wanglab/gogpt-training-data huggingface dataset:
Protein: Trehalase (EC 3.2.1.28) (Alpha-trehalose glucohydrolase) (A0A1D8PRR3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Trehalose-phosphatase
- Trehalose 6-phosphate synthase/phosphatase complex subunit
- Alpha,alpha-trehalose-phosphate synthase
- Cell wall acid trehalase ATC1
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- Peroxisomal catalase
- 1,4-alpha-glucan-branching enzyme
- phosphoglucomutase
- Alpha-1,4 glucan phosphorylase
Sequence:
MFTKNHRRMSSTSSDDDPFDVAEKYYGEERKKKLNRVRTFSAFESTKYGAGPISPLRPTYEPPPVIKETSEPLSSSSSTSSPPTLTPQTSQVQFNLGVGKTKNGSAIHSDSEEEEEDEDPVSNTKKGEADEKDPFDTTDSKLENENSTPSSITGKEIIPHPTGFRGSSEESAIRRKPSIIPIYHDNISQESVIRNANTPTTYNREKFHLRRGSLDESTFIRPKKYYINDVQGTLRELLANEDTDNNCQITIEDTGPKVLRLGTANSLGINQSSIRGTYRLSNLLQELTIASRFGRHQIVLDEARLSENPVDRMKRLISTSFWNNLTRIITKENIVDMAKDTKIKESWIDDQGKLHENQESHRIYVPYNRKDQYEFFQLIKKQRSDIQLDVQYLPQKIDADYIKSINKKPGLLSIATRPDPQAPDSGSLISWPYVVPGGRFNELYGWDSYMETLGLLTDVKIDPSGNPRNLRHLELARGMAENFIYEIHHYGKILNANRSYYLGRSQPPFLTDMALRIFNKTIEVTPELMDEAIDFLKRATLAAIKEYETIWCAHPRLDDKTGLSCYHPEGKGIPPETEPTHFNALLKPYLAKYNDIDQLDFIEKYNSGEIKEPELDEYFLHDRAVRESGHDTSYRLEGKCAYLATVDLNSLLYKYENDIAFILQSFFNDNLQDPYDDNNSYKIHSSKIWLERSHQRKLNVDKYLWNEQDGIYYDYNVKLQQQTNYESATTFWPLYAKLASSNQAAKLIDQSLHKFEEHGGLVAGTLKSRGEVGLTRPSRQWDYPFGWAPQQILAWIGLVNYGYDGIARRLAYRWLFMMTKSFVDYNGVIVEKYNVTKGAVPHRVDAEYGNQGLDFKGVATEGFGWVNASYVFGLTFLNLYAQRALGSLTPPEIFLRNMHPEQRKQYK
Protein: Proteasome subunit alpha type-5-A (20S proteasome alpha subunit E-1) (O81149)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-2-B
- 26S proteasome regulatory subunit 6B homolog
- Proteasome subunit beta type-1
- Proteasome subunit beta type-4
- Proteasome subunit beta type-6
- Proteasome subunit beta type-3-B
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3-A
- Proteasome subunit alpha type-6-A
- Proteasome subunit beta type-7-B
Sequence:
MFLTRTEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGVKTKEGVVLAVEKRITSPLLEPSSVEKIMEIDDHIGCAMSGLIADARTLVEHARVETQNHRFSYGEPMTVESTTQALCDLALRFGEGEEESMSRPFGVSLLIAGHDENGPSLYYTDPSGTFWQCNAKAIGSGSEGADSSLQEQFNKDLSLQEAETIAVSILKQVMEEKVTPNNVDIAKVAPAYHLYTPQEVEAVIARL
Protein: Kazrin (Q674X7)
Organism: Homo sapiens (Human)
Function: Component of the cornified envelope of keratinocytes. May be involved in the interplay between adherens junctions and desmosomes. The function in the nucleus is not known.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Cell junction, desmosome. Nucleus. Note=Observed at the apical plasma membrane of keratinocytes. Partially colocalizes with PPL and DP at desmosomes, and with PP at the interdesmosomal plasma membrane. Colocalizes with cortical actin-based membrane structures.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Cell junction, desmosome. Nucleus. Note=Observed at the apical plasma membrane of keratinocytes. Partially colocalizes with PPL and DP at desmosomes, and with PP at the interdesmosomal plasma membrane. Colocalizes with cortical actin-based membrane structures.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Cell junction, desmosome. Nucleus. Note=Observed at the apical plasma membrane of keratinocytes. Partially colocalizes with PPL and DP at desmosomes, and with PP at the interdesmosomal plasma membrane. Colocalizes with cortical actin-based membrane structures.
Interaction partners:
- Periplakin
- Rho GTPase-activating protein 5
Sequence:
MMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELSGGGGPGPGPGAAASASAAGDSAATNMENPQLGAQVLLREEVSRLQEEVHLLRQMKEMLAKDLEESQGGKSSEVLSATELRVQLAQKEQELARAKEALQAMKADRKRLKGEKTDLVSQMQQLYATLESREEQLRDFIRNYEQHRKESEDAVKALAKEKDLLEREKWELRRQAKEATDHATALRSQLDLKDNRMKELEAELAMAKQSLATLTKDVPKRHSLAMPGETVLNGNQEWVVQADLPLTAAIRQSQQTLYHSHPPHPADRQAVRVSPCHSRQPSVISDASAAEGDRSSTPSDINSPRHRTHSLCNGDSPGPVQKNLHNPIVQSLEDLEDQKRKKKKEKMGFGSISRVFARGKQRKSLDPGLFDDSDSQCSPTRQSLSLSEGEEQMDRLQQVELVRTTPMSHWKAGTVQAWLEVVMAMPMYVKACTENVKSGKVLLSLSDEDLQLGLGVCSSLHRRKLRLAIEDYRDAEAGRSLSKAAELDHHWVAKAWLNDIGLSQYSQAFQNHLVDGRMLNSLMKRDLEKHLNVSKKFHQVSILLGIELLYQVNFSREALQERRARCETQNIDPVVWTNQRVLKWVRDIDLKEYADNLTNSGVHGAVLVLEPTFNAEAMATALGIPSGKHILRRHLAEEMSAVFHPANSTGIREAERFGTPPGRASSVTRAGKEENSSGLKYKAGRLPLGKIGRGFSSKDPDFHDDYGSLQNEDCGDDDPQSRLEQCRLEGYNSLEVTNV
Protein: UDP-glucuronosyltransferase 1A7 (UGT1A7) (EC 2.4.1.17) (A2) (UDP-glucuronosyltransferase 1-7) (UDPGT 1-7) (UGT1*7) (UGT1-07) (UGT1.7) (UDP-glucuronosyltransferase 1A7C) (Q64633)
Organism: Rattus norvegicus (Rat)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormone epiestradiol. Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist caderastan, a drug which can inhibit the effect of angiotensin II. Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9HAW7}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAPADVPASLPLGLCLLLASGFGHAGKLLVVPMDGSHWFTMQMVVEKLLPKGHEVVVVVPEVSWQLGKPLNFTVKTYSVSHTQEDLNREFKFFIDSQWKTQQESGVLPLLTSPAQGFFELLFSHCRSLFKDKKLVEYLKQSSFDAVFLDPFDVCGLTVAKYFSLPSVVFSRGIFCHYLEEGSQCPSPPSYVPRPILKLTDTMTFKERVWNLLSYMGEHAFCPSFFKTATDIASEVLQTPVTMTDLFSPVSVWLLRTDFTLELPRPVMPNVIHIGGINCHQRKPVSKEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAEALGRIPQTLLWRYTGTRPSNLAKNTILVKWLPQNDLLGHPKARAFITHSGSHGIYEGICNGVPMVMMPLFGDQMDNAKRMETRGAGVTLNVLEMTADDLENALKTVINNKSYKENIMRLSSLHKDRPIEPLDLAVFWVEYVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAIVLTVVFIVYKSCAYGCRKCFGGKGRVKKSHKSKTH
Protein: Myelin basic protein (MBP) (P81558)
Organism: Sus scrofa (Pig)
Function: Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity).
Subcellular location: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
Interaction partners:
- Myelin-associated glycoprotein
- Myelin-oligodendrocyte glycoprotein
- Myelin proteolipid protein
- Glial fibrillary acidic protein
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- Oligodendrocyte transcription factor 2
- Transcription factor SOX-10
- Calmodulin like 5
- Uncharacterized protein.
- Lactoperoxidase
Sequence:
ASQKRPSQRHGSKYLASASTMDHARHGFLPRHRDTGIDSLGRFFGADRGAPKRGSGKDGHHAARTTHYGSLPQKAQHGRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRAPDYKPAHKGLKGAQDAQGTLSKIFKLGGRDSRSGSPMARR
Protein: Protein CRT10 (Constitutive RNR transcription regulator 10) (Q08226)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-CRT10). RTT101(MMS1-CRT10) may regulate nucleotide synthesis through transcriptional regulation of RNR genes encoding ribonucleotide reductases.
Interaction partners:
- DNA repair protein RAD1
- DNA repair protein RAD9
- DNA damage checkpoint control protein RAD17
- Cullin-8
- DNA damage checkpoint protein 1
Sequence:
MPPQIPNENDDLFTRWLKSRAIIQRAVSTRECFDSEVFLASGGWNITNEIITLKKYYQLKWPNSSCNSFHPKTVEFIKERLHNLEEHDSSWKIPNPAYSFKKAFLEDTKSAFSNLEPVWGPSRLLNPAELLLPQDEKLLVQEIPLEFAPFQYTNRFAYGGLQFKNNLFVTYGSYSFLAAGQCVEVHNFDILLNVSSLEICHALLPVIIPDDGDVRNFRNSSYVKFKDTQFNSIPELCSINFMKICNFMHQDFLLACGDNGIVYIWEINKVIKIFNKFTSDILGGKDNSRERYINVDPYMVLRVEESCWSVDVIDINGIIYIAVGHNKPGVTVFAFDKDVKKERRYIRPLDLPSSHNVPCVNFVPNSKDSVGYITLSYCSIFGNVVTVKLKEHDCTILTSFLDTQFFGDDLWTITPLTKKDFAKVDNFELLNLNYQDGFKESMLYSICRDDFLLGYYCDNAYLSGNFGIGTLLNQFQVPVTDLRLTSSAGIPDEVIPLRFTSFDRNYTTTGSIKYEYSREDFALILHAGDLDDMNDAVTKNTSCEQHLHQWTFWEDSGYKHYRATERGFSKYKDIINTFPQLITPSGRNKTSQYQNTSGRKICEPSTYKLTDLENDIEDISREFNRSIRNLKMDKQRQLRTSKEFKSLSSVNHIPNIESGNFLWYNTDAAADWRTLFGKDLNTVLKDPEICSLQLNSTEEDDVNSDPENEESGSSLTSFQRRYRDTEQRAHLKSESQKSWGFHNYVRNVKRLLESAVPGSEDSPLGYQLSEMHDEFFFLTTAHRLVLMKANPLIIISATHHEIFPLDGVVTCASKSLLQALNRINFVCHIKELNCIAVASQLGLISLLRLTEYRGIYSFRQEYILGWEVQDPVNPSPECRCNRNLFDAPMYGADGESSDTYCGVCDVYFPMGDICGLDYTYASDSEELKRKGYATLYVASRGSLRAFKITTEHGTTQQ
Protein: Reticulon-like protein B4 (AtRTNLB4) (VirB2-interacting protein 3) (Q9FFS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in the Agrobacterium-mediated plant transformation via its interaction with VirB2, the major component of the T-pilus.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17604024}; Multi-pass membrane protein {ECO:0000269|PubMed:17604024}.
Interaction partners:
- Reticulon-like protein B21
- Reticulon-like protein B18
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- Protein VACUOLELESS GAMETOPHYTES
- Ras-related protein RABE1a
Sequence:
MVEDHKHEESILEKIVEKIHGHGDSSSLSDSDDDKKSTSSSSSSFKSKIYRLFGREKPVHKVLGGGKPADIFLWRNKKVSGGVLGAVTASWVLFELFEYHLLAFLCHFAIFALAALFLWSNACTFIHKSTPHIPEVHIPEDPILQLVSGLRIEINRGLTLLRNIASGKDVKKFILVIAGLWVLSIIGSCYNFLTLFYTATVLLFTIPVLYEKYEDKVDAYGEKAMREIKKQYAVLDEKVLRKVISKIPRGALNKKKD
Protein: Phosphoprotein (Q77M42)
Organism: Measles virus (strain Edmonston-Moraten vaccine) (MeV) (Subacute sclerose panencephalitis virus)
Interaction partners:
Sequence:
MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTDARLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPECVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK
Protein: Myeloperoxidase (MPO) (EC 1.11.2.2) [Cleaved into: Myeloperoxidase light chain; Myeloperoxidase heavy chain] (P11247)
Organism: Mus musculus (Mouse)
Function: Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity. Mediates the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low density lipoprotein particles and limits vascular damage (By similarity).
Subcellular location: Lysosome.
Interaction partners:
- Neutrophil elastase
- Cathepsin G
- Myeloblastin
- Lactotransferrin
- Cathepsin S
- Runt-related transcription factor 1
- Matrix metalloproteinase-9
- Bactericidal permeability-increasing protein
- Membrane-spanning 4-domains subfamily A member 3
- Carboxylesterase 1D
Sequence:
MKLLLALAGLLAPLAMLQTSNGATPALLGEVENSVVLSCMEEAKQLVDRAYKERRESIKRSLQSGSASPTELLFYFKQPVAGTRTAVRAADYLHVALDLLKRKLQPLWPRPFNVTDVLTPAQLNLLSVSSGCAYQDVRVTCPPNDKYRTITGHCNNRRSPTLGASNRAFVRWLPAEYEDGVSMPFGWTPGVNRNGFKVPLARQVSNAIVRFPNDQLTKDQERALMFMQWGQFLDHDITLTPEPATRFSFFTGLNCETSCLQQPPCFPLKIPPNDPRIKNQKDCIPFFRSCPACTRNNITIRNQINALTSFVDASGVYGSEDPLARKLRNLTNQLGLLAINTRFQDNGRALMPFDSLHDDPCLLTNRSARIPCFLAGDMRSSEMPELTSMHTLFVREHNRLATQLKRLNPRWNGEKLYQEARKIVGAMVQIITYRDYLPLVLGPAAMKKYLPQYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLNNQYRPTGPNPRVPLSKVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIVVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPSTVGELGTVLKNLELARKLMAQYGTPNNIDIWMGGVSEPLEPNGRVGQLLACLIGTQFRKLRDGDRFWWENPGVFSKQQRQALASISLPRIICDNTGITTVSKNNIFMSNTYPRDFVSCNTLPKLNLTSWKET
Protein: TMAO-responsive two component signal transduction system response regulator TorR (Q8EHJ3)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Interaction partners:
- histidine kinase
- Sensory/regulatory protein RpfC
- Periplasmic component of the TorRS TMAO sensory system TorT
- Sensory/regulatory protein RpfC
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MAYSVLVVDDEVVIRARLKGYFEKEGYRVVEAADGEQMWYEFNRQHIDLIMLDINLPGVDGLSLTRELRSRSHVGIILVSGRDESIDKIVGLEMGADDYVTKPFELRELLVRVKNLLWRISLVKQAEQALVQELSQPDDLISFEGYQLELNSRKLRQGEELIKLTKAEFELLTVFVLHPQQVLSRERLMQQTSHRNQDVNDRTIDVIIRRLRNKLHAELFVTVHGEGYLFAAKVDD
Protein: mRNA export factor GLE1 (GLE1 RNA export mediator) (GLE1-like protein) (Nucleoporin GLE1) (Q6DRB1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. May be involved in the terminal step of the mRNA transport through the nuclear pore complex (NPC) (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q53GS7}. Cytoplasm {ECO:0000250|UniProtKB:Q53GS7}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q53GS7}.
Interaction partners:
- mRNA export factor
- Nucleoporin 214.
- Nucleoporin 155.
- Nuclear pore complex protein
- Nuclear pore complex protein Nup133
- Nuclear pore complex protein Nup153
- Nucleoporin 88
- DEAD/H
- Zgc:193690.
- Nucleoporin 205.
Sequence:
MPSENLRWETLEALKNSPKGKLKYSPDWVEKGEDVLAGCVEVPSLSPLSGQILKRMSPRMLLKNCSRSSSVRDTSPGLSEEAAVCRSAPISPRLKRSSCSLPAVSIQTEEEEEKEEEEKAEVVVEAPAVSPEASVSTPPAVSVLSPRATQISGCIRMCEQKHKAKAKMELSLRQEQQERLVATVANHESEQLKRFEEFMELKQRQEHQSIRDTNEKEAQESLGRQEKLREEHRHRMKILNLRLREMEQQRLREVELERQRQVEGRERHRAINAIQEEVLQLNRLLQPQQSTHAEVEHAPYITRGNQLCSQLSEVVPAAADDQFPSVEDLSVAERALQEMRSLVRSLQEAVSQAAERKKKKEQEEEEEKRRQEQLKAQQEEQKKSAALSAKEKAKKEGLQTGADDSTLKWYNSLQDLANQCAQAFDDLNKAKDTQTKKLKMELQKAATTPVSQIANSSGAPLKEAFEKIDKLLSRRPVTSAGKTVSTSQHPQGLEFASYRLAEKFVKQGEEEVASNHSAAFPIGAVASGIWELHPKIGDLILAHLHKKCPYAVPHYPPMESGTSVEDYQKILGYRVDEGKVEGQDSFLKRMSGMIRLYAAIIQMRWPYSSKQGLHLHGMNHGWRWMAQILNMEPLADITATILFDFLEVCGNALMKQYRVQFWKLILIINEEYFPRYLCFASILHFTCIHWLQNIE
Protein: Os08g0471401 protein (A0A0P0XGL9)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEFDMLNSNPEAQLELMNTMLQLEQLSAFPDHHGMVVPCSPTSPCMGAQGGHHHFSSVNHQPAHGVVSSGGANTGDGYRDQYYTQLLPAAAYSNAAGGGRGSEYHTTTTTRPASGGGGDGGVGPAAMREMIFHIAALQPVNIDPETVRPPKRRNVRISTDPQSVAARMRRERISERIRILQRLVPGGTKMDTASMLDEAIHYVKFLKTQVQSLERAAAANGHRPPPPTATSAAAATVAYPGLNGQW
Protein: Ubiquitin thioesterase OTUB2 (EC 3.4.19.12) (Deubiquitinating enzyme OTUB2) (OTU domain-containing ubiquitin aldehyde-binding protein 2) (Otubain-2) (Ubiquitin-specific-processing protease OTUB2) (Q96DC9)
Organism: Homo sapiens (Human)
Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- TNF receptor-associated factor 6
- Ubiquitin-conjugating enzyme E2 N
- E3 ubiquitin-protein ligase RNF128
- Zinc finger-containing ubiquitin peptidase 1
- TNF receptor-associated factor 3
- Ubiquitin-conjugating enzyme E2 D1
Sequence:
MSETSFNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDGNCFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMDTALNHHVFPEAATPSVYLLYKTSHYNILYAADKH
Protein: ORF39 (Q4JQT6)
Organism: Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3)
Subcellular location: Host Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004252}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004252}. Host nucleus membrane {ECO:0000256|ARBA:ARBA00004634}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004634}. Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MNPPQARVSEQTKDLLSVMVNQHPEEDAKVCKSSDNSPLYNTMVMLSYGGDTDLLLSSACTRTSTVNRSAFTQHSVFYIISTVLIQPICCIFFFFYYKATRCMLLFTAGLLLTILHHFRLIIMLLCVYRNIRSDLLPLSTSQQLLLGIIVVTRTMLFCITAYYTLFIDTRVFFLITGHLQSEVIFPDSVSKILPVSWGPSPAVLLVXAAVIYAMDCLVDTVSFIGPRVWVRVMLKTSISF
Protein: Non-centrosomal microtubule array protein 1 (G5EEK3)
Organism: Caenorhabditis elegans
Function: Plays a role in the assembly of microtubule arrays in the germline acting redundantly with ptrn-1 to control circumferential microtubule assembly along the body which is necessary for larval development, viability, and morphology and integrity of the epidermis. Required for microtubule stability and anchorage by binding to microtubule minus ends. Recruited to hemidesomosomes in early embryonic elongation to direct the nucleation and growth of non-centrosomal microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26371552}. Apical cell membrane {ECO:0000269|PubMed:26371552}. Cell junction, hemidesmosome {ECO:0000269|PubMed:26586219}. Cell junction, adherens junction {ECO:0000269|PubMed:26586219}. Note=Isoform h: Co-localizes with gamma-tubulin to the apical cell membrane. {ECO:0000269|PubMed:26371552}.
Interaction partners:
- Patronin
- Gamma-tubulin complex component
- Gamma-tubulin interacting protein 2
- Tubulin gamma chain
- Spastin homolog
- Zygote defective protein 9
Sequence:
MSNERVSTGSLGERLMLRTRSTRGSVRETLSKAIRSTLGRASSMERKDMPDRPKYGTALTAMTSTTPPSPKDRSSDSGDGDSPRPRKFSSKECARIYFSNTSSEHSSRSNSSTPRRVRHTTASSGYGSLSHLPPISYRKSSDPLNSLMSQSMYVQSPGMHIDEPKCTSLSQRRLYYEDSSETYIPSSPSLTTLKDFMMTNDDETFDDFDFDNDDVKSVISSASTSRIFSVDNRMSKYQKNQSLRQFLNSPVRLRKRGDTSRRDAVEAGFEPRDTVPRCHSTQSLRDVQRVRSYNNSQFQASDLSLNPNGSIRAACDSTSGSVAPTAVVNPARNHVISHRQQHHTSYEKDLIPHHNIDVDRRRSLQALNGSSALYQLNNGGSPNGVRSQFSPSDLSIHTPVHHVGSRVRVSSVNQICDSNSAPQFSIDQRRSVHNIGNPVRNSFVDGIKTTSTPKNQIAVAPLAHKSRHLSESRDEMRGGAERRGSGGQMNLPAYTNYLIRHSGEERLVDGPVTNASDARIAYLEKRIRELELTQKEQSSHSTPSQSRHSSSKSSHFNGSSNLSTSEQLRLQEMSDELANKDRKVTSLESKLLKAYQRIERLNEEYDGKIKNLMYDSERARDDLTRCVDKIQQLENELDETRAAVQNGDHANEQEYHELRDKIWKQERELQESRTLLTRLREKEAEFERMRSEKGYLELKNENLNKKLEAKKRAVEELERSVSTLRLEQTICQQSCSSGSTPLADEMEIMSDIRPSLARPYTKAHSTLGSHNMSPLSHSKSSGLTKSFSNFALNSSKQRDDITANMSRSIREQNRHITMCRAMVVCLKDTVDRMARGENPDVARLLGVKLNVMSESEMEDDEDHEADASQPFSMMSAESALSKQCGKLADLDKDLDTIRCQLADWHGQTNAEGDGDRDVCRVQ
Protein: cDNA FLJ51842 (B7Z2P8)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MFLSSVGFSVVMMSIWPYLQKIDPTADTSFLAWVIASYSLGQMVASPIFGLWSNYRPRKEPLIVSILISVAANCLYAYLHIPASHNKYYMLVARGLLGIGAGNVAVVRSYTAGATSLQERTSSMANISMCQALGFILGPVFQTCFTFLGEKGVTWDVIKLQINMYTTPVLLSAFLGILNIILILAILREHRVDDSGRQCKSINFEEASTDEAQVPQGNIDQVAVVAINVLFFVTLFIFALFETIITPLTMDMYAWTQEQAVLYNGIILAALGVEAVVIFLGVKLLSKKIGERAILLGGLIVVWVGFFILLPWGNQFPKIQWEDLHNNSIPNTTFGEIIIGLWKSPMEDDNERPTGCSIEQAWCLYTPVIHLAQFLTSAVLIGLGYPVCNLMSYTLYSKILGPKPQGVYMGWLTASGSGARILGPMFISQVYAHWGPRWAFSLVCGIIVLTITLLGVVYKRLIALSVRYGRIQE
Protein: Col18a1 protein (Collagen type XVIII alpha 1 chain a precursor) (B0S8G5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MMAELRFWLCLFILACVRIRHTHGWFWFDDSKEIEKGVQTPAYLTTVGPTSLPRTEPSRTTEESGVSLLQLIGDPPPNGVSKVFDQANSPGYVFGPSSNVGQSAAAHLPNPFYRDFSLIFNIKPTSSKPGVIFSITDPTQNIMYVGVKLSAVERGKQSIIFYYTEPDSQSSYEAARFSVSSMLNIWTRFSISVLNEQVSLYFNCDSDPQVVNFERSPDDMDMDAGAGVFVGHASGADPDKFLGVIGDLRVSRDPGAAERHCEEEEDDYATEASGDYGASGDGEQPSPVQPTPPSSRPIQRPPVISRDPIQRPPVISREPIQQTVARGEKGDRGEKGAKGDRGLAGPKGDVGSGSVSGGGSKGDKGVPGEKGMKGTSGFGYPGSKGDRGPPGPPGPPGPQGPSAEVEVRGDGSVVQKVTGPRGPPGPQGPPGPPGPEGEPGDPGEDGKAGQVGPSGFPGNPGNPGPKGDKGDRGESQPGPRGPPGPPGPPGPSSGFDRPTFVDMEGSGFDMDSVRAVPGLPGPPGPPGPPGPPGSASSGSGGFGPPGPPGQNGAPGQPGLSGVPGADGKPGLPGPKGEKGDAGELGLPGPVGEKGAKGSSGPPGTTGIGGPAGLPGPIGPIGLPGPPGPPGPSFNVGFDDMEGSGVHFSSVPGVRGPVGIPGPPGVPGPQGQPGFPGLPGEKGSLGAQGNDGLPGADGFPGPQGPKGDKGERGDRGEPGRDGHGHPGQPGPPGPPGQIIYRYSEHYDEVGGTGAQGGSGVPGQAGFPGPMGPKGDRGEPGLPGYDIKGEKGEPGLILGPDGNPLYLGGLTGQKGERGISGPVGPPGPAGPPGAKGEFGMPGRPGRPGVNGYKGEKGEPSSGSGYGYPGPPGPPGPPGPPGPAVPLDRFGRYEDYARLYPATKGEKGDQGAPGIPGSPGFSTNFDIYSLKNEMKGERGESGLKGEKGEPGGGFYDPRFGAVQGPPGNPGPAGPKGDSIRGPPGPQGPPGTPGVGYDGRPGNPGPPGPPGPPGSPSLPGPYRPPLSIPGPPGPPGPPGIPGTGSGVTVLRSHDIMIATARRQTEGTLIYILDRNDLYLRVRDGVRQVMLGDYKPLYGELDNEVAAVQPPPVVHYSQDHTANNGAEQISPPHQPIDFPTREQENRNPNPQPDPRYPDPRYPPYTDNRYTDPVEPNIRYPVQPERNPITPARRPIPPVNQPGGHAHTHTSGPGLHLIALNSPQVGNMRGIRGADFMCFQQARAVGMKGTFRAFLSSKLQDLYSIVRRSDRETLPIVNLKDQVLFSSWESLFSDSESRMKDNAPIYSFDGRDVLRDSAWPEKMIWHGSDGRGHRQTDNYCETWRAGDRAVTGLASSLQAGQLLQQTSSSCSSSYIVLCIENSYMTQSKK
Protein: GH28656p (Q95SF7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQGNTRGKLDIIRNVNEISPQEFNDLFKINKNLNQEGVRYSFAPDGKGFLLNGDVQTTGAELRASVQHNQGGNVLGKVSQPIPGSHAGSGRLQLGGVNQVSRLIGPLPTSHPRQEPSTYAAGVFALELSSVLVGGVVFVLEKYGKIIFEHVINAESFESLINIMANKLDPKVFDHIMLLTRAFMDTMLEDLTSVLKFFISTESVLYRILLYILRNFEDVQLSVIADHTCEIVEAVRVYFMSLNPNAFPGLLQKCPKCIGHFSVCPL
Protein: Uncharacterized protein C1687.23c (Q9C118)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MWILEKKNIFFKIIHIKSSRKFDFSNAIRIVLLPFSSNCCRNSYTVNNGTFTGRQIYTSICKSRIPPCLKGKNGKTTKSESEPMSQKHLKYVKKYINKVRILKK
Protein: Phototropic-responsive NPH3 family protein NPY4 (MAB4/ENP/NPY1-like proten 4) (Protein NAKED PINS IN YUC MUTANTS 4) (O64814)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). May play an essential role in auxin-mediated organogenesis and in root gravitropic responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21490067}. Cytoplasm, cytosol {ECO:0000269|PubMed:21490067}. Note=Polar localization at the cell periphery almost identical to PIN proteins polarity, in the upper side of the plasma membrane towards the tips of cotyledon primordia in the protodermal cells and in root epidermis, and in the basal side of provascular cells, root stele, pericycle, endodermis and cortex, and in radicle tip cells (PubMed:21490067). Weakly observed in the cytosol of root tip quiescent center (QC) and columella cells, sometimes close to the basal side of the plasma membrane (PubMed:21490067). {ECO:0000269|PubMed:21490067}.
Interaction partners:
- Embryo defective 2423
- Calcium-binding EF-hand family protein
- Pathogenesis-related thaumatin superfamily protein
- At5g05960
- Thaumatin-like protein
- Protein PIN-LIKES 4
- Probable membrane-associated kinase regulator 6
- Protein DETOXIFICATION 40
- CRIB domain-containing protein RIC11
- At5g60530/muf9_180
Sequence:
MKFMKLGTKPDSFLSKGDNVRYVTNELETEIIIIIGNVKFYLHKFPLLSKSGFLQKHIATSKNEEEKKNQIDEIDISEIPGGSVAFEICVKFCYGITVTLNAYNVVAVRCAAEFLEMNETFEKSNLVYKIDVFLNSTIFRSWKDSIIVLQTTKDLLSDDSEELVKRCLGSIASTASIDTSKVKWSYTYNRKKKLEKVRKPEDGVPKDWWVEDLCELHIDLYKQAIKAIKNRGKVPSNVIGEALHAYAIRRIAGFSKESMQLIDRSLINTIIELLPDEKGNISSSFLTKLHRASIFLGCEETVKEKLKKRVSEQLEETTVNDILMYDLDMVQSLVKEFMNRDPKTHSKVSVAKLIDGYLAEKSRDPNLPLQNFLSLAETLSSFPRHSHDVLYRAIDMFLKEHSGISKSEKKRVCGLMDCRKLSAEACEHAVQNERLPMRVIVQVLFFEQIRANGSSTGYSTPELTTTTLNTEDDEWDHEKEF