wanglab/gogpt-training-data huggingface dataset:
Protein: Endonuclease III-like protein 1 (hNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase) (P78549)
Organism: Homo sapiens (Human)
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines. Has also 8-oxo-7,8-dihydroguanine (8-oxoG) DNA glycosylase activity. Acts preferentially on DNA damage opposite guanine residues in DNA. Is able to process lesions in nucleosomes without requiring or inducing nucleosome disruption.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:10882850, ECO:0000269|PubMed:12531031, ECO:0000269|PubMed:9611236}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:9611236}.
Interaction partners:
- DNA repair nuclease/redox regulator APEX1
- N-glycosylase/DNA lyase
- Endonuclease 8-like 1 lyase Neil1)
- Endonuclease 8-like 2 lyase Neil2)
- DNA repair protein XRCC1
- Endonuclease 8-like 3
- Adenine DNA glycosylase
- Y-box-binding protein 1
- Uracil-DNA glycosylase
- DNA-3-methyladenine glycosylase
Sequence:
MTALSARMLTRSRSLGPGAGPRGCREEPGPLRRREAAAEARKSHSPVKRPRKAQRLRVAYEGSDSEKGEGAEPLKVPVWEPQDWQQQLVNIRAMRNKKDAPVDHLGTEHCYDSSAPPKVRRYQVLLSLMLSSQTKDQVTAGAMQRLRARGLTVDSILQTDDATLGKLIYPVGFWRSKVKYIKQTSAILQQHYGGDIPASVAELVALPGVGPKMAHLAMAVAWGTVSGIAVDTHVHRIANRLRWTKKATKSPEETRAALEEWLPRELWHEINGLLVGFGQQTCLPVHPRCHACLNQALCPAAQGL
Protein: Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (17-beta-hydroxysteroid dehydrogenase 12) (17-beta-HSD 12) (3-ketoacyl-CoA reductase) (KAR) (Estradiol 17-beta-dehydrogenase 12) (EC 1.1.1.62) (KIK-I) (O70503)
Organism: Mus musculus (Mouse)
Function: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q53GQ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53GQ0}.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Very-long-chain
- Very-long-chain
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Very-long-chain
- 17-beta-hydroxysteroid dehydrogenase type 1
- Very long chain fatty acid elongase 1
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8)
- Very long chain fatty acid elongase 5
Sequence:
MECAPPAAGFLYWVGASTIAYLALRASYSLFRAFQVWCVGNEALVGPRLGEWAVVTGGTDGIGKAYAEELAKRGMKIVLISRSQDKLNQVSNNIKEKFNVETRTIAVDFSLDDIYDKIKTGLSGLEIGVLVNNVGMSYEYPEYFLEIPDLDNTIKKLININVLSVCKVTRLVLPGMVERSKGVILNISSASGMLPVPLLTIYSATKAFVDFFSQCLHEEYKSKGIFVQSVMPYLVATKLAKIQKPTLDKPSAETFVKSAIKTVGLQTRTTGYVIHSLMGSINSIMPRWMYFKIIMGFSKSLRNRYLKKRKKN
Protein: Vascular endothelial growth factor B (VEGF-B) (VEGF-related factor) (VRF) (P49766)
Organism: Mus musculus (Mouse)
Function: Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis. VEGF-B seems to be required for normal heart function in adult but is not required for proper development of the cardiovascular system either during development or for angiogenesis in adults.
Subcellular location: Secreted. Note=Secreted but remains associated to cells or to the extracellular matrix unless released by heparin.
Interaction partners:
- Vascular endothelial growth factor receptor 1
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Neuropilin-1
- Adhesion G protein-coupled receptor L2
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L1
- Neuropilin-2
- Platelet-derived growth factor receptor beta
- Angiopoietin-1 receptor
Sequence:
MSPLLRRLLLVALLQLARTQAPVSQFDGPSHQKKVVPWIDVYARATCQPREVVVPLSMELMGNVVKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIQYPSSQLGEMSLEEHSQCECRPKKKESAVKPDRVAIPHHRPQPRSVPGWDSTPGASSPADIIHPTPAPGSSARLAPSAVNALTPGPAAAAADAAASSIAKGGA
Protein: AMP deaminase (EC 3.5.4.6) (X2JFA0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNFNRMDTAHRLRVDVRLYGGSMGNQLNDKGTASSTPTISSDDLSDLADSPVDEKAEADVEVTNEISAPYEVPQFPIEQIEKKLQIQRHLNEKQATGPRPVATAAVLATNRESSSSTEGRESAVTMERNDADINFQRVSISGEDTSGVPLEDLERASTLLIEALRLRSHYMAMSDQSFPSTTARFLKTVKLKDRINNLPVKEVSDIIRKMSVANIQDVHLRHSPMKITNPWNVEFPNDEDFKIKPLNGVFHIYENDDESSEIKYEYPDMSQFVNDMQVMCNMIADGPLKSFCYRRLCYLSSKYQMHVLLNELRELAAQKAVPHRDFYNTRKVDTHIHAASCMNQKHLLRFIKKTLKNNANEVVTVTNGQQMTLAQVFQSMNLTTYDLTVDMLDVHADRNTFHRFDKFNSKYNPIGESRLREVFLKTDNYLNGKYFAQIIKEVAFDLEESKYQNAELRLSIYGKSPDEWYKLAKWAIDNDVYSSNIRWLIQIPRLFDIFKSNKMMKSFQEILNNIFLPLFEATARPSKHPELHRFLQYVIGFDSVDDESKPENPLFDNDVPRPEEWTYEENPPYAYYIYYMYANMTVLNKFRQSRNMNTFVLRPHCGEAGPVQHLVCGFLMAENISHGLLLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLNYHRNPLPEYLARGLIISLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSSCDMCELARNSVMMSGFPHAIKQQWLGPIYYEDGIMGNDITRTNVPEIRVAYRYETLLDELSNIFKVNQTCSIADMNAT
Protein: Lycopene beta cyclase, chloroplastic (EC 5.5.1.19) (AtLCY) (Protein SUPPRESSOR OF ZEAXANTHIN-LESS 1) (Q38933)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in carotenoid biosynthesis. Catalyzes the double cyclization reaction which converts lycopene to beta-carotene and neurosporene to beta-zeacarotene. Major lycopene beta-cyclase that does not seem to be involved in neoxanthin synthesis. Involved in salt tolerance improvement by increasing synthesis of carotenoids, which impairs reactive oxygen species (ROS) and protects the photosynthetic system under salt stress.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Zeta-carotene desaturase, chloroplastic/chromoplastic
- Prolycopene isomerase, chloroplastic
- Protein LUTEIN DEFICIENT 5, chloroplastic
- Carotene epsilon-monooxygenase, chloroplastic
- Beta-carotene 3-hydroxylase 2, chloroplastic
- Phytoene synthase 1, chloroplastic
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- Beta-carotene 3-hydroxylase 1, chloroplastic
- 15-cis-zeta-carotene isomerase, chloroplastic
- Zeaxanthin epoxidase, chloroplastic
Sequence:
MDTLLKTPNKLDFFIPQFHGFERLCSNNPYHSRVRLGVKKRAIKIVSSVVSGSAALLDLVPETKKENLDFELPLYDTSKSQVVDLAIVGGGPAGLAVAQQVSEAGLSVCSIDPSPKLIWPNNYGVWVDEFEAMDLLDCLDTTWSGAVVYVDEGVKKDLSRPYGRVNRKQLKSKMLQKCITNGVKFHQSKVTNVVHEEANSTVVCSDGVKIQASVVLDATGFSRCLVQYDKPYNPGYQVAYGIVAEVDGHPFDVDKMVFMDWRDKHLDSYPELKERNSKIPTFLYAMPFSSNRIFLEETSLVARPGLRMEDIQERMAARLKHLGINVKRIEEDERCVIPMGGPLPVLPQRVVGIGGTAGMVHPSTGYMVARTLAAAPIVANAIVRYLGSPSSNSLRGDQLSAEVWRDLWPIERRRQREFFCFGMDILLKLDLDATRRFFDAFFDLQPHYWHGFLSSRLFLPELLVFGLSLFSHASNTSRLEIMTKGTVPLAKMINNLVQDRD
Protein: Anaphase-promoting complex subunit 4 WD40 domain-containing protein (Q386A1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRVLAVDNGKLCALSPNRSLYAIVKKGLVVVFIDYVRRTCQLKGETATTPNDVVPPVSNGDVVPPACRNDSVISKYTALDEIHELQWSPDSTLVALLLARRGIIEIVSVYGKICVARVDAGVVGLRAMHWHPSSRAVYWVGLLHAHVFSLLDSQLMQLPGGVKYSAQLAGLRLTVPSQGQRNASPLRSRSGGRKVGSDDRSGGSLWPGKPVSEAALIRFSLCHRFLFYVTPKLLHSPLSAVHAEKDSVHSASSEDALQSQAAMEQTNADSKCFQRRSEWLVVLSATTHEGLHAFSIAKFVPCVSDCIPLQGGIALVDYTQGSVALTTYDGTRLLHYEPTGVRNVTASKCGNVLLIVFGRACRAVIASKKRVVALRRIFFDSDVVLPFKMGELTVMEEPSSPEKSFVEFLQLSGGDKRNSSDVACLGKYDGWAAAGDDKELGAAGLAAISASGKLAAVILPLWPSTVIVIDVVQQRVLSVLCHRANAVGLYWPPSPHSKYWQFQRRHYMQPLRHGRDDGTGKVAQGGSASCGDGSRSTASTSVGQDEPLLITTDNCESKVFVWLSDRAMCFAAAGQGCPVSAGGALYMCPRKVDALSHNASGALRLRVNRGMFGEGAEGVVLVDDVQETAVMVTLDGETGEI
Protein: Nuclear RNA export factor 2 (Cancer/testis antigen 39) (CT39) (TAP-like protein 2) (TAPL-2) (Q9GZY0)
Organism: Homo sapiens (Human)
Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Subcellular location: Nucleus, nucleoplasm. Cytoplasm. Note=Localized in the nucleoplasm and at the nuclear envelope. Shuttles between the nucleus and the cytoplasm.
Interaction partners:
- NTF2-related export protein 1
- NTF2-related export protein 2
- mRNA export factor RAE1
- THO complex subunit 4
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup214
- THO complex subunit 5
- Nucleoporin NUP42
- Nuclear pore glycoprotein p62
- Eukaryotic initiation factor 4A-III
Sequence:
MCSTLKKCGTYRTEVAECHDHGSTFQGRKKGGSSFRDNFDKRSCHYEHGGYERPPSHCQENDGSVEMRDVHKDQQLRHTPYSIRCERRMKWHSEDEIRITTWRNRKPPERKMSQNTQDGYTRNWFKVTIPYGIKYDKAWLMNSIQSHCSDRFTPVDFHYVRNRACFFVQDASAASALKDVSYKIYDDENQKICIFVNHSTAPYSVKNKLKPGQMEMLKLTMNKRYNVSQQALDLQNLRFDPDLMGRDIDIILNRRNCMAATLKIIERNFPELLSLNLCNNKLYQLDGLSDITEKAPKVKTLNLSKNKLESAWELGKVKGLKLEELWLEGNPLCSTFSDQSAYVSAIRDCFPKLLRLDGRELSAPVIVDIDSSETMKPCKENFTGSETLKHLVLQFLQQYYSIYDSGDRQGLLGAYHDEACFSLAIPFDPKDSAPSSLCKYFEDSRNMKTLKDPYLKGELLRRTKRDIVDSLSALPKTQHDLSSILVDVWCQTERMLCFSVNGVFKEVEGQSQGSVLAFTRTFIATPGSSSSLCIVNDELFVRDASPQETQSAFSIPVSTLSSSSEPSLSQEQQEMVQAFSAQSGMKLEWSQKCLQDNEWNYTRAGQAFTMLQTEGKIPAEAFKQIS
Protein: Transcriptional coactivator yorkie (Protein yorkie) (Transcriptional coactivator YAP1 homolog) (Q45VV3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional coactivator which is the critical downstream regulatory target in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Regulates the expression of G1/S-specific CycE and diap1, thereby promoting cell proliferation and inhibiting apoptosis. Required for transcriptional activity of sd in wing imaginal disks. Induces expression of expression of vestigial (vg) in wing and haltere disks and the expression of transcription factor E2f (E2f).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18256197, ECO:0000269|PubMed:18313299, ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:22615583, ECO:0000269|PubMed:26954546}. Nucleus {ECO:0000269|PubMed:18256197, ECO:0000269|PubMed:18313299, ECO:0000269|PubMed:19900439, ECO:0000269|PubMed:31857346}. Note=Predominantly cytoplasmic (PubMed:18256197, PubMed:18313299, PubMed:19900439). sd promotes its nuclear localization (PubMed:18313299). 14-3-3epsilon, 14-3-3zeta and wts inhibit its nuclear localization (PubMed:18256197, PubMed:19900439). {ECO:0000269|PubMed:18256197, ECO:0000269|PubMed:18313299, ECO:0000269|PubMed:19900439}.
Interaction partners:
- Serine/threonine-protein kinase Warts
- Scalloped, isoform Q
- Serine/threonine-protein kinase hippo
- Protein expanded
- Scaffold protein salvador
- Homeobox protein homothorax
- MOB kinase activator-like 1
- Tondu-domain-containing growth inhibitor, isoform A
- Protein mothers against dpp
- Segment polarity protein dishevelled
Sequence:
MLTTMSASSNTNSLIEKEIDDEDMLSPIKSNNLVVRVNQDTDDNLQALFDSVLNPGDAKRPLQLPLRMRKLPNSFFTPPAPSHSRANSADSTYDAGSQSSINIGNKASIVQQPDGQSPIAAIPQLQIQPSPQHSRLAIHHSRARSSPASLQQNYNVRARSDAAAANNPNANPSSQQQPAGPTFPENSAQEFPSGAPASSAIDLDAMNTCMSQDIPMSMQTVHKKQRSYDVISPIQLNRQLGALPPGWEQAKTNDGQIYYLNHTTKSTQWEDPRIQYRQQQQILMAERIKQNDVLQTTKQTTTSTIANNLGPLPDGWEQAVTESGDLYFINHIDRTTSWNDPRMQSGLSVLDCPDNLVSSLQIEDNLCSNLFNDAQAIVNPPSSHKPDDLEWYKIN
Protein: AopB (Q6TLM0)
Organism: Aeromonas hydrophila
Subcellular location: Host membrane {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}.
Interaction partners:
Sequence:
MHSISSERPLSIGGMQPPLVEDSKGSSQATQVAAGDSHRHVEKHGQGVVLPQPMPGIGQQMSPPKQQELDQLRKTAQLGTANAAKLLGSSTLLNKLAFASPEEFEIELSKMTSELEQTQKKLKLADLERIRAENLKKIDENQTKMKEASEAADKAKKSGLASKIFGWISAIASMVIGAILIATGVGAAVGAMMIVGGAVGVANMAIQQAAADGRISPETMKVLGPIMIAAEILVAIVSIAVTFGASAASTAMKAVKFATQAADLVVDIGTGTAKAVDGGLQADAQIKQANLLENRQVMTELQGVMDKLKEVLSQMTESFQQVMEMIFQMITAKGAMLNSLASRPTAI
Protein: V-type proton ATPase subunit C (Q388J5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- H
- ATP synthase, putative
- Vacuolar ATP synthase subunit D, putative
- V-type proton ATPase subunit
- V-type ATPase, C subunit, putative
- 
- V-type proton ATPase subunit F
- V-type proton ATPase subunit a
- Vacuolar proton pump subunit B
Sequence:
MSEHFLLLGLPFLPTGADSFAFQYKNLVSLLGAAGKDVCSFAVPNFKVGTLDSLIEASDELAKLDLQVENSLEKQITIMQEICEEPRDVVATLRFNQTQEMTPAAFVKGFQWSSAQFDSNESILGLVEKFANYFATTEEGVRLVMTKYNETRNKLTTVTRKAQGNLSVKPIRELVTMKNRSHPFIVDTELLTNLFVAVPLSSKREWLNEYWSLNDFVCPDSNCIIAEDSEFVLNSIVVFRRVLEDVKLACRKRRYIVRDSDAADEPSIRDLNDFIKRAESEKKNFGLVLRQRYTGCYVAWVHLKAVRLFVESLLKYGLPPRCISIFLQVDKRKEAEIRKKISQLYPDLSVPFSNTSSVEDGSLQYEYPYVSIKMTNLQRC
Protein: Protein IQ-DOMAIN 8 (AtIQD8) (Q9CAI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Note=Recruits calmodulin (CaM2) to microtubules. {ECO:0000269|PubMed:28115582}.
Interaction partners:
Sequence:
MGGSGNWIKSLITNKKNITDDQEKNIKKKWKLWRTSSEGLISSSKGFKSRGGSYGTPSLGSDPPSFSADDSFTAAVAAVIRAPPKDFFLVKREWAATRIQAAFRAFLARQALRALKAVVRIQAIFRGRQVRKQADVTLRCMQALVRVQARVRAHCNRGPSDGQELEKPSDQQKDDPAKQAEKGWCDSPGSINEVRTKLQMRQEGAIKRERAMVYALTHQPRTCPSPAKASKQGSVKKNNGSCKSSPGWNWLDRWVADRPWEGRLMEGPTNSSENARKSESSVSEHDTVQVRKNNLTTRVLARPPPMSSSATSSESSSTSQSPVPFSGSFLEEGGYYRKPSYMSLTQSIKAKQRRSGSSSSCSKTPFEKKQSMSYNGDVNVRRSAGSDPLNNQWTDLYPPAQVTGRHMWAKSQRG
Protein: Plagl2 protein (Q8CFT9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTFFTSVPPWIQDAKQEEEVGWKLVPRPRGREAESQVKCQCEISGTPFSNGEKLRPHSLPHPEQRPYSCPQLHCGKAFASKYKLYRHMATHSAQKPHQCMYCDKMFHRKDHLRNHLQTHDPNKEALHCSECGKNYNTKLGYRRHLAMHAASSGDLSCNLDFLQVHHDTFVLLNWRGEEMKGIPYQPFPQSLTPPWTS
Protein: Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 (E-NPP 7) (NPP-7) (EC 3.1.4.12) (Alkaline sphingomyelin phosphodiesterase) (Intestinal alkaline sphingomyelinase) (Alk-SMase) (Q6UWV6)
Organism: Homo sapiens (Human)
Function: Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract. Has also phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation. Does not have nucleotide pyrophosphatase activity. May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:15205117}; Single-pass type I membrane protein {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:15205117}. Note=The catalytic domain is released into the extracellular medium when cells are treated with trypsin (PubMed:15205117). Localized at the surface of the microvillar membrane in small intestine enterocytes, and in endosome-like structures situated beneath the microvillar membrane, and in Golgi complex (PubMed:12671034, PubMed:12885774). {ECO:0000269|PubMed:12671034, ECO:0000269|PubMed:12885774, ECO:0000269|PubMed:15205117}.
Interaction partners:
- Sphingomyelin phosphodiesterase
- Sphingomyelin phosphodiesterase 2
- Sphingomyelin phosphodiesterase 4
- Sphingomyelin phosphodiesterase 3
- Ceramide synthase 6
- Ceramide synthase 4
- Ceramide kinase
- Ceramide synthase 5
- Sphingolipid delta
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
Sequence:
MRGPAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARDGVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWDNGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVMAWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLNLIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDALKDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDMDMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALPPDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA
Protein: Histone H3.3 type b (Histone 3, variant 3 type b) (Q55BN9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome. Note=Associated with pericentromeric heterochromatin.
Interaction partners:
- Histone H4
- Histone-lysine N-methyltransferase set1
- Histone H2B.v3
- Histone H2A.z
- VWFA domain-containing protein
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- PHD zinc finger-containing protein
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase qkgA
Sequence:
MARTKQTARKSTGAKVPRKHLGNKSSQKSFPSTQGLKKTHRFRPGTVALREIRRYQKSSELLIKKLPFQRLVREIAQEFKTDLRFQAAAIQALQEASEAYLVGLFEDTNLCAIHAKRVTIMVKDIQLARRIRGERA
Protein: Tetraspanin 68C, isoform A (Tetraspanin 68C, isoform C) (Q8IQK9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 1
- Elongator complex protein 5
- Elongator complex protein 2
- U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein
- Elongator complex protein 6
Sequence:
MACCFNYKFVLNLCNFLFLICGLLLVVSGLYIFSDNKRILLSRLLAASSDRLSSLPQPLLFYIALGVAIAGFVATLAAVVGFWASCLHTYCFLTIYFLSVVVLLLTESVLCLAITLWPHCLGISLDETQMVRSLQSNYGVPGQEQFTNALDLAQVRFGCCGMRSSLDYDTSLWRLQGYGQRNWPVPLSCCFLKNAGHSMAYLDPKPANESMCQSLERLSYERERHTESCLPHLDNWYREQYSIFLGASLILAMIEFCVLLAIIMSCTGLASQRARLKKPVQEMRTQKVKSRQTLIENIYEPDVELRENSNHSGDGIYLGPASRHVSSEDFKELYIKPRDLYKQHNLRTSPANRPTQMRNYLV
Protein: RE29964p (Ral guanine nucleotide dissociation stimulator-like, isoform B) (Ral guanine nucleotide dissociation stimulator-like, isoform C) (Ral guanine nucleotide dissociation stimulator-like, isoform D) (Q86BI2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSQNVADSLPTWRLWGEEHEKNAIFTVYLKKVRYHRPTPTASNDSDDEISHLEWETVRVRFVKAATLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRYDALHEKHLEELEQAQQNGQVMDPAYDPHASIHEQHKKTLVSALHVWLDGFPEDWHEDNLQQILAFATKRLKRSDLHIKVLNRLERLIKQSLYGNGGGSGGSENNGHSWLSAARSQQMQQFMIPTHYGSSYDLTDQFNGMYLSPMGHGPIYRGPTHFLQAFRFPHVPVRHFAEQLTRMDTELFKRLIPHQCLGHTWARRDSGGSETVVATINQFNAVLFRVVSSILIDRLKPQERALNISRWIDIAQELRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKREGTAKNPDPGSDHSDRHLQKLILNLGTQTSHGTIPYLGTFLTDLTMIHTANPDYLTENKLINFDKKRKEFEVLAQIKLLQGAANTYNLQADALFDHWFNSMPVFDEREAFELSCRLEPPPPAPRKSVVSTNTSLTNTTASSTASIMGHRKTDSIHSNSSSGAGSQFYCELNSSTSSRHNSLDRDVHHQHASLMSASSSVSNLSLDSSNSGGRQSGKLTHSQSMGNGLKSHGNGTTNGGSPHINAQLVQPSSGTPHSAPDFYIIRVTYETDNIELDGIVLYKSIMLGNNERTPQVIRNAMLKLGLEDDPDRFTLAQVLPDKELVMPKNANVYYAVNTNYNLNFILRPRKEEGVAGS
Protein: Tripartite motif-containing protein 3 (EC 2.3.2.27) (Brain-expressed RING finger protein) (RING finger protein 22) (O70277)
Organism: Rattus norvegicus (Rat)
Function: Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Positively regulates motility of microtubule-dependent motor protein KIF21B.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O75382}. Early endosome {ECO:0000250|UniProtKB:O75382}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9R1R2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9R1R2}. Note=Mainly located in the Golgi apparatus and transported to the early endosomes upon stimulation with dsRNA. {ECO:0000250|UniProtKB:O75382}.
Interaction partners:
- Polyubiquitin-C
Sequence:
MAKREDSPGPEVQPMDKQFLVCSICLDRYRCPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPDGAHDPEDPHPLSAVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSAAAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELCAEITGPDGMRLAVPVVDHKNGTYELVYTARTEGDLLLSVLLYGQPVRGSPFRVRALRPGDLPPSPDDVKRRVKSPGGPGSHVRQKAVRRPSSMYSTGGKRKDNPIVDELVFRVGSRGREKGEFTNLHPLSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ
Protein: Photoreceptor disk component PRCD (Progressive rod-cone degeneration protein) (E1B7R9)
Organism: Bos taurus (Bovine)
Function: Involved in vision.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:23672200, ECO:0000269|PubMed:27509380}. Membrane {ECO:0000269|PubMed:27509380}; Lipid-anchor {ECO:0000269|PubMed:27509380}; Cytoplasmic side {ECO:0000269|PubMed:27509380}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q00LT1}. Golgi apparatus {ECO:0000250|UniProtKB:Q00LT1}. Note=Localizes to photoreceptor disk membranes in the photoreceptor outer segment. {ECO:0000269|PubMed:27509380}.
Interaction partners:
Sequence:
MCTTLFLLSTLAMLWRRRFANRVQPEPNGVDGAVSGSSLETDLQSSGREKEPLK
Protein: Thermostable carboxypeptidase 1 (EC 3.4.17.19) (Carboxypeptidase Pfu) (PfuCP) (Q8U3L0)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.
Interaction partners:
Sequence:
MEEVFQNETIKQILAKYRRIWAIGHAQSVLGWDLEVNMPKEGILERSVAQGELSVLSHELLLHPEFVNLVEKAKGLENLNEYERGIVRVLDRSIRIARAFPPEFIREVSETTSLATKAWEEAKAKDDFSKFEPWLDKIISLAKRAAEYLGYEEEPYDALLDLYEEGLRTRDVEKMFEVLEKKLKPLLDKILEEGKVPREHPLEKEKYEREWMERVNLWILQKFGFPLGTRARLDVSAHPFTTEFGIRDVRITTRYEGYDFRRTILSTVHEFGHALYELQQDERFMFTPIAGGVSLGIHESQSRFWENIIGRSKEFVELIYPVLKENLPFMSNYTPEDVYLYFNIVRPDFIRTEADVVTYNFHILLRFKLERLMVSEEIKAKDLPEMWNDEMERLLGIRPRKYSEGILQDIHWAHGSIGYFPTYTIGTLLSAQLYYHIKKDIPDFEEKVAKAEFDPIKAWLREKIHRWGSIYPPKELLKKAIGEDMDAEYFVRWVKEKYL