wanglab/gogpt-training-data huggingface dataset:
Protein: RNA replication protein (165 kDa protein) (ORF1 protein) [Includes: RNA-directed RNA polymerase (EC 2.7.7.48); Helicase (EC 3.6.4.13)] (P17779)
Organism: Potato virus X (strain X3) (PVX)
Function: RNA replication. The central part of this protein possibly functions as an ATP-binding helicase (Probable).
Interaction partners:
Sequence:
MAKVREVYQSFTDSTTKTLIQDEAYRNIRPIMEKHKLANPYAQTVEAANDLEGFGIATNPYSIELHTHAAAKTIENKLLEVLGSILPQEPVTFMFLKPRKLNYMRRNPRIKDIFHNVAIEPRDVARYPKETIIDKLTEITTETAYISDTLHFLDPSYIVETFQNCPKLQTLYATLVLPVEAAFKMESTHPNIYSLKYFGDGFQYIPGNHGGGAYHHEFAHLQWLKVGKIKWRDPKDSFLGHLNYTTEQVEMHTVTVQLQESFAANHLYCIRRGDLLTPEVRTFGQPDRYVIPPQIFLPKVHNCKKPILKKTMMQLFLYVRTVKVAKNCDIFAKVRQLIKSSDLDKYSAVELVYLVSYMEFLADLQATTCFSDTLSGGLLTKTLAPVRAWIQEKKMQLFGLEDYAKLVKAVDFHPVDFSFKVETWDFRFHPLQAWKAFRPREVSDVEEMESLFSDGDLLDCFTRMPAYAVNAEEDLATIRKTPEMDVGQEVKEPAGDRNQYSNPAETFLNKLHRKHSREVKHQAVKKAKRLAEIQESMRAEGEAEPNETSGGMGAIPSNAELPGTSDARQELTLPTTKPVPARWEDASFTDSSVEEEQVRLLGEEAVKTATQQVIEGLPWKHWIPQLNAVGFKALLIQRDRSGTMIMPITEMVSGLEKEDFPEGTPKELARELLVMNRSPATIPLDLLRARDYGSDVKNKRIGAITKTQATSWGEYLTGKIESLTERKVATCVIHGAGGSGKSHAIQKALREIGKGSDITVVLPTNELRLDWSKKVPNTEPYMFKTYEKALIGGTGSIVIFDDYSKLPPGYIEALVCFYSKIKLIILTGDSRQSVYHETAEDASIRHLGPATEYFSKYCRYYLNATHRNKKDLANMLGVYSERTGVTEISMSAEFLEGIPTLVPSDEKRKLYMGTGRNDTFTYAGCQGLTKPKVQIVLDHNTQVCSANVMYTALSRATDRIHFVNTSANSSAFWEKLDSTPYLKTFLSVVREQALREYEPAEAEPIQEPEPQTHMCVENEESVLEEYKEELLEKFDREIHSESHGHSNCVQTEDTTIQLFSHQQAKDETLLWATIDARLKTSNQEANFREFLSKKDIGDVLFLNYQKAMGLPKERIPFSQEVWEACAHEVQSKYLSKSKCNLINGTVRQSPDFDENKIMVFLKSQWVTKVEKLGLPKIKPGQTIAAFYQQTVMLFGTMARYMRWFRQAFQPKEVFINCETTPEDMSVWALNNWNFSRPSLANDYTAFDQSQDGAMLQFEVLKAKHHCIPEEIIQAYIDIKTNAQIFLGTLSIMRLTGEGPTFDANTECNIAYTHTKFDIPAGTAQVYAGDDSALDCVPEVKHSFHRLEDKLLLKSKPVITQQKKGSWPEFCGWLITPKGVMKDPIKLHVSLKLAEAKGELKKCQDSYEIDLSYAYDHKDSLHDLFDEKQCQAHTLTCRTLIKSGRGTVSLPRLRNFL
Protein: ATPase-stabilizing factor 15 kDa protein (15 kDa ATPase inhibitor complex-stabilizing factor) (15K) (Hydrophilin STF2) (Stabilizing factor 2) (P16965)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This is one of two stabilizing factors of the inactive mitochondrial F0F1-ATPase. It binds to the F0 part and facilitates the binding of both the inhibitor and the 9 kDa protein to F1.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:6200468}. Cytoplasm {ECO:0000269|PubMed:22442684}.
Interaction partners:
- F
- Restriction of telomere capping protein 3
- Nicotinamidase
- Carboxypeptidase Y inhibitor
- Inactive diphosphatase DCS2
- Phosphoglucomutase 2
- Uncharacterized protein YBR053C
- Uncharacterized protein YJL144W
- Protein SIP18
- 6-phosphogluconolactonase 4
Sequence:
MTRTNKWTEREGKADPKYFSHTGNYGESPNHIKKQGSGKGNWGKPGDEIDDLIDNGEIPPVFKKDRRGSNLQSHEQKFENVQKE
Protein: MLO-like protein 5 (AtMlo5) (O22815)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Cytochrome P450 71B8
- Putative cytochrome P450 71A28
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
- MLP-like protein 329
Sequence:
MAGGGGGSTSGEGPRELDQTPTWAVSTVCGVIILISIVLELMIHKIGEVFTERRKKALYEALQKIKNELMVLGFISLLLTFGQNYIASLCVASRYGHAMSFCGPYDGPSGESKKPKTTEHLERRVLADAAPAQCKKGYVPLISLNALHQVHIFIFFLAVFHVIYSAITMMLGRAKIRGWKVWEEEVINDHEMMNDPSRFRLTHETSFVREHVNPWAKNRFSFYVMCFFRQMLRSVRKSDYLTMRHGFISVHLAPGMKFNFQKYIKRSLEDDFKVVVGISPELWAFVMLFLLFDVHGWYVTAVITMIPPLLTLAIGTKLQAIISDMALEIQERHAVIQGMPLVNVSDRHFWFSRPALVLHIIHFILFQNAFEITYFFWIWYEFGLRSCFHHHFALIIIRVALGVGVQFLCSYITLPLYALVTQMGSTMKRSVFDDQTSKALKNWHKNAKKKSETPGQTQPPLPNLRPKTGGDIESASPANITASVDVKESDQSQSRDLLSGP
Protein: NAD-specific glutamate dehydrogenase (EC 1.4.1.2) (Q5AW79)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glutamate synthase
- Glutamine synthetase
- NADP-specific glutamate dehydrogenase
- Glutamate decarboxylase
- Glutamate decarboxylase
- Aspartate aminotransferase
- Glutamine synthetase
- Glutamate pyruvate transaminase
- aspartate transaminase
- Aspartate aminotransferase
Sequence:
MVSPASSLQSLPDVHVNGNEPNKLPVRSAPKLYGSNDGASSGTGTPIGFQRQPHNKILDSVAGSNVRMPSPQPTHLAIPGSPHRVLSEEDPGYIAAKFEGKEHQMEEVMDQLEKKGFIPPEFIVGETEWFYNQLGIDDTYFQTETVEAIVTQILSLYAAKVAAYARDDKKLEIRLDKEAEDHAVYIDTSKPGFSSVNGPGYEQRIDKKYIDGSTHDHSYRIETFRSPTPVPGDDGQQLRCYFVYKCQFANPNPGPQETNIDIIGEKRFLQKATPNTKAIYQEIISNAVARAGPVIEMFEIEGSREKRLVIAYRQGSAMGLFSALSDLYHYYRLTSSRKYLENFSNGITVISLYLRPLKNAEVAAKFPPIEAAVHQIIKEISLLYCIPQNRFQHHFASGRLSLQETIYAHCAWVFVQQFLNRLGSEYTSLTDLLDSNNSTHAELLAKIKKRLRTETFTSDYIAEIVNKYPDLIHKLYLDFANTHYVQTQGPTEDDFLPTLSYLRLQVDQVLDSRQLKQLVSSTAANEHDEMVMSAFRVFNASILKTNFFTPTKVALSFRLDPHFLPEHEYPQRLYGMFLVISSEFRGFHLRFRDIARGGIRIVKSRNKEAYSINARSLFDENYNLANTQQRKNKDIPEGGAKGVILLDVNHQDKARVAFEKYIDSILDLLLPPASPGIKDPIVDLYGKDEILFMGPDENTAELVDWATEHARNRGAPWWKSFFTGLSPRLGGIPHDTYGMTTLSVRQYVLGIYRKLKIDPSTIRKLQTGGPDGDLGSNEILLANEKYTAIVDGSGVIVDPQGLNREELVRLAKKRATISEFDVSKLSPNGYRVLVDESNVHLPSGELVHNGMVFRNMFHLRKELTYDTFVPCGGRPESIDLSNVGKLIENGKSTIPYIVEGANLFITQDSKLRLEKAGCILFKDASANKGGVTSSSLEVLASLSFDDQGFVQNMCVGDDDSVPEFYREYVKQVQEVIKENATLEFEAIWREHEQTGIPRSVLSDRLSVAITQLDEELQKTELWDNVELRRSVLNDALPKLLLDKIGLDTILQRVPENYLRAIFGSHLASRFVYEYGSSPSQFSFFNFMTKRLAQSKA
Protein: Transcription initiation factor TFIID subunit 2 (Q3KRD7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPPTGLESSRMNRKKGDKGFESPRPYKLTHQVVCINNINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFSNAYAAAVSAVDPDAGNGELCIKVPSELWKHVDELKVLKIHINFSLDQPKGGLHFVVPSVEGSMAERGAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKTFHYVLAIPTAASNISLAIGPFEILVDPYMHEVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYHHWIKEELDKIVAYELKTGGVLLHPIFGGGKEKDNPASHLHFSIKHPHTLSWEYYTMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTASSQKFQSHMWSQMLVSTYGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVLELEIKQDYTSPGTQKYVGPLKVTVQELDGSFNHTLQIEENSLKHDIPCHSKKKKKK
Protein: Anion exchange protein (Q9VM31)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MAEKNEYIELPWTMNSSSGDDEAPKDPRTGGEDFTQQFTENDFEGHRAHTVYVGVHVPGGRRHSQRRRKHHHSGPGGGGGGGGGGGSIGGSGSVGGGAGKDNVSEKQQEVERPVTPPAQRVQFILGEDVDDGTHVSHPLFSEMGMLVKEGDEIEWKETARWIKFEEDVEEGGNRWSKPHVATLSLHSLFELRRLLVNGSVMLDMEAQNLEVMADLVCDHMVSAGTLPPGVKDKVKDALLRRHRHQHEYAKKTRLPIIRSLADMRNHSSSKKKKSNSKHSRPAQNLSSITEDMVKSPSNQSMARPGSGTELSEQQHKGNTHFMRKIPPGAEASNILVGEVDFLERTLSCFIRLSQAVVLGDLTEVPVPTRFVFILLGPPGSQSNFHEIGRAMATLMSDEIFHEVAYRARKRDHLLSGVDEFLDAVTVLPPGEWDPTIRIEPPAAIPSQEVRKRPPELPKEEVDEEEEEARLREENGLSRTGRLFGGLINDIKRKAPWYISDYKDALSMQCVASWIFLYFACLSPIITFGGLLAEATGKHMAAMESLVSGFVCGMGYGFFSGQPLTILGSTGPVLVFESIIYEFCLKMGWDYMTFRFWIGMWVAGICIVLTAIDASALVCYITRFTEENFATLIAFIFIYKAIENVMVIGKNFPVNQGIYDCVCTPPIGSNASVIDYAKYNWDSCESYNGTLVGGDCGTPPTENVFLMSVVLCAGTFLISTVLKEFKNALFFPSIVRQYISDFSVLIAIFAMSFFDYSLGVPTQKLEVPNELKPTLSTRGWLIPPFVEKNPWWSAIIAVFPALLGTILIFMDQQITAVIVNRKENKLKKGCGYHLDLFILSILIAICSMMGLPWFVAATVLSINHVNSLKLESECSAPGEKPQFLGVREQRVTHILIFLTIGVSVLLTPLLGNIPMPVLFGVFLYMGVASLKGLQFFDRILIMFMPAKYQPDYMFLRQVPIKRVHLFTMIQLACLIILWLIKSFSQTSILFPLMLVVMIGIRKALDLVFTRRELKILDDIMPEMTKRAAADDLHKLDAEVGLLARIFPWGKGSRSRVVTKPPGLDDGIVGSGGAVGAGLITCTTSNANEKEFEAQSSLLKK
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q7ZZA3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Tetraspanin
Sequence:
MATRTGIVLIFLAVFAFVAAEDGESKESVIEQLVVETLVMPESCTITSEMGDTLQIHYTGRLMDGKVIDTSLSREPLVVELGKRSVITGLEQALVGVCEGQKIKAMIPAHLAYGKRGYPPTIPGDSTLEFEVEVISLSQQTPWQKLINDILPLLCLALVPTLLGLVGLYLYNKAHAQPQGKKKSKDKKSKKK
Protein: 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) (A0A060WX43)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- GDH/6PGL endoplasmic bifunctional protein
- Hexose-6-phosphate dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Glucose-6-phosphate 1-dehydrogenase
- Transaldolase
- Transaldolase
- glucose-6-phosphate dehydrogenase
- Ribulose-phosphate 3-epimerase
- Transketolase N-terminal domain-containing protein
Sequence:
MAEADIALIGLAVMGQNIILNMNDHGFVVCAYNRTVSKVHDFLANEAKGTKIIGAESLEDMVAKLKKPRRIVMLVKAGQAVDDFIDKLVPLLEAGDIIIDGGNSEYRDTTRRCKSLKEKNLLFVGSGVSGGEEGARYGPSLMPGGHKEAWPHIKEIFQSIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMDHDVMAQAFEDWNKTELDSFLIEITAGILKFRDTDGTHLLPKIRDAAGQKGTGKWTAISALEYGTPVTLIGEAVFARCLSALKDERVEASRSLAGPQGAKFNGDKASFLEDIRKALYASKIISYAQGFMLLRQAAKEFGWSLNYGAIALMWRGGCIIRSVFLGKIKEAFDRDAELQNLLLDTFFSNAVQDCQDSWRRAVSIGVQQGIPMPCFTTALSFYDGYRHDMLPANLLQAQRDYFGAHTYELLSNPGKYIHTNWTGHGGNVSSSSYNA
Protein: Dual specificity phosphatase 21 (D3ZAQ8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Haloacid dehalogenase-like hydrolase domain-containing 5
Sequence:
MTTASCILPSQAIQQDNIYGLSQITTSLFISNSAVANDKLTLSNNHITTIINASVEVVNTFFEDIQYVHVPVSDAPNSYLYDFFDPIADHIHGVEMRNGRTLLHCAAGVSRSAALCLAYLMKYHTMTLLDAHTWTKSCRPIIRPNNGFWEQLIHYEFKLFSRNTVHMIYSPMGLIPNIYEKDAYLMELM
Protein: Cell cycle checkpoint control protein RAD9B (DNA repair exonuclease rad9 homolog B) (hRAD9B) (Q6WBX8)
Organism: Homo sapiens (Human)
Interaction partners:
- Checkpoint protein HUS1B
- Checkpoint protein HUS1
- Cell cycle checkpoint protein RAD1
- Cell cycle checkpoint protein RAD17
- DNA topoisomerase 2-binding protein 1
- Serine/threonine-protein kinase ATR
- Cell cycle checkpoint control protein RAD9A
- Replication factor C subunit 2
- Serine-protein kinase ATM
- Replication factor C subunit 4
Sequence:
MLKCVMSGSQVKVFGKAVQALSRISDEFWLDPSKKGLALRCVNSSRSAYGCVLFSPVFFQHYQWSALVKMSENELDTTLHLKCKLGMKSILPIFRCLNSLERNIEKCRIFTRSDKCKVVIQFFYRHGIKRTHNICFQESQPLQVIFDKNVCTNTLMIQPRLLADAIVLFTSSQEEVTLAVTPLNFCLKSSNEESMDLSNAVHSEMFVGSDEFDFFQIGMDTEITFCFKELKGILTFSEATHAPISIYFDFPGKPLALSIDDMLVEANFILATLADEQSRASSPQSLCLSQKRKRSDLIEKKAGKNVTGQALECISKKAAPRRLYPKETLTNISALENCGSPAMKRVDGDVSEVSESSVSNTEEVPGSLCLRKFSCMFFGAVSSDQQEHFNHPFDSLARASDSEEDMNNVCCRKEFNGSDAKYFCII
Protein: Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase) (P13663)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Homoserine dehydrogenase
- Aspartokinase
- Homoserine kinase
- Threonine synthase
- Protein ARG5,6
- Acetolactate synthase small subunit, mitochondrial
- Phosphoglycerate kinase
- Tryptophan synthase
- Ornithine decarboxylase
- Argininosuccinate synthase
Sequence:
MAGKKIAGVLGATGSVGQRFILLLANHPHFELKVLGASSRSAGKKYVDAVNWKQTDLLPESATDIIVSECKSEFFKECDIVFSGLDADYAGAIEKEFMEAGIAIVSNAKNYRREQDVPLIVPVVNPEHLDIVAQKLDTAKAQGKPRPGFIICISNCSTAGLVAPLKPLIEKFGPIDALTTTTLQAISGAGFSPGVPGIDILDNIIPYIGGEEDKMEWETKKILAPLAEDKTHVKLLTPEEIKVSAQCNRVAVSDGHTECISLRFKNRPAPSVEQVKTCLKEYVCDAYKLGCHSAPKQTIHVLEQPDRPQPRLDRNRDSGYGVSVGRIREDPLLDFKMVVLSHNTIIGAAGSGVLIAEILLARNLI
Protein: Ceramide phosphoethanolamine synthase (CPE synthase) (EC 2.7.8.48) (O77475)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the biosynthesis of ceramide phosphoethanolamine (CPE) through the transfer of a phosphatidyl head group from cytidine 5'-diphosphate (CDP)-ethanolamine on to the primary hydroxyl of ceramide.
Subcellular location: Membrane {ECO:0000269|PubMed:23449981}; Multi-pass membrane protein {ECO:0000269|PubMed:23449981}. Golgi apparatus membrane {ECO:0000269|PubMed:23449981}. Cell membrane {ECO:0000269|PubMed:23449981}. Note=The majority of protein localizes to the Golgi apparatus. {ECO:0000269|PubMed:23449981}.
Interaction partners:
- LD47749p
- U3 small nucleolar ribonucleoprotein protein IMP3
- Bystin
- ATP-dependent RNA helicase DHX15 homolog
- Pre-mRNA-processing factor 17
- Cell division cycle 5, isoform A
- Pre-mRNA-splicing factor syf1 homolog
- Protein crooked neck
- Eukaryotic initiation factor 4A-III
- LD31322p
Sequence:
MIGPSSQISKILLTLLFLLIIFYVFMDVELYLRIHNYAIERNYHTNVSLPASVVGPSTSESGSGSIGGSSSSSSSSSSSTSTKLPTAGDRQPSYEDHTWISCDINPLCHVTVKAILLDHTNHYLFAPLATMFDNVIGFSRSTFITPNMISFFHVGVACLAGKLVASDSLGYRRLGVLLFQIRTFLDDLDGHVARVRKHIRGERSEIGTSGYYVDGLCDGLGCIALLLGIFFYLKNNPPRRGYSIIPMSDSKLPEPTMMIPKMKATTRKVAKNVISFTGQLLLSSTAWNRYIAVYQNMLEREDVSGNQSHCQDYVFKSTWFFCVAWMWRIVNVHALLHCVLLSIFCDKLWDFLRAIRYSGYIILLVAICLTEMHILEAQNYIFNSTACSNISL
Protein: Polygalacturonate 4-alpha-galacturonosyltransferase (EC 2.4.1.43) (Alpha-1,4-galacturonosyltransferase 1) (Galacturonosyltransferase 1) (Like glycosyl transferase 1) (Q9LE59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pectin biosynthesis. Catalyzes the transfer of galacturonic acid from uridine 5'-diphosphogalacturonic acid onto the pectic polysaccharide homogalacturonan.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Galacturonosyltransferase
- Probable arabinosyltransferase ARAD2
- Probable galacturonosyltransferase 7
- Probable methyltransferase PMT14
- Probable arabinosyltransferase ARAD1
- UDP-glucuronate 4-epimerase 6
- UDP-glucuronate 4-epimerase 1
- UDP-glucuronate 4-epimerase 3
- Xylogalacturonan beta-1,3-xylosyltransferase
- Probable pectin methyltransferase QUA3
Sequence:
MALKRGLSGVNRIRGSGGGSRSVLVLLIFFCVFAPLCFFVGRGVYIDSSNDYSIVSVKQNLDWRERLAMQSVRSLFSKEILDVIATSTADLGPLSLDSFKKNNLSASWRGTGVDPSFRHSENPATPDVKSNNLNEKRDSISKDSIHQKVETPTKIHRRQLREKRREMRANELVQHNDDTILKLENAAIERSKSVDSAVLGKYSIWRRENENDNSDSNIRLMRDQVIMARVYSGIAKLKNKNDLLQELQARLKDSQRVLGEATSDADLPRSAHEKLRAMGQVLAKAKMQLYDCKLVTGKLRAMLQTADEQVRSLKKQSTFLAQLAAKTIPNPIHCLSMRLTIDYYLLSPEKRKFPRSENLENPNLYHYALFSDNVLAASVVVNSTIMNAKDPSKHVFHLVTDKLNFGAMNMWFLLNPPGKATIHVENVDEFKWLNSSYCPVLRQLESAAMREYYFKADHPTSGSSNLKYRNPKYLSMLNHLRFYLPEVYPKLNKILFLDDDIIVQKDLTPLWEVNLNGKVNGAVETCGESFHRFDKYLNFSNPHIARNFNPNACGWAYGMNMFDLKEWKKRDITGIYHKWQNMNENRTLWKLGTLPPGLITFYGLTHPLNKAWHVLGLGYNPSIDKKDIENAAVVHYNGNMKPWLELAMSKYRPYWTKYIKFDHPYLRRCNLHE
Protein: Vacuolar protein sorting-associated protein 26A (Vesicle protein sorting 26A) (Q6AY86)
Organism: Rattus norvegicus (Rat)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3.The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC complex seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required for retrograde transport of lysosomal enzyme receptor IGF2R. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for the endosomal localization of WASHC2 (indicative for the WASH complex). Required for the endosomal localization of TBC1D5. Mediates retromer cargo recognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP. Involved in retromer-independent lysosomal sorting of F2R. Involved in recycling of ADRB2. Acts redundantly with VSP26B in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1. Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P40336}. Endosome membrane {ECO:0000250|UniProtKB:P40336}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40336}. Early endosome {ECO:0000250|UniProtKB:O75436}. Note=Localizes to tubular profiles adjacent to endosomes. Predominantly found in early not late endosomes. {ECO:0000250|UniProtKB:O75436}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-1
- Sorting nexin-2
- Sorting nexin-27
- Sorting nexin-5
- Sorting nexin-3
- TBC1 domain family member 5
- VPS26 retromer complex component B
- Sorting nexin
Sequence:
MSFLGGFFGPICEIDVALSDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPGKRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYESYIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPEVNNSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAPVKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPEKLRKQRTNFHQRFESPESQASAEQPEM
Protein: Ubiquitin-like-conjugating enzyme ATG3 (Autophagy-related protein 3) (Q9VVS6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Autophagy-related 16, isoform F
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related 8b, isoform A
- Autophagy-related 8a, isoform A
- Autophagy protein 5
- Autophagy protein 12-like
- Autophagy-related 1, isoform B
- Cysteine protease
- Cysteine protease
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MQSVLNTVKGTALNVAEYLTPVLKESKFRETGVLTPEEFVAAGDHLVHHCPTWQWAAGDETKTKPYLPKDKQFLITRNVPCYRRCKQMEYVGEETLVEEESGDGGWVETHQLNDDGTTQLEDKICELTMEETKEEMHTPDSDKSAPGAGGQAEDEDDDEAIDMDDFEESGMLELVDPAVATTTRKPEPEAKASPVAAASGDAEASGDSVLHTRTYDLHISYDKYYQTPRLWVVGYDEQRKPLTVEQMYEDVSQDHAKKTVTMESHPHLPGPNMASVHPCRHADIMKKIIQTVEEGGGQLGVHLYLIIFLKFVQTVIPTIEYDFTQNFNMS
Protein: NPC intracellular cholesterol transporter 2 (16 kDa secretory protein) (Epididymal secretory protein E1) (Niemann Pick type C2 protein homolog) (O97763)
Organism: Sus scrofa (Pig)
Function: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment. Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. May bind and mobilize cholesterol that is associated with membranes (By similarity). NPC2 binds cholesterol with a 1:1 stoichiometry. Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (By similarity). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10366780}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61916}. Lysosome {ECO:0000250|UniProtKB:P61916}. Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. {ECO:0000250|UniProtKB:P61916}.
Interaction partners:
- NPC intracellular cholesterol transporter 1
- NPC1 like intracellular cholesterol transporter 1
- Sterol regulatory element-binding protein cleavage-activating protein
Sequence:
MHFLAAAFLLLTLSASALAEPVHFRDCGSGVGVIKEVNVNPCPTQPCQLHKGQSYSVNVTFTSNTQSKGSKAVVHGIVMGVPIPFPIPDPDGCKSGINCPIQKDQTYSYLNKLPVKAEYPSIKLVVEWKLQDDNDQCLFCWQIPVQIES
Protein: Vacuolar protein sorting-associated protein 28 (ESCRT-I complex subunit VPS28) (Q59SD1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
- Ubiquitin-binding ESCRT-I subunit protein
- Vacuolar protein-sorting-associated protein 36
- Vacuolar-sorting protein SNF7
- ESCRT-II subunit protein
- ESCRT-III subunit protein
- Vacuolar protein sorting-associated protein 27
- ESCRT-III subunit protein
- ER membrane protein complex subunit 4
- Vacuolar-sorting protein SNF8
- ESCRT-III subunit protein
Sequence:
MTSSPPEYAPTSTSSFTVSTSDVYNQEVTKSSLIKTPLHKSVYDSLAEIYSILPTLEMVENSYLKDYITDKERYTSTTYRLIHQYQMLIKVFTDDQTKFQLLQKEFLPGLLSDMSNFLDLLLSKFNDSYPHAVSRIKNGLPATIEQINGNQPTSASARLVAEITGNFITCMDAVKLNYKSKEQLHPLLSDLVVNLNELNEELQFTGKSKLVNWLIKINNLQTELTQEEADSFLNDLDIAYKGFYTTLE
Protein: dihydropyrimidine dehydrogenase (NADP(+)) (EC 1.3.1.2) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) (Q94914)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEFCRTEQNENDEWVEDEEQTQRLKANFVISAFGSGLEDQDVKAALAPLQFRGELPVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQGLPLDTPAALPLFYTDIDAVDISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDLVTNVSPRIVRGTTSGYKYGPQQGCFLNIELISEKRAEYWLKSIGELKRDFPEKIVIASIMCSFNEEDWTELAIKAEQSGADALELNLSCPHGMGERGMGLACGQDPELVEQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKREEPMRSAINTVQGLMGLKADSTAWPAIGKEQRTTYGGVSGNATRPMALKAISDIANRVPGFPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTALKALLYLKRIRHQSMVPSGMASHHPRRSIRRQARCPFDRRGKATLGFFGPYQRQRDIKMAELRSQKGALSWDAEQVKATPPASNGAPNPAPRIKDVIGAALDKIGSYNKLDNKQQKVALIDDDMCINCGKCYMTCADSGYQAIEFDKDTHIPHVNDDCTGCTLCVSVCPIIDCITMVPKKIPHVIKRGVEEKIFYTHALSQCQ
Protein: Phosphatidylinositol 4-kinase pik1 (PI4-kinase) (PtdIns-4-kinase) (EC 2.7.1.67) (Q10366)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate. PIK1 is part of a nuclear phosphoinositide cycle and could control cytokinesis through the actin cytoskeleton (By similarity).
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol 4-kinase lsb6
- Calcium-binding protein NCS-1
- Phosphatidylinositol 4-phosphate 5-kinase its3
- GTP-binding protein ypt3
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase stt4
- 1-phosphatidylinositol 3-phosphate 5-kinase fab1
- Uncharacterized protein C19F5.03
- Uncharacterized protein C3C7.01c
- Phosphatidylinositol 3-kinase pik3
Sequence:
MPSSNSGNELLLRFFESAHFTSQLCVAYLSRYPNNIGIHHFLCEKLATFPYEEIEFFIPQLIHLVLNKDSESVALEEFIISQCEQNTQCALITFWYLQAHMVDLGLQPHSSCFKICKRLYNRIQILVFMSSSSLIQSQQKISENVTPALILSGIMLGGVCVPELLKKAGPIAIAQGRKAPRQDPDESDVDVLRRLSTEPRYSLDVLRSSLNNSIVEQHSEVSLRLKAPELTRTHSYQSSATLSIDEQRRVLRSNYFQQEIQFLFALQDISIRLIIVPRQARLSSLRAELALLNNNLPADVNIPLLRSYHKEVSHKIVRIDPKEATILNSAERVPYLIMVEVLSGELSFEPQSKKNKAKVQKIVSHKNQRKRWFDLTDVDPYTNLQDSTDNDISESESEGGDLSMSPLIKGLVPDTLSLSKSFSSFGNVSLQVPSSHRDTDVVLLSGRHSDSDGNGALKRSKIYASEITARMRAAATMLSQLDAEGSRRPKAETERIKNSIILDMQRLEEERLNEPSIYPVSVDISCAEDLRFGKETQKAERKGDRDDPSAATFQEDWYAKKERIRKSSPYGHYPNWDLVSVIVKTGADLRQETFACQLIYAFQRVWLECKEKVWVRRMKILVTGDNSGLIETITNAISVHSIKKNLTKQLREAELAQGKIAGKNVVTLKDYFIKQFGDPNSSRYRQAQTNFLQSLVAYSIISYLLQLKDRHNGNVLIDSEGHIIHIDFGFLLTNTPGNVGFESAPFKLTADYLEILDDRFDEYRSLMKAAFKSVRKNADQIILLVEVMQNNSTMPCFRAGENTSAQLLQRFQLQLGDKECDDFVDLLIQKANCSVWTRLYDLFQNITNGIY