wanglab/gogpt-training-data huggingface dataset:
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8YG32)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XTEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKTLKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
Protein: Ifd6p (A0A1D8PD78)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glucoamylase 1
- Pyridoxine 4-dehydrogenase
- Oye32p
- Adh5p
- Glucoamylase 1
Sequence:
MSIDKSKMVTRLGKSGLKVNTVAIGTMRLGSNWMGYNGDIDECLKILKFCYDNGFRTFDTADVYSNGKSEELLGLFIKKYNIPRERIVILTKCYFPVNDSDDKNWEDFDPVDSLNGKGLSRKHILAAVEDSVKRLGTYIDVLQIHRLDHEVTYEEIMHSLNDVVEKGLTRYIGASSMKAWEFVELQNVAKANGWHQFISMQSHYSLLYREDDRELNDYCKKNGVGLIPWSPNSGGVLCRPFDSEKTQKFFENKDWASVFGLGEPREADKTIVNRVEELSVKYNATMMQISLAWCIAKGVIPIAGVSKFEQAEELVGIYNVNLTEEDIKYLDEPYHAKDLAKEVN
Protein: Regulatory particle triple-A ATPase 4 (EC 5.6.1.5) (Q9W414)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 26S proteasome regulatory subunit 4
- GH11341p
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory complex subunit p50
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 4
Sequence:
MTVTATPMPDNLRVKALSEYRKKLLEHKEIEGRLKEKREEIKDLTKLYDKSENDLKALQSVGQIVGEVLKQLTEDKFIVKATNGPRYVVGCRRQLDKAKLKSGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGDVTYSAIGGLTDQIRELREVIELPLLNPELFLRVGITPPKGCLLYGPPGTGKTLLARAVASQLDANFLKVVSSAIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDSLGQVKMIMATNRPDTLDPALLRPGRLDRKIEIPLPNEQARLEILKIHALKIAKHGEIDYEAIVKLSDNFNGADLRNVCTEAGLFAIRAEREYVIQEDFMKAVRKVSDNKKLESKLDYKPV
Protein: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 (Glucosaminyl N-deacetylase/N-sulfotransferase 1) (NDST-1) (Golgi heparan sulfate N-deacetylase/N-sulfotransferase) (N-heparan sulfate sulfotransferase 1) (N-HSST) (N-HSST 1) ([Heparan sulfate]-glucosamine N-sulfotransferase 1) (HSNST 1) [Includes: Heparan sulfate N-deacetylase 1 (EC 3.5.1.-); Heparan sulfate N-sulfotransferase 1 (EC 2.8.2.8)] (Q02353)
Organism: Rattus norvegicus (Rat)
Function: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Participates in biosynthesis of heparan sulfate that can ultimately serve as L-selectin ligands, thereby playing a role in inflammatory response (By similarity). Required for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11792394}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P52848}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:P52848}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Exostosin-2
- Exostosin-1
- Exostosin-like 3
- Heparan sulfate 2-O-sulfotransferase 1
- Syndecan-1
- Glypican-3
- Syndecan-2
Sequence:
MPALACLRRLCRHLSPQAVLFLLFVFCLFSVFVSAYYLYGWNRGLEPSADASESDCGDPPPVAPSRLLPIKPVQAVAPSRTDPLVLVFVESLYSQLGQEVVAILESSRFKYRTEIAPGKGDMPTLTDKGRGRFALIIYENILKYVNLDAWNRELLDKYCVAYGVGIIGFFKANENSLLSAQLKGFPLFLHSNLGLKDCSINPKSPLLYVTRPSEVEKGVLPGEDWTVFQSNHSTYEPVLLAKTRSSESIPHLGADAGLHAALHATVVQDLGLHDGIQRVLFGNNLNFWLHKLVFVDAVAFLTGKRLSLPLDRYILVDIDDIFVGKEGTRMKVEDVKALFDTQNELRTHIPNFTFNLGYSGKFFHTGTDAEDAGDDLLLSYVKEFWWFPHMWSHMQPHLFHNQSVLAEQMALNKKFAVEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKQVWNIRVTSTEEYPHLKPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSSELDKIINGGELFLTVLLNPISVFMTHLSNYGNDRLGLYTFKHLVRFLHSWTNLRLQTLPPVQLAQKYFQIFSEEKDPLWQDPCEDKRHKDIWSKEKTCDRFPKLLIIGPQKTGTTALYLFLGMHPDLSSNYPSSETFEEIQFFNGHNYHKGIDWYMEFFPIPSNTTSDFYFEKSANYFDSEVAPRRAAALLPKAKVLTILINPADRAYSWYQHQRAHDDPVALKYTFHEVITAGPDASSKLRALQNRCLVPGWYATHIERWLSAFHANQILVLDGKLLRTEPAKVMDTVQKFLGVTSTVDYHKTLAFDPKKGFWCQLLEGGKTKCLGKSKGRKYPEMDLDSRAFLKDYYRDHNIELSKLLYKMGQTLPTWLREDLQNTR
Protein: Anaphase-promoting complex subunit 5 (Q582J0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- FG-GAP repeat protein, putative
- FG-GAP repeat protein, putative
- Ankyrin repeat protein
- Uncharacterized protein
Sequence:
MVSRAPSFSVPNAVGVPQVDDIALFLCGRAIAAEWPKVSAANASAAEALAAWYLTKVAQMHERPTTDTKGASNLGMEERSPVREAEYYQTNEANFSDAFEALSRPAGEIDALVTQKLDREDHQRGWGLSKNLLDGFAKTSGLLLTEKDIMAIDDEMKRSFRCFEELLDICLHFGETTHCNNFIYHIICFNIDNTALSSHTTQMLWNEMGIDDRAAVILPVLSRLFSVCDELGSQHAAGSITHSFIVWLGVSWNCASFSWQTHVSRVTGCLLAELEKKLILVRKDPAALTAGLRDDSTPHARRGSRAKPSQKAFGVSGSNRQLNIVSMHKAMRRICEGRTLDSKGLLEALVESGSGAALPLRDYNNVLEYIFSEQAHGGAVGTQESQQQQWHHSILSNIMNGVLLYSQFYLSVRSLEASLRCAQMGVLVGHQWRSSELLTIAHYNSFLVHVACQDTPAAAGDIAIMLQLADAATRRDGNAETDVNAPRFRAGCLGYMGAALLLLISPGTVDTSLRSIIITGIVAGVRPTSETAGGAGNMRCGGSGSVSSNANALLCTAAEAATGGGSVVVQTTAQTVRHALWLSEMEAFLDPSSTVSTEVITSVARATLMLIAGHYGVCTCTKPIDSDSLAQQLSLIEESTLDSTNNVPEPSELLLRETMRLTAHHALAVQVGTAEAPSGAGPFRILHTYLTAVEKHYGASGLAAVEQNFFFVSTYRFLCAMWLRTCGYLKSAYQELTRLVESMLFYSRCGSDSHNENVSTPAPTTRKASTQPNLHTNADLLGVDEHLLGESPVKMAGSTVKEEETLQFWPPDHLLLWQHVQFERAQLAHYLGYSCVILEISETLRRVSAASHFVMGVLYADLIAAMTWTQRKNYFGALQALEKIESNAESIGLTLVQTHARVRRVSILLACSRWQEALDTLRVMQPIPSLLEHWYLLTHLHAQSEVLMACPDATEGDLATVVDRHIQEMEMCGSFVDVTGKEDSVGITLLDKMCLYACIDRHSAALPGRGRQSWDECLNVLARELQQRQLQEGKWQVLWNMPMRNVCNEVLSNALLKRVLKTS
Protein: Furin (paired basic amino acid cleaving enzyme) b (EC 3.4.21.75) (F1QKU2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- MamL-1 domain-containing protein.
- Mastermind-like transcriptional coactivator 3.
- Mastermind-like transcriptional coactivator 1.
- Tyrosine-protein kinase.
- CD154
- Angiotensin-converting enzyme
Sequence:
MEGRLILLLFLGAYLVLLAAEVHLITGQGIYINTWAVHIEGGVEEAERIAQKHGFVSHGQVFGDFYHFQHRGVVRRSLSSHRGVHVRLHTEPQVLWAEQQIAKRRRKRDIHMEPTDPKFPQQWYLYNPSHGDLNVKEAWAQGFTGRGVVVTILDDGIEKDHPDLAKNYDPDASYDVNDRDPDPQPRYTQLNDNRHGTRCAGEVAAAANNGVCGVGVAYNAKIGGVRMLDGEVTDVVEAQSLSLNSQHIHIYSASWGPEDDGKTVDGPAKLAKEAFLQGVTEGRSGLGSIFVWASGNGGRERDSCNCDGYTNSIYTLSISSTTQYGSVPWYSEACSSTLATTYSSGNLNEKQIVTTDLRKKCTDSHTGTSASAPLAAGIIALALEANMNLTWRDMQHLVVRTSRPAHLITNDWRTNGVGRLVSHSYGYGLLDATAMVALAQNWTSMGPQHKCVINMLTEPRDIKNHLTFSRSVEACSGQPDFVSSLEHVQARLTLSYNHRGNLAVHLISPLGTRSTLLAPRPQDNSAEGFNDWAFMTTHSWDEDPRGEWTLEIENVAGLNDYGVLSQFTLILYGTGSSATDPSVSDYTRPSNNSCKTFDTQQICIECSTGFSLFLQGCVKSCPPGFISGPQVLNLSLDNWVEHSTVQACLPCHPACLTCSGSGENECLSCPPHSHLVATSCLHQNQVQRKSPSIPVIQHEADSSSEESLRDPGLSSRLPALVAVLSCAFILATFAAVFVLLQLHSGAASAPFCRRTKLPVIDTGRGGIRVGFGFGLNRGKVSYRGIPTVWGDEDAAGGMNSESDSEELEFHSEKTAFIRTQSVL
Protein: Palladin, cytoskeletal associated protein (B2RTX2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGTSSHESFYDSLSDMQEESKNTDFFPGLSAFLSQEEINKSLDLARRAIADSETEDFDSEKEISQIFSTSPASLCEHPSHKETKLGEHASRRPQDNRSTPVQPLAEKQTKSISSPVSKRKPAMSPLLTRPSYIRSLRKAEKRGAKTPSTNVKPKTPHQRKGGPQSQLCDKAANLIEELTSIFKAAKPRNRSPNGESSSPDSGYLSPKNQPSALLSASASQSPMEDQGEMEREVKSPGARHCYQDNQDLAVPHNRKSHPQPHSALHFPAAPRFIQKLRSQEVAEGSRVYLECRVTGNPTPRVRWFCEGKELHNTPDIQIHCEGGDLHTLIIAEAFEDDTGRYTCLATNPSGSDTTSAEVFIEGASSTDSDSESLAFKSRAGAMPQAQKKTTSVSLTIGSSSPKTGVTTAVIQPLSVPVQQVHSPTSYLCRPDGTTTAYFPPVFTKELQNTAVAEGQVVVLECRVRGAPPLQVQWFRQGSEIQDSPDFRILQKKPRSTAEPEEICTLVIAETFPEDAGIFTCSARNDYGSATSTAQLVVTSANTENCSYESMGESNNDHFQHFPPPPPILETSSLELASKKPSEIQQVNNPELGLSRAALQMQFNAAERETNGVHPSRGVNGLINGKANSNKSLPTPAVLLSPTKEPPPLLAKPKLGFPKKASRTARIASDEEIQGTKDAVIQDLERKLRFKEDLLNNGQPRLTYEERMARRLLGADSATVFNIQEPEEETANQEYKVSSCEQRLISEIEYRLERSPVDESGDEVQYGDVPVENGMAPFFEMKLKHYKIFEGMPVTFTCRVAGNPKPKIYWFKDGKQISPKSDHYTIQRDLDGTCSLHTTASTLDDDGNYTIMAANPQGRISCTGRLMVQAVNQRGRSPRSPSGHPHVRRPRSRSRDSGDENEPIQERFFRPHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPVRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFSLELVVAAKEAHKPPVFIEKLQNTGVADGYPVRLECRVLGVPPPQIFWKKENESLTHSTDRVSMHQDNHGYICLLIQGATKEDAGWYTVSAKNEAGIVSCTARLDVYISRH
Protein: Delta(12) fatty acid desaturase fat-2 (FAT-2) (EC 1.14.19.-) (EC 1.14.19.6) (Fatty acid desaturase 2) (G5EGA5)
Organism: Caenorhabditis elegans
Function: Can function as a Delta(12)/Delta(15) bifunctional desaturase and behaves as a nu +3' desaturase. Introduces a double bond in the fatty acid chain three carbons away from an existing double bond to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Acts on a number of substrates like oleoyl-CoA ((9Z)-octadecenoyl-CoA, 18:1n-9), palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA, 16:1n-7), and gamma-linolenoyl-CoA ((6Z,9Z,12Z)-octadecatrienoyl-CoA, 18:3n-6), to generate linoleoyl-CoA ((9Z,12Z)-octadecadienoyl-CoA, 18:2n-6), (9Z,12Z)-hexadecadienoyl-CoA (16:2n-4) and (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA (18:4n-3) respectively. Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (Probable).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Delta
- Delta
- Delta
- Delta
- Delta
- Long chain fatty acid elongase 2
- Long chain fatty acid elongase 1
- Long chain fatty acid elongase 5
Sequence:
MTIATKVNTNKKDLDTIKVPELPSVAAVKAAIPEHCFVKDPLTSISYLIKDYVLLAGLYFAVPYIEHYLGWIGLLGWYWAMGIVGSALFCVGHDCGHGSFSDYEWLNDLCGHLAHAPILAPFWPWQKSHRQHHQYTSHVEKDKGHPWVTEEDYNNRTAIEKYFAVIPISGWLRWNPIYTIVGLPDGSHFWPWSRLFETTEDRVKCAVSGVACAICAYIAFVLCDYSVYTFVKYYYIPLLFQGLILVIITYLQHQNEDIEVYEADEWGFVRGQTQTIDRHWGFGLDNIMHNITNGHVAHHFFFTKIPHYHLLEATPAIKKALEPLKDTQYGYKREVNYNWFFKYLHYNVTLDYLTHKAKGVLQYRSGVEAAKAKKAQ
Protein: Sulfiredoxin-1 (EC 1.8.98.2) (Q9BYN0)
Organism: Homo sapiens (Human)
Function: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15448164}.
Interaction partners:
- Peroxiredoxin-1
- Nuclear factor erythroid 2-related factor 2
- Thioredoxin reductase 1, cytoplasmic
- Peroxiredoxin-2
- Thioredoxin
- NAD
- Glutamate--cysteine ligase regulatory subunit
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Peroxiredoxin-4
- Glutamate--cysteine ligase catalytic subunit
Sequence:
MGLRAGGTLGRAGAGRGAPEGPGPSGGAQGGSIHSGRIAAVHNVPLSVLIRPLPSVLDPAKVQSLVDTIREDPDSVPPIDVLWIKGAQGGDYFYSFGGCHRYAAYQQLQRETIPAKLVQSTLSDLRVYLGASTPDLQ
Protein: F-box/WD repeat-containing protein 8 (F-box and WD-40 domain-containing protein 8) (F-box only protein 29) (Q8N3Y1)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul7-RING ubiquitin-protein ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The Cul7-RING(FBXW8) complex mediates ubiquitination and consequent degradation of GORASP1, acting as a component of the ubiquitin ligase pathway that regulates Golgi morphogenesis and dendrite patterning in brain. Mediates ubiquitination and degradation of IRS1 in a mTOR-dependent manner: the Cul7-RING(FBXW8) complex recognizes and binds IRS1 previously phosphorylated by S6 kinase (RPS6KB1 or RPS6KB2). The Cul7-RING(FBXW8) complex also mediates ubiquitination of MAP4K1/HPK1: recognizes and binds autophosphorylated MAP4K1/HPK1, leading to its degradation, thereby affecting cell proliferation and differentiation. Associated component of the 3M complex, suggesting that it mediates some of 3M complex functions.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:21572988}. Golgi apparatus {ECO:0000269|PubMed:21572988}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8BIA4}. Note=Localizes to the cytosol when phosphorylated at Ser-85, promoting IRS1 ubiquitination. {ECO:0000250|UniProtKB:Q8BIA4}.
Interaction partners:
- Cullin-7
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase RBX1
- Cullin-1
- Glomulin
- Obscurin-like protein 1
- S-phase kinase-associated protein 2
- NEDD8-activating enzyme E1 catalytic subunit
- F-box only protein 4
- Insulin receptor substrate 1
Sequence:
MDDYSLDEFRRRWQEELAQAQAPKKRRRPEAAERRARRPEVGSGRGEQASGDPALAQRLLEGAGRPPAARATRAEGQDVASRSRSPLAREGAGGGEQLVDQLIRDLNEMNDVPFFDIQLPYELAINIFQYLDRKELGRCAQVSKTWKVIAEDEVLWYRLCQQEGHLPDSSISDYSCWKLIFQECRAKEHMLRTNWKNRKGAVSELEHVPDTVLCDVHSHDGVVIAGYTSGDVRVWDTRTWDYVAPFLESEDEEDEPGMQPNVSFVRINSSLAVAAYEDGFLNIWDLRTGKYPVHRFEHDARIQALALSQDDATVATASAFDVVMLSPNEEGYWQIAAEFEVPKLVQYLEIVPETRRYPVAVAAAGDLMYLLKAEDSARTLLYAHGPPVTCLDVSANQVAFGVQGLGWVYEGSKILVYSLEAGRRLLKLGNVLRDFTCVNLSDSPPNLMVSGNMDGRVRIHDLRSGNIALSLSAHQLRVSAVQMDDWKIVSGGEEGLVSVWDYRMNQKLWEVYSGHPVQHISFSSHSLITANVPYQTVMRNADLDSFTTHRRHRGLIRAYEFAVDQLAFQSPLPVCRSSCDAMATHYYDLALAFPYNHV
Protein: Vesicular glutamate transporter 3 (VGluT3) (Solute carrier family 17 member 8) (Q7TSF2)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter that mediates the uptake of L-glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation (By similarity). The symporter activity is electrogenic (By similarity). Moreover, operates synergistically with SLC18A3/VACHT under a constant H(+) gradient, thereby allowing striatal vesicular acetylcholine uptake.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12384506, ECO:0000269|PubMed:12388773, ECO:0000305|PubMed:12097496}. Cell membrane {ECO:0000250|UniProtKB:Q8NDX2}; Multi-pass membrane protein {ECO:0000305}. Synapse, synaptosome {ECO:0000269|PubMed:12384506, ECO:0000269|PubMed:12388773}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Vesicular acetylcholine transporter
- Synaptic vesicular amine transporter
- Chromaffin granule amine transporter
- Vesicular glutamate transporter 1
- Vesicular glutamate transporter 2
- Glutamate decarboxylase 1
Sequence:
MPFNAFDTFKEKILKPGKEGVKNAVGDSLGILQRKLDGTNEEGDAIELSEEGRPVQTSRARAPVCDCSCCGIPKRYIIAVMSGLGFCISFGIRCNLGVAIVEMVNNSTVYVDGKPEIQTAQFNWDPETVGLIHGSFFWGYIVTQIPGGFISNKFAANRVFGAAIFLTSTLNMFIPSAARVHYGCVMCVRILQGLVEGVTYPACHGMWSKWAPPLERSRLATTSFCGSYAGAVVAMPLAGVLVQYIGWASVFYIYGMFGIIWYMFWLLQAYECPAVHPTISNEERTYIETSIGEGANLASLSKFNTPWRRFFTSLPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFAISKVGLLSAVPHMVMTIVVPIGGQLADYLRSRKILTTTAVRKIMNCGGFGMEATLLLVVGFSHTKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGAMTKHKTREEWQNVFLIAALVHYSGVIFYGVFASGEKQDWADPENLSEEKCGIIDQDELAEETELNHEAFVSPRKKMSYGATTQNCEVQKTDRRQQRESAFEGEEPLSYQNEEDFSETS
Protein: Alpha-L-arabinofuranosidase B (ABF B) (Arabinosidase B) (EC 3.2.1.55) (Q8NK89)
Organism: Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Alpha-L-arabinofuranosidase.
- Alpha-L-arabinofuranosidase A
- Alpha-L-arabinofuranosidase.
- Exopolygalacturonase X
- Alpha-L-arabinofuranosidase E.
- Polygalacturonase
- Endo-xylogalacturonan hydrolase A
- Probable endopolygalacturonase II
- Hydrolase.
- Glycine cleavage system H protein
Sequence:
MFSRRNLLALGLAATVSAGPCDIYEAGDTPCVAAHSTTRALYSSFSGALYQLQRGSDDTTTTISPLTAGGIADASAQDTFCANTTCLITIIYDQSGNGNHLTQAPPGGFDGPDTDGYDNLASAIGAPVTLNGQKAYGVFMSPGTGYRNNEATGTATGDEAEGMYAVLDGTHYNDACCFDYGNAETSSTDTGAGHMEAIYLGNSTTWGYGAGDGPWIMVDMENNLFSGADEGYNSGDPSISYRFVTAAVKGGADKWAIRGANAASGSLSTYYSGARPDYSGYNPMSKEGAIILGIGGDNSNGAQGTFYEGVMTSGYPSDDTENSVQENIVAAKYVVGSLVSGPSFTSGEVVSLRVTTPGYTTRYIAHTDTTVNTQVVDDDSSTTLKEEASWTVVTGLANSQCFSFESVDTPGSYIRHYNFELLLNANDGTKQFHEDATFCPQAALNGEGTSLRSWSYPTRYFRHYENVLYAASNGGVQTFDSKTSFNNDVSFEIETAFAS
Protein: Protein kinase domain-containing protein ppk3 (O13733)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein kinase domain-containing protein ppk32
- Coatomer subunit delta
- Putative coatomer subunit alpha
Sequence:
MDFIKSAASFIAKAGSQFPYDLNEKIPLSSNSVWTLQTGSIRESAQPCSVFSISLSTHPEWAELADRACETMKTLRHPCIIKYLSTYKSSTHLYIATETVRPVTTELNELSAEIKTYGLWRVSAALSFLNDKNIVHGNLQMSSVYLNSADEWIIGDFFLAGDSPQFIKDNHDKILNWSRLVPFEIQSSTLNSASFIYLDSYELGKFISHLYNGTPGDLSQRGNIPANIFVSAKKLLNVEGKQKLLASEFLKLGERPGGFFRTHLITLYELLSEVRINEEEDRVKLKQLLSSKLEVIPKNYIQKVVLNILFLLLSIDTHSDVVELLFKCAQIVKGRPDIEKDFGVPLLSLLKQQSVPIRGLLLSGIINNPDVLPKNIYEDTSFSVFANLVRSNSPTLKEHAIVVFSIIAPKLSKKTLNNELLRSLAVVQNDQHPTLRTNSTICLGKIAEYLDASVRKPVLAAALSRSLKDPFVPAREAALKVLLSVQNYFDTKDVAIKLFPSVVPLLIDENEGIRRTAEDVTDQFLSRIKNFNLGEKENVSAPAKFNGSFWSKFIHSSSASPSPSIDMKKESLELKNDTTEIKEKKNSKSRVVGNTENSKDEFNNPLFETEEQIDESWMENWNDEEETENNVEESWGL
Protein: F-box protein SKIP2 (SKP1-interacting partner 2) (Q9FE83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Non-specific lipid transfer protein GPI-anchored 4
- GDSL esterase/lipase At2g31550
- AT3G45050 protein
- SKP1-like protein 1A
- Peptidyl-prolyl cis-trans isomerase CYP65
- RHOMBOID-like protein 2
- F-box only protein 13
Sequence:
MGQAPSSTAESNGRELDLRLWSPVIVAGGESMAVGNVVDRDFTGDLPDECLAHVFQFLGAGDRKRCSLVCKRWLLVDGQSRHRLSLDAKDEISSFLTSMFNRFDSVTKLALRCDRKSVSLSDEALAMISVRCLNLTRVKLRGCREITDLGMEDFAKNCKNLKKLSVGSCNFGAKGVNAMLEHCKLLEELSVKRLRGIHEAAELIHLPDDASSSSLRSICLKELVNGQVFEPLLATTRTLKTLKIIRCLGDWDKVLQMIANGKSSLSEIHLERLQVSDIGLSAISKCSNVETLHIVKTPECSNFGLIYVAERCKLLRKLHIDGWRTNRIGDEGLLSVAKHCLNLQELVLIGVNATHMSLAAIASNCEKLERLALCGSGTIGDTEIACIARKCGALRKFCIKGCPVSDRGIEALAVGCPNLVKLKVKKCKVVTGEIGDWLREQRRTLVVSMDGDETEAVVVVDGEVETVVEEPRVAQAGGIVAEIGSSNGGGGSRLAMIRSKLGFLAGRNLVTCTFRRWSHNDNASSST
Protein: Ribosomal RNA small subunit methyltransferase (EC 2.1.1.-) (18S nuclear rRNA (adenine(1785)-N(6)/adenine(1786)-N(6))-dimethyltransferase) (Adenosine dimethyl transferase 1A) (Dimethyladenosine transferase 1A) (O22268)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: N6-adenine methyltransferase which modifies the AA dinucleotide at the plant nuclear 18S rRNA nucleotides A1785 and A1786. Required for generating appropriate patterns of gene expression during root development, including the cell-specific expression of transcriptional regulators involved in root hair and non-hair cells patterning.
Subcellular location: Nucleus {ECO:0000269|PubMed:19929881, ECO:0000269|PubMed:22829145}. Nucleus, nucleolus {ECO:0000269|PubMed:19929881, ECO:0000269|PubMed:22829145}.
Interaction partners:
- Bystin
- Periodic tryptophan protein 2
- RNA-binding NOB1-like protein
- Putative U3 small nucleolar ribonucleoprotein
- At3g49990
- rRNA biogenesis protein RRP5
- Transducin family protein / WD-40 repeat family protein
- At1g42440/F7F22_7
- 18S rRNA
- Putative WD-repeat membrane protein
Sequence:
MAGGKIRKEKPKASNRAPSNHYQGGISFHKSKGQHILKNPLLVDSIVQKAGIKSTDVILEIGPGTGNLTKKLLEAGKEVIAVELDSRMVLELQRRFQGTPFSNRLKVIQGDVLKTELPRFDICVANIPYQISSPLTFKLLFHPTSFRCAVIMYQREFAMRLVAQPGDNLYCRLSVNTQLYARVSHLLKVGKNNFRPPPKVDSSVVRIEPRRPGPQVNKKEWDGFLRVCFIRKNKTLGSIFKQKSVLSMLEKNFKTLQAVLASLQNNGEPALNTTSMDLGDQSMGMEDDDNEMDDDDMEMDEGEGDGGETSEFKEKVMNVLKEGGFEEKRSSKLSQQEFLYLLSLFNKSGIHFT
Protein: C-C motif chemokine 9 (CCF18) (Macrophage inflammatory protein 1-gamma) (MIP-1-gamma) (Macrophage inflammatory protein-related protein 2) (MRP-2) (Small-inducible cytokine A9) [Cleaved into: CCL9(29-101); CCL9(30-101); CCL9(31-101)] (P51670)
Organism: Mus musculus (Mouse)
Function: Monokine with inflammatory, pyrogenic and chemokinetic properties. Circulates at high concentrations in the blood of healthy animals. Binding to a high-affinity receptor activates calcium release in neutrophils. It also inhibits colony formation of bone marrow myeloid immature progenitors.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 1
- C-C chemokine receptor type 2
- C-C chemokine receptor type 5
- C-C chemokine receptor 1-like protein 1
- C-X-C chemokine receptor type 3
- C-C motif chemokine 2
- Probable C-C chemokine receptor type 3
- C-C chemokine receptor type 8
- C-C chemokine receptor type 7
- C-C chemokine receptor type 6
Sequence:
MKPFHTALSFLILTTALGIWAQITHATETKEVQSSLKAQQGLEIEMFHMGFQDSSDCCLSYNSRIQCSRFIGYFPTSGGCTRPGIIFISKRGFQVCANPSDRRVQRCIERLEQNSQPRTYKQ
Protein: DnaJ protein P58IPK homolog B (OsP58B) (Chaperone protein dnaJ C15) (OsDjC15) (Q5JNB5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in protein folding in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:24153418}. Note=Localizes to the endoplasmic reticulum (ER) and to punctae around the ER. {ECO:0000269|PubMed:24153418}.
Interaction partners:
- DnaJ protein ERDJ3B
- Os02g0710900 protein
- Os01g0757900 protein
- Endoplasmin homolog
- Heat shock 70 kDa protein BIP4
- Os05g0181000 protein.
- Os11g0696600 protein
- 70 kDa heat shock protein
- Os06g0679800 protein
- Heat shock 70 kDa protein BIP5
Sequence:
MARWPWRWRVLLPLLLLHSSPVFAQEGQDNDPSTLFKRASEMMNLRKYDGSLGLLNAVLEVDPNHSEAYRQRASVLRHKCRYKEAEGDYSKYLELKPGSSSVEKELSQLLQAQNALESAYGQFESHDFSKVLEYINKIVLVFSPNCLKAKLLKAKALLALEDYSSVISETGFILKEDEDNLDALLLRGRAYYYLADHDVASRHYQKGLRLDPEHSELKKAYFGLKNLLKKTKSAEDNAAKGKLRVSAEDYKAALAMDPDHTSYNVHLYLGLCKVLVKLGRGKEAISSCTEALNIDGELVDALTQRGEAKLLTEDWEGAVQDLKEASQKSPQDMGIREALMRAEKQLKLSKRKDWYKILGISKTASAADIKRAYKKLALQWHPDKNVDNREEAENMFREIAAAYEVLGDEDKRVRYDRGEDLDEMNMGGGGGGFNPFGGGGQQYTFHYDGGFYGGGGFPGGGFPGGFQFNFG