wanglab/gogpt-training-data huggingface dataset:
Protein: Multiple inositol polyphosphate phosphatase 1 (EC 3.1.3.62) (2,3-bisphosphoglycerate 3-phosphatase) (2,3-BPG phosphatase) (EC 3.1.3.80) (Band 17) (Histidine phosphatase of the endoplasmic reticulum 1) (HiPER1) (F1NPQ2)
Organism: Gallus gallus (Chicken)
Function: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate (By similarity). May play a role in bone development (endochondral ossification) (By similarity). May play a role in the transition of chondrocytes from proliferation to hypertrophy.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:9472008}. Secreted {ECO:0000250|UniProtKB:Q9UNW1}. Cell membrane {ECO:0000250|UniProtKB:Q9Z2L6}. Note=Also associated with the plasma membrane in erythrocytes. {ECO:0000250|UniProtKB:Q9Z2L6}.
Interaction partners:
- Kinase
- Inositol-tetrakisphosphate 1-kinase
- SKICH domain-containing protein.
- IPPc domain-containing protein.
- inositol-polyphosphate 5-phosphatase
- Kinase
- Kinase
- Phosphoglycerate mutase 1
- Phosphoglycerate mutase
- Phosphoinositide phospholipase C
Sequence:
MAPRRAACLLPLLVAVASAGLGGYFGTKSRYEEVNPHLAEDPLSLGPHAAASRLPAACAPLQLRAVLRHGTRYPTAGQIRRLAELHGRLRRAAAPSCPAAAALAAWPMWYEESLDRLAPRGRRDMEHLARRLAARFPALFAARRRLALASSSKHRCLQSGAAFRRGLGPSLSLGADETEIEVNDALMRFFDHCDKFVAFVEDNDTAMYQVNAFKEGPEMRKVLEKVASALCLPASELNADLVQVAFLTCSYELAIKNVTSPWCSLFSEEDAKVLEYLNDLKQYWKRGYGYDINSRSSCILFQDIFQQLDKAVDESRSSKPISSPLIVQVGHAETLQPLLALMGYFKDAEPLQANNYIRQAHRKFRSGRIVPYAANLVFVLYHCEQKTSKEEYQVQMLLNEKPMLFHHSNETISTYADLKSYYKDILQNCHFEEVCELPKVNGTVADEL
Protein: Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma (EC 2.7.1.149) (Phosphatidylinositol 5-phosphate 4-kinase type II gamma) (PI(5)P 4-kinase type II gamma) (PIP4KII-gamma) (O88370)
Organism: Rattus norvegicus (Rat)
Function: Phosphatidylinositol 5-phosphate 4-kinase with low enzymatic activity. May be a GTP sensor, has higher GTP-dependent kinase activity than ATP-dependent kinase activity (By similarity). PIP4Ks negatively regulate insulin signaling through a catalytic-independent mechanism. They interact with PIP5Ks and suppress PIP5K-mediated PtdIns(4,5)P2 synthesis and insulin-dependent conversion to PtdIns(3,4,5)P3 (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:9685379}. Cytoplasm {ECO:0000269|PubMed:9685379}.
Interaction partners:
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Inositol polyphosphate 5-phosphatase OCRL
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
Sequence:
MASSSVPPATAPAAAGGPGPGFGFASKTKKKHFVQQKVKVFRAADPLVGVFLWGVAHSINELSQVPPPVMLLPDDFKASSKIKVNNHLFHRENLPSHFKFKEYCPQVFRNLRDRFAIDDHDYLVSLTRSPPSETEGSDGRFLISYDRTLVIKEVSSEDIADMHSNLSNYHQYIVKCHGNTLLPQFLGMYRVSVENEDSYMLVMRNMFSHRLPVHRKYDLKGSLVSREASDKEKVKELPTLKDMDFLNKNQKVYIGEEEKKVFLEKLKRDVEFLVQLKIMDYSLLLGIHDIIRGSEPEEEGPVREEESEWDGDCNLTGPPALVGSYGTSPEGIGGYIHSHRPLGPGEFESFIDVYAIRSAEGAPEGGVFHGLIDILTQYDAKKKAAHAAKTVKHGAGAEISTVHPEQYAKRFLDFISNIFA
Protein: Tubulin-specific chaperone A (H0Z0J2)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU364030}.
Interaction partners:
Sequence:
MYEKEAKQQEEKIEKMKAEACDDYGIKKQIPTPQSCPSTLILPRPSTLKLLLFTTEMTSTAMIEILQESRMMIPDCQRRLEVAHAELTQLLENEKELEEAEEYKEARSILESVKLEA
Protein: Pheromone-regulated membrane protein 10 (P42946)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YJL107C
Sequence:
MIVSFGDATTRTSEVQLVRCTQGLNLWKLHQVHAVYKRVVHDTLGADEGNALLDQILADTNLYPPWMCVLLYAFCSAMVTPYAFGGDWVNLAISFFMGLCVGSLQFILSQKSYMYSNVFEISASIVVSFCGRAFGSIPRSHICFGAVTQGSLALILPGYIILCGALELQSRSLVAGAVRMFYAIIYSLFLGFGITLGSALFGWMYHNATNEISCPQLISPWFRFLFVPAFTISISLLNQAHISQLPVMVFISCTGYVVTYWAGKHFANSTEFTAALAAFVIGVLGNLYSRIWKGLAVSAMLPAIFVQVPSGIASQNSLLSGLQSANTIVNANETITTSTSDPSSSMSFGMTMIQVCVGISVGLFASSLFVYPFGKKKTGLFSL
Protein: Transcription factor TB1 (Protein FINE CULM 1) (Protein TEOSINTE BRANCHED 1 homolog) (OsTB1) (TCP transcription factor 8) (OsTCP8) (Q8LN68)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor that functions as a negative regulator of lateral branching, presumably through its expression in axillary buds. Involved in the fine tuning of shoot branching. May function as an integrator of multiple signaling pathways to regulate the development of axillary buds. Works partially downstream of strigolactones to inhibit bud outgrowth. Binds to MADS57 to suppress the negative regulation of D14 by MADS57 and balance the expression of D14 for tillering.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701}.
Interaction partners:
- MADS-box transcription factor 57
Sequence:
MLPFFDSPSPMDIPLYQQLQLTPPSPKPDHHHHHHSTFFYYHHHPPPSPSFPSFPSPAAATIASPSPAMHPFMDLELEPHGQQLAAAEEDGAGGQGVDAGVPFGVDGAAAAAAARKDRHSKISTAGGMRDRRMRLSLDVARKFFALQDMLGFDKASKTVQWLLNMSKAAIREIMSDDASSVCEEDGSSSLSVDGKQQQHSNPADRGGGAGDHKGAAHGHSDGKKPAKPRRAAANPKPPRRLANAHPVPDKESRAKARERARERTKEKNRMRWVTLASAISVEAATAAAAAGEDKSPTSPSNNLNHSSSTNLVSTELEDGSSSTRHNGVGVSGGRMQEISAASEASDVIMAFANGGAYGDSGSYYLQQQHQQDQWELGGVVYANSRHYC
Protein: Mini zinc finger protein 1 (AtMIF1) (Q9CA51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibits zinc finger homeodomain (ZHD) transcription factors, such as ZHD5, by interacting with them to prevent both their nuclear localization and their DNA-binding properties. Involved in integrating signals from multiple hormones by preventing the expression of genes involved in gibberellic acid (GA), auxin and brassinosteroid signaling and by promoting the expression of abscisic acid (ABA)-responsive genes. Regulates several development aspects, including photomorphogenesis, apical dominance, longevity, flower morphology and fertility, as well as root and stem elongation. Promotes the formation of ectopic shoot meristems on leaf margins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21059647}.
Interaction partners:
- TRF-like 8
Sequence:
MMKKRQMVIKQRSRNSNTSSSWTTTSSSSSSSEISNVRYVECQKNHAANIGGYAVDGCREFMAAGVEGTVDALRCAACGCHRNFHRKEVDTEVVCEYSPPNA
Protein: Nuclear hormone receptor family member nhr-20 (Q09565)
Organism: Caenorhabditis elegans
Function: Orphan nuclear receptor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
Sequence:
MKQERSSGGYSGIPPTSKCLVCEHPDGGSAHFGSTSCLACAAFFRRTVSLNIQFQCKKDKNCVIFHELRMICRACRFDKCVKAGMRRECVQKRRSNKKIPKKHMNMLREDQIKMEYDECKFECSGDQTDDNSPLSIEKKSPPGLLPNDSPMMADFKFDPSDIPSTSGGSTQRLERSPSPKLAESKILSMNGEELLRFYVDQLKNSMDRRRMIFTDTALLAVIDDRGDVPFDATEPPPHSLKRQYESQRFDNLLAFDFCKCCPGFDFLSRVEKAIFFRSCSLAYCLLDIAWITVQAYPEEAAEPVLMYTDGSVCTVNNLSYGWDDEEDICAHDKKKLFLGFLGRFNDAICRPIRNLKMTHVEFAALKALCIWKLGYCEFTPSMKVIGKEHEEALLNGLHNYYDDLYGNPDETGMRIGNLILLMGTVFEMNQLIMETYKSAELFELFKLDALSKSLLTL
Protein: Uncharacterized protein YdjY (P76220)
Organism: Escherichia coli (strain K12)
Interaction partners:
- TVP38/TMEM64 family membrane protein YdjX
- TVP38/TMEM64 family inner membrane protein YdjZ
- Protein YnjB
- Inner membrane ABC transporter permease protein YnjC
- Uncharacterized ABC transporter ATP-binding protein YnjD
- Uncharacterized protein YnjA
- Thiosulfate sulfurtransferase YnjE
- Uncharacterized fimbrial chaperone YcbF
- UPF0410 protein YeaQ
- Uncharacterized protein YdiH
Sequence:
MLQHYSVSWKKGLAALCLLAVAGLSGCDQQENAAAKVEYDGLSNSQPLRVDANNHTVTMLVQINGRFLTDDTRHGIVFKDGSNGHKSLFMGYATPKAFYEALKEAGGTPGENMTMDNKETTHVTGSKLDISVNWQGAAKAYSFDEVIVDSNGKKLDMRFGGNLTAAEEKKTGCLVCLDSCPVGIVSNATYTYGAVEKRGEVKFKGNASVLPADNTLATVTFKIAE
Protein: OTU domain-containing protein 1 (EC 3.4.19.12) (DUBA-7) (Q5VV17)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin.
Interaction partners:
- Zinc finger-containing ubiquitin peptidase 1
- Receptor-interacting serine/threonine-protein kinase 1
- Polyubiquitin-C
Sequence:
MQLYSSVCTHYPAGAPGPTAAAPAPPAAATPFKVSLQPPGAAGAAPEPETGECQPAAAAEHREAAAVPAAKMPAFSSCFEVVSGAAAPASAAAGPPGASCKPPLPPHYTSTAQITVRALGADRLLLHGPDPVPGAAGSAAAPRGRCLLLAPAPAAPVPPRRGSSAWLLEELLRPDCPEPAGLDATREGPDRNFRLSEHRQALAAAKHRGPAATPGSPDPGPGPWGEEHLAERGPRGWERGGDRCDAPGGDAARRPDPEAEAPPAGSIEAAPSSAAEPVIVSRSDPRDEKLALYLAEVEKQDKYLRQRNKYRFHIIPDGNCLYRAVSKTVYGDQSLHRELREQTVHYIADHLDHFSPLIEGDVGEFIIAAAQDGAWAGYPELLAMGQMLNVNIHLTTGGRLESPTVSTMIHYLGPEDSLRPSIWLSWLSNGHYDAVFDHSYPNPEYDNWCKQTQVQRKRDEELAKSMAISLSKMYIEQNACS
Protein: RNA-binding protein VTS1 (VTI1-2 suppressor protein 1) (Q08831)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:11445562, ECO:0000269|PubMed:14562095}. Cytoplasm, P-body {ECO:0000250|UniProtKB:J9VVN9}.
Interaction partners:
- Suppressor protein MPT5
- mRNA-binding protein PUF3
- Polyadenylate-binding protein, cytoplasmic and nuclear
Sequence:
MKHPYEEFPTGSKSPYNMSRGAHPGAVLLSPQSSAINKNNPGSNSGNNQGNSSVTANVLSPQSHSMSLNDMLDQQSFMLDTAGTRAQPLQQQQQQQQQQQQASLPSLNIQTVSSTAAGSAIVSPMMQSPKALQSTLSSTSMYLDSFQRSPNNILGIPSQSGSIPLPQSRQSQQQSQSQKNDPNMGTNFSQDINQLCSWISMLNSSQQNTVMDNILSILNDDVLKYTKLKIETLTNTPFISPPLPAIASPIPNRDDTQILNIDSVFSSSPITNDPENTDNLLYQNWSPQPHSIPISQPIYDNITDASQRSKSAEPHVNSSPNLIPVQKQFNNGNSTKYKKLPSENPNYLSHSLSSSHSFFQPKKRSNMGNEYNSHHHHSLHHPLHNTTSYFSNTSRPSGTDLNKSNQNVFNNTITHPNAGPTSATSTSTSSNGNTPLSSNSSMNPKSLTDPKLLKNIPMWLKSLRLHKYSDALSGTPWIELIYLDDETLEKKGVLALGARRKLLKAFGIVIDYKERDLIDRSAY
Protein: P2Y purinoceptor 13 (P2Y13) (G-protein coupled receptor 86) (Q9D8I2)
Organism: Mus musculus (Mouse)
Function: Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- P2Y purinoceptor 12
- P2X purinoceptor 1
- P2X purinoceptor 6
- P2Y purinoceptor 4
- P2Y purinoceptor 14
- P2X purinoceptor
- P2X purinoceptor 2
- P2X purinoceptor 7
- P2X purinoceptor 3
- P2X purinoceptor 4
Sequence:
MLGTINTTGMQGFNKSERCPRDTRMTQLLFPVLYTVVFLAGILLNTVALWVFVHIPSNSTFIVYLKNTLVADLIMALMLPFKILSDSHLAPWQLRGFVCTLSSVVFYETMYVGIMMLGLIAFDRFLKIIMPFRKTFVKKTAFAKTVSISVWSLMFFISLPNMILNKEATPSSVKKCASLKSPLGLWWHQVVSHTCQFIFWAVFILMLLFYAVITKKVYNSYRKFRSKDSRHKRLEVKVFIVMAVFFVCFAPLHFVRIPYTYSQTTNKTDCRLENQLFIAKEATLFLATTNICMDPLIYIILCKKFTQKVPCVRWGKARTAGSSEDHHSSQTDNITLA
Protein: DNA polymerase delta subunit 2 (DNA polymerase delta subunit p50) (P49004)
Organism: Bos taurus (Bovine)
Function: Accessory component of both the DNA polymerase delta complex and the DNA polymerase zeta complex. As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair. Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS as a component of the DNA polymerase zeta complex. Along with POLD3, dramatically increases the efficiency and processivity of DNA synthesis of the DNA polymerase zeta complex compared to the minimal zeta complex, consisting of only REV3L and REV7.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49005}. Note=Recruited to DNA damage sites within 2 hours following UV irradiation. {ECO:0000250|UniProtKB:P49005}.
Interaction partners:
- DNA polymerase delta catalytic subunit
- DNA polymerase delta subunit 3
- DNA polymerase zeta catalytic subunit
- Proliferating cell nuclear antigen
- Mitotic spindle assembly checkpoint protein MAD2B
- Flap endonuclease 1
- DNA polymerase
- DNA polymerase epsilon catalytic subunit
- DNA polymerase epsilon subunit 2
- DNA polymerase delta subunit 4
Sequence:
MFSEQAAQRAHTLLSPPSASNATFARVPVVTYTNSSQPFRLGERSFSRQYAHIYATRLIQMRPFLVSRAQQRWGSGVLVKKLCELQPGEKCCVVGTLFKAMPLQPSILREVSEEHNLLPQPPRSKYIHPDDELILEDELQRIKLEGTIDVSKLVTGTVLAVLGSAGDDGKFLVEDHCFAGLAPQKPACPLDTDRFVLLVSGLGLGGGGGESLLGTQLLVDVVTGQLGDEGEQCSAAHVSRVILAGNLLSHNTQSRDSINKAKYLTKKTQAASVEAVKMLDEILLQLSASVPVDVMPGEFDPTNYTLPQQPLHPCMFPLATAYSTLQLVTNPYQATIDGVRFLGTSGQNVSDIFRYSSMEDHLEILEWTLQVRHISPTAPDTLGCYPFYKTDPFIFPECPHVYFCGNTPSFGSKIIQGPEDQTVLLVAVPDFSTTQTACLVNLRSLACQPISFSGFGAEDEDLGGLGLGP
Protein: Dynein regulatory complex subunit 5 (T-complex-associated testis-expressed protein 1) (Tcte-1) (A6H639)
Organism: Mus musculus (Mouse)
Function: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. May play a role in the assembly of N-DRC (By similarity). Required for sperm motility.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|Ref.2}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HMZ4}. Note=Detected along the length of the sperm flagellum. {ECO:0000269|Ref.2}.
Interaction partners:
- Dynein regulatory complex subunit 2
- Dynein regulatory complex subunit 3
- Dynein regulatory complex subunit 4
- Dynein regulatory complex protein 9
- Radial spoke head protein 9 homolog
- Dynein regulatory complex subunit 7
Sequence:
MQETPSVPSNSSSHSQSVLTIQRQVSALGSSSTGPTSLKTSSTPTPGQLKTKVPNVRRMRRIISEDAEWSLAIVPLLTELCIQHIVKNFQNNPILKQLPLEHQKKVLSNLPPELPLTVTANLIDDENYWHRCCIKRWSVCHVSRHGGSWKRMFFERHLENLLKLFIPGTTDPNVILDLLPLCRNYVRRIHVDQFLPPVRMPTPLQGEEQSDSGSEGEGSEPEKDHYQLQTLVGGLKHLEELDLVYGVKDCGMNFEWNLFLFTYRDCYSLAATIKACHTLKIFKLTRSKVDDDKARILIRSLLDHPALEELDLSHNLIGDRGARAAAKLLSHSRLRVLNLANNQLQAPGAQSLAHALAHNTNLVFLNLRLNCIEDEGGQAIAHALETNKCLSVLHLGGNKLSEPTATLLSQMLTVNTTLVSLNLSCNHIGQDGGKQLLEGISDNKTILEFDLRLSDVSQESEYLIGQVLHANREAARQRTLNPGHFSSPTNNCTENSVV
Protein: Serpin family I member 2 (G3V7A3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- WD repeat domain 49
Sequence:
MKKTILWSFLLFLSGSQTSRTMDQKNAEFAVDLYKAISLSNKNNVIFSPLGTTVLLGMVQLGAKGKAQQQIMQTLRMQKTSTGEEFSVLKSLFSAISKKKQEFTFNLASALYLQEGFIVKESYLHSNKEFFQSATKLVDFLDAKTSAQAISTWVESKTDGKIKNMFSEEDFGPLTRLVLVNAIYFKGDWKQKFRKEDTEMTDFSKKDGSTVKIPMMKALLRAKYGYFSESSMTYQVLELPYKADEFSLVILLPTEDVNIEEVEKQVTARHVQKWFSELHEEEVEVSLPRFKIEQKLDFKEALFSLNVTEIFSGGCDLSGITDSSELYVSRAMQKVFFEINEDGSEAAASTGINIPAIMSLTQTQFLANHPFLFIMKHIQTESILFMGKVTDPDIHTVKGRDLDSL
Protein: Biogenesis of lysosome-related organelles complex 1 subunit CNL1 (BLOC-1 subunit CNL1) (CNO-like protein 1) (Q06333)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1), a complex that is involved in endosomal cargo sorting.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Note=Punctate pattern.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit KXD1
- Biogenesis of lysosome-related organelles complex 1 subunit BLI1
- Biogenesis of lysosome-related organelles complex 1 subunit SNN1
- Biogenesis of lysosome-related organelles complex 1 subunit VAB2
- Biogenesis of lysosome-related organelles complex 1 subunit BLS1
Sequence:
MQDNSSHSRESASAGDDPLGIDKLTVDYDYLLYKMRDYVQSIQLDTTELCKKQNEVMVNGIIENTIDKNIAKFKELLEKCDTLENHYEMLNQLAIITDTFKERIAEAVNNYNSLKKGASKSK
Protein: Ras-related GTP-binding protein D (Rag D) (RagD) (EC 3.6.5.-) (Q9NQL2)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade. Forms heterodimeric Rag complexes with RRAGA or RRAGB and cycles between an inactive GTP-bound and an active GDP-bound form. In its active form participates in the relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11073942}. Nucleus {ECO:0000269|PubMed:11073942}. Lysosome membrane {ECO:0000269|PubMed:20381137}. Note=Predominantly cytoplasmic (PubMed:11073942). Recruited to the lysosome surface by the Ragulator complex (PubMed:20381137). May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA (PubMed:11073942). {ECO:0000269|PubMed:11073942, ECO:0000269|PubMed:20381137}.
Interaction partners:
- Ragulator complex protein LAMTOR5
- Ras-related GTP-binding protein C
- Ras-related GTP-binding protein B
- Ragulator complex protein LAMTOR3
- Ras-related GTP-binding protein A
- Regulatory-associated protein of mTOR
- Ragulator complex protein LAMTOR1
- Ragulator complex protein LAMTOR4
- Neutral amino acid transporter 9
- Serine/threonine-protein kinase mTOR
Sequence:
MSQVLGKPQPQDEDDAEEEEEEDELVGLADYGDGPDSSDADPDSGTEEGVLDFSDPFSTEVKPRILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKICREDVSNSSFVNFQIWDFPGQIDFFDPTFDYEMIFRGTGALIFVIDSQDDYMEALARLHLTVTRAYKVNTDINFEVFIHKVDGLSDDHKIETQRDIHQRANDDLADAGLEKIHLSFYLTSIYDHSIFEAFSKVVQKLIPQLPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSTPVDMQTYELCCDMIDVVIDISCIYGLKEDGAGTPYDKESTAIIKLNNTTVLYLKEVTKFLALVCFVREESFERKGLIDYNFHCFRKAIHEVFEVRMKVVKSRKVQNRLQKKKRATPNGTPRVLL
Protein: Transmembrane and coiled-coil domain protein 3 (Q9ULS5)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24454821, ECO:0000269|PubMed:30220460}; Multi-pass membrane protein {ECO:0000255}. Note=Concentrates in discrete patches along peripheral endoplasmic reticulum tubules. {ECO:0000269|PubMed:30220460}.
Interaction partners:
Sequence:
MPGSDTALTVDRTYSYPGRHHRCKSRVERHDMNTLSLPLNIRRGGSDTNLNFDVPDGILDFHKVKLTADSLKQKILKVTEQIKIEQTSRDGNVAEYLKLVNNADKQQAGRIKQVFEKKNQKSAHSIAQLQKKLEQYHRKLREIEQNGASRSSKDISKDHLKDIHRSLKDAHVKSRTAPHCMESSKSGMPGVSLTPPVFVFNKSREFANLIRNKFGSADNIAHLKNSLEEFRPEASARAYGGSATIVNKPKYGSDDECSSGTSGSADSNGNQSFGAGGASTLDSQGKLAVILEELREIKDTQAQLAEDIEALKVQFKREYGFISQTLQEERYRYERLEDQLHDLTDLHQHETANLKQELASIEEKVAYQAYERSRDIQEALESCQTRISKLELHQQEQQALQTDTVNAKVLLGRCINVILAFMTVILVCVSTIAKFVSPMMKSRCHILGTFFAVTLLAIFCKNWDHILCAIERMIIPR
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (ATP-specific succinyl-CoA synthetase subunit beta) (A-SCS) (Succinyl-CoA synthetase beta-A chain) (SCS-betaA) (Q9P2R7)
Organism: Homo sapiens (Human)
Function: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03220, ECO:0000269|PubMed:15877282, ECO:0000269|PubMed:17287286, ECO:0000269|PubMed:25944712}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
Sequence:
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Protein: Beta-1,4-N-acetylgalactosaminyltransferase bre-4 (EC 2.4.1.-) (Bacillus thuringiensis toxin-resistant protein 4) (Bt toxin-resistant protein 4) (Beta-4-GalNAcT) (Q9GUM2)
Organism: Caenorhabditis elegans
Function: Catalyzes the transfer of galactose onto proteins or lipids. Required for susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-3 and bre-5.
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-
- ILEI/PANDER domain-containing protein
- Beta-1,3-galactosyltransferase bre-5
- Beta-1,3-galactosyltransferase bre-2
- Beta-1,4-mannosyltransferase bre-3
- Hexosyltransferase
- Beta-1,4-N-acetylgalactosaminyltransferase
- UDP-galactose transporter
- Fucosyltransferase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Sequence:
MAFRHLAVARLKSLLVLCAVLLLVHAMIYKIPSLYENLTIGSSTLIADVDAMEAVLGNTASTSDDLLDTWNSTFSPISEVNQTSFMEDIRPILFPDNQTLQFCNQTPPHLVGPIRVFLDEPDFKTLEKIYPDTHAGGHGMPKDCVARHRVAIIVPYRDREAHLRIMLHNLHSLLAKQQLDYAIFIVEQVANQTFNRGKLMNVGYDVASRLYPWQCFIFHDVDLLPEDDRNLYTCPIQPRHMSVAIDKFNYKLPYSAIFGGISALTKDHLKKINGFSNDFWGWGGEDDDLATRTSMAGLKVSRYPTQIARYKMIKHSTEATNPVNKCRYKIMGQTKRRWTRDGLSNLKYKLVNLELKPLYTRAVVDLLEKDCRRELRRDFPTCF
Protein: Thioredoxin-3, mitochondrial (P25372)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion.
Interaction partners:
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin reductase 1
- Glutathione reductase
- Peroxiredoxin PRX1, mitochondrial
- Tryptophan synthase
- Glutathione peroxidase-like peroxiredoxin 1
- Glutathione peroxidase-like peroxiredoxin HYR1
- SUMO-conjugating enzyme UBC9
Sequence:
MLFYKPVMRMAVRPLKSIRFQSSYTSITKLTNLTEFRNLIKQNDKLVIDFYATWCGPCKMMQPHLTKLIQAYPDVRFVKCDVDESPDIAKECEVTAMPTFVLGKDGQLIGKIIGANPTALEKGIKDL