wanglab/gogpt-training-data huggingface dataset:
Protein: Glutathione S transferase E9 (EC 2.5.1.18) (Putative glutathione S-transferase) (Q7K8X7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutathione S transferase E7
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S transferase D9, isoform A
- Glutathione S transferase T1
- FI01423p
- Inactive glutathione S-transferase D3
- Uncharacterized protein, isoform C
- Glutathione S transferase E6
- FI03416p
- GH14654p
Sequence:
MGKLVLYGVEASPPVRACKLTLDALGLQYEYRLVNLLAGEHKTKEFSLKNPQHTVPVLEDDGKFIWESHAICAYLVRRYAKSDDLYPKDYFKRALVDQRLHFESGVLFQGCIRNIAIPLFYKNITEVPRSQIDAIYEAYDFLEAFIGNQAYLCGPVITIADYSVVSSVSSLVGLAAIDAKRYPKLNGWLDRMAAQPNYQSLNGNGAQMLIDMFSSKITKIV
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (Phospholipase A1) (EC 3.1.1.32) (Q29524)
Organism: Ovis aries (Sheep)
Function: Key enzyme in triglyceride metabolism (By similarity). Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (By similarity). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11151}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11151}; Extracellular side {ECO:0000250|UniProtKB:P11151}. Secreted {ECO:0000250|UniProtKB:P11151}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11151}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles. {ECO:0000250|UniProtKB:P11151}.
Interaction partners:
- Fibrinogen C-terminal domain-containing protein
- Snake toxin/toxin-like domain-containing protein
- Apolipoprotein C-II
- Angiopoietin-related protein 3
- triacylglycerol lipase
- Monoglyceride lipase
- Carboxylic ester hydrolase
- Hepatic triacylglycerol lipase
- Apolipoprotein E
- Beta-2-glycoprotein 1
Sequence:
MESKVLLLLALSVWLQSLTVSRGGLVAADRITRGKDFRDIESKFALRTPEDTAEDTCHLIPGVTESVANCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQQHYPVSAGYTKLVGQDVAKFMNWMADEFNYPLGNVHLLGYSLGAHAAGIAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEALRVIAERGLGDVDQLVKCSHERSVHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNMGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESNTYTNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLLYTEVDIGELLMLKLKWISDSYFSWSNWWSSPGFDIGKIRVKAGETQKKVIFCSREKMSYLQKGKSPVIFVKCHDKSLNRKSG
Protein: RuvB-like helicase (EC 3.6.4.12) (M0R0Y3)
Organism: Homo sapiens (Human)
Subcellular location: Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363048}.
Interaction partners:
Sequence:
MVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTTPYSEKDTKQILRIRVQKCRWMTSSGSTHSSWTSPAPRST
Protein: Ubiquitin-conjugating enzyme E2 variant 1C (Ubc enzyme variant 1C) (Protein MMS ZWEI HOMOLOG 3) (Q9SJ44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has no ubiquitin ligase activity on its own. The heterodimer with UBC catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. May play a role in the control of progress through the cell cycle and differentiation. May play a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 35
- Ubiquitin-conjugating enzyme E2 13
- Cytochrome b-c1 complex subunit Rieske-2, mitochondrial
- Ubiquitin-ribosomal protein eL40y fusion protein
- Probable disease resistance protein At1g51480
- Probable disease resistance protein At5g43730
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin-conjugating enzyme E2 variant 1B
- Ubiquitin-conjugating enzyme E2 variant 1A
- Ubiquitin-conjugating enzyme E2 22
Sequence:
MTLGSGSSVVVPRNFRLLEELERGEKGIGDGTVSYGMDDGDDIYMRSWTGTIIGPHNTVHEGRIYQLKLFCDKDYPEKPPTVRFHSRINMTCVNHDTGVVDSKKFGVLANWQRQYTMEDILTQLKKEMAASHNRKLVQPPEGTFF
Protein: Terminal flower 1b (B4XEW1)
Organism: Gossypium arboreum (Tree cotton) (Gossypium nanking)
Interaction partners:
Sequence:
MAREVEPLMVGRVIGDVMDSFIPSIKMSVTFNNKQVFNGHEFYPSTVVTKPRVEVVGGDMRTFFTLVMTDPDVPGPSDPYLREHLHWIVTDIPGTTDATFGREVVSYENPKPNIGIHRFVFVLFKQKRRQIIKSPCSRDNFNTRRFAFENDLGLPVAAVYFNAQRETAARRR
Protein: Malate dehydrogenase, cytoplasmic (EC 1.1.1.37) (Aromatic alpha-keto acid reductase) (KAR) (EC 1.1.1.96) (Cytosolic malate dehydrogenase) (O88989)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P40925}.
Interaction partners:
- Fumarate hydratase, mitochondrial
- Citrate synthase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Pyruvate carboxylase, mitochondrial
- ATP-citrate synthase
- Malic enzyme
- NADP-dependent malic enzyme
- Malic enzyme
Sequence:
MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLQDVIATDKEEVAFKDLDVAVLVGSMPRREGMERKDLLKANVKIFKSQGAALEKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKSQIALKLGVTADDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAISDHIRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKETAFEFLSSA
Protein: tRNA (guanine(37)-N(1))-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA methyltransferase 5) (Q8TFG7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152, ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
Interaction partners:
- Uncharacterized alpha-1,2-galactosyltransferase C637.06
- DNA-directed RNA polymerase II subunit rpb4
- PX domain-containing protein C1450.12
- Dehydrodolichyl diphosphate synthase complex subunit nus1
- Probable FAD synthase
Sequence:
MAELLHPNKVEMKPFLKNLDKNLFKKTYNLVAAKVSPKKVGLLNKVCKKDLLDWPRVKHVYQQNNEKLVLLNRDASLDGTRGLSDATVSFIKENNIELVPFQLTLDYDYWRADDILDAILPPGEKEDHPSGFTAVGHIAHMNLREEWLPYKYIIGKVILDKNPSIETVVNKTDTIDTKFRTFQMEVLAGKDDFIVTQSESNCKFRFDFSKVYWNSRLSTEHDRLIQQFQPGDAVCDVMAGVGPFACPAGKKNVIVFANDLNPYSYESLVENIFLNKVANFVKAFNQDGREFIRSSVQKLLGFSKDEKAITVFPPRKRARKLEENKDPVRQDIPIPPVFSHYVMNLPGSAIEFLDAFKGCYYGLEYLFKDRSLPKVHVHCFCRFPDPEEDLINRIYASLGYRFSPEEVDFYYVRKVAPNKDMYCCTFTLPGSIIFAKPVSG
Protein: BcDNA.LD23634 (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9V3Y5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE11167p
- Putative RNA-binding protein Alsin2
- U1 small nuclear ribonucleoprotein 70 kDa
- U1 small nuclear ribonucleoprotein C
- Probable U2 small nuclear ribonucleoprotein A'
- Nuclear cap-binding protein subunit 2
- Splicing factor 3B subunit 3
- LD24714p
- Probable ATP-dependent RNA helicase DDX46
- RH42690p
Sequence:
MSYPPRAPMPPFMNTAIPPPHIMQNMAKPPRSFRNSATISSQPTVYQRPPEPQPQFRGPIITVFVGNISERVPEALLKRILNACGVVINWKRVSTFGFCEFDGPIAAMRAVRLLSEMEIDGKKLVAKVDAKNKVLIEDYKEQECKNGDRSNPVDEKTEDEFAIAQMHEFLEEHKHEFEGFDSSSRADLYGSANRNKKTRREEDIKMKVLSENTLEEEKRNLISSEIGKFRMRAEEDEHRKELEKEKEKEKLAASKEKERKKQREMERMSSTSKSGSSSTAAASSSSATATSSTPAADGADMSDKTDKESVAVVIKETVKESKESASSTGRKESSSAAIEITQKERRSDSKETRRRRSKSRSKDRERERERELRELRDKERERERDRERERERERNEMRERERNEMREREREREREREREEKLLKPVRDTWREKEMEDELRDRKKAEKKAREKEIAYQTRLTDWEVREKRKAKENEKYRLKELLRQEERETDAKRLKEFVEDYDDERDDSLYYRGRELQQRLAERVREADADSKDREKEAEELAELKSKFFSGEYENPSLEFEKARLEIEKLYEPRILINVNQEPPAAATSSVHQRKQAASAPGEDDEGQKQRQKSQQLDSYDPDMAGTNDDDSISNDDRASMADTASNASGVYAKNNNNDQSLSNSLSRHNSESRDSLAQIHTPTQSAILNDQESGHDAILPSATPPMTMPLISLTLGNNLKKKKIEATGVFVNDDDNDENINPKKRKLVPLDYDDNISNTTPSNHAASSGSGAANNSSSSNNNNSSSADRQSSAVSAATAAAAAVSQKIAQAFGGGSSGSGSGSGSGSNASGGKNNGGGSSSSSNNKHNSNSKHGKNEAAASAGSSADAAAANIKKDENGAKVYDEKRRHIKSIIDRIPTQKEELFNYKLDRNEIDSGLMERKIRPWINKKIIEYIGEPEPTLVDFICSKVLAGSPPQSILDDVQMVLDEEAEVFVVKMWRLLIYELDAKKSGLAGK
Protein: BTB/POZ domain-containing protein KCTD7 (Q8BJK1)
Organism: Mus musculus (Mouse)
Function: May be involved in the control of excitability of cortical neurons.
Subcellular location: Cell membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
Sequence:
MVVVTGREPDSRHSDGAMSSSEAEDDFLEPATPTATQAGHGLPLLPQEFPEVVPLNIGGAHFTTRLSTLRRYEDTMLAAMFSGRHYIPTDSEGRYFIDRDGTHFGDVLNFLRSGDLPPREHVRAVHKEAQYYAIGPLLEQLENMQPLKGEKVRQAFLGLMPYYKDHLERIVEIARLRAVQRKARFAKLKVCVFKEEMPITPYECPLLNSLRFERSESDGQLFEHHCEVDVSFGPWEAVADVYDLLHCLVTDLSAQGLTVDHQCIGVCDKHLVNHYYCKRPIYEFKITWW
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 3A (SMEK homolog 1) (Q6IN85)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of serine/threonine-protein phosphatase 4. May regulate the activity of PPP4C at centrosomal microtubule organizing centers. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140' (gamma-H2AX) generated during DNA replication and required for DNA DSB repair.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18487071}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18487071}. Nucleus {ECO:0000269|PubMed:18487071}. Note=In interphase localized in the cytoplasm and in the nucleus (with higher levels). During metaphase located in pericentriolar regions.
Interaction partners:
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 3B
- Serine/threonine-protein phosphatase 2A activator
- CREB-regulated transcription coactivator 2
- Protein PPP4R3C
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Wings apart-like protein homolog
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Ran-specific GTPase-activating protein
Sequence:
MTDTRRRVKVYTLNEDRQWDDRGTGHVSSGYVERLKGMSLLVRAESDGSLLLESKINPNTAYQKQQDTLIVWSEAENYDLALSFQEKAGCDEIWEKICQVQGKDPSVDITQDLVDESEEERFDDMSSPGLELPSCELSRLEEIAELVASSLPSPLRREKLALALENEGYIKKLLELFHVCEDLENIEGLHHLYEIIKGIFLLNRTALFEVMFSEECIMDVIGCLEYDPALSQPRKHREFLTKTAKFKEVIPISDPELKQKIHQTYRVQYIQDMVLPTPSVFEENMLSTLHSFIFFNKVEIVGMLQEDEKFLTDLFAQLTDEATDEEKRQELVNFLKEFCAFSQTLQPQNRDAFFKTLSNMGILPALEVILGMDDTQVRSAATDIFSYLVEYNPSMVREFVMQEAQQNDDVSKKLTEQKITSKDILLINLIIEHMICDTDPELGGAVQLMGLLRTLVDPENMLATANKTEKTEFLGFFYKHCMHVLTAPLLANTTEDKPSKDDFQTAQLLALVLELLTFCVEHHTYHIKNYIINKDILRRVLVLMASKHAFLALCALRFKRKIIGLKDEFYNRYIMKSFLFEPVVKAFLNNGSRYNLMNSAIIEMFEFIRVEDIKSLTAHVIENYWKALEDVDYVQTFKGLKLRFEQQRERQDNPKLDSMRSILRNHRYRRDARTLEDEEEMWFNTDEDDMEDGEAVVSPSDKTKNDDDIMDPISKFMERKKLKESEEKEVLLKTNLSGRQSPSFKLSLSSGTKTNLTSQSSTTNLPGSPGSPGSPGSPGSPGSVPKNTSQTAAITTKGGLVGLVDYPDDDEDDDEDEDKEDTLPLSKKAKFDS
Protein: Archaic Translocase of outer membrane 14 kDa subunit (Q385K8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTEALYNFIESERFQRVSGIVSSGASTIYQWLSERAWAVYTTGAFVSVLVALGSAHEKQILADHLYGSHAPLQQQQERSNTIEGGKKLLQEEASQGVRQVVWMMPREDFMQEYRERHGI
Protein: Protein C-ets-2 (P10157)
Organism: Gallus gallus (Chicken)
Function: Probable transcription factor.
Subcellular location: Nucleus.
Interaction partners:
- Mitogen-activated protein kinase.
- Transforming protein p68/c-ets-1
- Runt-related transcription factor
Sequence:
MSEFAIRNMDQVAPVSNMYRGMLKRQPAFDTFDSSNSLFAGYFLSLNEDQTLQEVPTGFDSTSYESNNCELPLLTPCSKAVMSQALKDTFSGFTKEQCRLGIPNNPWLWTEQHVCQWLAWATNEFSLANVNIHQFLMSGQDLCNLGKERFLELAPDYVGDILWEHLEQMIKDSQEKTQDQYVESSHLTSVPHWVNNNSLTVNVDQTPYGIQMPGYPKALSYPKPNLLSDICQTSTGPNLLSPEQDFSLFPKTQVDAVSVNYCTVNQDFTRSNLNLLIDNSGKLREHESSESGAESYESSDSMLQSWNSQSSLVDLQRVPSYESFEDDCSQSLCMSKPTMSFKDYIQDRSDPVEQGKPVIPAAILAGFTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLADPDEVARRWGRRKNKPKMNYEKLSRGLRYYYDKNIIHKTSGKRYVYRFVCDLQNLLGYTAEELHAMLGVQPDTED
Protein: AcGAP protein (Q9N9Z9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALSALASFDDLRRCMQVLTDGTPEEEFLRFLRMFEQYHEKCAGYAAETARIQNELDKSLTKMGDLEGKLFHARRIIDMEIKARRQAEHERDAMESKIMAVADLLRHERNLNNETRDKLAFLHTLPSSRKRKSLNAVREDESYGDINSTGSLLSDLSITHSEDDFLDVRTSKSWREHRPSLPKNQIPSVGNKRSRLSTGLNGSMSGTTPTTGKSRRSSVGIGVEQHTVDVGQGAERFCATTKVTIPQDGQGVIRAESTIESLPVIAGNERIGDGLSSTPRRSVLKEATAPPLTPVNAMAPHVVAESGTPLQHRPLMRNHTFSQKTFLRGDNCVQCQKRIRFGAVGLRCRDCPVRCHIDCRYLLTVSCVPQTGTPTTKTMTGYVTDFAPSIAPMIPALIVHCVNEIEARGLTEVGLYRLSSSEREYKALKEQFLRGKATPHLGNTDIYVLCCCVKDFLRSLTEPLIPTSQWKDFANAVQNPDTKTAQDMLVKSVKQLPQANRDTLAFLILHFQRIAQCPVVLMPIDNISLIFGPTIVGYSTPDPDQHAIYTEVFTQKQVMKALLELPVSFWEQYIVIDPTRTPATVIKRVPSNKNDLLSLYATPFKGGTIKKRKFYGTPPASAHKK
Protein: Cytosolic iron-sulfur assembly component 2A (MIP18 family protein FAM96A) (Q9DCL2)
Organism: Mus musculus (Mouse)
Function: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. As a CIA complex component and in collaboration with CIAO1 specifically matures ACO1 and stabilizes IREB2. May play a role in chromosome segregation through establishment of sister chromatid cohesion. May induce apoptosis in collaboration with APAF1.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable cytosolic iron-sulfur protein assembly protein CIAO1
- MMS19 nucleotide excision repair protein homolog
- Cytosolic iron-sulfur assembly component 3
- Cytosolic iron-sulfur assembly component 2B
Sequence:
MERVSGLLSWTLSRVLWLSGFSEHGAAWQPRIMEEKALEVYDLIRTIRDPEKPNTLEELEVVTESCVEVQEINEDDYLVIIKFTPTVPHCSLATLIGLCLRVKLQRCLPFKHKLEIYISEGTHSTEEDINKQINDKERVAAAMENPNLREIVEQCVLEPD
Protein: Matrix remodeling-associated protein 8 (Adipocyte-specific protein 3) (Dual Ig domain-containing cell adhesion molecule) (DICAM) (Limitrin) (Q9DBV4)
Organism: Mus musculus (Mouse)
Function: Transmembrane protein which can modulate activity of various signaling pathways, probably via binding to integrin ITGAV:ITGB3. Mediates heterophilic cell-cell interactions in vitro. Inhibits osteoclastogenesis downstream of TNFSF11/RANKL and CSF1, where it may function by attenuating signaling via integrin ITGB3 and MAP kinase p38. Plays a role in cartilage formation where it promotes proliferation and maturation of growth plate chondrocytes. Stimulates formation of primary cilia in chondrocytes. Enhances expression of genes involved in the hedgehog signaling pathway in chondrocytes, including the hedgehog signaling molecule IHH; may also promote signaling via the PTHLH/PTHrP pathway. Plays a role in angiogenesis where it suppresses migration of endothelial cells and also promotes their apoptosis (By similarity). Inhibits VEGF-induced activation of AKT and p38 MAP kinase in endothelial cells (By similarity). Also inhibits VTN (vitronectin)-mediated integrin ITGAV:ITGB3 signaling and activation of PTK2/FAK (By similarity). May play a role in the maturation and maintenance of the blood-brain barrier.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14603461, ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:22492581}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000269|PubMed:18366072}. Cytoplasm {ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:29702220}. Cell projection, cilium membrane {ECO:0000269|PubMed:29702220}. Nucleus {ECO:0000269|PubMed:18366072}. Note=Primarily localizes to the cell membrane (PubMed:18366072). Detected in the cilium of primary chondrocytes (PubMed:29702220). Highly expressed at areas of cell-cell contact and may localize to tight junctions (PubMed:18366072). Also found in the nucleus where it is detected in the soluble (as opposed to chromatin-bound) fraction (PubMed:18366072). {ECO:0000269|PubMed:18366072, ECO:0000269|PubMed:29702220}.
Interaction partners:
- Adipocyte enhancer-binding protein 1
Sequence:
MELLSRVLLWKLLLLQSSAVLSSGPSGTAAASSSLVSESVVSLAAGTQAVLRCQSPRMVWTQDRLHDRQRVVHWDLSGGPGSQRRRLVDMYSAGEQRVYEPRDRDRLLLSPSAFHDGNFSLLIRAVDRGDEGVYTCNLHHHYCHLDESLAVRLEVTEDPLLSRAYWDGEKEVLVVAHGAPALMTCINRAHVWTDRHLEEAQQVVHWDRQLPGVSHDRADRLLDLYASGERRAYGPPFLRDRVSVNTNAFARGDFSLRIDELERADEGIYSCHLHHHYCGLHERRVFHLQVTEPAFEPPARASPGNGSGHSSAPSPDPTLTRGHSIINVIVPEDHTHFFQQLGYVLATLLLFILLLITVVLATRYRHSGGCKTSDKKAGKSKGKDVNMVEFAVATRDQAPYRTEDIQLDYKNNILKERAELAHSPLPAKDVDLDKEFRKEYCK
Protein: Opioid growth factor receptor (OGFr) (Protein 7-60) (Zeta-type opioid receptor) (Q9NZT2)
Organism: Homo sapiens (Human)
Function: Receptor for opioid growth factor (OGF), also known as Met-enkephalin. Seems to be involved in growth regulation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The OGF/OGFR complex is probably translocated to the nucleus.
Interaction partners:
- Proenkephalin-A
Sequence:
MDDPDCDSTWEEDEEDAEDAEDEDCEDGEAAGARDADAGDEDEESEEPRAARPSSFQSRMTGSRNWRATRDMCRYRHNYPDLVERDCNGDTPNLSFYRNEIRFLPNGCFIEDILQNWTDNYDLLEDNHSYIQWLFPLREPGVNWHAKPLTLREVEVFKSSQEIQERLVRAYELMLGFYGIRLEDRGTGTVGRAQNYQKRFQNLNWRSHNNLRITRILKSLGELGLEHFQAPLVRFFLEETLVRRELPGVRQSALDYFMFAVRCRHQRRQLVHFAWEHFRPRCKFVWGPQDKLRRFKPSSLPHPLEGSRKVEEEGSPGDPDHEASTQGRTCGPEHSKGGGRVDEGPQPRSVEPQDAGPLERSQGDEAGGHGEDRPEPLSPKESKKRKLELSRREQPPTEPGPQSASEVEKIALNLEGCALSQGSLRTGTQEVGGQDPGEAVQPCRQPLGARVADKVRKRRKVDEGAGDSAAVASGGAQTLALAGSPAPSGHPKAGHSENGVEEDTEGRTGPKEGTPGSPSETPGPSPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPSPAGPTRDEPAESPSETPGPRPAGPAGDEPAESPSETPGPRPAGPAGDEPAESPSETPGPSPAGPTRDEPAKAGEAAELQDAEVESSAKSGKP
Protein: Peripheral plasma membrane protein CASK (EC 2.7.11.1) (Calcium/calmodulin-dependent serine protein kinase) (Q62915)
Organism: Rattus norvegicus (Rat)
Function: Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (By similarity). Multidomain scaffolding protein with a role in synaptic transmembrane protein anchoring and ion channel trafficking.ontributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10749215}. Cytoplasm {ECO:0000269|PubMed:12641734, ECO:0000269|PubMed:15994232}. Cell membrane {ECO:0000269|PubMed:14627983}; Peripheral membrane protein {ECO:0000269|PubMed:14627983}.
Interaction partners:
- Amyloid-beta A4 precursor protein-binding family A member 1
- Whirlin
- Disks large homolog 1
- Protein lin-7 homolog A
- Protein lin-7 homolog B
- Neurexin-2
- Nephrin
- Syndecan-2
- Neurexin-3
- Neurexin-1
Sequence:
MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHHVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNADLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPERFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFPPFVVFIAAPTITPGLNEDESLQRLQKESDVLQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY
Protein: Transcription repressor (Ovate family protein) (B3H6R4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367028}.
Interaction partners:
- At3g63430
- GPI-anchored adhesin-like protein, putative
- mRNA cap guanine-N
- Transcription repressor OFP14
- BEL1-like homeodomain protein 6
- Homeobox protein knotted-1-like 7
- Probable serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit TON2
Sequence:
MTTGKSKKKKMVLKAVSVVDIGCGNCKFPSLSSFFNPSPKKPRLYSSNYGHCHSSTPTTASSSSAVPSTSHWFSDTSSSSATPSAAAVAVEKDSDDPYLDFRQSMLQMILENEIYSKNDLRELLHCFLSLNEPYHHGIIIRAFSEIWDGVFSAAKRRGDVQESPLVHRHGSRASHRNHYHRSK
Protein: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase) (AtPNG1) (Q9FGY9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ubiquitin receptor RAD23c
- Ubiquitin receptor RAD23b
- Ubiquitin receptor RAD23d
- Probable ubiquitin receptor RAD23a
- Ubiquitin receptor RAD23
- Cell division control protein 48 homolog E
- Cell division control protein 48 homolog D
- Cell division control protein 48 homolog B
- Cell division control protein 48 homolog C
- Probable ubiquitin conjugation factor E4
Sequence:
MVARKFVVRHEDSSFDVDYNTEDGLEVLRFLIFSLTLVPPEEQKIVAEDDNRLVSDESDLASLSERLRLVSVGEDSVENSDAEMLKSDEELARMLQAEEDAIMFQQFVAARDNGEFEGRIRPYVSQVLMYEDPVRQDAARKTVPKDELEEKALVSLAKEGNFEPSKEERDYAFLLQLLFWFKKSFRWVNEPPCDFCGNKTIGQGMGNPLTSELAYGANRVEIYRCTMCPTTTRFPRYNDPLKLVETKKGRCGEWANCFTLYCRTFGYDSRLIMDFTDHVWTECYSHSLKRWIHLDPCEGVYDKPMLYEKGWNKKLNYVIAISKDGVCDVTKRYTKKWHEVLSRRTLTTESSLQDGLRTLTRERRRSLMFESLSKLELRDRNEQEELERNLHSADNASVSLPGRQSGDREWRIMRSEFGSDENSSVSSSSCPVRKCVDDHVTNIYDSFLPILTQFVEDGLPVARTNEVLKMIKQVLVDLKNAPYKTRKARLTLDSDNSSSFPEQFLPALGDLLLALSLKSERDTNGKSVTISVDGKLTKTAIALPVALDALRELVADLSKYQNLNKDSLSFPLVKQNRVCSGSVLASGEELPSGIATAAFDGIQESKWEEPNGAKGCWIVYKTLYNQMHQLIAYELMSANDAPERDPKDWILEGSNDGGSTWCVLDKQTSQVFEERFQRKSYKITTPGFQANLFRFRFLSVRDVNSTSRLQLGSIDLYRSHQ