wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphate-binding protein PstS (PBP) (O51233)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Binds inorganic phosphate with a Kd of 1.2 uM. Part of the ABC transporter complex PstSACB involved in phosphate import (Probable).
Subcellular location: Cell membrane {ECO:0000305|PubMed:24318969}; Lipid-anchor {ECO:0000305|PubMed:24318969}.
Interaction partners:
- Phosphate import ATP-binding protein PstB
- Phosphate transport system permease protein PstA
- Phosphate transport system permease protein
- Phosphate-specific transport system accessory protein PhoU homolog
- Lipoprotein, putative
- Elongation factor P
Sequence:
MKKVIILIFMLSTSLLYNCKNQDNEKIVSIGGSTTVSPILDEMILRYNKINNNTKVTYDAQGSSVGINGLFNKIYKIAISSRDLTKEEIEQGAKETVFAYDALIFITSPEIKITNITEENLAKILNGEIQNWKQVGGPDAKINFINRDSSSGSYSSIKDLLLNKIFKTHEEAQFRQDGIVVKSNGEVIEKTSLTPHSIGYIGLGYAKNSIEKGLNILSVNSTYPTKETINSNKYTIKRNLIIVTNNKYEDKSVTQFIDFMTSSTGQDIVEEQGFLGIKT
Protein: Myeloid differentiation primary response protein MyD88 (Q5XJ85)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Adapter protein involved in the Toll-like receptor and Il-1 receptor signaling pathway in the innate immune response.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Toll-like receptor 2.
- Interleukin-1 receptor-associated kinase 1
- TNF receptor-associated factor 6
- Interleukin-1 receptor-associated kinase 4.
- Toll-like receptor 4
- Toll-like receptor 4b, duplicate a.
- Toll-interleukin 1 receptor
- Toll-like receptor 9
- Toll-like receptor 4
- Interferon regulatory factor 7
Sequence:
MASKLSIDHEAIPVTALNCSFRKKLGLFLNPTNTVAADWRTVAELMDFTYLEIKNFEKRDCPFEKVLTDWETRPDATVANLLSILEKAERKDVISELKEILDDDCRKYMERQQRKPLQVPVVDSCGPRTQEREGITLYDDPQGLTPETFDAFICYCQSDIQFVHEMIKQLEHTEYNLKLCVFDRDVLPGTCVWTIASELIEKRCKRMVVVISDDYLDSDACDFQTKFALSLCPGARTKRLIPVVYKSMKRPFPSILRFLTICDYSKPCTQVWFWTRLAKALSLP
Protein: SPX domain-containing protein 2 (Protein SPX DOMAIN GENE 2) (AtSPX2) (O48781)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May inhibit PHR1 DNA-binding activity in a Pi-dependent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:18315545}.
Interaction partners:
- Protein PHOSPHATE STARVATION RESPONSE 1
- Protein PHR1-LIKE 1
- Myb family transcription factor PHL4
- SEC12-like protein 1
- Phosphate transporter PHO1
- Protein PHR1-LIKE 2
- Monogalactosyldiacylglycerol synthase 2, chloroplastic
- Probable ubiquitin-conjugating enzyme E2 24
- Inorganic phosphate transporter 1-4
- Phosphate transporter PHO1 homolog 1
Sequence:
MKFGKSLSNQIEETLPEWRDKFLSYKELKKKLKLMEPRSVENRPNKRSRSDSNSVDTDPTVGMTKEELDFISLLEDELEKFNSFFVEQEEEYIIRLKELKDQVAKAKNSNEEMINIKKEIVDFHGEMVLLMNYSALNYTGLAKILKKYDKRTGALIRLPFIQKVLQEPFFTTDLLNTFVKECEAMLDRLFPSNKSRNLDEEGEPTTSGMVKTGTDDSELLRVPKELSEIEYMESLYMKSTVSALKVLKEIRSGSSTVSVFSLPPLPASGLEDDSWKKKVGVLEQVAK
Protein: PCNA-interacting partner (PARI) (PARP-1 binding protein) (PARP1-binding protein) (PARPBP) (Q9NWS1)
Organism: Homo sapiens (Human)
Function: Required to suppress inappropriate homologous recombination, thereby playing a central role DNA repair and in the maintenance of genomic stability. Antagonizes homologous recombination by interfering with the formation of the RAD51-DNA homologous recombination structure. Binds single-strand DNA and poly(A) homopolymers. Positively regulate the poly(ADP-ribosyl)ation activity of PARP1; however such function may be indirect.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20931645, ECO:0000269|PubMed:22153967}. Note=Localizes to chromatin in response to S phase arrest but not in mitosis. Targeted to chromatin via its interaction with PCNA.
Interaction partners:
- Pro-MCH
- Poly [ADP-ribose] polymerase 1
- Hyaluronan mediated motility receptor
- Condensin complex subunit 3
- Cyclin-dependent kinase 1
- Kinesin-like protein KIF18A
- Centromere protein I
- FIGNL1-interacting regulator of recombination and mitosis
- RAD51-associated protein 1
Sequence:
MAVFNQKSVSDMIKEFRKNWRALCNSERTTLCGADSMLLALQLSMAENNKQHSGEFTVSLSDVLLTWKYLLHEKLNLPVENMDVTDHYEDVRKIYDDFLKNSNMLDLIDVYQKCRALTSNCENYNTVSPSQLLDFLSGKQYAVGDETDLSIPTSPTSKYNRDNEKVQLLARKIIFSYLNLLVNSKNDLAVAYILNIPDRGLGREAFTDLKHAAREKQMSIFLVATSFIRTIELGGKGYAPPPSDPLRTHVKGLSNFINFIDKLDEILGEIPNPSIAGGQILSVIKMQLIKGQNSRDPFCKAIEEVAQDLDLRIKNIINSQEGVVALSTTDISPARPKSHAINHGTAYCGRDTVKALLVLLDEEAANAPTKNKAELLYDEENTIHHHGTSILTLFRSPTQVNNSIKPLRERICVSMQEKKIKMKQTLIRSQFACTYKDDYMISKDNWNNVNLASKPLCVLYMENDLSEGVNPSVGRSTIGTSFGNVHLDRSKNEKVSRKSTSQTGNKSSKRKQVDLDGENILCDNRNEPPQHKNAKIPKKSNDSQNRLYGKLAKVAKSNKCTAKDKLISGQAKLTQFFRL
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Ca(2+)-ATPase) (Calcium pump) (Calcium-dependent ATPase) (Q47910)
Organism: Myroides odoratus (Flavobacterium odoratum)
Function: Catalyzes the hydrolysis of ATP coupled with the transport of calcium. Has some hydrolysis activity also with dATP, GTP, UTP, ITP and 4-nitrophenyl phosphate as substrate. No activity with ADP, CTP, acetyl dihydrogen phosphate or AMP-PNP as substrate.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}; Peripheral membrane protein {ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}; Periplasmic side {ECO:0000269|PubMed:1386366, ECO:0000269|PubMed:8617788, ECO:0000269|PubMed:8632017}.
Interaction partners:
Sequence:
MNFKSTVITAMCCFFSFAVLASEKLEKPKLVVGLVVDQMRWDYLYRYYDRYSENGFKRLLNEGFSSENTLIDYVPTYTAIGHSTIYTGSVPAINGIAGNDFIIQATGQNMYCTQDDSVQAVGGEGKVGQQSPKNLLVSTITDQLKLATNFQSKVIGIAIKDRGGILPAGHFANAAYWLDGKTGDWITSTYYMKDLPKWVKGFNKEKVVDQYYKQGWKTLYPIDTYVLSTADDNLYEETFKGEKTPTFPRDLVKLKKENGYELIKSTPQGNTLTLDFAKRAIENEQLGNNPLQVTDFLAVSLSSTDYIGHQFAINSIEIEDTYLRLDRDIADFLAYLDQNIGKGNYTLFLSADHGAAHNPKFFADQKGNSGYFDTKAIRKDLNEKLASKFGVADLVKSLANYQVHLNYEVIEANDVEEDEVIAAAIKLLKKVDGVAFVVDMNEAAESSVPQILRERIINGYNFKRSGAIQLILEPQWFSGSKDGKGTTHGSWNSYDAHIPAVFLGWGVKPGKTTRQTHMTDIAPTIAQILKIEFPNGNIGTPIQEAIEQ
Protein: Thymic stromal lymphopoietin (Thymic stroma-derived lymphopoietin) (Q9JIE6)
Organism: Mus musculus (Mouse)
Function: Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10974033}.
Interaction partners:
- Interleukin-7 receptor subunit alpha
- Cytokine receptor-like factor 2
- Interleukin-1 receptor-like 1
- Interleukin-33
- Interleukin-4
- Interleukin-4 receptor subunit alpha
- Interleukin-13 receptor subunit alpha-1
- Cytokine receptor common subunit gamma
- Interleukin-13
- Interleukin-5
Sequence:
MVLLRSLFILQVLVRMGLTYNFSNCNFTSITKIYCNIIFHDLTGDLKGAKFEQIEDCESKPACLLKIEYYTLNPIPGCPSLPDKTFARRTREALNDHCPGYPETERNDGTQEMAQEVQNICLNQTSQILRLWYSFMQSPE
Protein: Protein-arginine N-acetylglucosaminyltransferase NleB (Arginine GlcNAcyltransferase NleB) (NleBc) (EC 2.4.1.-) (Non-LEE-encoded type III effector B) (A0A482PDI9)
Organism: Citrobacter rodentium
Function: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis. Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins FADD, TNFRSF1A and RIPK1: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling. Has preference for host FADD as substrate compared to TNFRSF1A and RIPK1. Also acts on host proteins without a death domain: catalyzes GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2 and TRAF3, leading to inhibit NF-kappa-B signaling and type I interferon production, respectively. Also displays intra-bacterial activity by mediating GlcNAcylation of glutathione synthetase GshB. Catalyzes auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:16552063}. Host cell {ECO:0000269|PubMed:16552063}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:16552063}.
Interaction partners:
Sequence:
MLSPLNVLQFNFRGETALSDSAPLQTVSFAGKDYSMEPIDEKTPILFQWFEARPERYGKGEVPILNTKEHPYLSNIINAAKIENERVIGVLVDGDFTYEQRKEFLSLEDEHQNIKIIYRENVDFSMYDKKLSDIYLENIHEQESYPASERDNYLLGLLREELKNIPYGKDSLIESYAEKRGHTWFDFFRNLAVLKGGGLFTETGKTGCHNISPCGGCIYLDADMIITDKLGVLYAPDGIAVYVDCNDNRKSLENGAIVVNRSNHPALLAGLDIMKSKVDAHPYYDGVGKGLKRHFNYSSLQDYNVFCNFIEFKHKNIIPNTSMYTNSSW
Protein: TLE family member 1, transcriptional corepressor (F6T2C8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
HEKASTPVLKSSTPTPRSDMPTPGTSATPGLRPGLGKPPAIDPLVNQAAAGLRTPLAVPGPYPAPFGMVPHAGMNGELTSPGAAYASLHNMSPQMSAAAAAAAVVAYGRSPMVGFDPPPHMRVPTIPPNLAGIPGGKPSLVPAPAH
Protein: Aminopeptidase (EC 3.4.11.-) (Q0P5U8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGPPSSSGFYVSRAVALLLAGLVAALLLALAVLAALYGHCERVPPSELPGLRDSEAESSPPLRQKPTPTPKPSSARELAVTTTPSNWRPPGPWDQLRLPPWLVPLHYDLELWPQLRPDELPAGSLPFTGRVNITVRCTVATSRLLLHSLFLSPGTGNATVGRVPVDDVWFALDTEYMVLELSEPLKPGSSYELQLSFSGLVKEDLREGLFLNVYTDQGERRALLASQLEPTFARYVFPCFDEPALKATFNITMIHHPSYVALSNMPKLGQSEKEDVNGSKWTVTTFSTTPHMPTYLVAFVICDYDHVNRTERGKEIRIWARKDAIANGSADFALNITGPIFSFLEDLFNISYSLPKTDIIALPSFDNHAMENWGLMIFDESGLLLEPKDQLTEKKTLISYVVSHEIGHQWFGNLVTMNWWNNIWLNEGFASYFEFEVINYFNPKLPRNEIFFSNILHNILREDHALVTRAVAMKVENFKTSEIQELFDIFTYSKGASMARMLSCFLNEHLFVSALKSYLKTFSYSNAEQDDLWRHFQMAIDDQSTVILPATIKNIMDSWTHQSGFPVITLNVSTGVMKQEPFYLENIKNRTLLTSNDTWIVPILWIKNGTTQPLVWLDQSSKVFPEMQVSDSDHDWVILNLNMTGYYRVNYDKLGWKKLNQQLEKDPKAIPVIHRLQFIDDAFSLSKNNYIEIETALELTKYLAEEDEIIVWHTVLVNLVTRDLVSEVNIYDIYSLLKRYLLKRLNLIWNIYSTIIRENVLALQDDYLALISLEKLFVTACWLGLEDCLQLSKELFAKWVDHPENEIPYPIKDVVLCYGIALGSDKEWDILLNTYTNTTNKEEKIQLAYAMSCSKDPWILNRYMEYAISTSPFTSNETNIIEVVASSEVGRYVAKDFLVNNWQAVSKRYGTQSLINLIYTIGRTVTTDLQIVELQQFFSNMLEEHQRIRVHANLQTIKNENLKNKKLSARIAAWLRRNT
Protein: Signal peptide, CUB and EGF-like domain-containing protein 1 (Q6NZL8)
Organism: Mus musculus (Mouse)
Function: Could function as an adhesive molecule and its matrix bound and soluble fragments may play a critical role in vascular biology.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8IWY4}. Cell membrane {ECO:0000250|UniProtKB:Q8IWY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IWY4}.
Interaction partners:
- Signal peptide, CUB and EGF-like domain-containing protein 3
Sequence:
MGAAAVRWHLYLLLALGARGRLVGGSGLPGAVDVDECSEGTDDCHIDAICQNTPKSYKCLCKPGYKGEGRQCEDIDECENDYYNGGCVHDCINIPGNYRCTCFDGFMLAHDGHNCLDVDECQDNNGGCQQICVNAMGSYECQCHSGFFLSDNQHTCIHRSNEGMNCMNKDHGCAHICRETPKGGVACDCRPGFDLAQNQKDCTLTCNYGNGGCQHSCEDTDTGPMCGCHQKYALHADGRTCIEKDEAAIERSQFNATSVADVDKRVKRRLLMETCAVNNGGCDRTCKDTATGVRCSCPVGFTLQPDGKTCKDINECLMNNGGCDHFCRNTVGSFECGCQKGHKLLTDERTCQDIDECSFERTCDHICINSPGSFQCLCRRGYTLYGTTHCGDVDECSMNNGSCEQGCVNTKGSYECVCPPGRRLHWNQKDCVEMNGCLSRSKASAQAQLSCGKVGGVENCFLSCLGHSLFMPDSESSYILSCGVPGLQGKTLPKRNGTSSSTGPGCSDAPTTPIRQKARFKIRDAKCHLQPRSQERAKDTLRHPLLDNCHVTFVTLKCDSSKKRRRGRKSPSKEVSHITAEFEVEMKVDEASGTCEADCMRKRAEQSLQAAIKILRKSIGRNQFYVQVLGTEYEVAQRPAKALEGTGTCGIGQILQDGKCVPCAPGTYFSGDPGQCMPCVSGTYQDMEGQLSCTPCPSSEGLGLAGARNVSECGGQCSPGYFSADGFKPCQACPVGTYQPEPGRTGCFPCGGGLLTKHTGTASFQDCEAKVHCSPGHHYNTTTHRCIRCPVGTYQPEFGQNHCISCPGNTSTDFDGSTNVTHCKNQHCGGELGDYTGYIESPNYPGDYPANAECVWHIAPPPKRRILIVVPEIFLPIEDECGDVLVMRKSASPTSVTTYETCQTYERPIAFTSRSRKLWIQFKSNEANSGKGFQVPYVTYDEDYQQLIEDIVRDGRLYASENHQEILKDKKLIKALFDVLAHPQNYFKYTAQESKEMFPRSFIKLLRSKVSRFLRPYK
Protein: Macrophage migration inhibitory factor (MIF) (EC 5.3.2.1) (L-dopachrome isomerase) (L-dopachrome tautomerase) (EC 5.3.3.12) (Phenylpyruvate tautomerase) (Q02960)
Organism: Gallus gallus (Chicken)
Function: Pro-inflammatory cytokine. Involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P14174}. Cytoplasm {ECO:0000250|UniProtKB:P14174}. Note=Does not have a cleavable signal sequence and is secreted via a specialized, non-classical pathway. Secreted by macrophages upon stimulation by bacterial antigens (By similarity). {ECO:0000250|UniProtKB:P14174}.
Interaction partners:
- Invariant chain isoform p41
- Tyrosine aminotransferase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- 4-hydroxyphenylpyruvate dioxygenase.
- Amine oxidase.
- C-X-C chemokine receptor type 2
- C-X-C motif chemokine receptor 4
Sequence:
MPMFTIHTNVCKDAVPDSLLGELTQQLAKATGKPAQYIAVHIVPDQMMSFGGSTDPCALCSLYSIGKIGGQQNKTYTKLLCDMIAKHLHVSADRVYINYFDINAANVGWNGSTFA
Protein: Cadherin-2 (Neural cadherin) (N-cadherin) (CD antigen CD325) (P15116)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells. Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17988630, ECO:0000269|PubMed:26403541, ECO:0000269|PubMed:9655503}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Cell junction {ECO:0000269|PubMed:26750727}. Cell junction, adherens junction {ECO:0000269|PubMed:15479741}. Cell junction, desmosome {ECO:0000269|PubMed:15479741}. Cell surface {ECO:0000269|PubMed:25232112, ECO:0000269|PubMed:9655503}. Note=Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes (PubMed:26403541). Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (PubMed:23392350). {ECO:0000269|PubMed:23392350, ECO:0000269|PubMed:26403541}.
Interaction partners:
- Catenin delta-1
- Catenin beta-1
- Junction plakoglobin
- Cadherin-1
- Glutamate receptor 2
- Catenin alpha-1
- Cadherin-11
- Gap junction alpha-1 protein
- Neural cell adhesion molecule 1
- Catenin alpha-2
Sequence:
MCRIAGAPRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLPKDVHEGQPLLNVKFSNCNRKRKVQYESSEPADFKVDEDGTVYAVRSFPLTAEQAKFLIYAQDKETQEKWQVAVNLSREPTLTEEPMKEPHEIEEIVFPRQLAKHSGALQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGSVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDVIVANLTVTDKDQPHTPAWNAAYRISGGDPTGRFAILTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTLTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPEPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTINRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRLDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGDQDYDYLNDWGPRFKKLADMYGGGDD
Protein: Ras-related protein Rab-6B (EC 3.6.5.2) (P61294)
Organism: Mus musculus (Mouse)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Recruits VPS13B to the Golgi membrane. Regulates the compacted morphology of the Golgi. Seems to have a role in retrograde membrane traffic at the level of the Golgi complex. May function in retrograde transport in neuronal cells. Plays a role in neuron projection development.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NRW1}; Lipid-anchor {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q9NRW1}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9NRW1}. Note=Colocalizes with BICD1 at vesicular structures that align along microtubules. {ECO:0000250|UniProtKB:Q9NRW1}.
Interaction partners:
- Rab GDP dissociation inhibitor beta
- Rab GDP dissociation inhibitor alpha
- Guanine nucleotide exchange factor subunit RIC1
- GRIP and coiled-coil domain-containing protein 2
- ADP-ribosylation factor-like protein 1
- Vam6/Vps39-like protein
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- TATA element modulatory factor
- Protein bicaudal D homolog 2
Sequence:
MSAGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNLNSFQQTSKWIDDVRTERGSDVIIMLVGNKTDLADKRQITIEEGEQRAKELSVMFIETSAKTGYNVKQLFRRVASALPGMENVQEKSKEGMIDIKLDKPQEPPASEGGCSC
Protein: 14-3-3-like protein GF14 mu (General regulatory factor 9) (Q96299)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P48349}. Cytoplasm {ECO:0000250|UniProtKB:P48349}. Note=Translocates from the cytosol to the nucleus when phosphorylated. {ECO:0000250|UniProtKB:P48349}.
Interaction partners:
- Ankyrin repeat family protein
- Ankyrin repeat family protein
- Plastid-lipid-associated protein 6, chloroplastic
- Dual specificity phosphatase Cdc25
- FAM10 family protein At4g22670
- Protein transport protein SEC13 homolog A
- Probable plastid-lipid-associated protein 9, chloroplastic
- DEAD-box ATP-dependent RNA helicase 15
Sequence:
MGSGKERDTFVYLAKLSEQAERYEEMVESMKSVAKLNVDLTVEERNLLSVGYKNVIGSRRASWRIFSSIEQKEAVKGNDVNVKRIKEYMEKVELELSNICIDIMSVLDEHLIPSASEGESTVFFNKMKGDYYRYLAEFKSGNERKEAADQSLKAYEIATTAAEAKLPPTHPIRLGLALNFSVFYYEIMNAPERACHLAKQAFDEAISELDTLNEESYKDSTLIMQLLRDNLTLWTSDISEEGGDDAHKTNGSAKPGAGGDDAE
Protein: Ribosomal RNA large subunit methyltransferase J (EC 2.1.1.266) (23S rRNA (adenine(2030)-N6)-methyltransferase) (23S rRNA m6A2030 methyltransferase) (P37634)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the adenine in position 2030 of 23S rRNA. Nascent 23S rRNA seems to be the natural substrate. Appears to be not necessary for ribosome assembly. Required for the utilization of extracellular DNA as the sole source of carbon and energy.
Interaction partners:
- Ribosomal RNA large subunit methyltransferase F
- Ribosomal RNA small subunit methyltransferase A
- Uncharacterized protein YbaV
- tRNA1
Sequence:
MLSYRHSFHAGNHADVLKHTVQSLIIESLKEKDKPFLYLDTHAGAGRYQLGSEHAERTGEYLEGIARIWQQDDLPAELEAYINVVKHFNRSGQLRYYPGSPLIARLLLREQDSLQLTELHPSDYPLLRSEFQKDSRARVEKADGFQQLKAKLPPVSRRGLILIDPPYEMKTDYQAVVSGIAEGYKRFATGIYALWYPVVLRQQIKRMIHDLEATGIRKILQIELAVLPDSDRRGMTASGMIVINPPWKLEQQMNNVLPWLHSKLVPAGTGHATVSWIVPE
Protein: Twist-related protein 1 (Q568M7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPEEPARDSSSSPVSPADSLSNSDGEPDRPPKRCARKRRSSKKNGEDSDSSTLGKRGKKSSNSSNSPQSFEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLCQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH
Protein: Phospholipid-transporting ATPase accessory subunit CDC50 (Cell division control protein 50) (P25656)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for polarized cell growth.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21212072, ECO:0000305|PubMed:16956384}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:12589066}; Multi-pass membrane protein {ECO:0000269|PubMed:12589066}.
Interaction partners:
- Phospholipid-transporting ATPase DRS2
- Phospholipid-transporting ATPase DNF1
- Probable phospholipid-transporting ATPase DNF3
- Phospholipid-transporting ATPase DNF2
- Phospholipid-transporting ATPase NEO1
- Phospholipid-transporting ATPase accessory subunit LEM3
- Recyclin-1
- ADP-ribosylation factor 1
- Protein MON2
- ADP-ribosylation factor GTPase-activating protein GCS1
Sequence:
MVSLFKRGKAPPLTKEGPTSKKPPNTAFRQQRLKAWQPILSPQSVLPLLIFVACIFTPIGIGLIVSATKVQDLTIDYSHCDTKASTTAFEDIPKKYIKYHFKSKVENKPQWRLTENENGEQSCELQFEIPNDIKKSIFIYYKITNFYQNHRRYVQSFDTKQILGEPIKKDDLDTSCSPIRSREDKIIYPCGLIANSMFNDTFSQVLSGIDDTEDYNLTNKHISWSIDRHRFKTTKYNASDIVPPPNWMKKYPDGYTDENLPDIHTWEEFQVWMRTAAFPKFYKLTLKNESASLPKGKYQMNIELNYPISLFGGTKSFVLTTNGAIGGRNMSLGVLYLIVAGLCALFGIIFLVKLIFQPRAMGDHTYLNFDDEENEDYEDVHAENTTLREIL
Protein: NADH-ubiquinone oxidoreductase chain 5 (EC 7.1.1.2) (Q2F999)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MYLLIVFLPLLGSSVAGFFGRFLGSEGTAIMTTTCVSFSSILSLIAFYEVALGASACYLRIAPWISSEMFDASWGFFFDSLTVVMLIVVTFISSLVHLYSISYMSEDPHSPRFMCYLSIFTFFMLMLVTGDNFLQLFLGWEGVGLASYLLIHFWFTRLQADKAAIKAMLVNRVGDFGLALGIFGCFTLFQTVDFSTIFACASAPRNEWIFCNMRLNAITLICILLFIGAVGKSAQIGLHTWLPDAMEGPTPVSALIHAATMVTAGVFMIARCSPLFEYSPTALIVITFAGAMTSFLAATTGILQNDLKRVIAYSTCSQLGYMIFACGISNYSVSVFHLMNHAFFKALLFLSAGSVIHAMSDEQDMRKMGGLASSFPLTYAMMLMGSLSLIGFPFLTGFYSKDVILELAYTKYTISGNFAFWLGSVSVLFTSYYSFRLLFLTFLVPTNSFGRDRLRCHDAPIPMAIPLILLALGSLFVGYLAK
Protein: Slow termination of phototransduction, isoform A (Q9VA06)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSQLLQAFQRLVSQLKSQFVWVRCWLPFPRHFYGFRRETESRARLRLRVREQLRRNPANRASHQRNRRTQRRHLVMDYIFECFFDDTFEQISRNGLQDRQSRRDVLDHLSSIIKGCSGGQNSQTDEVAAIAVTAAMRYHRMAKEQNGQVCLMGKYHNILYIGLRTCWDWGVRDSEVVVKLLVAIYECEKTYERIFLGALFGPHAPHFIAGWRSDFQDQHENVRAMVYFLKHATREQLTLPVWIPRFEQERQLRFIDVPIESCGKSSPLRIALQANAPELLLILLRYGAAPQPPDGGASVIIALLDKLIEDGRNYSFELVMCLKILLRNVVMIEMPFKPLLYAARREMFFDRYGRLLMDKIIGKEQVYGVPSLRHLCRCCIRDVMRMHNQLPSGIDTLRLPKRLQRYIDLTEELEGPEAQDTEDKDQQRGKSSAKCKMGSEMGRLDTISSAGESEDESENQAQLLQAVTDPEKAALAAFMATGDGAYTEEAKKAAVEAYVAACPPDFDPDFPPISLPGEPR