphate aminotransferase
- Glutamate synthase
Sequence:
MCGILALMLADPHQQACPEIYEGLYSLQHRGQDAAGIVTAGNKGRLYQCKGSGMVADVFSQHQLRQLVGSMGIGHLRYPTAGSCAHSEAQPFYVNSPYGLVLGHNGNLINGPELRRFLDTEAHRHVNTGSDSELLLNIFAYELQRLDKFRINENDIFEALRNVYDRVNGGYACVAMIAGLGVLGFRDPNGIRPLVIGERDTPEGKDYMLASESVVLTQFGYRTFRDIRPGECVFIRRSNREDILAGFRGPRLFSRQILPCLRFTPDIFEYVYFARPDSVIDGLSVYQSRLNMGEKLAHTIMKRFGPDYMEKIDAVIPVPDSARTSALALAQTAQLPYVEAFIKNRYIGRTFIMPGQQIRRKSVRRKLNVQPQEFFDKNVLIVDDSIVRGTTSREIVQMARESGAKNVYLASCAPMITHPHVYGIDLADCKDLIAYGKTEDEVAEAISADGVIYQTLEDLLDSCRTAELTEFEVGLFTGEYTTGASKEYLVHLEQMRIANNRARKHSFAEDEEREAPEDISLHNTHSDVTFDFV
Protein: Dentin matrix acidic phosphoprotein 1 (DMP-1) (Dentin matrix protein 1) (Q13316)
Organism: Homo sapiens (Human)
Function: May have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite.
Subcellular location: Nucleus {ECO:0000269|PubMed:12615915}. Cytoplasm {ECO:0000269|PubMed:12615915}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12615915}. Note=In proliferating preosteoblasts it is nuclear, during early maturation stage is cytoplasmic and in mature osteoblast localizes in the mineralized matrix. Export from the nucleus of differentiating osteoblast is triggered by the release of calcium from intracellular stores followed by a massive influx of this pool of calcium into the nucleus.
Interaction partners:
- Matrix extracellular phosphoglycoprotein
- Matrix metalloproteinase-9
- Dentin sialophosphoprotein
- Integrin-binding sialoprotein
- Osteopontin
- Integrin alpha-V
- Integrin beta-3
- Fibroblast growth factor 23
- Stromelysin-1
- Phosphate-regulating neutral endopeptidase PHEX
Sequence:
MKISILLMFLWGLSCALPVTRYQNNESEDSEEWKGHLAQAPTPPLESSESSEGSKVSSEEQANEDPSDSTQSEEGLGSDDHQYIYRLAGGFSRSTGKGGDDKDDDEDDSGDDTFGDDDSGPGPKDRQEGGNSRLGSDEDSDDTIQASEESAPQGQDSAQDTTSESRELDNEDRVDSKPEGGDSTQESESEEHWVGGGSDGESSHGDGSELDDEGMQSDDPESIRSERGNSRMNSAGMKSKESGENSEQANTQDSGGSQLLEHPSRKIFRKSRISEEDDRSELDDNNTMEEVKSDSTENSNSRDTGLSQPRRDSKGDSQEDSKENLSQEESQNVDGPSSESSQEANLSSQENSSESQEEVVSESRGDNPDPTTSYVEDQEDSDSSEEDSSHTLSHSKSESREEQADSESSESLNFSEESPESPEDENSSSQEGLQSHSSSAESQSEESHSEEDDSDSQDSSRSKEDSNSTESKSSSEEDGQLKNIEIESRKLTVDAYHNKPIGDQDDNDCQDGY
Protein: ATP synthase F(0) complex subunit g, mitochondrial (ATPase subunit g) (ATP synthase membrane subunit g) (Q9CPQ8)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
Sequence:
MAKFIRNFAEKAPSMVAAAVTYSKPRLATFWHYAKVELVPPTPAEIPTAIQSVKKIIQSAKTGSFKHLTVKEAVLNGLVATEVWMWFYIGEIIGKRGIVGYDV
Protein: DNA helicase (EC 3.6.4.12) (A0A2R8Y5J0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKELGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKKKKKDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDLEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESIEGEKEVKSTAPETAIECTQAPAPASEDEKVVVEPPEGEEKVEKAEVKERTEEPMETEPKGAADVEKVEEKSAIDLTPIVVEDKEEKKEEEEKKEVMLQNGETPKDLNDEKQKKNIKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKVLKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPTPQQVAQQQ
Protein: PsbP domain-containing protein 6, chloroplastic (OEC23-like protein 1) (Q9LXX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the redox regulation of photosystem II.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:11826309, ECO:0000269|PubMed:18431481}.
Interaction partners:
- PsbP domain-containing protein 5, chloroplastic
- PsbP-like protein 1, chloroplastic
- Photosynthetic NDH subunit of lumenal location 1, chloroplastic
- PsbP domain-containing protein 3, chloroplastic
- Thylakoid lumenal 19 kDa protein, chloroplastic
- Photosynthetic NDH subunit of lumenal location 2, chloroplastic
- Chlorophyll a-b binding protein
- Oxygen-evolving enhancer protein 2-1, chloroplastic
- Tagatose-6-phosphate ketose/aldose isomerase, putative
- Uncharacterized protein At5g19190
Sequence:
MATASLVPTSKIFSVSPKSSASIKARSRVVVASSQQQQQPRRRELLLKSAVAIPAILQLKEAPISAAREVEVGSYLPLSPSDPSFVLFKAKPSDTPALRAGNVQPYQFVLPPNWKQLRIANILSGNYCQPKCAEPWIEVKFENEKQGKVQVVASPLIRLTNKPNATIEDLGEPEKVIASLGPFVTGNSYDSDELLKTSIEKIGDQTYYKYVLETPFALTGSHNLAKATAKGSTVVLFVVSATEKQWQSSQKTLEAILDSFQL
Protein: Secretory 16, isoform D (A8JUU3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MLHNNAPWLPPHQQQQQQAPQQHPTPQQQHAMPQQQQTLPAQQQQQQVYASQMFQQHQPNYWPEDQHQQQQQPQSLNYNNYFPGQQQQHPMQQQQLPPQQQLPPQQQQPTQQQHTIQQQLYYPTQQQPQVPAPAEPALDSFDNNNSGGGGGGGRSDGWGDWGDWNDNSNNNNSNGTDGLLEPTGQLLEDSFNVQSSQGSWQAFATSNNVNNNGELPPPANPQSTSLQQQPLNQQSIPLLHQQPQSPPELGQEPELDAIVPPQAFQNQPPTAAPPPTSLTSFSAQMTAVGSPIYAVGASSAHSAGVGASPAPPTGVVAPPAHLAGIGAPPAHLAGVGASPAPSALVGASPAPIIGVGAPPVGAPPVGAPPADATTIAPPAALPPSIVPSSGSNPFKRSTGLNKRVNIMADPAAGAPSPPAPAAAIAPVAPVAPIPPPADQLFGMPAEAHGEGFNLIAAPPVEASLGTPLSAPIPAPIPVPNASLYASPAVPQAFAHLEPDNQEVLSAPNDERAQYLQTSHLSEQLGEGEADQDAGLLPPPGLSRLVLGQPELDSQQQRQVTGATEQPPLNVAQAAALHMQERRADGEDTSDGEQQVRNIQTPPRRVVTGVETNAPSLREQREVVLDGENLEDREAIPPPTLAELPTTSVHHNILPDEAEQLHHNNPPQAMTPLNAQQPHQQQSTLQQQHQQHSTTQQEKKRAAVGRRTTASLDLESDESDEFLQSERERDRERERRDLMEERHSRGRSHSHYPYEGETEDSVRGAAHHETKSLRETHHKRNHDSARSRRHQDPKVERERERDRERDRTWRRRSNKYHSGGEDPDRSYDHSRRYNNSNYEGESDNPEYNHMGDAELDGSGGRSSKTSRHRRSAAEEDFDDYERERNRSRRSTKPQSSAEKSRSSGGRRNYENSGRSARADDGRRRYQDQRNPGAQYPVSATGYVPYGMYEQMSRNPQVYADMYAKFYGQMINSMNAAVSAAASKGGVPAGAGVIPGLMPSAVPVSAAQLVAATSGGSVSGSSEAAMLRERERAAADAAPSTYGGVAGTAGPVTNTAVARPPRRRTPLQFSRPHLVASYAMSLLLKVKPKYAGRGRLRNDVEVAPPRIRDGTSSLLRMYPGPLQGRKLHKDKIISFCKEQIRLGPTKGCTALYATQKKPQGSVTKYRASHALMWHLLILLLRQNGYIADTDVGDLLLENQQEYPYDPSEFEAENEPDADAEQDAAAPADKTVDSDLDSESAAGVTPAEPLAAGAATSSINGADAANAATPLSEQAATDKFRSYVLRGNVEEALQWATDNGLWTHAFFLALYEDRYALTDVAQKFLNRAIKANDPLQTLYQMKSCHTPACVSQLRDEQWGDWRSHLSILVTNKSRQPEYDRSSVVALGDTLFQRGDIYAAHFCYLVAQEEFGRYDSSATELTTLTANVPRLILLGSSHYKHFNEFASNEAIIMTEIYEYARSLFDPKFSIAHFQHYKFLLATRILDYGQHFRCTNYLEQIARHIELKPESYDSNFIQRVCGLAERLRYHDPILINRVSFASPPNATSKDSAAAEEKAWLRQLRSLAYVQPQQEQLQQLQQNQQVQQEQNDIDQQFAEVNKQFRELNMQYESNSNMENTLQPQLPPVDQQPPQQQQQVLSESYQQPTQQYYEPPPQAPTESDPYGQGQPSYYDPNAGQLHYDPNAAQHQYDQQQPQPQPTPSYGQIEPGTEAYQPGQATADPAAVPSGYGYDYWSGTQQPPYGDEPNENQAALKDEEEEDEEQDEQQILQYAKQQILQQTKQQQLQQEQHTRSNGAASINNRFKSNALKQERSSGSLRKRQEASRTATIAAAAAAIAQITPATVAAAATPPAASAKAFNLNDVSSFSSTNKRHQATSSSNNRSSSNQAAAAAAATKAAAIATVPAAPNQLLSCRKSNSQNSPYLATPKTLTTPTRFIAAKAATVTATPTAPATSTTTSTTIGARGSSTKRVYFNLPSTIAESEQEFEHELDYDEEMEEENSMALAQAKPNVHLARKPHIVFNGTYPIDMPLTQGQSQLKSNSYDPEANADRGDLQRYRNYMLHDYVIDEDAEGEEQAEEEGEEDEYGDGDEDLFPYADDDESFDDGDYYTHQLLNKYGIIPSGEKQRVERTPASVEAATSAAQPQHVWSMKELIANPAIPLNYKKMCSEVEQSLSRFENYLDSKKEQQVPPGAAVRTFDIDAPTRRGHRSSTSTNAGLDLRSKKKL
Protein: Flagellar motor switch protein FliM (Q44457)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
Subcellular location: Cell inner membrane; Peripheral membrane protein. Bacterial flagellum basal body.
Interaction partners:
- Flagellar motor switch protein FliG
- Flagellar motor switch protein FliN
- Flagellar protein FliL
- Flagellar hook-associated protein 1
- Flagellar hook-basal body complex protein FliE
- Flagellar protein FlgA
- Flagellar protein
- Flagellar basal body rod protein FlgB
- Motility protein A
- Flagellar M-ring protein
Sequence:
MIMAKAAAQKASAPTIDTALLAKLTGGLTDRKTIAKIGADIGHLYSEFLPDTFHSETGIAIDVEYIGSESGLMTDLIANVGQNVAVADCSLRNWCPNFMMAVGNGFVIALMERMLGASPDSIGDPDERNLSHIELDLAAMVLGRIAGVLRSGVNAPGGFEATIDPPFNANGKSAFDEMIAGLYGVTIRMKIDIGKVSSEFSLIVPQRPLLKTSIVAPKASAQALKKQEEWMDMISQQVKRSQVTLEARIKLETLTLRTISRLVAGDVIPFQDLKQDDIGVEVSANGSKLYNCEFGKSGDRYMVRVKNNVSTDDEILRHLMG
Protein: Claudin-19 (Q9ET38)
Organism: Mus musculus (Mouse)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:25678664, ECO:0000269|PubMed:28028216}. Cell membrane {ECO:0000269|PubMed:25678664}; Multi-pass membrane protein {ECO:0000269|PubMed:25678664}. Note=Cotrafficks with CLDN16 from ER to tight junctions. Colocalizes with CLDN16 and CLDN3 in cell-cell contact areas of the TAL spatially separated from CLDN10b paracellular channels. {ECO:0000250|UniProtKB:Q8N6F1, ECO:0000269|PubMed:28028216}.
Interaction partners:
- Claudin-16
- Tight junction protein 1
- Occludin
- Claudin-3
- Transient receptor potential cation channel subfamily M member 6
- Tight junction protein ZO-3
- Claudin-23
- Claudin-13
- Claudin-14
- Claudin-9
Sequence:
MANSGLQLLGYFLALGGWVGIIASTALPQWKQSSYAGDAIITAVGLYEGLWMSCASQSTGQVQCKLYDSLLALDGHIQSARALMVVAVLLGFVAMVLSVVGMKCTRVGDSNPTAKSRVAISGGALFLLAGLCTLTAVSWYATLVTQEFFNPSTPVNARYEFGPALFVGWASAGLAMLGGSFLCCTCPEPERANSIPQPYRSGPSTAAREPVVKLPASVKGPLGV
Protein: MIOREX complex component 6 (Mitochondrial organization of gene expression protein 6) (P48564)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25683707}.
Interaction partners:
- Protein PET20, mitochondrial
- Mitochondrial acidic protein MAM33
- Protein SUE1
Sequence:
MEHQALRRLVLYCPNFIRRGALRQNMTRVSCRHMSGKGGGRDEKGDCNEEKDSSKDLGRVPSKMKRAYDGETVIKEGDSHAESLAQQGKQPTDLAYNSRSKISGSNLHLLVPRVASTDYISNKEVHTEGLFAGYRPLFLGNSGFPSDARKGKNFHELDDVLPNIQVVDASEKDGKLNVQEIIEDLQRTSLRESIHSMEQLPSSHKRKPVIPWDASISGMVYNDMPFKYVPKNIILKMKPFKLLRIERKSQAKNARKPTMIKLQFHNRRINDTPELVNLYHNKSRLHESLYNTKPLQESGYSSANTSKRQKMLKARSDFEHKQKNYAYKHTFIKNDQELFRNELTKLNKILAREFKKLTKLSIHNEFKREHLPLAVYVSKSKGTKKLFRRSLKMKIMDHIYPVYTTILSTLTNSRDSKKFENKIKAYIEKIIVRLSDEVPSTYFFQDGVDCIIQPSPIHNFKRMHWLRYTKRHNTFWGRTIHKDVQVSFNDKYVVTRSGVRYTRYPTNLNTQLLETAFEEWDYYE
Protein: cDNA FLJ10506 fis, clone NT2RP2000510 (Q9NVU3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVCCPVNENAAALVVSDGRVMIWELKSAVCNRNSRNSSSGVSPLYSPVSFCGIPVGVLQNKLPDLSLDNMIGQSAIAGEEHPRGSILREVHLKFLLTGLLSGLPAPQFAIRMCPPLTTKNIKMYQPLLAVGTSNGSVLVYHLTSGLLHKELSIHSCEVKGIEWTSLTSFLSFATSTPNNMGLVRNELQLVDLPTGRSIAFRGERGNDESAIEMIKVSHLKQYLAVVFRDKPLELWDVRTCTLLREMSKNFPTITALEWSPSHNLKSLRKKQLATREAMARQTVVSDTELSIVESSVISLLQEAESKSELSQNISARGHFVFTDIDGQVYHLTVEGNSVKDSARIPPDGSMGSITCIAWKGDTLVLGDMDGNLNFWDLKGRVSRGIPTHRSWVRKIRFAPGKGNQKLIAMYNDGAEVWDTKEVQMVSSLRSGRNVTFRILDVDWCTSDKVILASDDGCIRVLEMSMKSACFRMDEQELTEPVWCPYLLVPRASLALKAFLLHQPWNGQYSLDISHVDYPENEEIKNLLQEQLNSLSNDIKKLLLDPEFTLLQRCLLVSRLYGDESELHFWTVAAHYLHSLSQEKSASTTAPKEAAPRDKLSNPLDICYNVLCENAYFQKFQLERVNLQEVKRSTYDHTRKCTDQLLLLGQTDRAVQLLLETSADNQHYYCDSLKACLVTTVTSSGPSQSTIKLVATNMIANGKLAEGVQLLCLIDKAADACRYLQTYGEWNRAAWLAKVRLNPEECADVLRRWVDHLCSPQVNQKSKALLVLLSLGCFFSVAETLHSMRYFDRAALFVEACLKYGAFEVTEDTEKLITAIYADYARSLKNLGFKQGAVLFASKAGAAGKDLLNELESPKEEPIEE
Protein: Secreted frizzled-related protein 2 (sFRP-2) (Q9IA96)
Organism: Gallus gallus (Chicken)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP2 appears to be associated with myogenesis.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Protein Wnt
- Protein Wnt-3a
- Protein Wnt-9a
- Protein Wnt-2b
- Protein Wnt-11
- Protein Wnt
- Protein Wnt-4
- Protein Wnt-1
- Protein Wnt
- Protein Wnt-7b
Sequence:
MPRRLCALLLLASQCLGSTAGLFPFGEPDFSYKRSNCKPIPAPMLLCRGIEYQSMRLPNLLGHETVQEVLEQATTWIPLVQKQCHPDTRKFLCSLFAPVCIDDLDEIIQPCHSLCEEVKESCAPVMSAFGFPWPDMLDCSRFPKDNDLCIPLASSDHILPVTREAPKVCDACKNKNEDDNDIMENLCKNDFALKIKVKEIAYINGDTKITPETKSKTIYKLNGLTERDLRKIVLWLKGGLQCTCDEMNDINVPYLVMGQKQAGELVITSLKRWQKGQRAFKRFSRSIRKLQC
Protein: Nicotinate dehydrogenase FAD-subunit (NDH) (EC 1.17.1.5) (Nicotinic acid hydroxylase FAD-subunit) (NAH) (Q0QLF4)
Organism: Eubacterium barkeri (Clostridium barkeri)
Function: Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.
Interaction partners:
- Nicotinate dehydrogenase medium molybdopterin subunit
- Nicotinate dehydrogenase large molybdopterin subunit
- Nicotinate dehydrogenase small FeS subunit
- Selenium-dependent xanthine dehydrogenase
- Carbon-monoxide dehydrogenase small subunit
- Carbon-monoxide dehydrogenase small subunit
- Xanthine dehydrogenase accessory factor
- Xanthine dehydrogenase molybdenum-binding subunit
- Xanthine dehydrogenase, molybdenum binding subunit apoprotein
- 6-hydroxynicotinate reductase
Sequence:
MKDFEFFAPKTLEEAKGLLHQYKDVPPAIIAGGTDLVIEINDRWEKPDVVIDIKKLKELEYIRVEENTIHIGALSTFTQIENHPFIRSHVRALYKAASQVGSPQIRNLGTIGGNLSTSSVAGDGVSAMTTLDATVVLESVRGTRQMKLTDFFDGEGFKRRNALEADEIMTEVIIDRPDAHSASAFYKLAKRKSLAISVIGGGMAVKVDDAGVCTWASMRGGCIGRYPLHFKQAEEMLVGAPLTMETMEATLPILHDTVYDMARARPSVLYKKESVQGVFKKLFVDILDQLEGGCNE
Protein: E3 ubiquitin-protein ligase Jade-2 (EC 2.3.2.27) (Jade family PHD finger protein 2) (PHD finger protein 15) (Q9NQC1)
Organism: Homo sapiens (Human)
Function: Scaffold subunit of some HBO1 complexes, which have a histone H4 acetyltransferase activity. Acts as a E3 ubiquitin-protein ligase mediating the ubiquitination and subsequent proteasomal degradation of target protein histone demethylase KDM1A. Also acts as a ubiquitin ligase E3 toward itself. Positive regulator of neurogenesis (By similarity).
Interaction partners:
- Inhibitor of growth protein 4
- Histone acetyltransferase KAT7
- Chromatin modification-related protein MEAF6
- Inhibitor of growth protein 5
- Inhibitor of growth protein 3
- Histone-lysine N-methyltransferase SETD1A
Sequence:
MEEKRRKYSISSDNSDTTDSHATSTSASRCSKLPSSTKSGWPRQNEKKPSEVFRTDLITAMKIPDSYQLSPDDYYILADPWRQEWEKGVQVPAGAEAIPEPVVRILPPLEGPPAQASPSSTMLGEGSQPDWPGGSRYDLDEIDAYWLELINSELKEMERPELDELTLERVLEELETLCHQNMARAIETQEGLGIEYDEDVVCDVCRSPEGEDGNEMVFCDKCNVCVHQACYGILKVPTGSWLCRTCALGVQPKCLLCPKRGGALKPTRSGTKWVHVSCALWIPEVSIGCPEKMEPITKISHIPASRWALSCSLCKECTGTCIQCSMPSCVTAFHVTCAFDHGLEMRTILADNDEVKFKSFCQEHSDGGPRNEPTSEPTEPSQAGEDLEKVTLRKQRLQQLEEDFYELVEPAEVAERLDLAEALVDFIYQYWKLKRKANANQPLLTPKTDEVDNLAQQEQDVLYRRLKLFTHLRQDLERVRNLCYMVTRRERTKHAICKLQEQIFHLQMKLIEQDLCRGLSTSFPIDGTFFNSWLAQSVQITAENMAMSEWPLNNGHREDPAPGLLSEELLQDEETLLSFMRDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPILATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPKVSLHFDTETDGYFSDGEMSDSDVEAEDGGVQRGPREAGAEEVVRMGVLAS
Protein: Transmembrane 9 superfamily member 2 (p76) (Q99805)
Organism: Homo sapiens (Human)
Function: In the intracellular compartments, may function as a channel or small molecule transporter.
Subcellular location: Endosome membrane {ECO:0000305|PubMed:9729438}; Multi-pass membrane protein {ECO:0000255}. Golgi outpost {ECO:0000250|UniProtKB:Q66HG5}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q66HG5}. Note=Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation. {ECO:0000250|UniProtKB:Q66HG5}.
Interaction partners:
- Transmembrane emp24 domain-containing protein 10
Sequence:
MSARLPVLSPPRWPRLLLLSLLLLGAVPGPRRSGAFYLPGLAPVNFCDEEKKSDECKAEIELFVNRLDSVESVLPYEYTAFDFCQASEGKRPSENLGQVLFGERIEPSPYKFTFNKKETCKLVCTKTYHTEKAEDKQKLEFLKKSMLLNYQHHWIVDNMPVTWCYDVEDGQRFCNPGFPIGCYITDKGHAKDACVISSDFHERDTFYIFNHVDIKIYYHVVETGSMGARLVAAKLEPKSFKHTHIDKPDCSGPPMDISNKASGEIKIAYTYSVSFEEDDKIRWASRWDYILESMPHTHIQWFSIMNSLVIVLFLSGMVAMIMLRTLHKDIARYNQMDSTEDAQEEFGWKLVHGDIFRPPRKGMLLSVFLGSGTQILIMTFVTLFFACLGFLSPANRGALMTCAVVLWVLLGTPAGYVAARFYKSFGGEKWKTNVLLTSFLCPGIVFADFFIMNLILWGEGSSAAIPFGTLVAILALWFCISVPLTFIGAYFGFKKNAIEHPVRTNQIPRQIPEQSFYTKPLPGIIMGGILPFGCIFIQLFFILNSIWSHQMYYMFGFLFLVFIILVITCSEATILLCYFHLCAEDYHWQWRSFLTSGFTAVYFLIYAVHYFFSKLQITGTASTILYFGYTMIMVLIFFLFTGTIGFFACFWFVTKIYSVVKVD
Protein: Transcription factor Sox-14 (Q32PP9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a negative regulator of transcription. May function as a switch in neuronal development (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9W7R6, ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MSKPADHIKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSESEKRPYIDEAKRLRAQHMKEHPDYKYRPRRKPKNLLKKDRYVFPLPYLGDTDHLKGLPVSATDSLLGSSEKARAFLPPTSAPYSFLDPSQFSSSAIQKMTEMPHTLATSTLPYASSLGYQNGAFGSLGCPSQHTHTHPSPTNPGYVVPCNCTAWSASSLQPPVAYILFPGMTKSGIDPYSSAHAAAM
Protein: DNA-directed RNA polymerase subunit Rpo1N (EC 2.7.7.6) (DNA-directed RNA polymerase subunit A') (B8YB53)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00863, ECO:0000269|PubMed:22848102}.
Interaction partners:
Sequence:
MSEKNIKGIKFGILSPDEIRKMSVTAIITPDVYDEDGTPIEGSVMDPRLGVIEPGQKCPTCGNTLGNCPGHFGHIELVRPVIHVGFVKHVYEFLKATCRRCGRVKISEDEIEKYSRIYNAIKKRWPSAARRLTEYVKKTAMKAQVCPHCGEKQFKIKLEKPYNFYEERKEGVAKLTPSDIRERLEKVPESDVEILGYDPTTSRPEWMILTVLPVPPITIRPSIMIESGIRAEDDLTHKLVDIVRINERLKESIDAGAPQLIIEDLWDLLQYHVATYFDNEIPGLPPSKHRSGRPLRTLAQRLKGKEGRFRGNLSGKRVDFSSRTVISPDPNISIDEVGVPEIIARTLTVPERITPWNIEKLRQFVINGPDKWPGANYVIRPDGRRIDLRYVKDRKELASTLAPGYVVERHLTDGDVVLFNRQPSLHRISMMAHRVRVLKGLTFRLNLLVCPPYNADFDGDEMNLHVPQSEEAIAEAKEIMLVHKNIITPRYGGPIIGAAQDYISGAYLLTVKTTLLTKEEAQQILGVADVKIDLGEPAILAPREYYTGKQVVSAFLPKDFNFHGQANVSSGPRLCKNEDCPHDSYVVIKNGILLEGVFDKKAIGNQQPESILHWLIKEYSDEYGKWLMDNLFRVFIRFVELQGFTMRLEDVSLGDDVKKEIYNEIDRAKVEVDNLIQKYKNGELEPIPGRTLEESLENYILDTLDKLRSTAGDIASKYLDPFNFAYVMARTGARGSVLNITQMAAMLGQQSVRGERIKRGYMTRTLPHFKPYDISPEARGFIYSSFRTGLKPTELFFHAAGGREGLVDTAVRTSQSGYMQRRLINALSDLRAEYDGTVRSLYGEVIQVAYGDDGVFPMYSAHGKTVDVNRIFERVVGWKT
Protein: UDP-glucose 4-epimerase 4 (AtUGE4) (EC 5.1.3.2) (Protein ROOT EPIDERMAL BULGER 1) (Protein ROOT HAIR DEFECTIVE 1) (UDP-galactose 4-epimerase 4) (Q9C7W7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion between UDP-glucose and UDP-galactose. Involved in channeling UDP-D-galactose (UDP-D-Gal) into cell wall polymers. Required for the galactosylation of xyloglucan (XyG) and type II arabinogalactan (AGII). Cooperates with UGE2 in cell wall carbohydrate biosynthesis and growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16644739}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:16644739}.
Interaction partners:
- ADP-glucose phosphorylase
- UDP-sugar pyrophosphorylase
- UTP--glucose-1-phosphate uridylyltransferase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- UDP-sulfoquinovose synthase, chloroplastic
- Galactinol synthase 10
- Galactinol synthase 5
Sequence:
MVGNILVTGGAGYIGSHTVLQLLLGGYNTVVIDNLDNSSLVSIQRVKDLAGDHGQNLTVHQVDLRDKPALEKVFSETKFDAVMHFAGLKAVGESVAKPLLYYNNNLIATITLLEVMAAHGCKKLVFSSSATVYGWPKEVPCTEESPLSGMSPYGRTKLFIEDICRDVQRGDPEWRIIMLRYFNPVGAHPSGRIGEDPCGTPNNLMPYVQQVVVGRLPNLKIYGTDYTTKDGTGVRDYIHVVDLADGHICALQKLDDTEIGCEVYNLGTGKGTTVLEMVDAFEKASGMKIPLVKVGRRPGDAETVYASTEKAERELNWKANFGIEEMCRDQWNWASNNPFGYGSSPNST