wanglab/gogpt-training-data huggingface dataset:
Protein: RuvB-like 2 (EC 3.6.4.12) (Reptin) (Q9DE27)
Organism: Xenopus laevis (African clawed frog)
Function: Has single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). Proposed core component of the chromatin remodeling INO80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding (By similarity). Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Dynein axonemal particle {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}.
Interaction partners:
Sequence:
MATMAATKVPEVRDVTRIERIGAHSHIRGLGLDDALEPRQVSQGMVGQLASRRAAGVILEMIKEGKIAGRAVLIAGQPGTGKTAIAMGMAQALGSDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEVQIDRPATGTGAKVGKLTLKTTEMETIYDLGTKMIESLTKEKVQAGDVITIDKATGKITKLGRAFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIECFSFLNRALESDMAPVLIMATNRGITRIRGTNYQSPHGIPIDLLDRLLIISTSPYNEKETKQILKIRCEEEDVDMSEDAYTVLTRIGLETSLRYSMQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFMFNEMKTDTMDTS
Protein: Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.11.23) (EC 2.7.12.1) (Dual specificity YAK1-related kinase) (Protein kinase minibrain homolog) (MNBH) (RP86) (Q63470)
Organism: Rattus norvegicus (Rat)
Function: Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Exhibits a substrate preference for proline at position P+1 and arginine at position P-3 (By similarity). Plays an important role in double-strand breaks (DSBs) repair following DNA damage (By similarity). Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR) (By similarity). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A (By similarity). May play a role in a signaling pathway regulating nuclear functions of cell proliferation (By similarity). Modulates alternative splicing by phosphorylating the splice factor SRSF6. Has pro-survival function and negatively regulates the apoptotic process. Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1. This in turn inhibits p53/TP53 activity and apoptosis (By similarity). Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434'.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:22767602, ECO:0000269|PubMed:9748265}.
Interaction partners:
- DDB1 and CUL4-associated factor 7.
- Protein lin-52 homolog
- Forkhead box protein M1
- Protein lin-54 homolog
- Calcipressin-1
- RING-type E3 ubiquitin transferase
- Lin-37 DREAM MuvB core complex component
- Family with sequence similarity 53, member C
- Lin-9 DREAM MuvB core complex component
Sequence:
MHTGGETSACKPSSVRLAPSFSFHAAGLQMAAQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWSLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFAAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS
Protein: Octopamine receptor beta-1R (DmOA2) (DmOct-beta-1R) (Q9VCZ3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Autoreceptor for octopamine, which is a neurotransmitter, neurohormone, and neuromodulator in invertebrates. Negatively regulates synaptic growth by activating the inhibitory G protein Galphao and limiting cAMP production. Antagonizes the action of Octbeta2R which stimulates synaptic growth.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTLLQRLQAMSATTTRTILEGSISSFGGGTNEPLASKIPVLEESASHARYLKFIADGLIDEGLGSAVGSGSSIAVSVEDVVAGQAQDIQASEGSTDDADGSSHLALVFVKCFIIGFIILAAILGNMLVIVSVMRHRKLRIITNYFVVSLAVADMLVALCAMTFNASVMISGKWMFGSVMCDMWNSFDVYFSTASIMHLCCISVDRYYAIVQPLDYPLIMTQRRVFIMLLMVWLSPALLSFLPICSGWYTTTENYKYLKSNPHICEFKVNKAYAIVSSSMSFWIPGIVMLSMYYRIYQEADRQERLVYRSKVAALLLEKHLQISQIPKPRPSIQVEQSTISTMRRERKAARTLGIIMSAFLICWLPFFLWYIVSSLCDSCITPRLLVGILFWIGYFNSALNPIIYAYFNRDFRAAFKKTLKSLFPYAFYFCRRGRGRDDDRDLEFGGPSRRGTNGAQRTGSGSAEMANCVNSTASSEIHMSVMRARQYAVNVTPTTDAQMQQLHPLYTN
Protein: DNA polymerase eta (EC 2.7.7.7) (Radiation-sensitive protein 30) (Q04049)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA polymerase zeta processivity subunit
- DNA repair protein REV1
- Proliferating cell nuclear antigen
- DNA polymerase zeta catalytic subunit
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- DNA repair protein RAD5
- Ubiquitin-conjugating enzyme variant MMS2
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin-conjugating enzyme E2 2
- N-glycosylase/DNA lyase
Sequence:
MSKFTWKELIQLGSPSKAYESSLACIAHIDMNAFFAQVEQMRCGLSKEDPVVCVQWNSIIAVSYAARKYGISRMDTIQEALKKCSNLIPIHTAVFKKGEDFWQYHDGCGSWVQDPAKQISVEDHKVSLEPYRRESRKALKIFKSACDLVERASIDEVFLDLGRICFNMLMFDNEYELTGDLKLKDALSNIREAFIGGNYDINSHLPLIPEKIKSLKFEGDVFNPEGRDLITDWDDVILALGSQVCKGIRDSIKDILGYTTSCGLSSTKNVCKLASNYKKPDAQTIVKNDCLLDFLDCGKFEITSFWTLGGVLGKELIDVLDLPHENSIKHIRETWPDNAGQLKEFLDAKVKQSDYDRSTSNIDPLKTADLAEKLFKLSRGRYGLPLSSRPVVKSMMSNKNLRGKSCNSIVDCISWLEVFCAELTSRIQDLEQEYNKIVIPRTVSISLKTKSYEVYRKSGPVAYKGINFQSHELLKVGIKFVTDLDIKGKNKSYYPLTKLSMTITNFDIIDLQKTVVDMFGNQVHTFKSSAGKEDEEKTTSSKADEKTPKLECCKYQVTFTDQKALQEHADYHLALKLSEGLNGAEESSKNLSFGEKRLLFSRKRPNSQHTATPQKKQVTSSKNILSFFTRKK
Protein: TSC complex subunit 2 (A0A2R8Y7C8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAKPTSKDSGLKEKFKILLGLGTPRPNPRSAEGKQTEFIITAEILRELSMECGLNNRIRMIGQICEVAKTKKFEEHAVEALWKAVADLLQPERPLEARHAVLALLKAIVQGQGERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHITYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEYIARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAESLPLFIVTLCRTINVKELCEPCWKLMRNLLGTHLGHSAIYNMCHLMEDRAYMEDAPLLRGAVFFVGMALWGAHRLYSLRNSPTSVLPSFYQAMACPNEVVSYEIVLSITRLIKKYRKELQVVAWDILLNIIERLLQQLQTLDSPELRTIVHDLLTTVEELCDQNEFHGSQERYFELVERCADQRPESSLLNLISYRAQSIHPAKDGWIQNLQALMERFFRSESRGAVRIKVLDVLSFVLLINRQFYEEELINSVVISQLSHIPEDKDHQVRKLATQLLVDLAEGCHTHHFNSLLDIIEKVMARSLSPPPELEERDVAAYSASLEDVKTAVLGLLVILQTKLYTLPASHATRVYEMLVSHIQLHYKHSYTLPIASSIRLQAFDFLLLLRADSLHRLGLPNKDGVVRFSPYCVCDYMEPERGSEKKTSGPLSPPTGPPGPAPAGPAVRLGSVPYSLLFRVLLQCLKQESDWKVLKLVLGRLPESLRYKVLIFTSPCSVDQLCSALCSMLSGPKTLERLRGAPEGFSRTDLHLAVVPVLTALISYHNYLDKTKQREMVYCLEQGLIHRCASQCVVALSICSVEMPDIIIKALPVLVVKLTHISATASMAVPLLEFLSTLARLPHLYRNFAAEQYASVFAISLPYTNPSKFNQYIVCLAHHVIAMWFIRCRLPFRKDFVPFITKGLRSNVLLSFDDTPEKDSFRARSTSLNERPKSLRIARPPKQGLNNSPPVKEFKESSAAEAFRCRSISVSEHVVRSRIQTSLTSASLGSADENSVAQADDSLKNLHLELTETCLDMMARYVFSNFTAVPKRSPVGEFLLAGGRTKTWLVGNKLVTVTTSVGTGTRSLLGLDSGELQSGPESSSSPGVHVRQTKEAPAKLESQAGQQVSRGARDRVRSMSGGHGLRVGALDVPASQFLGSATSPGPRTAPAAKPEKASAGTRVPVQEKTNLAAYVPLLTQGWAEILVRRPTGNTSWLMSLENPLSPFSSDINNMPLQELSNALMAAERFKEHRDTALYKSLSVPAASTAKPPPLPRSNTDSAVVMEEGSPGEVPVLVEPPGLEDVEAALGMDRRTDAYSRSSSVSSQEEKSLHAEELVGRGIPIERVVSSEGGRPSVDLSFQPSQPLSKSSSSPELQTLQDILGDPGDKADVGRLSPEVKARSQSGTLDGESAAWSASGEDSRGQPEGPLPSSSPRSPSGLRPRGYTISDSAPSRRGKRVERDALKSRATASNAEKVPGINPSFVFLQLYHSPFFGDESNKPILLPNESFERSVQLLDQIPSYDTHKIAVLYVGEGQSNSELAILSNEHGSYRYTEFLTGLGRLIELKDCQPDKVYLGGLDVCGEDGQFTYCWHDDIMQAVFHIATLMPTKDVDKHRCDKKRHLGNDFVSIVYNDSGEDFKLGTIKGQFNFVHVIVTPLDYECNLVSLQCRKDMEGLVDTSVAKIVSDRNLPFVARQMALHANMASQVHHSRSNPTDIYPSKWIARLRHIKRLRQRICEEAAYSNPSLPLVHPPSHSKAPAQTPAEPTPGYEVGQRKRLISSVEDFTEFV
Protein: Protein ECERIFERUM 2 (Q39048)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in biosynthesis of the epicuticular wax. Plays a role in very-long-chain fatty acid (VLCFA) biosynthesis and is required for C28 fatty acid elongation in stem. Despite its classification as a BAHD acyltransferase based on sequence homology, CER2 does not seem to share the catalytic mechanism of the members of the BAHD family.
Subcellular location: Endoplasmic reticulum. Nucleus {ECO:0000305}.
Interaction partners:
- 3-ketoacyl-CoA synthase 2
- Very-long-chain enoyl-CoA reductase
- 3-ketoacyl-CoA synthase 6
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Very-long-chain
- 3-ketoacyl-CoA synthase 9
- Protein ECERIFERUM 26-like
- Very-long-chain aldehyde decarbonylase CER1
- Fatty acyl-CoA reductase 3
- 3-ketoacyl-CoA synthase 1
Sequence:
MEGSPVTSVRLSSVVPASVVGENKPRQLTPMDLAMKLHYVRAVYFFKGARDFTVADVKNTMFTLQSLLQSYHHVSGRIRMSDNDNDTSAAAIPYIRCNDSGIRVVEANVEEFTVEKWLELDDRSIDHRFLVYDHVLGPDLTFSPLVFLQITQFKCGGLCIGLSWAHILGDVFSASTFMKTLGQLVSGHAPTKPVYPKTPELTSHARNDGEAISIEKIDSVGEYWLLTNKCKMGRHIFNFSLNHIDSLMAKYTTRDQPFSEVDILYALIWKSLLNIRGETNTNVITICDRKKSSTCWNEDLVISVVEKNDEMVGISELAALIAGEKREENGAIKRMIEQDKGSSDFFTYGANLTFVNLDEIDMYELEINGGKPDFVNYTIHGVGDKGVVLVFPKQNFARIVSVVMPEEDLAKLKEEVTNMII
Protein: Pentraxin family member (A3KPG5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362112}.
Interaction partners:
- Sex hormone-binding globulin
Sequence:
MLVLFFCLLSLTLAATEVGLGGKTLFFPTNTDSSYVQIDPDKPLSLSAFTLCMRVRLELLVDRVVILFAYRTSEVDELNVWREKDGRVGLVIQSDKDAAMVHLSPRSTFQTHLCITWDSATGLTGFWEDGRRSVYQMYRKGYSIRPGGTVLLGQDPDSFVGSFDAAQSFVGEITDVQMWDYVLPSTQIKAVYSNQDDRVKGNVFDWNTIKYDVTGNVLVVPDN
Protein: Small ribosomal subunit protein eS19A (40S ribosomal protein S19-A) (RP55A) (S16a) (YP45) (YS16A) (P07280)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eS19 is required for proper maturation of the small (40S) ribosomal subunit. Binds to 40S pre-ribosomal particles, probably required after association of NOC4 but before association of ENP1, TSR1 and RIO2 with 20/21S pre-rRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS9A
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS25B
- Small ribosomal subunit protein eS24A
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS4B
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS12A
- Large ribosomal subunit protein eL38
- Small ribosomal subunit protein uS13A
Sequence:
MPGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSSGNEMPPQDAEGWFYKRAASVARHIYMRKQVGVGKLNKLYGGAKSRGVRPYKHIDASGSINRKVLQALEKIGIVEISPKGGRRISENGQRDLDRIAAQTLEEDE
Protein: Sister chromatid cohesion protein (Q385W6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU364107}.
Interaction partners:
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- SCD domain-containing protein
- Sister chromatid cohesion protein
- separase
- EF-hand domain-containing protein
- Double-strand-break repair protein rad21 homolog, putative
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- DNA polymerase eta
Sequence:
MASIPNGAAPIPPDVTCTINPLLDLLAAFPVPQLAAIPPTRYCENDVAHCEPDAAREEAITNTIEESARTLIASSSYELLREATVCIDSSVATVPKGGSIRPTLSPLAQRIHERLLQLEKNVRVGGIRNVPGGGSPHKGRVPWERQPARQMTLRPRREPSQDAARTAEQEDGSESPRIETKQSPMAVQKNEQTYGEFKTEAYRSMEVADIFNEKLMDSKSLDALLGMLSSATQPFRDVEGETITAFLTALVQPSVSPPSTKKKCLDDVETDISVELMERVIACCSCVSHPSFNPSHIPEDLINHLITKLAVLLRQVARRASGRSKKSKGTSTELQCLRALLGCFSLLVSDERLDVCSPGELIRLEELCYQSLFVATSGFGHQEVVTYAAYVMSHALQLYRCLWNHLKVERDITTERFFLQLPLGGNLLLRLQQLPSGEKVMPLTAAVVNAAQSLDIGTETIGLRDAECLVQQCRSWAARFVQHFVLGKRELQDRDTVWTLVLQFVDDLANMLGLPEYPAADAILQSLLASLAHYASVTAVTLGERNAANFSLLPLFVEVIYRVSRVALGGSLQKALCVKVPPASRLLSSAQMRQWRYLTYYDTTATKKKGSNISADYENKNEDDSLQVGLDDYRAILYTALSQSSNLPPSDFGDVSLHLRAAHVLTWAVHDKCFHELTLDKLVRSRHIVEGGVSVDWGMLRACSLRLSAERERSLLNRAAKERLLSLLLSVFQVWEEEPQGSLGSLEVARKKALTYIAELTELHPPLLDKIWPIVQRCARCDNARVREATVALLLTLISGICRDTKRESGLTESAVADMLTDVVSMLLHFLRDHNAAVVARSIAALDTLLTEEPYTKLFEQMSKVEHLVTFTQSKLLTLITPSAAVLEVPDCQHQAALHRLFIRRWTAQMPGDFEQYHVHIRVAKELLRLTGSTIKYPYDASESLHLVTLLRGMCSELTAVKPKRRGPKKAEDARRQALCGVMVGAAKALWSEWQRLSPGSGAAAALATIHILSMACNDWVDPLLDALAQVLLQQQQLLVKTDMANGDSEVTGITLLHVCRIMHTVLMGSRRPPLPLDPLAQVLTSLISRYVGPHQQKILLSATGALVSTITCGHDRLSKQVNTKYLTLCYSLMNTYYVHVASFAPTLRTNQCNVGYTLRFLFLLSEFLRLYPGWKHRHPELAALTTTTSCAGSAGATTVPNQLACGDGICANIYSAVELVLRECPERERGRTTVIALRVMGSLCMLQPTTYLRHCEPYIRRAIHPASDVQQQLQGLTFIRDFLRDEDSRVHEAAMAAGATLPIQWQDNGNCSTQPASPNNGCRLLKLQASAETQVEEQNSGMATWLLQQFHEHVTLLCGSYMLPVRELAMEILHLCAAGGLLPPPRYTKALIVLGADPQSGDVRRTAVAYVLEQCERHGDLMVASSTAGIVKAFDLHAVCGVDVVKSAIGVYDTQHHNGQGEGEYCVHAYLFKSLHKKYRDAIVSSLMCYFHEEARVGQWMREHKLTCSGGAASGSKGLMELTPSPLPFLIHLTVVLAHIPFQLESDVVHLLDSCRTVVDLSGPSCMEFVQQQLALLQASTGTGARGSRGVGDVGVTKVTDSALDVWRCYGVSCVLHLNTFLHSAYDLRGSKRYRQSGVGRPVGRAARSDSRRVASTAFLNKMNELLQSMNVLWGGKSDAEGKLNNCKIQSMKSLLTSLAGAAGLEDTDAVLECPSGPRMKTKASTRHHKKAKKRGRPCCRLSNVVNDSSSSSSERATSAESFQRGIDHARHGECISEWADDFFHTEQ
Protein: Intracellular hyaluronan-binding protein 4 (IHABP-4) (IHABP4) (Hyaluronic acid-binding protein 4) (Q9JKS5)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that plays a role in the regulation of transcription, pre-mRNA splicing and mRNA translation. Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress. Plays a role in pre-mRNA splicing regulation. Binds (via C-terminus) to poly(U) RNA. Involved in mRNA translation regulation, probably at the initiation step. Seems to play a role in PML-nuclear bodies formation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q5JVS0}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A1L1K8}. Nucleus, nuclear body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus speckle {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q5JVS0}. Nucleus, gem {ECO:0000250|UniProtKB:Q5JVS0}. Note=Transported into the nuclear compartment in activated leukocytes. Inhibition of methylation alters its distribution between the nuclear and cytoplasmic compartments. Methylation may be required for its localization in subnuclear structures, such as nucleoli, nuclear speckles, Cajal bodies and Gemini of coiled bodies (gems). Colocalizes with FMR1, FXR1 and FXR2 in cytoplasmic stress granules. In myocardial cells, localization at the sarcoplasm is reduced in response to mechanical stress. {ECO:0000250|UniProtKB:A1L1K8, ECO:0000250|UniProtKB:Q5JVS0}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL32
Sequence:
MKGALGSPVAAAGAAMQETFGCVVANRFHQLLDDESDPFDILREAEHRRQQQLQRKRRDEAAAASGAGHRGGRSPAVASGHRPGAGGRRESQKERKSLAASGAQQPDSPGGPQPPGQKRTPRRGEQQGWNDNRGTDVVLERAERRSYREYRPYETERQADLPVEKFTDEKPVDRFDRDRPLRGRGGPRGGLRSRGRGGPGNRAFDSFDQRGKRDFERYSSNDKTNRMEDSMGGCGIRPWGSGKDTSDTEPPAPMEETSMMEECQGTLDEESAAKVPELEVEEENQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSRYRDDMVKEDYEDESHVFRKAANDITSQLEINFGNLPRPGRGARGSTRGGRGRMRRTENYGPRAEVVTQDVAPNPDDPEDFPALA
Protein: Adherens junction-associated protein 1 (Membrane protein shrew-1) (Q9UKB5)
Organism: Homo sapiens (Human)
Function: Plays a role in cell adhesion and cell migration.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:16707570}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:16707570}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, adherens junction {ECO:0000269|PubMed:14595118}. Note=Mainly basolateral (PubMed:16707570). Localization is mediated by AP1M2 (PubMed:16707570). {ECO:0000269|PubMed:16707570}.
Interaction partners:
- Cadherin-1
- Basigin
- Catenin beta-1
- Peptidyl-prolyl cis-trans isomerase B
Sequence:
MWIQQLLGLSSMSIRWPGRPLGSHAWILIAMFQLAVDLPACEALGPGPEFWLLPRSPPRPPRLWSFRSGQPARVPAPVWSPRPPRVERIHGQMQMPRARRAHRPRDQAAALVPKAGLAKPPAAAKSSPSLASSSSSSSSAVAGGAPEQQALLRRGKRHLQGDGLSSFDSRGSRPTTETEFIAWGPTGDEEALESNTFPGVYGPTTVSILQTRKTTVAATTTTTTTATPMTLQTKGFTESLDPRRRIPGGVSTTEPSTSPSNNGEVTQPPRILGEASGLAVHQIITITVSLIMVIAALITTLVLKNCCAQSGNTRRNSHQRKTNQQEESCQNLTDFPSARVPSSLDIFTAYNETLQCSHECVRASVPVYTDETLHSTTGEYKSTFNGNRPSSSDRHLIPVAFVSEKWFEISC
Protein: Large ribosomal subunit protein eL31x (60S ribosomal protein L31-3) (P51420)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL30y
- Large ribosomal subunit protein uL1z
- Large ribosomal subunit protein eL24z
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL1x
- Large ribosomal subunit protein eL13z
- Large ribosomal subunit protein eL28y
- Large ribosomal subunit protein uL22z
- Large ribosomal subunit protein uL2x
- Large ribosomal subunit protein uL24z
Sequence:
MSEKKGRKEEVITREYTINLHRRLHKCTFKKKAPKAIKEIRKFAEKAMGTKDVRVDVKLNKQIWSKGIRGPPRRIRVRVARKRNDDEDAKEEFFSLVTVAEIPAEGLSGLGTKVIEEED
Protein: Transcription initiation factor TFIID subunit 10 (Q21172)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR017246}.
Interaction partners:
Sequence:
MNDPEQYEPSSSTESVLMPPPALPQRPAAAPQVYSTLEPSVQNLRSSLHKPLTGNQQQFVQKTLENVQKNPSQDDTHEFINQLADYPPTIPDSVTLHFLKSAGVDGSDPRVTRMISLAAQKHVSDIILDAMTSARMKGLGQTKKGTKDTKYTLTEELLDEILKEYGHQNTRPPYHT
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q8GWU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKAQKGSSKKKGTNSGLVAVAVDNNKGSQHALKWAADHLVSKGQTIILLHVILRSSSDSGEITAEKHKQAENLFVTFHCYCSRKEIQCLDVTLEDDNIVKSLAEYVSSGVIENLILGAPSRHGFMRKFKISDTPSNVAKAAPDFCTVYVISKGKISSVRHASRAAPYRSPLMGQIENHSEIINYEKFRNTMSFRDRAPPRSSTASSIEDYGKSPMARTSNYANSFFDLEDSENDISFVCSGRPSTASSGRPSTSTGRSDISFVSSGRPSTSTTGSPSFIYDFPDSGLTPRESTSSGHSMRLGIRFNDTNIQHDFSFVSQDSGRSSCSCSPQNLEEVEAEMRRLKQELKHAIDMYGSACREALAAKQEAKELQRQKIEEEGWVQEGQLSEKSTKSIVEKERAHKAAKDASETAGKIAELETQRRAIEAAGSFSDSSLRYRRYVIGEIEEATNSFDKANKIGEGGYGPVYKGYLDHTPVAIKALKADAVQGRSQFQREVEVLSCIRHPHMVLLIGACPEYGVLVYEYMAKGSLADRLYKYGNTPPLSWELRFRIAAEVATGLLFLHQTKPEPIVHRDLKPGNILIDQNYVSKIGDVGLAKLVPAVAENVTQCHVSSTAGTFCYIDPEYQQTGMLGVKSDVYSFGILLLELLTAKRPTGLAYTVEQAMEQGKFKDMLDPAVPNWPVEEAMSLAKIALKCAQLRRKDRPDLGKEVLPELNKLRARADTNMEWMMFNLSRGRLTPNHSQVSLPPVDELSVCSDKSYTHSSTVSDTEKNSDQNEED
Protein: Sodium/hydrogen exchanger 1 (DdNHE1) (NHE1) (Na-H exchanger 1) (Q552S0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Regulation of intracellular pH homeostasis in response to cAMP, which is essential for chemotaxis. Necessary for F-actin localization and the kinetics of actin polymerization during chemotaxis and cell polarity but not for directional sensing.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Predominantly localizes to the leading-edge of the chemotaxing polarized cells. {ECO:0000269|PubMed:15851518}.
Interaction partners:
- Sodium/hydrogen exchanger
Sequence:
MKLNKSYILIVVLLLSLFYSSVSSTKTTLIKSNNHYNSDNSNNDNKNININNNNDGDGDDDDDNNKILITPENQNHLIHDIGIDSSSTEILFGSSSNSGSCGEKNNTKQNALANQREANTIIFIIMLILTGSVLIVYFIISLDIPFVPESVAVVTYGIILGIVFRFFYSDIVNHVVSFEPENFFLFILPTIIFETGYSLHKTDFFNNIGPILMFAVFGTIITFLVVGFGIYIVGYFGVSIALSLKDSFAFGSIISSTDPVCTLAIFQALNVDPMLYILVLGESILNDATSMMLYSVVEDTSTRDIIISCAMFTVVAIGSVILGVVMALLLSLILKWINIGKFPALETIFMVMFSYMSYVLAGALDISGVLAVFFFGITLNQYGAYSLSPYTKLTSGQLFRTAAFISETFLFLYFGLSLTAHEFKFDLGLFSWSILFTCLARAISVFPMCFLLNKFLKTKIPWVIQVAIWFAGLRGAFAFSLSLDYISEDEHMNAYIRTNTLLVVVFTIFVFGMGTYPLLRVLGIKTSQTDQSLDNISKPMSKQTKQKDRTKLYESFDDKYFKPWFRKRVPPLANEAIEIFEKMVIQSSHDHELDSNPLRFDDDEEDDDDEDLDFDSDLDLNININTDSIHQSDNNNNDNGNNNNNNNNIIINNNSQHHSNDGSNNKNNDTLPLI
Protein: V-type proton ATPase subunit G 2 (V-ATPase subunit G 2) (V-ATPase 13 kDa subunit 2) (Vacuolar proton pump subunit G 2) (O95670)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular location: Melanosome {ECO:0000269|PubMed:17081065}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q0VCV6}; Peripheral membrane protein {ECO:0000305}. Note=Highly enriched in late-stage melanosomes. {ECO:0000269|PubMed:17081065}.
Interaction partners:
- V-type proton ATPase subunit E 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit E 2
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit C 2
Sequence:
MASQSQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREHEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCDVRPQVHPNYRISA