wanglab/gogpt-training-data huggingface dataset:
Protein: Cytosol aminopeptidase (EC 3.4.11.1) (Cysteinylglycine-S-conjugate dipeptidase) (EC 3.4.13.23) (Leucine aminopeptidase 3) (LAP-3) (Leucyl aminopeptidase) (Peptidase S) (Proline aminopeptidase) (EC 3.4.11.5) (Prolyl aminopeptidase) (P28838)
Organism: Homo sapiens (Human)
Function: Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}.
Interaction partners:
- Aminopeptidase N
- Xaa-Pro aminopeptidase 1
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 6
- Glutathione hydrolase 7
- Glutathione hydrolase 1 proenzyme
- Proline dehydrogenase
- Glutathione synthetase
- Glutathione-specific gamma-glutamylcyclotransferase 2
- Glutathione-specific gamma-glutamylcyclotransferase 1
Sequence:
MFLLPLPAAGRVVVRRLAVRRFGSRSLSTADMTKGLVLGIYSKEKEDDVPQFTSAGENFDKLLAGKLRETLNISGPPLKAGKTRTFYGLHQDFPSVVLVGLGKKAAGIDEQENWHEGKENIRAAVAAGCRQIQDLELSSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKMAVSAKLYGSGDQEAWQKGVLFASGQNLARQLMETPANEMTPTRFAEIIEKNLKSASSKTEVHIRPKSWIEEQAMGSFLSVAKGSDEPPVFLEIHYKGSPNANEPPLVFVGKGITFDSGGISIKASANMDLMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRAKNGKTIQVDNTDAEGRLILADALCYAHTFNPKVILNAATLTGAMDVALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLFEHYTRQVVDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGVMTNKDEVPYLRKGMTGRPTRTLIEFLLRFSQDNA
Protein: Serine/threonine-protein kinase PLK2 (EC 2.7.11.21) (Polo-like kinase 2) (PLK-2) (Serine/threonine-protein kinase SNK) (Serum-inducible kinase) (P53351)
Organism: Mus musculus (Mouse)
Function: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase. {ECO:0000250}.
Interaction partners:
- Centrosomal P4.1-associated protein
- Separin
- Nucleophosmin
Sequence:
MELLRTITYQPAAGTKMCEQALGKACGGDSKKKRPQQPSEDGQPQAQVTPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRLLHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYNDTHNKVSKEDEDIYKLRHDLKKVSITQQPSKHRADEEPQPPPTTVARSGTSAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICNQSEEYLLTYINEDRISTTFRLTTLLMSGCSLELKNRMEYALNMLLQRCN
Protein: Rolling pebbles, isoform F (M9PFC6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
Sequence:
MFPLTNRSSSGNRTNNNPSNNNNNQTTSFIIGGTTNINNNNNQLGGTNSAKDKGNFENNWSCNKTTGRRSGSGNSCSFLDLQSIRRLLEHDASGSVCPSCRISFDKGKRRKLIDTCGHERCYSCMFRNDQCPMCMNSSLKDVDGANAQGYDTGIGGSTSTIVSPLGSPQPQLRSHAQRNAALARYMQHRQESQSPDYHHRYASNGKLPRAAALSTNGNGFTTGTTQTVTVDVHHQLGGGGGGAAAAAKQLMANGISGHSRSSSMSHNIHAAAYSELSAAPPAFATPPTRRRFFNHKNLRSALTGGSGGGSGVGGGVGGAGGVGGGHRRTASNGGCPIDTASILSGDHTHQHHHRDNQPEGKESNALNTSTCSDSAVTRRRRKNVSNHNLKTSARHGASSENRLNRLSLAGTSVYAGHLSSLVFGKIKSLWSVNSSNSSEAGLNQLAGSDAIDHHSSFLNEKLQKDQLHARLGLLLNDPGSNGNSSSSGSGCEPISAHSTTSTTSSSGVGAASTTTSGSSQNVSPEQTLASGAGMLSGSQLSVATSHGVKEDALSLCGKFKAGCSMLHVYEALPSKSRKGNVRRSTRGQQGSSSSASAASAVGSRVTASSLAAVQLALKPLFFEVPLQEPDPPYVGRQWLVQQLSNILLGTETRVVLINGQPGTGKTAFCLQLVEYSCFGRRQMQDDPDGIYSQLQLGAHCERMRGLASHMVGYHFCQADANLTCQVPDFVHSLAAQLCQAPQLTAYRDYLLSEPHLQDILSVRECIADAERVMKLAILEPLAHLHRAGKIPAKVAVIVVDALCEAEYHRPDHGHTIASFLAQLTPHFPAWLKLVATVRTQMLELVKAPSYTQLTLDSWASSQALQQDMLDYIGARLADSPEIRMNIGGGGGQNSQSGSQPQTKFVSHLQSLSRGSMLYAKLILDLIARGQLVIKSSSYKVLPVSLAQIFLLHFNLRFPTARSFEQAAPILNICLAALYPLTLDEIYYSMEALSHGREALSWPDFMQRFKLLDGFLIKRLDNTYMFFHSSLREWLMRRDEGESNKFLCDARLGHAGIAFRLSRLQAPLSPQLTLELGHHMLKAHLYGGTSLTLLSPRDLQSYWLAGAADNISSSLGALRNVYSPNLKVSRLVLLAGASPNHRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACDWSPRPHSQDVTRSVALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKLGPTTWSMAMGKPEILVILLNKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNLLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQSGVLCEVVEVLKRIQTELLTRISISSEDQTGRMSNIGGGASVAYESHHEITDL
Protein: Developmental pluripotency-associated protein 2 (Embryonic stem cell-associated transcript 15-2 protein) (ECAT15-2) (Pluripotent embryonic stem cell-related gene 1 protein) (Q9CWH0)
Organism: Mus musculus (Mouse)
Function: Binds to target gene promoters, including NKX2-5 and SYCE1, but not GATA4, and may be involved in the maintenance of the active epigenetic status of these genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:21896782}.
Interaction partners:
- Developmental pluripotency-associated protein 5A
- Developmental pluripotency-associated protein 4
- Zinc finger protein 42
- Homeobox protein NANOG
- Growth/differentiation factor 3
- Undifferentiated embryonic cell transcription factor 1
Sequence:
MSYFGLETFNENQSEENLDEESVILTLVPFKEEEEPNTDYATQSNVSSSTLDHTPPARSLVRHAGIKHPTRTIPSTCPPPSLPPIRDVSRNTLREWCRYHNLSTDGKKVEVYLRLRRHSYSKQECYIPNTSREARMKQGPKKSKIVFRGIGPPSGCQRKKEESGVLEILTSPKESTFAAWARIAMRAAQSMSKNRCPLPSNVEAFLPQATGSRWCVVHGRQLPADKKGWVRLQFLAGQTWVPDTPQRMNFLFLLPACIIPEPGVEDNLLCPECVHSNKKILRNFKIRSRAKKNALPPNMPP
Protein: PDZ domain-containing protein GIPC1 (GAIP C-terminus-interacting protein) (RGS-GAIP-interacting protein) (RGS19-interacting protein 1) (Synectin) (Tax interaction protein 2) (TIP-2) (O14908)
Organism: Homo sapiens (Human)
Function: May be involved in G protein-linked signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32413282, ECO:0000269|PubMed:9770488}. Membrane {ECO:0000269|PubMed:9770488}; Peripheral membrane protein.
Interaction partners:
- Unconventional myosin-VI
- Regulator of G-protein signaling 19
- Neuropilin-1
- DCC-interacting protein 13-alpha
- Syndecan-4
- Low-density lipoprotein receptor-related protein 2
- Tax1-binding protein 3
- Endoglin
- Rho guanine nucleotide exchange factor 12
- Plexin-D1
Sequence:
MPLGLGRRKKAPPLVENEEAEPGRGGLGVGEPGPLGGGGSGGPQMGLPPPPPALRPRLVFHTQLAHGSPTGRIEGFTNVKELYGKIAEAFRLPTAEVMFCTLNTHKVDMDKLLGGQIGLEDFIFAHVKGQRKEVEVFKSEDALGLTITDNGAGYAFIKRIKEGSVIDHIHLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGRTFTLKLTEPRKAFDMISQRSAGGRPGSGPQLGTGRGTLRLRSRGPATVEDLPSAFEEKAIEKVDDLLESYMGIRDTELAATMVELGKDKRNPDELAEALDERLGDFAFPDEFVFDVWGAIGDAKVGRY
Protein: Secreted protein (O05592)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0039c
- Uncharacterized protein Rv0010c
- Nucleoside triphosphate pyrophosphohydrolase
- Probable para-aminobenzoate synthase component I PABD
- Probable conserved proline, glycine, valine-rich secreted protein
- Uncharacterized protein
- Uncharacterized protein Rv2047c
- DUF4333 domain-containing protein
- Conserved protein
- Uncharacterized protein Rv2598
Sequence:
MVLRSRKSTLGVVVCLALVLGGPLNGCSSSASHRGPLNAMGSPAIPSTAQEIPNPLRGQYEDLMEPLFPQGNPAQQRYPPWPASYDASLRVSWRQLQPTDPRTLPPDAPDDRKYDFSVIDNALTRLADRGMRLTLRVYAYSSCCKASYPDGTNIAIPDWERAIASTNTSYPGPATDPSTGVVQVVPNFNDSTYLNDFAQLLAALGRRYDGDERLSVFEFSGYGDFSENHVAYLRDTLGAPGPGPDESVATLGYYSQFRDQNITTASIKQLIAANVSAFPHTQLVTSPANPEIVRELFADEVTNKLAAPVGVRSDCLGVDAPLPAWAESSTSHYVQTKDPVVAALRQRLATAPVITEWCELPTGSSPRAYYEKGLRDVIRYHVSMTSSVNFPDQTATSPMDPALYLVWAQANAAAGYRYSVEAQPGSQALAGKVATISVTWTNYGAAAATEKWVPGYRLVDSTGQVVRTLPAAVDLKTLVSDQRGDRSSDQPTPASVAETVRVDLSGLPAGHYTLRAAIDWQQHKPNGSHVVNYPPMLLSRDGRDDSGFYPVATLDIPRDAQTAVNAS
Protein: Mucin-1 (B2GV31)
Organism: Rattus norvegicus (Rat)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004247}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004247}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Catenin beta-1
- Receptor protein-tyrosine kinase
- Galectin-3
- Mucin 6, oligomeric mucus/gel-forming.
- Mucin-13
- Mucin 20, cell surface associated
- Intercellular adhesion molecule 1
- Mucin 15, cell surface associated
- Mucin-2
- Epithelial cell adhesion molecule
Sequence:
MTPGIRVPLLLLLLLASLKVRSGASSSTTSLPGDSFSTAVPSGASSSATSPPVDSTTSPVHSSTSFPATSPPGDSTSTAVLSGDSDPATSPPGDSSSTAVPNGASSSATSPPVDSTTSPVHSSTSFPATSSPGDSTSTAVTSGTSSSATSPPEDSSSTAVTSGTSSPATSPPGDSSSTAVTSGTSSPATSPILDSSSTAVLSGTSSPATSPPEDSTSTAVTSGTSSPATSPPEDSTSTAVTSGTSSPATSPILDSSSTAIHSGTSSPATSPPGDSSSTAVLSGASTQTTKAVSDLASTPTHNGIMVPTTWSALSSATSPVYSGSSATTNSSESDMATTPVYSGTPFSSTTATSAITPDHNGSLVRTTSSVLGLATSPAHDTSAVATTPVRNDTQSSVPSQQPISPTIPAISSHSTVSSSSYYSTAVFPTFSSNSSPQLSVGVSFFSLSFYIRNHPFNSSLEDPSSRYYQELKRNISGLFLQVFNGDFLGVSTIKFRSGSVVVASTVIFREGTFSASEVKSQLVQHKKEAADYNLTISEVNVNEMQFPSSAQSWPGVPGWGIALLVLVCILVALVIVYLIALALCQCRRKSYGQLDLFPTRDTYHPMSEYPTYHTHGRYVPPATTKRSPYEEVSTGNGSSGLSYTNPAVATTSANL
Protein: G protein-activated inward rectifier potassium channel 3 (GIRK-3) (Inward rectifier K(+) channel Kir3.3) (Potassium channel, inwardly rectifying subfamily J member 9) (Q63511)
Organism: Rattus norvegicus (Rat)
Function: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G protein-activated inward rectifier potassium channel 2
- G protein-activated inward rectifier potassium channel 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Guanine nucleotide-binding protein G
- Gamma-aminobutyric acid type B receptor subunit 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MAQENAAFSPGSEEPPRRRGRQRYVEKDGRCNVQQGNVRETYRYLTDLFTTLVDLQWRLSLLFFVLAYALTWLFFGAIWWLIAYGRGDLEHLEDTAWTPCVNNLNGFVAAFLFSIETETTIGYGHRVITDQCPEGIVLLLLQAILGSMVNAFMVGCMFVKISQPNKRAATLVFSSHAVVSLRDGRLCLMFRVGDLRSSHIVEASIRAKLIRSRQTLEGEFIPLHQTDLSVGFDTGDDRLFLVSPLVISHEIDAASPFWEASRRALERDDFEIVVILEGMVEATGMTCQARSSYLVDEVLWGHRFTSVLTLEDGFYEVDYASFHETFEVPTPSCSARELAEAAARLDAHLYWSIPSRLDEKVEEEGAGEGAGAGDGADKEQNGCLPPPESESKV
Protein: DnaA regulatory inactivator Hda (DnaA paralog) (Dp) (Protein IdaB) (P69931)
Organism: Escherichia coli (strain K12)
Function: Mediates the interactions of DNA replication initiator protein DnaA with DNA polymerase subunit beta sliding clamp (dnaN). Stimulates hydrolysis of ATP-DnaA to ADP-DnaA, rendering DnaA inactive for reinitiation, a process called regulatory inhibition of DnaA or RIDA. ADP-binding activates Hda to hydrolyze DnaA-ATP; Hda monomers bind to ADP with about 200-fold greater affinity than for ATP. RIDA function can be genetically separated from viability, suggesting this protein has another function as well.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12618445}. Note=More protein is found in the inner than outer membrane fractions. {ECO:0000269|PubMed:12618445}.
Interaction partners:
- Beta sliding clamp
- Chromosomal replication initiator protein DnaA
- Negative modulator of initiation of replication
- Replicative helicase loader DnaC
- Replicative DNA helicase DnaB
- DnaA initiator-associating protein DiaA
- DNA polymerase I
- DNA polymerase III subunit tau
Sequence:
MNTPAQLSLPLYLPDDETFASFWPGDNSSLLAALQNVLRQEHSGYIYLWAREGAGRSHLLHAACAELSQRGDAVGYVPLDKRTWFVPEVLDGMEHLSLVCIDNIECIAGDELWEMAIFDLYNRILESGKTRLLITGDRPPRQLNLGLPDLASRLDWGQIYKLQPLSDEDKLQALQLRARLRGFELPEDVGRFLLKRLDREMRTLFMTLDQLDRASITAQRKLTIPFVKEILKL
Protein: Cyclin-dependent kinase 19 (D3ZDM6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cyclin-C
- Mediator complex subunit 12
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 31
- Mediator complex subunit 12L
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MDYDFKAKLAAERERVEDLFEYEGCKVGRGTYGHVYKARRKDGKDEKEYALKQIEGTGISMSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDEPEEKGDKNQPQQQNPHQQPVAPQQQAAAPTQAPPPQQSSAQTNGTAGGATTGGGAAGAGLQHSQDSGLNQVPPNKKPRIGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQGTLGYSSSQQSTQYHPSHQAHRY
Protein: G-protein coupled receptor aex-2 (Aboc, expulsion defective protein 2) (G5ECD9)
Organism: Caenorhabditis elegans
Function: G-protein coupled receptor for the nlp-40 neuropeptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Plays a role in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds. Specifically, acts in GABAergic neurons, such as AVL and DVB, to control the expulsion step of defecation. Required for fatty acid uptake and metabolism by intestinal cells and therefore regulates the levels of triglycerides in the intestine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23583549}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:18852466}.
Interaction partners:
- Neuropeptide-like peptides nlp-40
- C2 domain-containing protein aex-1
- t-SNARE protein aex-4
- Endoprotease aex-5
- Calponin-like protein clik-2
Sequence:
MNSTDIIANVTKPFVENLTLGETAFYISCGIVGTVFNALVLWIALTYINTEDKPRQIIVINMTVADLLMCIVYMKTRPWLSHFNLWLCHPYYVIIWTCQMCSCLNLVWLNVDKLIYIQFPLHYYQIVNRKRLLWITAATWGGLYAMNIALVTFLKITRGSCLGVSLNPYVYLLSPIFYVVMILTSFSLSALIYCIAHNLTHMEERQRSKLFRRLFFLFSSTLWTFFTCLPYRLLYLFSIFCGETCQINNYYKTATNLFFRLLIVGIMINPVITIWTQRIYRLRLMRMFGRLRENSSTEVLMVSNRRASERPPEHTPLRCDM
Protein: Whirlin (Autosomal recessive deafness type 31 protein) (Q9P202)
Organism: Homo sapiens (Human)
Function: Involved in hearing and vision as member of the USH2 complex. Necessary for elongation and maintenance of inner and outer hair cell stereocilia in the organ of Corti in the inner ear. Involved in the maintenance of the hair bundle ankle region, which connects stereocilia in cochlear hair cells of the inner ear. In retina photoreceptors, required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q80VW5}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q80VW5}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q80VW5}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q80VW5}. Synapse {ECO:0000250|UniProtKB:Q810W9}. Note=Detected at the level of stereocilia in inner and outer hair cells of the cochlea and vestibule. Localizes to both tip and ankle-link stereocilia regions. Colocalizes with the growing ends of actin filaments. Colocalizes with MPP1 in the retina, at the outer limiting membrane (OLM), outer plexifirm layer (OPL), basal bodies and at the connecting cilium (CC). In photoreceptors, localizes at a plasma membrane microdomain in the apical inner segment that surrounds the connecting cilia called periciliary membrane complex. {ECO:0000250|UniProtKB:Q80VW5, ECO:0000250|UniProtKB:Q810W9, ECO:0000269|PubMed:17584769}.
Interaction partners:
- Adhesion G-protein coupled receptor V1
- Unconventional myosin-XV
- Usherin
- pre-mRNA splicing regulator USH1G
- Epidermal growth factor receptor kinase substrate 8
- Unconventional myosin-VIIa
- Peripheral plasma membrane protein CASK
- 55 kDa erythrocyte membrane protein
- Taperin
- Espin
Sequence:
MNAPLDGLSVSSSSTGSLGSAAGAGGGGGAGLRLLSANVRQLHQALTALLSEAEREQFTHCLNAYHARRNVFDLVRTLRVLLDSPVKRRLLPMLRLVIPRSDQLLFDQYTAEGLYLPATTPYRQPAWGGPDSAGPGEVRLVSLRRAKAHEGLGFSIRGGSEHGVGIYVSLVEPGSLAEKEGLRVGDQILRVNDKSLARVTHAEAVKALKGSKKLVLSVYSAGRIPGGYVTNHIYTWVDPQGRSISPPSGLPQPHGGALRQQEGDRRSTLHLLQGGDEKKVNLVLGDGRSLGLTIRGGAEYGLGIYITGVDPGSEAEGSGLKVGDQILEVNGRSFLNILHDEAVRLLKSSRHLILTVKDVGRLPHARTTVDETKWIASSRIRETMANSAGFLGDLTTEGINKPGFYKGPAGSQVTLSSLGNQTRVLLEEQARHLLNEQEHATMAYYLDEYRGGSVSVEALVMALFKLLNTHAKFSLLSEVRGTISPQDLERFDHLVLRREIESMKARQPPGPGAGDTYSMVSYSDTGSSTGSHGTSTTVSSARNTLDLEETGEAVQGNINALPDVSVDDVRSTSQGLSSFKPLPRPPPLAQGNDLPLGQPRKLGREDLQPPSSMPSCSGTVFSAPQNRSPPAGTAPTPGTSSAQDLPSSPIYASVSPANPSSKRPLDAHLALVNQHPIGPFPRVQSPPHLKSPSAEATVAGGCLLPPSPSGHPDQTGTNQHFVMVEVHRPDSEPDVNEVRALPQTRTASTLSQLSDSGQTLSEDSGVDAGEAEASAPGRGRQSVSTKSRSSKELPRNERPTDGANKPPGLLEPTSTLVRVKKSAATLGIAIEGGANTRQPLPRIVTIQRGGSAHNCGQLKVGHVILEVNGLTLRGKEHREAARIIAEAFKTKDRDYIDFLVTEFNVML
Protein: Putative methyltransferase SPBC8D2.16c (EC 2.1.1.-) (O13641)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit cbf5
- U3 small nucleolar ribonucleoprotein protein imp4
- H/ACA ribonucleoprotein complex subunit gar1
Sequence:
MEKESEIQSLPPTRRYTISLALPISSLNVAYNLQLKTSFVWKISRIVSLYGIDEIILLEDPEYVQNTQVHTLSSDAYLKDPTKFLTDLLCYFETPFFMRKELFPLNPHLKYTSCFPLLPLRNDKASTVNIEFPYREGIVTHPSPQAKNKYIINAGLSHNVIVSSPSVLAPRTRVTVRLKAQSPNEEGQLQGDIVSFSAPREKGGHYWGYKVRSCLSSQLCKSSPYKGGYDFVVQINSQTSAITSKELEASLPSSFRHAVLVLQDNVVQKELVDSTAKSISFNPFPVSFLNDPIPEEILLAAMTRLSDMLLMHGRR
Protein: Succinate-CoA ligase ADP-forming subunit beta (Q5T9Q8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASMFYGRLVAVATLRNHRPRTAQRAAAQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDK
Protein: Solute carrier family 2, facilitated glucose transporter member 5 (Fructose transporter) (Glucose transporter type 5, small intestine) (GLUT-5) (P43427)
Organism: Rattus norvegicus (Rat)
Function: Functions as a fructose transporter that has only low activity with other monosaccharides. Can mediate the uptake of deoxyglucose, but with low efficiency. Essential for fructose uptake in the small intestine (By similarity). Plays a role in the regulation of salt uptake and blood pressure in response to dietary fructose (By similarity). Required for the development of high blood pressure in response to high dietary fructose intake (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9WV38}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9WV38}. Cell membrane {ECO:0000269|PubMed:26416735, ECO:0000269|PubMed:8333543, ECO:0000269|PubMed:9820812}; Multi-pass membrane protein {ECO:0000269|PubMed:26416735}. Cell membrane, sarcolemma {ECO:0000269|PubMed:9820812}. Note=Localized on the apical membrane of jejunum villi, but also on lateral plasma membranes of the villi. Transport to the cell membrane is dependent on RAB11A. {ECO:0000250|UniProtKB:Q9WV38}.
Interaction partners:
- Ig-like domain-containing protein.
- Ig-like domain-containing protein.
- Ig-like domain-containing protein.
- Sodium/glucose cotransporter 1
- Ketohexokinase
- Sodium/myo-inositol cotransporter 2
- Solute carrier family 15 member 1
Sequence:
MEKEDQEKTGKLTLVLALATFLAAFGSSFQYGYNVAAVNSPSEFMQQFYNDTYYDRNKENIESFTLTLLWSLTVSMFPFGGFIGSLMVGFLVNNLGRKGALLFNNIFSILPAILMGCSKIAKSFEIIIASRLLVGICAGISSNVVPMYLGELAPKNLRGALGVVPQLFITVGILVAQLFGLRSVLASEEGWPILLGLTGVPAGLQLLLLPFFPESPRYLLIQKKNESAAEKALQTLRGWKDVDMEMEEIRKEDEAEKAAGFISVWKLFRMQSLRWQLISTIVLMAGQQLSGVNAIYYYADQIYLSAGVKSNDVQYVTAGTGAVNVFMTMVTVFVVELWGRRNLLLIGFSTCLTACIVLTVALALQNTISWMPYVSIVCVIVYVIGHAVGPSPIPALFITEIFLQSSRPSAYMIGGSVHWLSNFIVGLIFPFIQVGLGPYSFIIFAIICLLTTIYIFMVVPETKGRTFVEINQIFAKKNKVSDVYPEKEEKELNDLPPATREQ
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FT06)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- t-SNARE affecting a late Golgi compartment protein 1
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
Sequence:
MSSSVPYDPYVTPEQDETNEQSQSKAAALKAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAISAQGFKRGANRVRKQMWYKDLKMKFCLFVVIICLLVAIVVPIAVHFS
Protein: Homeobox protein MSX-1 (Homeobox protein Hox-7) (CHOX-7) (Msh homeobox 1-like protein) (P28361)
Organism: Gallus gallus (Chicken)
Function: Probable morphogenetic role.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P13297}.
Interaction partners:
Sequence:
MGGEEESDKPKVSPSPLPFRRWKGSWPTAERGRQRRSRGFRAPSRRPSQPRRSDDGGTDVAAPSRRPLPVRRGAGQAARGRAAQSREPREAGATPWMQSPRFSPPPPRAEPPACTLRKHKTNRKPRTPFTTAQLLALERKFRQKQYLSIAERAEFSSSLSLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPPAAFGISFPLGGPAVAGASLYGASSPFQRAGLPVAPVGLYTAHVGYSMYHLT
Protein: Ferredoxin-1, chloroplastic (Ferredoxin I) (P09911)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MATTPALYGTAVSTSFLRTQPMPMSVTTTKAFSNGFLGLKTSLKRGDLAVAMASYKVKLVTPDGTQEFECPSDVYILDHAEEVGIDLPYSCRAGSCSSCAGKVVGGEVDQSDGSFLDDEQIEAGFVLTCVAYPTSDVVIETHKEEDLTA