wanglab/gogpt-training-data huggingface dataset:
Protein: Protein transport protein Sec61 subunit beta (Q9CQS8)
Organism: Mus musculus (Mouse)
Function: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (By similarity). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (By similarity). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (By similarity). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (By similarity). Required for PKD1/Polycystin-1 biogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P60468}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein transport protein Sec61 subunit gamma
- Translocation protein SEC63 homolog
- Protein transport protein Sec61 subunit alpha isoform 1
- Protein transport protein Sec61 subunit alpha isoform 2
- Ubiquitin-like protein FUBI
- Translocon-associated protein subunit delta
- Translocon-associated protein subunit beta
- Translocon-associated protein subunit gamma
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein eL19
Sequence:
MPGPTPSGTNVGSSGRSPSKAVAARAAGSTVRQRKNASCGTRSAGRTTSAGTGGMWRFYTEDSPGLKVGPVPVLVMSLLFIAAVFMLHIWGKYTRS
Protein: Ring assembly protein 3 (O74994)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential for actinomyosin ring assembly during cytokinesis. Has a role, in conjunction with F-actin, in assembling myosin II-containing proteins, such as myo2, at the division site.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10852821}. Note=Associated with the actinomyosin ring.
Interaction partners:
- Myosin type-2 heavy chain 1
- Heat shock protein 90 homolog
- Myosin-1
- Myosin type-2 heavy chain 2
- Myosin-51
- Actin
- Myosin-52
Sequence:
MTHELSSTPQIDLLNDILKNSVESNVFSDYQKKQIVTLILKSKISTAIVLLSPKSTAASEWNYLCNLQDLHECVLCVDTILPANLQTIAKRIFSLVLLPPLNDWCKQLRDAFLRFVSQPSICPTDFPLKLFFLSTVGIELLIVNEKIIPQKTQKYLLYELFSSPSSITANEIARLCQEANNRNYLLQSLTSATDARRAFLNNPNYRLLSAIIFQDGPSNLAFVLAKDCVLLARQPETIPVSFERMSSLLLMCLPSHPDFISPEFCHEWTELAERNGLQEEWLNILNTACNFKECRAIIHKECSEFIKDNHTSRVAILISMKLAFQYQLSQVIPTLKLLLQSKVYDSVLLEALRQSSTLGPVKQLIADDSCLLNNLSKLLLDTNISPLDASSIATIIYNMCKFKITKSEHERELNQLRNMAEASKTIDYKEDETAPTERRIQKILEYDILSKLFSAAKHYNSLNGLLAMILVHMANYKLARRKLVQIGALKFLTRQCFIQTQDSNAAFALAKILISVAPHSIFTKAFPSNRAIHPMSKLLSTNSADTEYPILLGKFEVLLALTNLASHDEESRQAIVQECWRELDELIIETNPLIQRATTELINNLSLSPYCLIKFIGDKDSDFENTRLHIVLALSDTEDTPTRLAACGILVQITSVDEGCKKILSLQNDFNYIVRMLTDQDEGIQHRGLVCICNIVYSKDQEIFNKFIKTPKAVETLRTYITKQAALKELQHEALVMIDSRLQGSK
Protein: Exocyst complex component SEC6 (P32844)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm.
Interaction partners:
- Protein transport protein SEC9
- Exocyst complex component SEC8
- Exocyst complex component SEC3
- Exocyst complex component SEC10
- Exocyst complex component EXO70
- Exocyst complex component EXO84
- Exocyst complex component SEC5
- Exocyst complex component SEC15
- Ras-related protein SEC4
- Protein transport protein SEC1
Sequence:
MSSDPLQQVCDLIKGDLSLERVRDIKEQLLKEKSVVEYQLNKESDKYYGEVEESLKLLNLSKNSVTSIKQQINEVNKLGNDNRFAINRYDILFRATKLYETVNTTSSIYDRIYNFVALMEHIERLLVAELAEDALETGCPHLLEIHFLLTSARDFQEQVVVMAKEATEDAQRTVMKLFSRLSGIISKFDKLLDGLTYDIVEMARAEQISLAIRLFKIYDLEEREDLRIEAIRNIIKKKEIEIEKSSIKKLPNSKNTARLQDETPKVIEYPTNKGLYQEIMSGTISTRTAPRGYKHFLINGINNSISEMFGEMREKYVGDQKFDVLDNMDWIFNELIIVKEHIANCCPPHWNIFEVYFDQYYKELHSLITDLVESEPETIIILDILAFDKTFQDTLKQDFGFTKSEVKSVIGDKEKETLFKDYLNLIVVKMTEWIGNLEKAEFDVFLERSTPPHSDSDGLLFLDGTKTCFQMFTQQVEVAAGTNQAKILVGVVERFSDLLTKRQKNWISKISEEIKKQINYNHKYDIDPESITPEDECPGGLVEYLIAVSNDQMKAADYAVAISSKYGKLVSKVYEKQITNHLEGTLDGFAEVAQCSSLGLITLMFDDLRKPYQEIFSKTWYMGSQAQQIADTLDEYLLDIKPQMNSVLFVNFIDNVIGETIIKFLTALSFEHSFKNKNNKFLEAMKRDFEIFYQLFVKVLDGNESKDTLITQNFTVMEFFMDLSCEPIDSILDIWQKYLEVYWDSRIDLLVGILKCRKDVSSSERKKIVQQATEMLHEYRRNMEANGVDREPTLMRRFVLEFEKQ
Protein: Outer spore wall protein 2 (Q12202)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in a late step of spore wall assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15590821}. Prospore membrane {ECO:0000269|PubMed:15590821}. Note=In mature spores. Localized around the prospore membrane during meiosis II.
Interaction partners:
- Outer spore wall protein 6
- Lipid droplet organization protein LDO16
- Outer spore wall protein 1
- Spore wall maturation protein DIT1
- Outer spore wall protein RRT8
- Outer spore wall protein 7
- Ectonucleotide pyrophosphatase/phosphodiesterase 2
Sequence:
MEENQLTCLIVGETPAAQFLGWRLSLSNSFIILVSQYVSSDELVAWKSTKLGANFYTPNILTKDIKELHHKLKHNGANTYSIDIVLVSAISLQSFETTCRLLSDYTNDNTTVLISTDFGCELEPIAISYFGGKCKCVISISCEVECRQLSLGSYALVNDDQCVITLGLTYCDANFEASPTILENTKAASLELQGIKGSNVRRFLLGLTVAKWMKSKLILDPKQMALKMWELLIPKISLNILSIIYEQFDYEKMLENKSTEIIFKDLVKELLGICFAQCGSKIARFLLVKSQGEEEINFGKIVEYCKGKKLQLINSTANEHPEYLSLPFEPYCFYHRFEYPAQILLHQPIILAKKYGVSCSNLNFLYGFYTRLLTLSGLSINGGRCEHALSMLDSRIGGGINVASGINSGQDFTDGDNEDQDKGKNRVDKNVKEGSFISLTQRFTMTSPLGVNDPALPADLEKLYLGAEYISNCDANTSGGQKRVKSPTKADTGYDDKHLPDDTIHTFEDEYLADEDDFSCLGIDKRSSTKPTKPLEKFGVVAVPHFIRRFSIKRSSKDKSNDMKRPYTTSSLELQLRSNHFMFAKEYQDLHRQLYYEVKPRTQSELDARRRNYSELESQMWKIKHRFNIHRGALPRPRTNPYELLLDHIDVLNRGNTGDILRFTTSRYGGVDTYDSILRDQSTIMELLDKRCAYSPPVLFDNEAKERDHDRDCYQDYNHDHRSH
Protein: Transcriptional repressor p66-alpha (Hp66alpha) (GATA zinc finger domain-containing protein 2A) (Q86YP4)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}. Nucleus {ECO:0000269|PubMed:27732854, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}. Chromosome {ECO:0000269|PubMed:27732854}. Note=Speckled nuclear localization requires both CR1 and CR2 regions (PubMed:16415179). Localizes to sites of DNA damage in a manner partially dependent on ZMYND8 (PubMed:27732854). {ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:27732854}.
Interaction partners:
- Histone deacetylase 2
- Metastasis-associated protein MTA1
- Chromodomain-helicase-DNA-binding protein 3
- Chromodomain-helicase-DNA-binding protein 4
- Methyl-CpG-binding domain protein 2
- Histone-binding protein RBBP4
- Histone-binding protein RBBP7
- Histone deacetylase 1
- Metastasis-associated protein MTA2
- Metastasis-associated protein MTA3
Sequence:
MTEEACRTRSQKRALERDPTEDDVESKKIKMERGLLASDLNTDGDMRVTPEPGAGPTQGLLRATEATAMAMGRGEGLVGDGPVDMRTSHSDMKSERRPPSPDVIVLSDNEQPSSPRVNGLTTVALKETSTEALMKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTGSVGSTVTTPPPLVRGTQNIPAGKPSLQTSSARMPGSVIPPPLVRGGQQASSKLGPQASSQVVMPPLVRGAQQIHSIRQHSSTGPPPLLLAPRASVPSVQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTPASLKGTTATSAQANSTPTSVASVVTSAESPASRQAAAKLALRKQLEKTLLEIPPPKPPAPEMNFLPSAANNEFIYLVGLEEVVQNLLETQGRMSAATVLSREPYMCAQCKTDFTCRWREEKSGAIMCENCMTTNQKKALKVEHTSRLKAAFVKALQQEQEIEQRLLQQGTAPAQAKAEPTAAPHPVLKQVIKPRRKLAFRSGEARDWSNGAVLQASSQLSRGSATTPRGVLHTFSPSPKLQNSASATALVSRTGRHSERTVSAGKGSATSNWKKTPLSTGGTLAFVSPSLAVHKSSSAVDRQREYLLDMIPPRSIPQSATWK
Protein: Phosphotriesterase homology protein (EC 3.1.-.-) (P45548)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of phosphorylated glyceryl acetates in which the presence of a phosphate group is required for the enzymatic hydrolysis. Hydrolyzes a dibutyl glycerol derivative suggesting it acts on phosphoglycerol substrates with a butyrate leaving group. Also active with aromatic acetates and propionates. No activity with various sugar phosphates, with various nitrophenylphosphate or nitrophenylphosphonate derivatives, or with phosphorylated or non-phosphorylated sugar lactones tested. Does not hydrolyze non-phosphorylated carboxyesters with long chain leaving groups. No general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities detected when tested with the following non-specific substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate.
Interaction partners:
- Uncharacterized protein YhfX
- Uncharacterized protein YhfS
- Uncharacterized protein YhfW
- Uncharacterized protein YhfT
- Uncharacterized protein YhfU
- Uncharacterized protein YhfZ
- Uncharacterized protein YhfY
- Acetylornithine/succinyldiaminopimelate aminotransferase
- Malonyl-[acyl-carrier protein] O-methyltransferase
- DNA adenine methylase
Sequence:
MSFDPTGYTLAHEHLHIDLSGFKNNVDCRLDQYAFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGIDGTELKAGIIAEIGTSEGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQLALLQAHGVDLSRVTVGHCDLKDNLDNILKMIDLGAYVQFDTIGKNSYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDYLLTTFIPQLRQSGFSQADVDVMLRENPSQFFQ
Protein: Indole prenyltransferase tdiB (EC 2.5.1.-) (Terrequinone biosynthesis protein B) (A7XRY3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Indole prenyltransferase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent. The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD. The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules. The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain. TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1. Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5.
Interaction partners:
- Didemethylasterriquinone D synthetase tdiA
- Probable NADPH-dependent quinone reductase tdiC
- Probable methyltransferase tdiE
Sequence:
MATEYWSRHLRSVLAPLFAAAGTYSPEDQESHLAFIDEHIAPNLGPLPWEPHGPYSTPSSLVGSPFDPSINIVSSGKAKVRFDFDVISPPDRTGPDPFAEGSAREILHRLADLVGADTQWMGYLMDALYLTPAEAEVAKTKLPPGVAIPPSSVGFDFDGPERTLKFYIPSVRKALATGQDVSELMLKTLRGLQPLGSELVPAMDLIASYLSTRTNDAMLPLVGIDCLDPRTHKNARVKCYLHTSSNSFAVVRDVLTLGGRLSDDTSLKRVETLKSVWPLLINELEGPQSDAATMDESWSKPERLNRTGYSGIQYTIEITPGQAIPDTKIYVPLFQYTDSSEVAERNFESALKKLGNEWGLSGKYRSVMQEIFKDVENYGQTYASFSYTEGKGVYTTSYVAMPIKDEGGGSLAGDFGFRN
Protein: Receptor-type tyrosine-protein phosphatase alpha (Protein-tyrosine phosphatase alpha) (R-PTP-alpha) (EC 3.1.3.48) (LCA-related phosphatase) (PTPTY-28) (P18052)
Organism: Mus musculus (Mouse)
Function: Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation. Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22801373}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000269|PubMed:22801373}. Note=Localizes to focal adhesion sites following integrin engagement. {ECO:0000269|PubMed:22801373}.
Interaction partners:
- Tyrosine-protein kinase Fyn
- Growth factor receptor-bound protein 2
- 6-pyruvoyl tetrahydrobiopterin synthase
- Neural cell adhesion molecule 1
- Focal adhesion kinase 1
- Integrin alpha-V
- Neural cell adhesion molecule L1-like protein
- Proto-oncogene tyrosine-protein kinase Src
Sequence:
MDSWFILVLFGSGLIHVSANNATTVSPSLGTTRLIKTSTTELAKEENKTSNSTSSVISLSVAPTFSPNLTLEPTYVTTVNSSHSDNGTRRAASTESGGTTISPNGSWLIENQFTDAITEPWEGNSSTAATTPETFPPADETPIIAVMVALSSLLVIVFIIIVLYMLRFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPFLSLAVSKDAVKALNKTTPLLERRFIGKSNSRGCLSDDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNVRVSVEDVTVLVDYTVRKFCIQQVGDVTNRKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHSERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTELEVTSLETHLQKIYNKIPGTSNNGLEEEFKKLTSIKIQNDKMRTGNLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLLHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQEYIDAFSDYANFK
Protein: Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3 (EC 5.1.3.2) (EC 5.1.3.5) (UDP-D-xylose 4-epimerase) (UDP-L-arabinose 4-epimerase) (UDP-galactose 4-epimerase 3) (UDP-glucose 4-epimerase 3) (AtUGE3) (Q8LDN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion between UDP-glucose and UDP-galactose and the interconversion between UDP-arabinose and UDP-xylose. Cooperates with UGE2 in pollen development. May preferentially act in the UDP-galactose to UDP-glucose direction, therefore displaying a role in carbohydrate catabolism (Probable).
Interaction partners:
- UDP-sugar pyrophosphorylase
- ADP-glucose phosphorylase
- 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 RHM2
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
- UDP-sulfoquinovose synthase, chloroplastic
- Galactinol synthase 6
- Galactinol synthase 10
Sequence:
MGSSVEQNILVTGGAGFIGTHTVVQLLNQGFKVTIIDNLDNSVVEAVHRVRELVGPDLSTKLEFNLGDLRNKGDIEKLFSNQRFDAVIHFAGLKAVGESVGNPRRYFDNNLVGTINLYETMAKYNCKMMVFSSSATVYGQPEIVPCVEDFELQAMNPYGRTKLFLEEIARDIHAAEPEWKIILLRYFNPVGAHESGRIGEDPKGIPNNLMPYIQQVAVGRLPELNVFGHDYPTMDGSAVRDYIHVMDLADGHVAALNKLFSDSKIGCTAYNLGTGQGTSVLEMVSSFEKASGKKIPIKLCPRRAGDATAVYASTQKAEKELGWKAKYGVDEMCRDQWNWANKNPWGFQKKP
Protein: Ubiquitin-like modifier-activating enzyme ATG7 (Autophagy-related protein 7) (Q7JY94)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU366022}. Preautophagosomal structure {ECO:0000256|RuleBase:RU366022}.
Interaction partners:
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagy protein 12-like
- Autophagy-related 8a, isoform A
- Autophagy-related 8b, isoform A
- Autophagy protein 5
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy-related 16, isoform F
- Cysteine protease
- Cysteine protease
- NAD-dependent histone deacetylase sirtuin-1
Sequence:
MSTEKEIILQFAPWESFVSPTFWHKLAELKLDHDRLSDSKRSITGHYTNRNASGCLLEVDYTAYNRMAKPPKFSHSAIGTIYNKNTIEEFKALDKLQLLADEGKELLADMCSGGALRDPSLLTRFFVLSFADLKCHSYYYWFAFPCPLTPTLKLQGAVQKLRDLPNSSSYIMALKALPTESQNFFILYANVEKNIFEARSLSSLDDKNVEFCYFGFADPSEYEHPAWIMRNYAAFLLQQCPSFVGKPLKFLGLRHNQQMNIDDSLVWKVIQTEACDLSQSENIKFVGWELNKNGKMGPRMVCMRDSMDPAKLAENSVNLNLKLMKWRLVPDLNLEIISQTKCLLFGAGTLGCAVARNLLSWGFKHITLLDSGKVGFSNPVRQNLYTHADAVAGNRMKATTAAQRLKEINPSAETAGYVLEIPMPGHTIGESLLAQTKEHLKVIEKLVQDHDVIFLLTDSRESRWLPTLLGAAKEKIVINAALGFDSYLVMRHGTTRKEAGDDGQEIEGLKCINGDQLGCYFCNDVTAPGNSLKDRTLDQQCTVTRPGVSNIAASYAVELLVALLQHPRKELAPAYYAQSGRGRSEETEEKVPEGLLGILPHSIRGMLCNYENILPATQKFAQCIACSAAVLNEYKKEGHAFLFKTFETAKFLEDLTGISEFKRLNSEIIDFDDEEFDMSDSDED
Protein: Glycosyltransferase (O-glucosyltransferase-like protein (DUF821)) (F4I232)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTSLFSKPRALTSHITNFKTYRPVIGKLHVATLTLLLFLIAAGIAVTSSLWLNKTTKAFDRPTLVATKPEPELEPPHETGVLVNCTSFLNQNRSGSCSRTPLLNKKKPSHRPTITTIKPVPVRVSEKKSPEETGSSVDCSSFLNQNRSGSCSRTLQSGYNQNQTESNRSCPDYFKWIHEDLKPWRETGITKEMVERGKTTAHFRLVILNGKVFVENYKKSIQTRDAFTLWGILQLLRKYPGKLPDVDLMFDCDDRPVIRSDGYNILNRTVENAPPPLFRYCGDRWTVDIVFPDWSFWGWQEINIREWSKVLKEMEEGKKKKKFMERDAYAYWKGNPFVASPSREDLLTCNLSSLHDWNARIFIQDWISEGQRGFENSNVANQCTYRYKIYIEGYAWSVSEKYILACDSVTLMVKPYYYDFFSRTLQPLQHYWPIRDKDKCRSIKFAVDWLNNHTQKAQEIGREASEFMQRDLSMENVYDYMFHLLNEYSKLLKYKPQVPKNSVELCTEALVCPSEGEDVNGVDKKFMIGSLVSRPHASGPCSLPPPFDSNGLEKFHRKKLNLIRQVEKWEDSYWQKVL
Protein: Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (p120 CAND1) (Q6ZQ38)
Organism: Mus musculus (Mouse)
Function: Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q86VP6}. Nucleus {ECO:0000250|UniProtKB:Q86VP6}. Note=Predominantly cytoplasmic. {ECO:0000250|UniProtKB:Q86VP6}.
Interaction partners:
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- Cullin-4B
- Cullin-4A
- Cullin-3
- Cullin-2
- Ubiquitin-like protein NEDD8
- Cullin-5
- NEDD8-conjugating enzyme Ubc12
- RING-box protein 2
Sequence:
MASASYHISNLLEKMTSSDKDFRFMATNDLMTELQKDSIKLDDDSERKVVKMILRLLEDKNGEVQNLAVKCLGPLVSKVKEYQVETIVDTLCTNMLSDKEQLRDISSIGLKTVIGELPPASSGSALAANVCKKITGRLTSAIAKQEDVSVQLEALDIMADMLSRQGGLLVNFHPSILTCLLPQLTSPRLAVRKRTIIALGHLVMSCGNIVFVDLIEHLLSELSKNDSMSTTRTYIQCIAAISRQAGHRIGEYLEKIIPLVVKFCNVDDDELREYCIQAFESFVRRCPKEVYPHVSTIINICLKYLTYDPNYNYDDEDEDENAMDADGGDDDDQGSDDEYSDDDDMSWKVRRAAAKCLDAVVSTRHEMLPEFYKTVSPALIARFKEREENVKADVFHAYLSLLKQTRPVQSWLCDPDAMEQGDTPLTMLQSQVPNIVKALHKQMKEKSVKTRQCCFNMLTELVNVLPGALTQHIPVLVPGIIFSLNDKSSSSNLKIDALSCLYVILCNHSPQVFHPHVQALVPPVVACVGDPFYKITSEALLVTQQLVKVIRPLDQPSSFDATPYIKDLFTCTIKRLKAADIDQEVKERAISCMGQIICNLGDNLGPDLSNTLQIFLERLKNEITRLTTVKALTLIAGSPLKIDLRPVLGEGVPILASFLRKNQRALKLGTLSALDILIKNYSDSLTAAMIDAVLDELPPLISESDMHVSQMAISFLTTLAKVYPSSLSKISGSILNELIGLVRSPLLQGGALSAMLDFFQALVVTGTNNLGYMDLLRMLTGPVYSQSTALTHKQSYYSIAKCVAALTRACPKEGPAVVGQFIQDVKNSRSTDSIRLLALLSLGEVGHHIDLSGQLELKSVILEAFSSPSEEVKSAASYALGSISVGNLPEYLPFVLQEITSQPKRQYLLLHSLKEIISSASVAGLKPYVENIWALLLKHCECAEEGTRNVVAECLGKLTLIDPETLLPRLKGYLISGSSYARSSVVTAVKFTISDHPQPIDPLLKNCIGDFLKTLEDPDLNVRRVALVTFNSAAHNKPSLIRDLLDSVLPHLYNETKVRKELIREVEMGPFKHTVDDGLDIRKAAFECMYTLLDSCLDRLDIFEFLNHVEDGLKDHYDIKMLTFLMLVRLSTLCPSAVLQRLDRLVEPLRATCTTKVKANSVKQEFEKQDELKRSAMRAVAALLTIPEAEKSPLMSEFQSQISSNPELAAIFESIQKDSSSTNLESMDTS
Protein: Interleukin-20 receptor subunit alpha (IL-20 receptor subunit alpha) (IL-20R-alpha) (IL-20RA) (Cytokine receptor class-II member 8) (Cytokine receptor family 2 member 8) (CRF2-8) (IL-20R1) (ZcytoR7) (Q9UHF4)
Organism: Homo sapiens (Human)
Function: The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and IL24. The IL20RA/IL10RB dimer is a receptor for IL26.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Interleukin-24
- Interleukin-20 receptor subunit beta
- Interleukin-19
- Interleukin-26
- Interleukin-10 receptor subunit beta
- Interleukin-20
- Interleukin-22
- Tyrosine-protein kinase JAK1
- Interleukin-22 receptor subunit alpha-1
- Interferon lambda-1
Sequence:
MRAPGRPALRPLPLPPLLLLLLAAPWGRAVPCVSGGLPKPANITFLSINMKNVLQWTPPEGLQGVKVTYTVQYFIYGQKKWLNKSECRNINRTYCDLSAETSDYEHQYYAKVKAIWGTKCSKWAESGRFYPFLETQIGPPEVALTTDEKSISVVLTAPEKWKRNPEDLPVSMQQIYSNLKYNVSVLNTKSNRTWSQCVTNHTLVLTWLEPNTLYCVHVESFVPGPPRRAQPSEKQCARTLKDQSSEFKAKIIFWYVLPVSITVFLFSVMGYSIYRYIHVGKEKHPANLILIYGNEFDKRFFVPAEKIVINFITLNISDDSKISHQDMSLLGKSSDVSSLNDPQPSGNLRPPQEEEEVKHLGYASHLMEIFCDSEENTEGTSLTQQESLSRTIPPDKTVIEYEYDVRTTDICAGPEEQELSLQEEVSTQGTLLESQAALAVLGPQTLQYSYTPQLQDLDPLAQEHTDSEEGPEEEPSTTLVDWDPQTGRLCIPSLSSFDQDSEGCEPSEGDGLGEEGLLSRLYEEPAPDRPPGENETYLMQFMEEWGLYVQMEN
Protein: Tubulin beta-3 chain (Q9ASR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-3
- Mitotic spindle checkpoint protein MAD2
- Nascent polypeptide-associated complex subunit alpha-like protein 4
- Tubulin alpha-2 chain
- Microtubule-associated protein RP/EB family member 1A
- Actin-4
- Tubulin alpha-4 chain
- Tubulin alpha-6 chain
- Tubulin-folding cofactor A
- Tubulin alpha-3 chain
Sequence:
MREILHIQGGQCGNQIGAKFWEVVCAEHGIDPTGRYTGDSDLQLERINVYYNEASCGRFVPRAVLMDLEPGTMDSLRSGPYGQTFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRSLTVPELTQQMWDSKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEGDYEDEEEGEYQQEEEY
Protein: Integrin beta (Q9PUU4)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
Interaction partners:
- Integrin alpha-M-like
- Junctional adhesion molecule 3B
- Junctional adhesion molecule C-like.
- Junctional adhesion molecule A
- Uncharacterized protein LOC108257178
- Intercellular adhesion molecule 2
- Integrin alpha-4
- Integrin alpha-D
- Focal adhesion kinase 1-like isoform X2
- Focal adhesion kinase 1 isoform X5
Sequence:
MPQAAKIVLLLLFGQYVYSQEKECIKSSVVSCKDCINSGPGCAWCQELNFTKTGEPEAVRCDTEEKLKEKGCSQQKIISPSSHLENVANKPLSGSDRTKNPVQVQPQEIKLNLRPGQAFTFNLQFKRAVGYPVDLYYLMDLSYSMEDDLTNVKDLGIQILKRLQQITGNARIGFGSFVDKTLLPFTDTTEEKLKKPCPAKRKQCQPAFGYHHVLSLTQNETLFSTMVSGQEISGNLDTPEGGLDAIMQVATCVNKIGWGNSTRLLVLATDAGFHKAGDGKLAGILEPNQETCQLDNKNIYSMSNNWDYPSVGQIARKLGEETIQPIFAVTEDVSHIHQELSKLIPKSEVGVLSSDSSNVVKLIVDAYNKLSSNIIVTHDGLPEDISVTFTSNCPGGEKPSDRGTCNNVAIGQGVTFSVTVKAAKCLDKAYFQTGPLGFSEKLKVNIKTRCECECDNQPGVQLYCNQHGTIVCGTCSCVPGFLGQRCECSLGQKDEATLKAQCRKDNGTECEGRGDCECGVCKCHQTEGGKSYYGPHCECDDEHCEKYQNKLCGGNGDCRCGVCKCNEGYEGTACQCKKSNEFCETGKTICHGRGKCVCNQCVCERRYKGITCETCPTCELPCQESGSCVECNAFGTGPFEKTCNASCYHLDVEVVEKLAKRECQVKDNEGCRMIFSMTEQDGFDKYIVKVLKDRECPEGPNVALIVGGTLAGVALIGLLLLILIKALFYFKDLKEWKKFEKEAQRRQWAKGENPLFQNATTTVANPAFTGDS
Protein: Dihydrofolate reductase (EC 1.5.1.3) (Q6QGJ4)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Provides the tetrahydrofolates necessary for the synthesis of nucleotides and amino acids. Bacteriophage T5 induces high levels of dihydrofolate reductase in the host cell, probably for the viral replication.
Interaction partners:
Sequence:
MITAMYAVGPNGEFGLRGKLPWGSFKEELDAFYSQLDVLNPDNIIIGAGTYLALPYAVRERMIGASDLFIRADRPLPDDITHDIYTPISMIGDTLPTFLKDQQTVVLGGANLLLEMYQHGHIESAFVSTIFSEQKLEADTHLDSMILDYNYESTRLVYAVGANSDNSLRFVQELVTY