wanglab/gogpt-training-data huggingface dataset:
Protein: Protein adenylyltransferase SelO, mitochondrial (EC 2.7.7.-) (EC 2.7.7.108) (Selenoprotein O) (SelO) (Q9BVL4)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr and Tyr residues of target proteins (AMPylation). May be a redox-active mitochondrial selenoprotein which interacts with a redox target protein.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24751718}.
Interaction partners:
- Selenoprotein K
- Selenoprotein N
- Thioredoxin reductase-like selenoprotein T
- Selenoprotein S
- Selenoprotein W
- Methionine-R-sulfoxide reductase B1
- Selenide, water dikinase 2
- Selenoprotein M
- Selenoprotein F
- Ethanolaminephosphotransferase 1
Sequence:
MAVYRAALGASLAAARLLPLGRCSPSPAPRSTLSGAAMEPAPRWLAGLRFDNRALRALPVEAPPPGPEGAPSAPRPVPGACFTRVQPTPLRQPRLVALSEPALALLGLGAPPAREAEAEAALFFSGNALLPGAEPAAHCYCGHQFGQFAGQLGDGAAMYLGEVCTATGERWELQLKGAGPTPFSRQADGRKVLRSSIREFLCSEAMFHLGVPTTRAGACVTSESTVVRDVFYDGNPKYEQCTVVLRVASTFIRFGSFEIFKSADEHTGRAGPSVGRNDIRVQLLDYVISSFYPEIQAAHASDSVQRNAAFFREVTRRTARMVAEWQCVGFCHGVLNTDNMSILGLTIDYGPFGFLDRYDPDHVCNASDNTGRYAYSKQPEVCRWNLRKLAEALQPELPLELGEAILAEEFDAEFQRHYLQKMRRKLGLVQVELEEDGALVSKLLETMHLTGADFTNTFYLLSSFPVELESPGLAEFLARLMEQCASLEELRLAFRPQMDPRQLSMMLMLAQSNPQLFALMGTRAGIARELERVEQQSRLEQLSAAELQSRNQGHWADWLQAYRARLDKDLEGAGDAAAWQAEHVRVMHANNPKYVLRNYIAQNAIEAAERGDFSEVRRVLKLLETPYHCEAGAATDAEATEADGADGRQRSYSSKPPLWAAELCVTUSS
Protein: BTB/POZ domain-containing protein KCTD4 (Q8WVF5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MERKINRREKEKEYEGKHNSLEDTDQGKNCKSTLMTLNVGGYLYITQKQTLTKYPDTFLEGIVNGKILCPFDADGHYFIDRDGLLFRHVLNFLRNGELLLPEGFRENQLLAQEAEFFQLKGLAEEVKSRWEKEQLTPRETTFLEITDNHDRSQGLRIFCNAPDFISKIKSRIVLVSKSRLDGFPEEFSISSNIIQFKYFIKSENGTRLVLKEDNTFVCTLETLKFEAIMMALKCGFRLLTSLDCSKGSIVHSDALHFIK
Protein: Protein AFG1 (P32317)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- ATPase family gene 2 protein
- Histone deacetylase HOS3
- Palmitoyltransferase AKR1
Sequence:
MIALKPNAVRTFRQVQHCSFRICRYQSTKSNKCLTPLQEYDRLVKLGKLRDDTYQRGIISSLGDLYDSLVKYVPPVVKTPNAVDQVGGWLNGLKSVFSRGKPKNIGAYVDVSKIGNSIPRGVYLYGDVGCGKTMLMDLFYTTIPNHLTKKRIHFHQFMQYVHKRSHEIVREQNLKELGDAKGKEIDTVPFLAAEIANNSHVLCFDEFQVTDVADAMILRRLMTALLSDDYGVVLFATSNRHPDELYINGVQRQSFIPCIELIKHRTKVIFLNSPTDYRKIPRPVSSVYYFPSDTSIKYASKECKTRRETHIKEWYNYFAQASHTDDSTDSHTVHKTFYDYPLTIWGREFKVPKCTPPRVAQFTFKQLCGEPLAAGDYLTLAKNFEAFIVTDIPYLSIYVRDEVRRFITFLDAVYDSGGKLATTGAADFSSLFVEPEQILNDFELRPTTKEPDSVDTGMVDEMVEKHGFSKEIAKKSQMFALDEERFAFARALSRLSQMSSTDWVTKPTY
Protein: Elongation factor 3A (EF-3) (EF-3A) (EC 3.6.4.-) (Eukaryotic elongation factor 3) (eEF3) (Translation elongation factor 3A) (Yeast elongation factor 3) (P16521)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ribosome-dependent ATPase that functions in cytoplasmic translation elongation. Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis. Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied. Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved or repleted cells.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS8A
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL23
Sequence:
MSDSQQSIKVLEELFQKLSVATADNRHEIASEVASFLNGNIIEHDVPEHFFGELAKGIKDKKTAANAMQAVAHIANQSNLSPSVEPYIVQLVPAICTNAGNKDKEIQSVASETLISIVNAVNPVAIKALLPHLTNAIVETNKWQEKIAILAAISAMVDAAKDQVALRMPELIPVLSETMWDTKKEVKAAATAAMTKATETVDNKDIERFIPSLIQCIADPTEVPETVHLLGATTFVAEVTPATLSIMVPLLSRGLNERETGIKRKSAVIIDNMCKLVEDPQVIAPFLGKLLPGLKSNFATIADPEAREVTLRALKTLRRVGNVGEDDAIPEVSHAGDVSTTLQVVNELLKDETVAPRFKIVVEYIAAIGADLIDERIIDQQAWFTHITPYMTIFLHEKKAKDILDEFRKRAVDNIPVGPNFDDEEDEGEDLCNCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVDGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVKKCPAAKAYEELSNTDLEFKFPEPGYLEGVKTKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIESHLDKTPSEYIQWRFQTGEDRETMDRANRQINENDAEAMNKIFKIEGTPRRIAGIHSRRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWIPRGELVESHSKMVAEVDMKEALASGQFRPLTRKEIEEHCSMLGLDPEIVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSGHNWVSGQGAGPRIEKKEDEEDKFDAMGNKIAGGKKKKKLSSAELRKKKKERMKKKKELGDAYVSSDEEF
Protein: Tetratricopeptide repeat protein 8 (Zgc:136718) (Q1RLX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEVTVSMDPLFLAWSSCRRRRFQRCADICSTLLAESPYDQAVWSLKTRALTEMVYIDEVEVEQEGIADMMLDESSIAQVARPGTSLRRPATSQAGAPTPAVRPMTQSGRPITGFVRPSTLSGRPETMEQAIRTPRTASTARPVSSASGRFVRLGTASMLTHPDGPFINLSRLNLAKYAKRPNLCKTLFEYIFHHENDVKTALDLAALATEHAQFKDWWWKVQLGKCYYRLGLLREAEKQFRSALAQQEFVDTHLYLAKVYQRLDQPITALTVFKQGLDHFPAEVTLLTGIARIHEEMNNMSSATEYYREVLKQDNTHVEAIACIGSTHFYTDQPEIALRFYRRLLQMGVFNCQLYNNLGLCCFYAQQYDMSLSCLERALALVSGDEEQADVWYNLGHVAVGIGDLTLAYQCFKLSLAFNNNHGEAYNNLAVLELRKGHIEQAKAFLQTAASLSPHMYEPHYNYATLSDKVGDLQSSFTAAQKSEDAFPEHVDTQQILRSLRQHFSSL
Protein: E3 ubiquitin-protein ligase RNF19B (EC 2.3.2.31) (IBR domain-containing protein 3) (Natural killer lytic-associated molecule) (RING finger protein 19B) (Q6ZMZ0)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death.
Subcellular location: Cytoplasmic granule membrane {ECO:0000269|PubMed:10438909}; Multi-pass membrane protein {ECO:0000269|PubMed:10438909}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:27485036}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uridine-cytidine kinase-like 1
- Ubiquitin/ISG15-conjugating enzyme E2 L6
Sequence:
MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTLHSVFSASARGRRARAKPQAEPPPPAAQPPPAPAPAAAQGPPPEALPAEPAAEAEAEAAAAAAEPGFDDEEAAEGGGPGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLIGAPVGISLIAGIAIPAMVIGIPVYVGRKIHSRYEGRKTSKHKRNLAITGGVTLSVIASPVIAAVSVGIGVPIMLAYVYGVVPISLCRGGGCGVSTANGKGVKIEFDEDDGPITVADAWRALKNPSIGESSIEGLTSVLSTSGSPTDGLSVMQGPYSETASFAALSGGTLSGGILSSGKGKYSRLEVQADVQKEIFPKDTASLGAISDNASTRAMAGSIISSYNPQDRECNNMEIQVDIEAKPSHYQLVSGSSTEDSLHVHAQMAENEEEGSGGGGSEEDPPCRHQSCEQKDCLASKPWDISLAQPESIRSDLESSDAQSDDVPDITSDECGSPRSHTAACPSTPRAQGAPSPSAHMNLSALAEGQTVLKPEGGEARV
Protein: Cyclotide hyen-M (C0HLP7)
Organism: Pigea enneasperma (Spade flower) (Afrohybanthus enneaspermus)
Function: Probably participates in a plant defense mechanism (By similarity). Has cytotoxic activity against HUVEC cells (LC(50)= 1.83 uM) and various cancer cells including HeLa (LC(50)= 1.81 uM), MCF-7 and K562. Displays very weak hemolytic activity.
Interaction partners:
Sequence:
SIPCAESCVWIPCTVTALLGCSCSDKVCYN
Protein: RE17845p (Rab9) (Q9VIW6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}. Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004616}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004616}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004616}.
Interaction partners:
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting 33B
- Vacuolar protein sorting-associated protein 33A
- Vacuolar fusion protein MON1 homolog
- Vacuolar fusion protein CCZ1 homolog
- Rab GDP dissociation inhibitor
Sequence:
MTNMRPPQKSKLLKVVILGDGGVGKSALLTRFVANRYEENNFHTIGVEFMNKDIVVDGERYTLQIWDTAGQERFRALRTPFYRGSDICLLCYALDDRDSLKGLGVWRNEFLNYADVDQDKFPFIVVGNKNDIPAQKRQVSSDAVQQWCAEQKVACHIETSSKAATNVTDAFVLGLRQWRHMECVAEAELRQHGDTIDLTRPIRLVQRRICCTGGGGGGGGVGQDADGDDAAMHSPGKKVFGQKRNASKAPATNYRL
Protein: Delta-like protein dsl-1 (DSL-domain containing protein dsl-1) (O45201)
Organism: Caenorhabditis elegans
Function: Probable secreted Notch ligand involved in the mediation of Notch signaling. Involved in the lin-12/Notch pathway-mediated signaling of cell fate in vulval precursor cells (VPCs), acting redundantly with lag-2, apx-1 and osm-11. May also be involved in glp-1/Notch signaling.
Subcellular location: Secreted {ECO:0000269|PubMed:14960273}.
Interaction partners:
- Anterior pharynx in excess protein 1
- Protein lin-12
- EGL-17
- Protein lin-3
Sequence:
MLKYLIFLAILISVVHSNGYMTIRLKSAFPLNVTVEVAEEVYFPTNKRSFNLQLKPNRVGFVSNIPVKFGRPGLVLVDCSPVEKFQIHRVTLRSIRWNTHVRSVASDNIFLPFTGFRYDIKCNRYWHGLHCDHFCNDDFARTINRRCTQNGTLGCLEGFHGPNCELPVPADSCKCQNGGKCVSSLENTWAQNGSLICECRLGHFEGKHCEKKSFNYFPKIEATTYATKDSHLARQFYNNSRVPNELATLPRL
Protein: Proline and serine-rich protein 2 (Q86WR7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPVTHRKSDASDMNSDTSPSCRLRAFSRGGSLESRSSSSRSRSFTLDDESLKYLTHEEKDVLLFFEETIDSLDEDFEEPVLCDGGVCCLCSPSLEESTSSPSEPEDVIDLVQPAPGAGEAEGLPEGTQAAGPAPAGKEHRKQDAETPPPPDPPAPETLLAPPPLPSTPDPPRRELRAPSPPVEHPRLLRSVPTPLVMAQKISERMAGNEALSPTSPFREGRPGEWRTPAARGPRSGDPGPGPSHPAQPKAPRFPSNIIVTNGAAREPRRTLSRAAVSVQERRAQVLATIHGHAGAFPAAGDAGEGAPGGGSSPERVARGRGLPGPAESLRAGGQAPRGPALANGFPSAHEALKSAPSSFAPAGKSLCFRPGPALPSTRARQSFPGPRQPNGAQDWRRADSLPRPQGITVQFAGRGSSEEARREALRKLGLLRESS
Protein: Recombining binding protein suppressor of hairless-like protein (Transcription factor RBP-L) (Q9UBG7)
Organism: Homo sapiens (Human)
Function: Putative transcription factor, which cooperates with EBNA2 to activate transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pancreas transcription factor 1 subunit alpha
- Mastermind-like protein 1
- Mastermind-like protein 2
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Mastermind-like protein 3
- Neurogenic locus notch homolog protein 1
- Corepressor interacting with RBPJ 1
- Neurogenic locus notch homolog protein 4
- Recombining binding protein suppressor of hairless
Sequence:
MDPAGAADPSVPPNPLTHLSLQDRSEMQLQSEADRRSLPGTWTRSSPEHTTILRGGVRRCLQQQCEQTVRILHAKVAQKSYGNEKRFFCPPPCVYLSGPGWRVKPGQDQAHQAGETGPTVCGYMGLDSASGSATETQKLNFEQQPDSREFGCAKTLYISDADKRKHFRLVLRLVLRGGRELGTFHSRLIKVISKPSQKKQSLKNTDLCISSGSKVSLFNRLRSQTVSTRYLSVEDGAFVASARQWAAFTLHLADGHSAQGDFPPREGYVRYGSLVQLVCTVTGITLPPMIIRKVAKQCALLDVDEPISQLHKCAFQFPGSPPGGGGTYLCLATEKVVQFQASPCPKEANRALLNDSSCWTIIGTESVEFSFSTSLACTLEPVTPVPLISTLELSGGGDVATLELHGENFHAGLKVWFGDVEAETMYRSPRSLVCVVPDVAAFCSDWRWLRAPITIPMSLVRADGLFYPSAFSFTYTPEYSVRPGHPGVPEPATDADALLESIHQEFTRTNFHLFIQT
Protein: Regulator of nonsense transcripts 1, putative (Q582F1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- MIF4G domain-containing protein
- PIH1D1/2/3 CS-like domain-containing protein
- RRM domain-containing protein
- Nuclear cap-binding protein subunit 2
- Eukaryotic release factor 3, putative
- Polyadenylate-binding protein
- RNA-binding protein, putative
- RNA-binding protein RBP14, putative
- RNA-binding protein, putative
- Borealin N-terminal domain-containing protein
Sequence:
MFSEHASDERALGVATTPVASGETNKKPSCSYCSEESPTCLAFCNGCSKWFCNGSNGTSGSHIILHLVKSGHNSLKLHAENSLGDSTLECYICRSSNIFSLGFMPSKEEAVVVLVCREPCLHSKTLRDLNWDSSTWLPLIEERRLLPWICSIPSTLRRPLTLHDIKALEMSWEQKVKEFVDPVESVPEVPLYFESGTKYVEVFSSLIALDSQGARDSKDTSFEGIQCTQQKKIGGRHFFVLKPFPLFDVGVNRGDNVSIRVKGSESSLSGTITEVSATSVDNEHAVFVTDTTARSVDKKAVNEILAATTVTISPEYNGVADKRKMEALQQFARSEGSVSAYLYFTILGQKERAAHRNSGFDTEPEPRGHHNLNYSQEQALRVALRNPLTLIQGPPGTGKTSTSVAIIRELHSHVKSRILVCAPSNVAVDHLAQRVSGTGLKVVRLQAKYRNDIPCSVESIGLERQVGDYINASSGLERLKELLDSMQTGKSLNDKDYGTYKDGVEKIERLILRNADVVCCTCIGAGDYRLKTMKFKHVLIDEATQGTEPEVLIPLVRGAKQVILVGDHCQLRPLVFSTAAEKAGYQRSLFERLVLMGHRPVRLDVQYRMNPSLSFFPSHHYYEGTLQNGVTAEQRDASEVFPWPDVTKPIFFYNATGNEELGSNGRSYLNRAEAALTEQIVTKLIQGGVEPGDIGVITPYRSQCRYLRSYLSRSGRLPMEVYDRVEISSVDAFQGREKEFIILSCVRSNHRQGAGFVTDGRRLNVSLTRAKRGLIIMGNVQLFSRYPGWHELLVHMNSLSLIVEGPIDDLVPSAVVLQKPRKRGGKLKGEESDSPLFLPGES
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial (EC 2.7.11.2) (PDK p48) (Pyruvate dehydrogenase kinase isoform 1) (PDH kinase 1) (Q63065)
Organism: Rattus norvegicus (Rat)
Function: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- [Pyruvate dehydrogenase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Ac1164
- L-lactate dehydrogenase A chain
- RAC-alpha serine/threonine-protein kinase
- Hexokinase-2
Sequence:
MRLARLLRGGTSVRPLCAVPCASRSLASDSASGSGPASESGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKTIYEFTDTVIRIRNRHNDVIPTMAQGVTEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGSPSHRKHIGSINPNCDVVEVIKDGYENARRLCDLYYVNSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHADKGVYPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTESIERLPVYNKAAWKHYRTNHEADDWCVPSREPKDMTTFRSS
Protein: Serine/threonine-protein kinase Nek1 (EC 2.7.11.1) (Never in mitosis A-related kinase 1) (NimA-related protein kinase 1) (Renal carcinoma antigen NY-REN-55) (Q96PY6)
Organism: Homo sapiens (Human)
Function: Phosphorylates serines and threonines, but also appears to possess tyrosine kinase activity. Involved in DNA damage checkpoint control and for proper DNA damage repair. In response to injury that includes DNA damage, NEK1 phosphorylates VDAC1 to limit mitochondrial cell death. May be implicated in the control of meiosis (By similarity). Involved in cilium assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:15604234, ECO:0000305|PubMed:21211617}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P51954}. Cytoplasm {ECO:0000269|PubMed:18843199}. Note=Associated with the pericentriolar material (PubMed:21211617). Localizes to centrosome during interphase and mitosis (By similarity). Translocated from cytoplasm to discrete nuclear foci at sites of DNA damage (PubMed:15604234). {ECO:0000250|UniProtKB:P51954, ECO:0000269|PubMed:15604234, ECO:0000269|PubMed:21211617}.
Interaction partners:
- Cytoplasmic dynein 2 heavy chain 1
- Alsin
- Kinesin-like protein KIF3A
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial
- Vesicle-associated membrane protein-associated protein B/C
Sequence:
MEKYVRLQKIGEGSFGKAILVKSTEDGRQYVIKEINISRMSSKEREESRREVAVLANMKHPNIVQYRESFEENGSLYIVMDYCEGGDLFKRINAQKGVLFQEDQILDWFVQICLALKHVHDRKILHRDIKSQNIFLTKDGTVQLGDFGIARVLNSTVELARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYELCTLKHAFEAGSMKNLVLKIISGSFPPVSLHYSYDLRSLVSQLFKRNPRDRPSVNSILEKGFIAKRIEKFLSPQLIAEEFCLKTFSKFGSQPIPAKRPASGQNSISVMPAQKITKPAAKYGIPLAYKKYGDKKLHEKKPLQKHKQAHQTPEKRVNTGEERRKISEEAARKRRLEFIEKEKKQKDQIISLMKAEQMKRQEKERLERINRAREQGWRNVLSAGGSGEVKAPFLGSGGTIAPSSFSSRGQYEHYHAIFDQMQQQRAEDNEAKWKREIYGRGLPERGILPGVRPGFPYGAAGHHHFPDADDIRKTLKRLKAVSKQANANRQKGQLAVERAKQVEEFLQRKREAMQNKARAEGHMVYLARLRQIRLQNFNERQQIKAKLRGEKKEANHSEGQEGSEEADMRRKKIESLKAHANARAAVLKEQLERKRKEAYEREKKVWEEHLVAKGVKSSDVSPPLGQHETGGSPSKQQMRSVISVTSALKEVGVDSSLTDTRETSEEMQKTNNAISSKREILRRLNENLKAQEDEKGKQNLSDTFEINVHEDAKEHEKEKSVSSDRKKWEAGGQLVIPLDELTLDTSFSTTERHTVGEVIKLGPNGSPRRAWGKSPTDSVLKILGEAELQLQTELLENTTIRSEISPEGEKYKPLITGEKKVQCISHEINPSAIVDSPVETKSPEFSEASPQMSLKLEGNLEEPDDLETEILQEPSGTNKDESLPCTITDVWISEEKETKETQSADRITIQENEVSEDGVSSTVDQLSDIHIEPGTNDSQHSKCDVDKSVQPEPFFHKVVHSEHLNLVPQVQSVQCSPEESFAFRSHSHLPPKNKNKNSLLIGLSTGLFDANNPKMLRTCSLPDLSKLFRTLMDVPTVGDVRQDNLEIDEIEDENIKEGPSDSEDIVFEETDTDLQELQASMEQLLREQPGEEYSEEEESVLKNSDVEPTANGTDVADEDDNPSSESALNEEWHSDNSDGEIASECECDSVFNHLEELRLHLEQEMGFEKFFEVYEKIKAIHEDEDENIEICSKIVQNILGNEHQHLYAKILHLVMADGAYQEDNDE
Protein: Protein polyglycylase TTLL10 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 10) (A4Q9F3)
Organism: Mus musculus (Mouse)
Function: Polyglycylase which modifies both tubulin and non-tubulin proteins, generating polyglycine side chains of variable lengths on the gamma-carboxyl groups of specific glutamate residues of target proteins. Involved in the elongation step rather than the initiation step of the polyglycylation reaction. Polyglycylates alpha-tubulin and beta-tubulin. Polyglycylates non-tubulin proteins such as nucleosome assembly protein NAP1.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510}. Cell projection, cilium {ECO:0000305}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}.
Interaction partners:
Sequence:
MALHPQAGRPHRDGSEAQAEAAAQDLGRLPSPSKVGAAVCRIQGLGHRAARRPRRGIGTTSASRVPRPGALMPATRNRPRFIHCRGQPPRTRVSSKRSKRSRIHPCHTEVPGWTHEKQMGSSVKERLRPELSQLDQDADDLEEEEAARLPVTSPDGLLMEGDKQPSPGQGPFFYIGGTNGASIISNYCESKGWQRTQDSHCEDYKLKWCEIKCRDNYCSFREGQQLLFQLPNNKLLTTKIGLLSALREHARTLSKARMLPSTQTKVLKMEEFFPETYRLDIRDERQAFFALFDETQMWICKPTASNQGKGIFLIRSQEEAAALQAKTQSIEDDPIYRKMPFRAPQARVVQRYVQNPLLLDGKKFDVRSYMLIACAMPYMVFFGHGYARLTLSLYNPHSSDLSGHLTNQFMQKKSPLYTLLKESTVWTMEHLNRYINDKFRKTKGLPRDWVFTTFTKRMQQIMSHCFLAVKSKLECKLGYFDLIGCDFLIDENFKVWLLEMNANPALHTNCEVLKAVIPGVVIETLDLALETCQKSLHSQKMLPLLSQRRFVLLYNGETTDLWPRLASSRPLNRLPNPNPNPNPNANPHPHPHPNPHPHPNPHPNANPHPPRPTCEAASSALSSARAAISERPGARKSMPSRGAPVCTPRKSRLSDSSGSSIAESEPSLCSGSLEGSRDTAREPSLGPPEEEREEEQRSTSHRGS
Protein: GRB2-associated and regulator of MAPK protein 1 (GRB2-associated and regulator of MAPK1) (Q9H706)
Organism: Homo sapiens (Human)
Function: Acts as an adapter protein that plays a role in intracellular signaling cascades triggered either by the cell surface activated epidermal growth factor receptor and/or cytoplasmic protein tyrosine kinases. Promotes activation of the MAPK/ERK signaling pathway. Plays a role in the regulation of cell proliferation.
Interaction partners:
- Growth factor receptor-bound protein 2
- SHC-transforming protein 1
Sequence:
MDPAPSLGCSLKDVKWSSVAVPLDLLVSTYRLPQIARLDNGECVEGLRENDYLLIHSCRQWTTITAHSLEEGHYVIGPKIEIPVHYAGQFKLLEQDRDIKEPVQYFNSVEEVAKAFPERVYVMEDITFNVKVASGECNEDTEVYNITLCTGDELTLMGQAEILYAKTFKEKSRLNTIFKKIGKLNSISKLGKGKMPCLICMNHRTNESISLPFQCKGRFSTRSPLELQMQEGEHTIRNIVEKTRLPVNVTVPSPPPRNPYDLHFIREGHRYKFVNIQTKTVVVCCVLRNNKILPMHFPLHLTVPKFSLPEHLVKGESWPETLVHHWLGICQEQFDIDEYSRAVRDVKTDWNEECKSPKKGRCSGHNHVPNSLSYARDELTQSFHRLSVCVYGNNLHGNSEVNLHGCRDLGGDWAPFPHDILPYQDSGDSGSDYLFPEASEESAGIPGKSELPYEELWLEEGKPSHQPLTRSLSEKNRCDQFRGSVRSKCATSPLPIPGTLGAAVKSSDTALPPPPVPPKSEAVREECRLLNAPPVPPRSAKPLSTSPSIPPRTVKPARQQTRSPSPTLSYYSSGLHNISVTKTDTNPSESTPVSCYPCNRVKTDSVDLKSPFGSPSAEAVSSRLSWPNHYSGASESQTRSDFLLDPSRSYSYPRQKTPGTPKRNCPAPFDFDGCELLASPTSPVTAEFSSSVSGCPKSASYSLESTDVKSLAAGVTKQSTSCPALPPRAPKLVEEKVASETSPLPLKIDGAEEDPKSGSPDLSEDQYFVKKGMQDIFSASYPFSSPLHLQLAPRSCGDGSPWQPPADLSGLSIEEVSKSLRFIGLSEDVISFFVTEKIDGNLLVQLTEEILSEDFKLSKLQVKKIMQFINGWRPKI
Protein: Olfactory receptor 13C2 (Olfactory receptor OR9-12) (Q8NGS9)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MEWENHTILVEFFLKGLSGHPRLELLFFVLIFIMYVVILLGNGTLILISILDPHLHTPMYFFLGNLSFLDICYTTTSIPSTLVSFLSERKTISLSGCAVQMFLGLAMGTTECVLLGMMAFDRYVAICNPLRYPIIMSKDAYVPMAAGSWIIGAVNSAVQSVFVVQLPFCRNNIINHFTCEILAVMKLACADISDNEFIMLVATTLFILTPLLLIIVSYTLIIVSIFKISSSEGRSKASSTCSAHLTVVIIFYGTILFMYMKPKSKETLNSDDLDATDKIISMFYGVMTPMMNPLIYSLRNKDVKEAVKHLLNRRFFSK
Protein: Immunoglobulin superfamily member 10 (IgSF10) (Calvaria mechanical force protein 608) (CMF608) (Q6WRH9)
Organism: Rattus norvegicus (Rat)
Function: Involved in the control of early migration of neurons expressing gonadotropin-releasing hormone (GNRH neurons) (By similarity). May be involved in the maintenance of osteochondroprogenitor cells pool.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6WRI0}.
Interaction partners:
Sequence:
MQVRGREVSGLLISLTAVCLVVTPGSRACPRRCACYVPTEVHCTFRYLTSIPDGIPANVERINLGYNSLTRLTENDFDGLSKLELLMLHSNGIHRVSDKTFSGLQSLQVLKMSYNKVQIIRKDTFYGLGSLVRLHLDHNNIEFINPEAFYGLTSLRLVHLEGNRLTKLHPDTFVSLSYLQIFKTSFIKYLFLSDNFLTSLPKEMVSYMPNLESLYLHGNPWTCDCHLKWLSEWMQGNPDIIKCKKDRSSSSPQQCPLCMNPRISKGRPFAMVPSGAFLCTKPTIDPSLKSKSLVTQEDNGSASTSPQDFIEPFGSLSLNMTDLSGNKADMVCSIQKPSRTSPTAFTEENDYIMLNASFSTNLVCSVDYNHIQPVWQLLALYSDSPLILERKPQLTETPSLSSRYKQVALRPEDIFTSIEADVRADPFWFQQEKIVLQLNRTATTLSTLQIQFSTDAQIALPRAEMRAERLKWTMILMMNNPKLERTVLVGGTIALSCPGKGDPSPHLEWLLADGSKVRAPYVSEDGRILIDKNGKLELQMADSFDAGLYHCISTNDADADVLTYRITVVEPYGESTHDSGVQHTVVTGETLDLPCLSTGVPDASISWILPGNTVFSQPSRDRQILNNGTLRILQVTPKDQGHYQCVAANPSGADFSSFKVSVQKKGQRMVEHDREAGGSGLGEPNSSVSLKQPASLKLSASALTGSEAGKQVSGVHRKNKHRDLIHRRRGDSTLRRFREHRRQLPLSARRIDPQRWAALLEKAKKNSVPKKQENTTVKPVPLAVPLVELTDEEKDASGMIPPDEEFMVLKTKASGVPGRSPTADSGPVNHGFMTSIASGTEVSTVNPQTLQSEHLPDFKLFSVTNGTAVTKSMNPSIASKIEDTTNQNPIIIFPSVAEIRDSAQAGRASSQSAHPVTGGNMATYGHTNTYSSFTSKASTVLQPINPTESYGPQIPITGVSRPSSSDISSHTTADPSFSSHPSGSHTTASSLFHIPRNNNTGNFPLSRHLGRERTIWSRGRVKNPHRTPVLRRHRHRTVRPAIKGPANKNVSQVPATEYPGMCHTCPSAEGLTVATAALSVPSSSHSALPKTNNVGVIAEESTTVVKKPLLLFKDKQNVDIEIITTTTKYSGGESNHVIPTEASMTSAPTSVSLGKSPVDNSGHLSMPGTIQTGKDSVETTPLPSPLSTPSIPTSTKFSKRKTPLHQIFVNNQKKEGMLKNPYQFGLQKNPAAKLPKIAPLLPTGQSSPSDSTTLLTSPPPALSTTMAATQNKGTEVVSGARSLSAGKKQPFTNSSPVLPSTISKRSNTLNFLSTETPTVTSPTATASVIMSETQRTRSKEAKDQIKGPRKNRNNANTTPRQVSGYSAYSALTTADTPLAFSHSPRQDDGGNVSAVAYHSTTSLLAITELFEKYTQTLGNTTALETTLLSKSQESTTVKRASDTPPPLLSSGAPPVPTPSPPPFTKGVVTDSKVTSAFQMTSNRVVTIYESSRHNTDLQQPSAEASPNPEIITGTTDSPSNLFPSTSVPALRVDKPQNSKWKPSPWPEHKYQLKSYSETIEKGKRPAVSMSPHLSLPEASTHASHWNTQKHAEKSVFDKKPGQNPTSKHLPYVSLPKTLLKKPRIIGGKAASFTVPANSDVFLPCEAVGDPLPIIHWTRVSSGLEISQGTQKSRFHVLPNGTLSIQRVSIQDRGQYLCSAFNPLGVDHFHVSLSVVFYPARILDRHVKEITVHFGSTVELKCRVEGMPRPTVSWILANQTVVSETAKGSRKVWVTPDGTLIIYNLSLYDRGFYKCVASNPSGQDSLLVKIQVITAPPVIIEQKRQAIVGVLGGSLKLPCTAKGTPQPSVHWVLYDGTELKPLQLTHSRFFLYPNGTLYIRSIAPSVRGTYECIATSSSGSERRVVILTVEEGETIPRIETASQKWTEVNLGEKLLLNCSATGDPKPRIIWRLPSKAVIDQWHRMGSRIHVYPNGSLVVGSVTEKDAGDYLCVARNKMGDDLVLMHVRLRLTPAKIEQKQYFKKQVLHGKDFQVDCKASGSPVPEVSWSLPDGTVLNNVAQADDSGYRTKRYTLFHNGTLYFNNVGMAEEGDYICSAQNTLGKDEMKVHLTVLTAIPRIRQSYKTTMRLRAGETAVLDCEVTGEPKPNVFWLLPSNNVISFSNDRFTFHANRTLSIHKVKPLDSGDYVCVAQNPSGDDTKTYKLDIVSKPPLINGLYANKTVIKATAIRHSKKYFDCRADGIPSSQVTWIMPGNIFLPAPYFGSRVTVHPNGTLEMRNIRLSDSADFTCVVRSEGGESVLVVQLEVLEMLRRPTFRNPFNEKVIAQAGKPVALNCSVDGNPPPEITWILPDGTQFANRPHNSPYLMAGNGSLILYKATRNKSGKYRCAARNKVGYIEKLILLEIGQKPVILTYEPGMVKSVSGEPLSLHCVSDGIPKPNVKWTTPGGHVIDRPQVDGKYILHENGTLVIKATTAHDQGNYICRAQNSVGQAVISVSVMVVAYPPRIINYLPRNMLRRTGEAMQLHCVALGIPKPKVTWETPRHSLLSKATARKPHRSEMLHPQGTLVIQNLQTSDSGVYKCRAQNLLGTDYATTYIQVL
Protein: Methyltransferase (EC 2.1.1.-) (Q9PB32)
Organism: Xylella fastidiosa (strain 9a5c)
Interaction partners:
- Methyltransferase
Sequence:
MIVASSAAYRLHEGDALRLLCDIDSASVDAVITDPPYCSGAMRMSDRFQPTKKKYINNGTKHVAPDFDCDFRDHRGFLAWSSQWLSECRRVTRPGGVLLVFTDWRMLPTLTDAVQSAGWAWQGIVVWDKTPACRPQLGRFRSQAEFIVWASCGLMNPKAHPVTPVGVFPTGTAPREKRHQVGKPLALMEHLIKIVPPASTILDPFAGSGTTGVAALRAGHRFIGMEIAPYYCDVAKQRLADRA