wanglab/gogpt-training-data huggingface dataset:
Protein: 40S ribosomal protein S27 (Q9VBU9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS7A
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein uL18
- GEO07453p1
Sequence:
MPLAKDLLHPLPAEEKRKHKLKRLVQHPNSYFMDVKCPGCYRITTVFSHAQGVVVCAGCATILCQPTGGRAKLTEGCSFRRKPQ
Protein: DNA replication helicase (EC 3.6.4.12) (P143) (P24307)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Essential for initiation of viral DNA replication, it may contribute to other functions such as controlling the switch to the late phase and leading to the inhibition of host protein synthesis. Required for late and very late gene expression.
Subcellular location: Host nucleus {ECO:0000269|PubMed:16103143}. Note=LEF-3 is responsible for transporting the helicase to the host nucleus. {ECO:0000269|PubMed:16103143}.
Interaction partners:
Sequence:
MIDNILQFFLKNVPQDKTYEINNLQDANHLIIRNTRTGTRRLFEYVNNFQQFLNTIRNNFNGPCAKHDMGASCEDTEEPAEKHAAQTLDGHDWVLESNDFCIFVKPFILKKHYDIIQKYINFEDFFKSTDPGYINKCVQAGDYYYWPNWPKKQAFSFNGWQLFLNIKFGIVIEPTIPIIHNKKLGPVDLFVFDPKCFLNVELSLRTNHDPPQTLFVNGKTKFDDSHEDLFILKMADGTVATCKVNGELVNSDKNFFNYIRDDINLEECITVPKYKHIVNVNLKSLRVFENNNFDKNDVDLSDTRSRKPRIVPIISASSENADYIQTQINLGLIAIHENMVKVLATHERANDPNLLQQYFEKSKFKNFDFLIYVLWKILTKNENFSYRETDIKLFLELLCESLFACDKEALNEALKRCEPYKKQEKIVFNRACNHWFDFDDTKLCVSLGYYFGIHYMIYLTQSAKNEILDHDELWAYTYENVMALNLPPDIVCKGFFRKLENVVTGVNLVFNGKHYQIVKKEDDLFKLTKSNCYKLSNIKFNNWKYLYLTTHGVYNVFTNSFHSSCPFLLGTTLPQTFKKPTDEKYLPEDAFNYMLSTSADELSIYRTYHIAKMCRDVKMLKTNTAIVNYMGNCNTCQADMRVALNNLFRDLWNLDDENLITLALYVNKNRVSDMLHNLKCKPCRSTVSGSRPKCKCYKKIKINRKALKVCLMADMFGNDAELSELIWMLIFTNKTYVSTTLIRTNSEFVNQHGEFFSKEHNKIIQYLYRTIHKIEYVDMLMDKFNDKRLFLTELRDDVAREPDVQFEESDNISKFYTHHADALMILKKYNVWWDKIILARSTDDLPTWLTRFYMRIIMSKVDLKEYSYNYLKKIVEGYLYFKRFTNFNHANAIMLMHFAASLAIPVDYGKKAIYMPGEPGSGKSSFFELLDYLVLMHKFDDDNHSGESNKETSDKEVSKLNSQLYTINELKQCSESYFKKHADSSKSDSKSRKYQGLLKYEANYKMLIVNNKPLYVDDYDDGVQDRFLIVYTNHKFVDSVKFAGSVYEHIKSKQFPIESMYYESLVTPVRLFLSHVLMYRRDPKTGFVVYKTLLSNDPMHKHNLMCLSTNNSPLYALIYILNIKTVRSATITIGEDKMEEMIGIAVQHFKNFLHPSFVQYNYKKNINASSSKSFVFNEQVLLQQIKNKFKNNYNKTTNVFYNMTMALNRNDLNTSVPNFVC
Protein: WASH complex subunit 4 (WASH complex subunit SWIP homolog) (Q54R74)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- WASH complex subunit 5
- WASH complex subunit 3
- WAS protein family homolog DDB_G0292878
- WASH complex subunit 2
- Maestro heat-like repeat-containing protein family member 1
Sequence:
MATSYSANNGQNEEYTFDAFEDGSSKLVGEQQLTKLNQFAVDYAQQIWKIEEALDETLNEVWDINIDPVSIYNKPHEQLDLIELVKTDHKIFNKVILVFSSICNQTRILKETAESKFYSPLTVFGEITGESSEGDVQIEVGKLLPFMIDLSAFVNRCYSLIRNIISQFASIYQSQKNIHTQFFKNVHLQAVYYSMIDIFSVLINLDSIITQNTALDSSWGRYLRMVKSVKQEPNKYSVSGEEDKLWQLEKLLLSLKGQLLEGFIFQSCIQQEFDFPGVIDVKGNKVLKAEFQYNVKVLWSMFGTKIMDSSELNLRERFPGFMGLYAFYIALFKDITDKSFFKQVWEVTKRVPMVSINVNVFWFPADFIQQLMPGMIKIVGSTFNHMEIRRDYLRNVDKEFSGRVKSYYLQVSRWMVRMESSQTRGGTLWDVSLSKVGQIIQGVQLSYHISHLLKTMIGLHMHLTAPLKSSDVRKLFQCAEMLKSIENTFHRRSAMISAHISMMVQQLTDIINEKLNVVRSKYAGRSNYSEIELDVIVALSLCSDLLCGVATNERITVVRLCLNVIYQSNILKENDIEELRLHIKRLEFISDIGKIVKASCDCSILFWSRDLFPTYLQFLYQNPSQATSLQYTLTGLKDVVSVLDKAIHVDNAKQRLIDVYRNEMEEMIDKNIIQPLGKDVETDLRLHIHAFLNIEEKDPFKTGIKEFGKFLELKPLRFFDRTIDIKSRISHYLDQTFYNLNTVALFDWKTYSEMRNMAFYKYGLQLLEVHLPGSTLEQGLDVLEIMRNIHIFVSRYNYNLNNQIFIQRSSNSKTLNTINITHISNSIRTHGSGIMNTTINFAYRFLVQKFSIFSEFLFDDQIKSKLYKNIKYFRENKEQLNNMYPSELVTELERDIRQLGVSETGLTFLDHFRLLITHIGNAMGYIRLVRSGGLHYCSNAIKFVPDLKKIPKFQDLTSKDALSPETIQASTNLDSIIHNLSNNLSEGTEYFKMLVNVFATEFRNIANQHLKNFYIIVPALASNYIDHMINSKDKLFKKSKAIGAEALLFTDDGFAIGLAYILKLLDQNKDFDSLHWFDRIQLKCETDQKRMLAEANAKGIKEDQNHLAIKKIQNFQQEYELFKYSFSGSRIFFKD
Protein: Chaperone protein YscB (Yop proteins translocation protein B) (Q56973)
Organism: Yersinia pestis
Function: Functions as a specific chaperone for YopN. It could facilitate the secretion and the subsequent translocation of YopN.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9733695}. Cell inner membrane {ECO:0000269|PubMed:9733695}; Peripheral membrane protein {ECO:0000269|PubMed:9733695}. Note=Not exported across the inner membrane.
Interaction partners:
Sequence:
MQNLLKNLAASLGRKPFVADKQGVYRLTIDKHLVMLAPHGSELVLRTPIDAPMLREGNNVNVTLLRSLMQQALAWAKRYPQTLVLDDCGQLVLEARLRLQELDTHGLQEVINKQLALLEHLIPQLTPFSVASRVGWN
Protein: Neuronal membrane glycoprotein M6-a (M6a) (P35802)
Organism: Mus musculus (Mouse)
Function: Involved in neuronal differentiation, including differentiation and migration of neuronal stem cells. Plays a role in neuronal plasticity and is involved in neurite and filopodia outgrowth, filopodia motility and probably synapse formation. Gpm6a-induced filopodia formation involves mitogen-activated protein kinase (MAPK) and Src signaling pathways. Conflictingly, PubMed:22162747 reports that induced cellular protrusions are simple membrane-wrapped tubules without actin or tubulin-based cytoskeletons and with Gpm6a gliding along membrane edges indicative for a function in actin-independent membrane deformation. May be involved in neuronal NGF-dependent Ca(2+) influx. May be involved in regulation of endocytosis and intracellular trafficking of G-protein-coupled receptors (GPCRs); enhances internalization and recycling of mu-type opioid receptor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21714103}; Multi-pass membrane protein {ECO:0000269|PubMed:21714103}. Cell projection, axon {ECO:0000269|PubMed:21714103}. Cell projection, growth cone {ECO:0000269|PubMed:21714103}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q812E9}. Cell projection, filopodium {ECO:0000250|UniProtKB:Q812E9}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q812E9}. Note=Localizes to cholesterol-rich lipid rafts of the plasma membrane of hippocampal neurons. Localized to plasma membrane of cell bodies and neurites of hippocampal neurons. Localized in membrane protrusions (filopodia and spines) of primary hippocampal neurons (By similarity). Localized to the growth cone edge membrane of elongating axons (PubMed:21714103). {ECO:0000250|UniProtKB:Q812E9, ECO:0000269|PubMed:21714103}.
Interaction partners:
Sequence:
MEENMEEGQTQKGCFECCIKCLGGIPYASLIATILLYAGVALFCGCGHEALSGTVNILQTYFELARTAGDTLDVFTMIDIFKYVIYGIAAAFFVYGILLMVEGFFTTGAIKDLYGDFKITTCGRCVSAWFIMLTYLFMLAWLGVTAFTSLPVYMYFNVWTICRNTTLVEGANLCLDLRQFGIVTIGEEKKICTASENFLRMCESTELNMTFHLFIVALAGAGAAVIAMVHYLMVLSANWAYVKDACRMQKYEDIKSKEEQELHDIHSTRSKERLNAYT
Protein: Ephrin-A5b (AL-1) (EPH-related receptor tyrosine kinase ligand 7) (LERK-7) (ZfEPHL4) (P79728)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the epha3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor epha2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation (By similarity). Controls axon growth and may be involved in the creation of the retino-tectal map.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Ephrin type-A receptor 4a
- Eph receptor A2 a.
- Ephrin-B2b
- Efnb3 protein
- Ephrin type-A receptor 7
- Eph receptor A4b.
- Ephrin type-A receptor 3.
- Ephrin-B1
- Ephrin-B3
- EPH receptor B1.
Sequence:
MLQAEMIVFVGVILWMCVFSQEPSSKVMADRYAVFWNRTNPRFQRGDYHIDVCINDYLDVYCPHYEDSVPEERTERYVLYMVNYDGYSTCDHTAKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYYYISSMITETGRRSCLKLKVFVRPPNGCEKTIGVHDRVFVDDKVDNALEPRDDTSHEAEPSRSDVSTSGLRHQTSRPLLALLLLCISLYLLL
Protein: Platelet-derived growth factor C (PDGF-C) (Fallotein) (Spinal cord-derived growth factor) (SCDGF) (VEGF-E) [Cleaved into: Platelet-derived growth factor C, latent form (PDGFC latent form); Platelet-derived growth factor C, receptor-binding form (PDGFC receptor-binding form)] (Q8CI19)
Organism: Mus musculus (Mouse)
Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16443219}. Secreted {ECO:0000269|PubMed:15372073}. Nucleus {ECO:0000250|UniProtKB:Q9NRA1}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9NRA1}. Cell membrane {ECO:0000269|PubMed:16443219}. Note=Sumoylated form is predominant in the nucleus (PubMed:16443219). Stored in alpha granules in platelets (By similarity). {ECO:0000250|UniProtKB:Q9NRA1, ECO:0000269|PubMed:16443219}.
Interaction partners:
- Platelet-derived growth factor receptor alpha
- Vascular endothelial growth factor receptor 2
- Platelet-derived growth factor subunit A
- Platelet-derived growth factor subunit B
- Platelet-derived growth factor receptor beta
- Vascular endothelial growth factor receptor 3
- Vascular endothelial growth factor receptor 1
- Platelet-derived growth factor D
- Epidermal growth factor receptor
- Insulin-like growth factor 1
Sequence:
MLLLGLLLLTSALAGQRTGTRAESNLSSKLQLSSDKEQNGVQDPRHERVVTISGNGSIHSPKFPHTYPRNMVLVWRLVAVDENVRIQLTFDERFGLEDPEDDICKYDFVEVEEPSDGSVLGRWCGSGTVPGKQTSKGNHIRIRFVSDEYFPSEPGFCIHYSIIMPQVTETTSPSVLPPSSLSLDLLNNAVTAFSTLEELIRYLEPDRWQVDLDSLYKPTWQLLGKAFLYGKKSKVVNLNLLKEEVKLYSCTPRNFSVSIREELKRTDTIFWPGCLLVKRCGGNCACCLHNCNECQCVPRKVTKKYHEVLQLRPKTGVKGLHKSLTDVALEHHEECDCVCRGNAGG
Protein: RE48016p (Rad, Gem/Kir family member 1, isoform A) (Q6NR39)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPFYKRICRSLSKRYKEPSLSLDNTVETLLIKNEGDFISVEQGKELVARKRNSQQLAHPPAHLHHHTQNHAHNHHTLQQQQHQQQQQQQHKRDENMRQLLDVTNTLTIEELRDFQMRYGSPHHSRSQSVKMPGSRASGRPNQLCLPQQRSRVASMPNTGVEEEYYRLRHFSITGKGVVNRGDSLKSRRSRSNNSVASSNSSTEHLTTQQQLSAPASVSARTSLASSRESSTSNPGNGPYRVLMLGGPAVGKSSLVSQFMTSEYLHAYDTSIDDESGEKAVSVLLSGEESELIFIDHGYTEMTPDECLTNYDPHGYCVIYSAADRSSFSVAEQVLQVLWTNQNIAQKAVILVSNKADLARSRLVTSEEGKAMATAYDCKFIETSVGINHNVDELLVGLLSQIRLKLENPEKSRDLFRKRSIRKSKRRACSPLNAGCLNANTPLGPLGEAVATPPGSAQSSPRKYRGSRTSTSLKVKGLLGRVWTRDSKSKSCENLHVL
Protein: Transcriptional repressor FrmR (P0AAP3)
Organism: Escherichia coli (strain K12)
Function: Repressor of the frmRAB operon.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- S-
- S-formylglutathione hydrolase FrmB
- Uncharacterized protein YbeL
Sequence:
MPSTPEEKKKVLTRVRRIRGQIDALERSLEGDAECRAILQQIAAVRGAANGLMAEVLESHIRETFDRNDCYSREVSQSVDDTIELVRAYLK
Protein: Alsin homolog (Amyotrophic lateral sclerosis 2 protein homolog) (Q9VNZ8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has guanine nucleotide exchange factor (GEF) activity towards Rab5. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab5 into its active GTP-bound form.
Interaction partners:
- Charged multivesicular body protein 2b
- Ras-related protein Rab5
- FIG4 phosphoinositide 5-phosphatase
- Ellipsoid body open, isoform C
- GH13165p
- LD26789p
- Exportin-1
- Importin subunit alpha
- RH51096p
- Importin subunit alpha
Sequence:
MASAADDSALGGQEERESFTIYHEGRELQLHWRGLPPLQRFPASRICSNAGGELLLLTTDHALYSAKLQANREHMDLQLLRTDVVDMDFCSGSQELFVVLTNGSVQRQATGSGRDVGHPHAWQTLGFDPLELHAEGVRIRRVCCSAQGVVFVGASGETYVMGSCGEVFKAEQQPRHMRLYEEGKELLDLAAGNEHFVMLVAPYNLADDALQLSVASAKEEPEDERASVKSISSGHSERSVAANTRHLLHQGYALLHTQLFTFGASNNGLLGSGDHIRRANVMRLQKLDSMGVCSIAAGLEHTVARTLDGRLYHWGLNNHSQLGEDVSSPMEITITENTAALPIEQNSALEATCGDYHTLLLNASGQIHSLQPAPPMRHLQQSSTYAQTLLQLQLGAAWPRQLRLLMCSGGYTLQNQRQFQRQYHYYLSHLQSQLQLLLKHRQAVQTLEIWQRQSALEPLSALGPLLINWERILCLLVATLHSLEGFYRADFVQPADLLFICHYKEYIDLFDGYTKAYCDVFSVNGFGEAVVAITGLSSPLAELNEESYVTRLFQQPFSIYQLFVQFMELLVRTQSEYGEHRVAWSEFARHSCISQELAVNTKDFWSSNDRNPRIVQFRGRHRRVILTSALVPLKLVTSGISRSSNSFILFSDFLCQVSGNSLYSYPLTTLWVWTEGDSLRLTTPEKSFLVSTRSQEMRKVWLDQLQSSIIASLGKPLGSPVPSYRSTGYEFSREHPKFSRVKACGTWRKGVLHGNCYLEYPDGSVYCGELQHGIIEGFGKMVIPTTGLYVGNFKGGRFHGHGVYEMHCKDSPESEVYEGNFCEGLFHGHGVMRNNRYIYVGEYQANARSGYGVIEDLVSGDKYMGMFADNKRSGIGSCITNRGDYFEGSFSGDDLTGSGVAVFENDYYYEGELTLLGPNGRGEYYMPSGDACGGSGAMGTGEFDDTCELIGNKMFGQLSGTWDTVRIQAGELVLNRRFPKYPSSLGRQVVDHNRKWRSLFNNFESDLANCTASTSSSGGNQSAGTLRKSSKPTLSTAQIWNCIAVYMSKQRAREGTKPGNYFNNILLSLPLPQKTSSPLAKARTTTSALSKLQTEAASALDFLGFPPRRIQSQEALNSKPGGLQRADSLISMGHNTSRDLDNSSLASFQLDQSLMNSTVNGDESSTFNESFSKLSHNNNNSISKHMNNIDCSITSTTSTTSAVLDQVPSFGMALVLTEQDVTSIRLYLEQAFKDRHHPLYVLNERIANCFHYSYGYWKVKPTPILAKQAMREWESISRRIYRFVRKMFPALPEELCQMEGSREVISHITLLYPLVLSEGIYSTLFVLYANKYSRKDEMYRQNLNLAEKLKDQELVELMGHESFLHNVMLDPKFVESVQTLKELQEKFSPQDMLTVIQRSTQLLTEAYEHAMAANAAQLNADNMIPLTMLTMLRAAVPHLGAELALLDDLTGGPNFQAEMNGMAGYCYTTLKAAYEHVTSRALQKIP
Protein: PEP-dependent dihydroxyacetone kinase 2, ADP-binding subunit DhaL (EC 2.7.1.121) (Q92EU3)
Organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Function: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22773791}.
Interaction partners:
- PTS-dependent dihydroxyacetone kinase 2, dihydroxyacetone-binding subunit DhaK
- PEP-dependent dihydroxyacetone kinase 2, phosphoryl donor subunit DhaM
- PTS-dependent dihydroxyacetone kinase 1, dihydroxyacetone-binding subunit DhaK
- PEP-dependent dihydroxyacetone kinase 1, phosphoryl donor subunit DhaM
- NAD-dependent glycerol dehydrogenase
- Triosephosphate isomerase 2
- PEP-dependent dihydroxyacetone kinase 1, ADP-binding subunit DhaL
- Ribose-5-P isomerase B
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MSELVMDSAFFGHVLQDMGALIEKERDYLTGLDSDIGDGDHGINLSIGFREVNKQLDELLTVSPDIATLLKKSGMILLGKVGGASGPLYGSFFMKCGADVPGKTEVNFDELCGMIINGAAAVQHRGKAELGDKTMMDAFLPGVEVLQNRDTNADPIETFSAFVDAMHAGAQSTIPLIAKKGRALRLGERAIGHLDPGSESSWMLMNVILENLKKAV
Protein: Phospholipase A2 trimorphin (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (P84736)
Organism: Trimorphodon lambda (Sonoran lyre snake) (Trimorphodon biscutatus lambda)
Function: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:15225559}.
Interaction partners:
Sequence:
NLYQFSNMIQCTIPGSDPLSDYGNYGCYCGYGGSGTPVDELLRCCQVHDD
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (Q386I5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRRLFKPQLMVPWSRQPPTCCSSQIINIISRGLSQRGEPLGAAAPSSVSSVSVPPVASLHTPVMHSNAFAASEVKKLLAKAQYSLFTLGWNPGTDDYCIYCATTNELVRAKKDTLWKAIFWMEGRIGDDYIAGLLFPSDGTPALTEVAAMVREKCRRQVVVAPDTWGICYLTLKNQRDFVRGMELPASLEHAAFLLMRAMFNSSLIEPSVFDVTSGAYISASCADSVSAARDCLVSWWVLFNVHKKFGTSGSRKLIDPVEQIVRRVVKTVNVFVVDINVRVGKGTISEGFTMIVTIYDAQRRSQSVHMIRSLAEESAKRNTLNGLLFGEGTSAISLFVPTDRTKSSQLLAFARSCRPSCPFFVTEPSSLTPFFSGAPVTDGLSEQSDPRSTWALIRTNCFAQCPGRRLEEVLDRKLLQGFTAVANRLYSDRLHRVSPALMSAASSIPLREEPRVAWERVASLVEEERKNPVAHVNKSAFLNNVTITDAEVVFRLQQWHSTIYESPDRLEREREALEGLQRYLVVDLETTTVRRYKRVANPFTKENYVVLSGARDYRGQVFMPSRYYSRNVALRYDDLHVTSTHSLVKGSSKHSLFLPPLDDYDVLVGHNIKFDLLHMWRDVELRRFLKRGGKIWDTMYAEYLLTGHEVKLGHGAGLEEVAKSYGGQTPKLDAVKQAWSSGKDTCEIPYRTLTQYLHGDLENTELIFKKHIERALAQRQVVIILARMDGLLCTTEMEYNGLKTNVQLALSQSNELMCKVKELRRHLDNSIPKEISIDCRKYFNWASNQHLIAFFFGGKLKLSTNARESRLLPGEVFERHTLYARPEDYDKTEFPKGVFLRPPVYVVGPADCLMATGVSLDKGTKFFKMYFEAYVKQAGFRKSSSVTDSLRRAMVSVSRIDQEKCSNPDALVNLLPKRHLFLFAAFTPTSDGTISKLFLKNAITGESLTIAGDCANKVERLRAFMEGQVEAHTEMLVDADGDGSAPANNNAFADAHITILARDAPFSCARLLHSDEGISAYLSLHDGLNPQEDVGQRYVITLADTVSTLSYYRYMYGSDTEAAYADKTKVDESKLVVPMKALPRPCSSRGATSEAFKKKLVQEAAMKPEDWCNLYIDIFLHIGHAALCRESLETEAGSKKARKSKGKGGIRTPGDLPILLRERSAFIGYYNSLPDDERKKLALMTMLGRTCGTAFDAFAVMCSHDDIVEVNIGGRLNQYVPSQLDAEQVMRKFRSPTTRQLQVGEDSLTYFKKTHGDKTAETILELRAMEKLIGTYYENTDDGTGMVSLVHDDDSCIHHELIHNKTNTGRLASANPNCQNIPKEDKSPLREMFVSRYGEKGMCIEADYSQLEVVALAVLANDQQMLEDLRSNVDFHCKRVAMMRPDLQYTEILKKAKKDKEPEFVKLRQQAKIFSFQRQYGAGVKMISESTGLTQDQVRHLIEKERETYRGVDVFNSMVALSANKFDASLQNGSRNVRGHQIFKGMFPVITGSRYIFTESDVPEGLLRNKSLAVKSTNFSPTHLKNYPVQGFAGEIVQIMLGVLWRHFLRKDNYGGLAVLINTVHDCVWIDCHMDVLQDVVLETDGIMSSVRDVLNRLYPEMEVSVDFPCDVVAGENMGALRPVVIEETL
Protein: Sorting nexin-3 (C8VAL9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Prevacuolar compartment membrane {ECO:0000256|ARBA:ARBA00004179}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004179}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004179}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26, putative
- Vacuolar protein sorting-associated protein 29
- Vacuolar fusion protein mon1
- Vacuolar protein sorting-associated protein 17
- Vacuolar protein sorting-associated protein Vps5, putative
- Ubiquitin carboxyl-terminal hydrolase
Sequence:
MQAVPESRQQTFEEIYGPPENFLEIEVRNPQTHGTSRNMYTSYEIVCRTNIPAFKLKHSVVRRRYSDFEYFRDILERESTRVTIPPLPGKVFTNRFSDDVIEHRREGLQRFLQIVAGHPLLQTGSKVLASFIQDPNWDRNAW
Protein: Histidinol-phosphate aminotransferase (EC 2.6.1.9) (Imidazole acetol-phosphate transaminase) (P36605)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- Histidinol dehydrogenase
- Probable prephenate dehydrogenase [NADP
- Tryptophan synthase
- Imidazole glycerol phosphate synthase hisHF
- Histidine biosynthesis bifunctional protein his7
- Multifunctional tryptophan biosynthesis protein
- ATP phosphoribosyltransferase
- Probable histidinol-phosphatase
- Putative prephenate dehydratase
Sequence:
MFDLNTCLRKNILELQPYRCARDDFSEGVLLDANECAYGSVISVDGVEFNRYPDPRQIEVKQRLCDLRNKELSITKPLTPDNICMGVGSDEIIDSLIRISCIPGKDKILMCPPSYGMYTVSAKINDVEVVKVLLEPDFNLNVDAICETLSKDSAIKVFFACSPGNPTAKALKLEDIKKILEHPTWNGIVVVDEAYIDFSAPDMSALTLVNEYPNLAVCQTLSKSFGLAGIRIGFCLTSKPIATIMNSLKAPYNISEPTSRLALDALSPQSIDKMHTYRDAIIQQRVRLCKELTTIKGMGKIIGGYDANFILIQVLDRPEGGKPSNDAAKYLYLQMATMHKVVVRFRGTEPLCEGALRITVGTEEENTILLKTIKLVLQEYYTKK
Protein: 11-beta-hydroxysteroid dehydrogenase B (EC 1.1.1.146) (17-beta-hydroxysteroid dehydrogenase B) (EC 1.1.1.62) (Seed oil body protein 3) (Steroleosin-B) (Q8LKV5)
Organism: Sesamum indicum (Oriental sesame) (Sesamum orientale)
Function: Has dehydrogenase activity against corticosterone (11 beta-hydroxysteroid) and estradiol (17 beta-hydroxysteroid), with similar activities to both sterols in the presence of NADP(+), but negligible activity to either sterol in the presence of NAD(+). May be involved in signal transduction regulated by various sterols.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:15331088, ECO:0000269|PubMed:9816677}. Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Note=Surface of oil bodies. Exists at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MDLINSLLNFVVPPASLLMLAFTWPTLFFITTCEWLYNTYLNSENMENKVVLITGASSGIGEQIAYQYAKRGANLVLVARREHRLRGISENARRLGAPNVLIMAADVVKEEECRRFINETINYYGRVDHLVNTVSLGHTFYFEEASDSSVFPILMDINFWGNVYPTYVALPYLRESNGRIIVNASVENWLPLPRMSLYSAAKSALINFYETLRFEVKNEVGITVATHGWIGTEMTRGKFMVEEGAEMQWKEEREVHVTGGPVEEFAKQIVSGACRGDPYVKYPSWYDIFFLYRVFAPKVLDWTFRFLLTNGGARRTSFIGTGRPLLETSSPRRSAVMEGSSPRRLPPGPLTFSPAFQQQKSE
Protein: Ras-related protein R-Ras (EC 3.6.5.-) (p23) (P10301)
Organism: Homo sapiens (Human)
Function: Regulates the organization of the actin cytoskeleton. With OSPBL3, modulates integrin beta-1 (ITGB1) activity.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Inner surface of plasma membrane possibly with attachment requiring acylation of the C-terminal cysteine (By similarity with RAS).
Interaction partners:
- Ral guanine nucleotide dissociation stimulator
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Plexin-B1
- RAF proto-oncogene serine/threonine-protein kinase
- Ras GTPase-activating protein 1
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Ras association domain-containing protein 5
- RalA-binding protein 1
- Plexin-B2
Sequence:
MSSGAASGTGRGRPRGGGPGPGDPPPSETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDPTIEDSYTKICSVDGIPARLDILDTAGQEEFGAMREQYMRAGHGFLLVFAINDRQSFNEVGKLFTQILRVKDRDDFPVVLVGNKADLESQRQVPRSEASAFGASHHVAYFEASAKLRLNVDEAFEQLVRAVRKYQEQELPPSPPSAPRKKGGGCPCVLL
Protein: StAR-related lipid transfer protein 3 (Metastatic lymph node gene 64 protein) (MLN 64) (Protein CAB1) (START domain-containing protein 3) (StARD3) (Q14849)
Organism: Homo sapiens (Human)
Function: Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes. Creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB. Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes. May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane. However, such results need additional experimental evidences; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes. Does not activate transcriptional cholesterol sensing. Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:11053434, ECO:0000269|PubMed:16709157, ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:28377464, ECO:0000269|PubMed:29858488}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2. {ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:29858488}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein A
- Motile sperm domain-containing protein 2
- STARD3 N-terminal-like protein
- GPI-specific phospholipase A2-like PGAP3
- Vesicle-associated membrane protein-associated protein B/C
- Phosphatidylcholine transfer protein
- NPC intracellular cholesterol transporter 2
- Protrudin
- NPC intracellular cholesterol transporter 1
- Growth factor receptor-bound protein 7
Sequence:
MSKLPRELTRDLERSLPAVASLGSSLSHSQSLSSHLLPPPEKRRAISDVRRTFCLFVTFDLLFISLLWIIELNTNTGIRKNLEQEIIQYNFKTSFFDIFVLAFFRFSGLLLGYAVLRLRHWWVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAAQVAVARGPLLFSGALSEGQFYSPPESFAGSDNESDEEVAGKKSFSAQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNPRVCTFVWILNTDLKGRLPRYLIHQSLAATMFEFAFHLRQRISELGARA