wanglab/gogpt-training-data huggingface dataset:
Protein: Pickpocket 23 short form (Q86LG2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPQEKRHPPESRTQRFLETLVIFRRSLIYQTKEFFQNSTLHGVRYIAESGRPIGEKFMWFCFTSIGAVTALVIIMSLWEKFQTNPTITGLDTDFHNQNVVFPTTVVCPEAAFDHDKTYEKVYNTLANYDEAQAQMYTPFLRILTSLNFENVRDAKVLSQSIPQNLLDAHTIREWAFEGHIDCKNVFVSCKYRDEDIPCCDHFEPIYTEHGFCYAFNSRFKSTPTEDVKTGAPHDLYETDKKWALFFIPNSTSRIFIFSNEEYFGSDFNAQIDWSEPQLVEVRISKKNTYTTDDARQLSIGQRKCIFSDEVKLNYFPDAYTFSSCMKQCRMNKAIKLCKCNPPFYKPINVPMCSIKDFDCLDEFKSNITNIKDCLQCELSCSKTVFNIDKLIKMSDRPESLGVLVEFLTWPIIRYKREVLFGWVDLLVSFGGIASLFLGFSLLSGVEIIYYFTLRACCMVYKNRVNYANRIFQSTSI
Protein: Protein PTHB1 (Bardet-Biedl syndrome 9 protein) (Parathyroid hormone-responsive B1 gene protein) (Q3SYG4)
Organism: Homo sapiens (Human)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for proper BBSome complex assembly and its ciliary localization.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.
Interaction partners:
- BBSome complex member BBS1
- BBSome complex member BBS5
- Tetratricopeptide repeat protein 8
- BBSome complex member BBS4
- BBSome complex member BBS7
- BBSome complex member BBS2
- Leucine zipper transcription factor-like protein 1
- BBSome complex assembly protein BBS10
- Chaperonin-containing T-complex member BBS12
- Rab-3A-interacting protein
Sequence:
MSLFKARDWWSTILGDKEEFDQGCLCLANVDNSGNGQDKIIVGSFMGYLRIFSPHPAKTGDGAQAEDLLLEVDLRDPVLQVEVGKFVSGTEMLHLAVLHSRKLCVYSVSGTLGNVEHGNQCQMKLMYEHNLQRTACNMTYGSFGGVKGRDLICIQSMDGMLMVFEQESYAFGRFLPGFLLPGPLAYSSRTDSFLTVSSCQQVESYKYQVLAFATDADKRQETEQQKLGSGKRLVVDWTLNIGEQALDICIVSFNQSASSVFVLGERNFFCLKDNGQIRFMKKLDWSPSCFLPYCSVSEGTINTLIGNHNNMLHIYQDVTLKWATQLPHIPVAVRVGCLHDLKGVIVTLSDDGHLQCSYLGTDPSLFQAPNVQSRELNYDELDVEMKELQKIIKDVNKSQGVWPMTEREDDLNVSVVVSPNFDSVSQATDVEVGTDLVPSVTVKVTLQNRVILQKAKLSVYVQPPLELTCDQFTFEFMTPDLTRTVSFSVYLKRSYTPSELEGNAVVSYSRPTDRNPDGIPRVIQCKFRLPLKLICLPGQPSKTASHKITIDTNKSPVSLLSLFPGFASQSDDDQVNVMGFHFLGGARITVLASKTSQRYRIQSEQFEDLWLITNELILRLQEYFEKQGVKDFACSFSGSIPLQEYFELIDHHFELRINGEKLEELLSERAVQFRAIQRRLLARFKDKTPAPLQHLDTLLDGTYKQVIALADAVEENQGNLFQSFTRLKSATHLVILLIALWQKLSADQVAILEAAFLPLQEDTQELGWEETVDAAISHLLKTCLSKSSKEQALNLNSQLNIPKDTSQLKKHITLLCDRLSKGGRLCLSTDAAAPQTMVMPGGCTTIPESDLEERSVEQDSTELFTNHRHLTAETPRPEVSPLQGVSE
Protein: Ankyrin repeat domain-containing protein 1 (Cardiac adriamycin-responsive protein) (Cardiac ankyrin repeat protein) (Q8R560)
Organism: Rattus norvegicus (Rat)
Function: May play an important role in endothelial cell activation. May act as a nuclear transcription factor that negatively regulates the expression of cardiac genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:9043061, ECO:0000269|PubMed:9278441}.
Interaction partners:
- Titin
- Myopalladin
- CCN family member 1
- CCN family member 2
- Cysteine and glycine-rich protein 3
- Transcriptional coactivator YAP1
Sequence:
MMVFRVEELVTGKKNSNGSSGEFLPGEFRNGEYEAAVALEKQEDLKTLPANSVNLGEEQRKSEKVREAELKKKKLEQRSKLENLEDLEIIVQLKKRKKYKKTKVPVVKEPEPEIITEPVDVPRFLKAALENKLPVVEKFLSDKNSPDVCDEYKRTALHRACLEGHLAIVEKLMEAGAQIEFRDMLESTAIHWACRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLMTFGADLNVKNCAGKTPMDLVLHWQNGTKAIFDSLKENAYKNSRIATF
Protein: NGG1 interacting factor 3-like (Q384V6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTSLISRVARVMEEIAPLHLADRSWDNVGVLVESPMSNNSGVVVLTIDLTPEVMEECLRHNAEVIIAYHPPIFTPFKRLTLTDPKQKIILQTIRHGASIYSPHTSLDAVSGGINDWLASIVDARGRCYPIRPCEIYMQDKNCGKVDATVGIGRIVSLSGPKEIHTLVQDIKQGLGLPTVRVSLPSCWTGNTPVERVAICAGSGGSVFSGLKEHVDVLLAGEMGHHEVLAANAKGQAVILCEHSNTERGYLSSELLPKLKKAMGEEVSVITSTVDKDPLVVW
Protein: DNA/RNA-binding domain-containing protein (SMG-7) (G5EF47)
Organism: Caenorhabditis elegans
Interaction partners:
- Nonsense-mediated mRNA decay protein
- PIN domain-containing protein
- Nonsense-mediated mRNA decay factor SMG9
- Nonsense-mediated mRNA decay factor SMG8
- UPF3 domain-containing protein
- Telomerase reverse transcriptase
- Serine/threonine-protein kinase smg-1
- 5'-3' exoribonuclease 1
- Regulator of nonsense transcripts 1
- MIF4G domain-containing protein
Sequence:
MSDEWEQLTVELRKIPRGTEAAPQYLRHLMKMFVADFETAVSKRFDVKFWNKLKSMMDEITKAMENDRLVNHNVQNLAIGFLTDLSLLVHYHYEIPNYGNDISKQLTWTPDVFLNRKPIKSKKNSRVFMAYVLLRMGDLMRYKENYPKAQEYYEQSCRINPADGAVWNQLGLISSLGAKNLESVYFHTRALHATMEFPTASGGLTNIFKNFANRDISRPMPIKDLYLSCLGRIHFLLEIEDSSVHLQKIGEEAATSKEMIVPLMSVYKHLEDGTELEQRAVEYVKTIWCTAYRSLLKTLDDYKEESKKLADVPHLLHILALLLCAPKLLRGIEDQTEDEVTSICEWLLCANCDEKIKDSDAFGYFHCLQRIQYPLTRTQLAQKLVEIEDEDESKDSDQSTIPEEDQKSLSTDTSRIQNEDSEPESESESSDEEVLQRGRRRGRNPNLDESVETDEDEF
Protein: Aggression-stimulating peptide (LASP) (P84816)
Organism: Leptodactylus fallax (Mountain chicken frog) (Leptodactylus dominicensis)
Function: Stimulates aggressive behavior in male frogs. No effect on female frogs.
Subcellular location: Secreted {ECO:0000269|PubMed:15752573}.
Interaction partners:
Sequence:
GLWDDLKAAAKKVVSSLASAAIEKL
Protein: HTH OST-type domain-containing protein (Q4GYS2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial RNA binding protein
- Guide RNA binding protein
- Uncharacterized protein
- Treble clef zinc finger domain-containing protein
Sequence:
MRTFLAPTFPRWCGLFAKSPVLLMSISETGLQSAFRRACAEEGVDLREGLPEDVLAAVIAAPGQVTVEEARAQLNSSTSFRVDAGLVHLTADGAREQSQMETMLLKLATKIPPTGVSGAQFRAILEDEAPHFQPSAVGALSLKEAVQRYPRLFDVETDTTGKWFVRPAGVGKDGRASVGKNSGPISIINFCSERALMGNQADYVPLHVAMREESVASEGVLRDLVDSEELSKQLQIRFSVRLRPKRPVTNAFCFVDGDEIGLEAVDAIWKEMNLSDKSTRLVARQPTSRKHNSSDIVAPADMPTYAVVERKARELSLTQSVVLQDVIYMCSLRQFSLYADHIAKLNAFPDADVYVCCPSKVKLVAQKQFVPL
Protein: Parkinsonism associated deglycase (K7ELW0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNGKEVAAQVKAPLVLKD
Protein: Flavonol 3-O-glucosyltransferase UGT89B1 (EC 2.4.1.91) (Flavonol 7-O-beta-glucosyltransferase UGT89B1) (EC 2.4.1.237) (UDP-glycosyltransferase 89B1) (Q9C9B0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses quercetin 3-O-glucosyltransferase, 7-O-glucosyltransferase and 4'-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives.
Interaction partners:
Sequence:
MKVNEENNKPTKTHVLIFPFPAQGHMIPLLDFTHRLALRGGAALKITVLVTPKNLPFLSPLLSAVVNIEPLILPFPSHPSIPSGVENVQDLPPSGFPLMIHALGNLHAPLISWITSHPSPPVAIVSDFFLGWTKNLGIPRFDFSPSAAITCCILNTLWIEMPTKINEDDDNEILHFPKIPNCPKYRFDQISSLYRSYVHGDPAWEFIRDSFRDNVASWGLVVNSFTAMEGVYLEHLKREMGHDRVWAVGPIIPLSGDNRGGPTSVSVDHVMSWLDAREDNHVVYVCFGSQVVLTKEQTLALASGLEKSGVHFIWAVKEPVEKDSTRGNILDGFDDRVAGRGLVIRGWAPQVAVLRHRAVGAFLTHCGWNSVVEAVVAGVLMLTWPMRADQYTDASLVVDELKVGVRACEGPDTVPDPDELARVFADSVTGNQTERIKAVELRKAALDAIQERGSSVNDLDGFIQHVVSLGLNK
Protein: LexA repressor 1 (EC 3.4.21.88) (P61608)
Organism: Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- DNA polymerase IV
- DNA polymerase IV
- DNA repair protein RecN
- Lipoprotein
Sequence:
MQELAPRQQQVLAFITGFIAENGYPPTLREIAAHLKISGTLGVSKHLEALERKGYLRREANSSRGIALVGRTDTALSLPVAGVVRAGLPQPAVEDIEEYFAIDRSMVRGGTFFLRVKGDSMINAAIVEGDLALVRPQATAENRDIVVAMVDGEATLKRFYRQRDQIRLQPENPNMDPIIIRPGEGDVAIIGKVVGIYRPLE
Protein: Sulfotransferase 1C3 (ST1C3) (EC 2.8.2.1) (EC 2.8.2.2) (Q6IMI6)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor. Has sulfotransferase activity towards various substrates, such as bile acids, thyroid hormones and toward xenobiotic compounds such as chloro phenols and hydroxypyrenes. Lithocholic acid appears to be the best substrate among the endogenous compounds tested and 3,3',5,5'-tetrachloro-4,4'-biphenyldiol shows the highest specific activity among the xenobiotic compounds.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q80VR3}.
Interaction partners:
- Carbohydrate sulfotransferase 6
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Heparan sulfate glucosamine 3-O-sulfotransferase 3A1
- Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Heparan sulfate glucosamine 3-O-sulfotransferase 2
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3
Sequence:
MAKIEKNAPTMEKKPELFNIMEVDGVPTLILSKEWWEKVCNFQAKPDDLILATYPKSGTTWMHEILDMILNDGDVEKCKRAQTLDRHAFLELKFPHKEKPDLEFVLEMSSPQLIKTHLPSHLIPPSIWKENCKIVYVARNPKDCLVSYYHFHRMASFMPDPQNLEEFYEKFMSGKVVGGSWFDHVKGWWAAKDMHRILYLFYEDIKKDPKREIEKILKFLEKDISEEILNKIIYHTSFDVMKQNPMTNYTTLPTSIMDHSISPFMRKGMPGDWKNYFTVAQNEEFDKDYQKKMAGSTLTFRTEI
Protein: Ribose 5-phosphate isomerase, putative (EC 5.3.1.6) (Q384D1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Transketolase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Ribokinase
- ribose-phosphate diphosphokinase
- ribose-phosphate diphosphokinase
- Ribose-phosphate pyrophosphokinase, putative
- ribose-phosphate diphosphokinase
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Transaldolase
Sequence:
MTRKVAIGADHIGFPIHESIVRYVREAGEEFEPVYIGPHSLERVDYPDYALNVARMVARGEADVGILVCGSGIGMSIAANKVPGIRAALCFDHYTAVMARQHNDANVVCLGERTTGPAVLREIIMTFLQTPYSGEDRHTQRLEKIKAAESNTNGC
Protein: Septin-10 (Q9P0V9)
Organism: Homo sapiens (Human)
Function: Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12711328}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8C650}. Note=Detected in the annulus of the sperm flagellum and in the neck region in spermatids and mature sperm (By similarity). Using a GFP-fusion protein, detected in the nucleus. {ECO:0000250|UniProtKB:Q8C650, ECO:0000269|PubMed:12711328}.
Interaction partners:
- Septin-7
- Septin-11
- Uncharacterized protein C17orf47
- Septin-1
- Septin-2
- Septin-5
- Septin-9
- Septin-8
- Septin-6
- Neuronal-specific septin-3
Sequence:
MASSEVARHLLFQSHMATKTTCMSSQGSDDEQIKRENIRSLTMSGHVGFESLPDQLVNRSIQQGFCFNILCVGETGIGKSTLIDTLFNTNFEDYESSHFCPNVKLKAQTYELQESNVQLKLTIVNTVGFGDQINKEESYQPIVDYIDAQFEAYLQEELKIKRSLFTYHDSRIHVCLYFISPTGHSLKTLDLLTMKNLDSKVNIIPVIAKADTVSKTELQKFKIKLMSELVSNGVQIYQFPTDDDTIAKVNAAMNGQLPFAVVGSMDEVKVGNKMVKARQYPWGVVQVENENHCDFVKLREMLICTNMEDLREQTHTRHYELYRRCKLEEMGFTDVGPENKPVSVQETYEAKRHEFHGERQRKEEEMKQMFVQRVKEKEAILKEAERELQAKFEHLKRLHQEERMKLEEKRRLLEEEIIAFSKKKATSEIFHSQSFLATGSNLRKDKDRKNSNFL
Protein: Capsid assembly scaffolding protein (Gene product 11) (Gp11) (Head morphogenesis protein) (Scaffold protein) (Q38580)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Function: Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid (Probable).
Interaction partners:
Sequence:
MSLKEQLGEELYGQVLAKLGEGAKLVDISDGSFIPKEKFDAVNSEKKSLEQQLTDRDQQLQELSTKATGHDELSAKIADLQKANEEAKQAFEAEKQQLKYEHALETALRDSGAKNPKAVKALLDTESIKLDGDKLLGFEDQIKALKEQEDYLFKGTEPNGGVQGTPPPGKGADLGGLPTKKNPFKQGPDFNLTEQGILFRENPELAKKLQAEAQ
Protein: CUB and LDLa domain, isoform E (A8JNN6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLAEALGYGYLLAYVICLLCWPGEAYPASSSYRDLDICNHWDGRRHFLELGSPAGEVHARNVTTTAYRSSPLVFKNDAVAGDVWYQCSLELVTCAECVIRVAFTYANFSKSCGNTGGKSSMCPCEHIQFSEPPYDSTISGQEFCGDGKVFRSKTRTLQLKFFYRASNAHVFSLQYFSERKI
Protein: Protein EARLY FLOWERING 3 (Nematode-responsive protein) (O82804)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a transcription factor part of a circadian clock input pathway. Acts within a 'zeitnehmer' feedback loop and is involved in its own circadian regulation. Has no role in regulating circadian clock function in the dark. Part of a corepressor complex consisting of ELF4, ELF3, and LUX involved in the transcriptional regulation of APRR9. The activity of the protein may be decreased in long day conditions due to its interaction with phytochrome B (phyB). Can regulate the initiation of flowering independently of phyB. Also involved in responses to nematode parasitism, like the formation of the nematode feeding structure.
Subcellular location: Nucleus {ECO:0000269|PubMed:22327739}. Note=Forms nuclear bodies. {ECO:0000269|PubMed:22327739}.
Interaction partners:
- Protein EARLY FLOWERING 4
- Transcription factor LUX
- Phytochrome B
- Protein CCA1
- Protein GIGANTEA
- E3 ubiquitin-protein ligase COP1
- Two-component response regulator-like APRR1
- Transcription factor PIF4
- Cryptochrome-2
- Cryptochrome-1
Sequence:
MKRGKDEEKILEPMFPRLHVNDADKGGPRAPPRNKMALYEQLSIPSQRFGDHGTMNSRSNNTSTLVHPGPSSQPCGVERNLSVQHLDSSAANQATEKFVSQMSFMENVRSSAQHDQRKMVREEEDFAVPVYINSRRSQSHGRTKSGIEKEKHTPMVAPSSHHSIRFQEVNQTGSKQNVCLATCSKPEVRDQVKANARSGGFVISLDVSVTEEIDLEKSASSHDRVNDYNASLRQESRNRLYRDGGKTRLKDTDNGAESHLATENHSQEGHGSPEDIDNDREYSKSRACASLQQINEEASDDVSDDSMVDSISSIDVSPDDVVGILGQKRFWRARKAIANQQRVFAVQLFELHRLIKVQKLIAASPDLLLDEISFLGKVSAKSYPVKKLLPSEFLVKPPLPHVVVKQRGDSEKTDQHKMESSAENVVGRLSNQGHHQQSNYMPFANNPPASPAPNGYCFPPQPPPSGNHQQWLIPVMSPSEGLIYKPHPGMAHTGHYGGYYGHYMPTPMVMPQYHPGMGFPPPGNGYFPPYGMMPTIMNPYCSSQQQQQQQPNEQMNQFGHPGNLQNTQQQQQRSDNEPAPQQQQQPTKSYPRARKSRQGSTGSSPSGPQGISGSKSFRPFAAVDEDSNINNAPEQTMTTTTTTTRTTVTQTTRDGGGVTRVIKVVPHNAKLASENAARIFQSIQEERKRYDSSKP
Protein: Deformed epidermal autoregulatory factor 1 homolog (Nuclear DEAF-1-related transcriptional regulator) (NUDR) (Suppressin) (Zinc finger MYND domain-containing protein 5) (O75398)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Required for neural tube closure and skeletal patterning. Regulates epithelial cell proliferation and side-branching in the mammary gland. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 4. Isoform 4 may inhibit transcriptional activity of isoform 1 by interacting with isoform 1 and retaining it in the cytoplasm. Transcriptional activator of EIF4G3.
Subcellular location: [Isoform 1]: Nucleus. Cytoplasm. Note=Cytoplasmic in non-mucinous colorectal carcinoma. When expressed alone, localized almost exclusively in the nucleus but, when expressed with isoform 4, nuclear expression decreases to 32% and cytoplasmic expression increases by 270%.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted. Note=Secreted in some cell types.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted. Note=Secreted in some cell types.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus. Note=When expressed alone, localizes mainly in the cytoplasm but, when expressed with isoform 1, nuclear localization is enhanced.
Interaction partners:
- Zinc finger MYND domain-containing protein 11
- Zinc finger MYND domain-containing protein 19
Sequence:
MEDSDSAAKQLGLAEAAAVAAAAAVAAAAAAAAGGEAEEPVLSRDEDSEEDADSEAERETPRVTAVAVMAAEPGHMDMGAEALPGPDEAAAAAAFAEVTTVTVANVGAAADNVFTTSVANAASISGHVLSGRTALQIGDSLNTEKATLIVVHTDGSIVETTGLKGPAAPLTPGPQSPPTPLAPGQEKGGTKYNWDPSVYDSELPVRCRNISGTLYKNRLGSGGRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDDMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTFTVTPSGQITTSGALTFDRASTVEATAVISESPAQGDVFAGATVQEASVQPPCRASHPEPHYPGYQDSCQIAPFPEAALPTSHPKIVLTSLPALAVPPPTPTKAAPPALVNGLELSEPRSWLYLEEMVNSLLNTAQQLKTLFEQAKHASTYREAATNQAKIHADAERKEQSCVNCGREAMSECTGCHKVNYCSTFCQRKDWKDHQHICGQSAAVTVQADEVHVAESVMEKVTV
Protein: Carbohydrate sulfotransferase 12 (EC 2.8.2.5) (Chondroitin 4-O-sulfotransferase 2) (Chondroitin 4-sulfotransferase 2) (C4ST-2) (C4ST2) (Sulfotransferase Hlo) (Q9NRB3)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin and desulfated dermatan sulfate. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Activity toward partially desulfated dermatan sulfate is however lower. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Carbohydrate sulfotransferase 13
- Carbohydrate sulfotransferase 11
- Carbohydrate sulfotransferase 7
- Carbohydrate sulfotransferase 15
- Carbohydrate sulfotransferase 3
Sequence:
MTKARLFRLWLVLGSVFMILLIIVYWDSAGAAHFYLHTSFSRPHTGPPLPTPGPDRDRELTADSDVDEFLDKFLSAGVKQSDLPRKETEQPPAPGSMEESVRGYDWSPRDARRSPDQGRQQAERRSVLRGFCANSSLAFPTKERAFDDIPNSELSHLIVDDRHGAIYCYVPKVACTNWKRVMIVLSGSLLHRGAPYRDPLRIPREHVHNASAHLTFNKFWRRYGKLSRHLMKVKLKKYTKFLFVRDPFVRLISAFRSKFELENEEFYRKFAVPMLRLYANHTSLPASAREAFRAGLKVSFANFIQYLLDPHTEKLAPFNEHWRQVYRLCHPCQIDYDFVGKLETLDEDAAQLLQLLQVDRQLRFPPSYRNRTASSWEEDWFAKIPLAWRQQLYKLYEADFVLFGYPKPENLLRD
Protein: Basic leucine zipper 24 (F4J5N9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFCCCKDCRGNQRVSNFDSLTGVFFGDLEFGPQNQRYIKMNEEEDKDQDRVTRGCSHTHSCNPPGPEDASHSHTCFHAHTHLIISQDQQENDHSDSSNKKRLCGNREAVRKYREKKKARTAYLEDEVMRLQSLNEQFLRKLQSQEMVETELIRLRALLVEMQGKIEVELCSFSFQKQCNGSGFVFKEDGCNLATSNMMCEAARVECEEGQTLHDPIQSFVPQPPPFSR
Protein: Feruloyl CoA ortho-hydroxylase F6H1-3 (IbF6H1-3) (EC 1.14.11.61) (2-oxoglutarate-dependent dioxygenase F6H1-3) (2OGD F6H1-3) (G9M9M2)
Organism: Ipomoea batatas (Sweet potato) (Convolvulus batatas)
Function: 2-oxoglutarate (OG)- and Fe(II)-dependent dioxygenase (2OGD) involved in scopoletin biosynthesis. Converts feruloyl CoA into 6'-hydroxyferuloyl CoA, and, at low efficiency, caffeoyl-CoA into 6'-hydroxycaffeate, but has no activity with p-coumaroyl-CoA.
Interaction partners:
Sequence:
MPAVLSSVLSNITDFVVHEGNGVKGLADMGLQSLPKQYIQPAEERITTSTVIVDDTIPVIDLSEWGSDPKVGDLICEAAEKWGFFQIVNHGVPLEVLEEVKAATYRFFRLPAEEKNKHSKDNSPSNNVRYGTSFTPHAEKALEWKDFLSLFYVSDEEAAALWPSACRDEALTFMRNCDAVIKRLLKSLMKGLNVTEIDGTKESLLMGSKRINMNYYPKCPNPELTVGVGRHSDVSTLTILLQDQIGGLYVRKLDSDTWVHVPPINGAIVINVGDALQILSNGRYKSIEHRVIANGSNNRISVPIFVNPRPNDIIGPLPELLESGEKAVYKNVLYSDYVKHFFRKAHDGKETVDFAKIN
Protein: Zinc finger X-linked protein ZXDA (P98168)
Organism: Homo sapiens (Human)
Function: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein ZXDC
Sequence:
MEIPKLLPARGTLQGGGGGGIPAGGGRVHRGPDSPAGQVPTRRLLLPRGPQDGGPGRRREEASTASRGPGPSLFAPRPHQPSGGGDDFFLVLLDPVGGDVETAGSGQAAGPVLREEAKAGPGLQGDESGANPAGCSAQGPHCLSAVPTPAPISAPGPAAAFAGTVTIHNQDLLLRFENGVLTLATPPPHAWEPGAAPAQQPRCLIAPQAGFPQAAHPGDCPELRSDLLLAEPAEPAPAPAPQEEAEGLAAALGPRGLLGSGPGVVLYLCPEALCGQTFAKKHQLKMHLLTHSSSQGQRPFKCPLGGCGWTFTTSYKLKRHLQSHDKLRPFGCPAEGCGKSFTTVYNLKAHMKGHEQENSFKCEVCEESFPTQAKLGAHQRSHFEPERPYQCAFSGCKKTFITVSALFSHNRAHFREQELFSCSFPGCSKQYDKACRLKIHLRSHTGERPFLCDFDGCGWNFTSMSKLLRHKRKHDDDRRFMCPVEGCGKSFTRAEHLKGHSITHLGTKPFVCPVAGCCARFSARSSLYIHSKKHLQDVDTWKSRCPISSCNKLFTSKHSMKTHMVKRHKVGQDLLAQLEAANSLTPSSELTSQRQNDLSDAEIVSLFSDVPDSTSAALLDTALVNSGILTIDVASVSSTLAGHLPANNNNSVGQAVDPPSLMATSDPPQSLDTSLFFGTAATGFQQSSLNMDEVSSVSVGPLGSLDSLAMKNSSPEPQALTPSSKLTVDTDTLTPSSTLCENSVSELLTPAKAEWSVHPNSDFFGQEGETQFGFPNAAGNHGSQKERNLITVTGSSFLV
Protein: Brahma associated protein 155 kDa (LD22973p) (Moira, isoform A) (Q9VF03)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Polybromo
- Brahma-associated protein of 60 kDa
- ATP-dependent helicase brm
- Brahma associated protein 55kD
- Brahma associated protein 111kD
- GH08712p
- Supporter of activation of yellow protein
- Brahma associated protein 170kD
- Bromodomain containing 7/9
- Trithorax group protein osa
Sequence:
MNTLGPKKDGSPNIDFFQSPETLQGFESIRQWLQKNCKKYLAHSSEPITKESLAQLLIHFLQYVEAKLGKNSADPPATRIPMRCFLDFKSGGGLCIIFSTMFRFRAEQRGKKFDFSIGKNPTRKDPNIQLLIEIEQALVEADLYRIPYIYIRPEIEKGFEGKLREILDNRRVEIVSDEEDATHIVYPVVDPHPDEYARPIFKRGGHVMLHWYYFPESYDSWAVNNFDLPDHIPENPESPAERWRVSASWIVDLEQYNEWMAEEDYEVDEQGKKKTHKQRMSIDDIMSFGDEKKKPAASSGGGKQKRRRSPSPASSASTSKPGKRKRSPAVVHKKSRNDDDDEDLTRDLDDPPAEPNVQEVHKANAALQSTASPAPGGKSRGDNDMMPIKGGTMTDLDDEMTGGSAAQAMSTGDGENSQTGKTSDNSNTQEFSSSAKEDMEDNVTEQTHHIIVPSYSAWFDYNSIHVIEKRAMPEFFNSKNKSKTPEIYMAYRNFMIDTYRLNPTEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQIDADVRPTPMGPPPTSHFHILSDTPSGLQSINPQKTQQPSAAKTLLDLDKKPLGKDGGLELGDKSGLTGIKTEALENGAAGGLSSGVSQFGLKLDQYAKKPAAMRNRTAASMAREWTDQETLLLLEGLEMHKDDWNKVCEHVGSRTQDECILHFLRLPIEDPYLEDDGGFLGPLACQPIPFSKSGNPIMSTVAFLASVVDPRVAAAAAKAAMEEFAAIKDEVPATIMDNHLKNVEKASAGGKFNPNFGLANSGIAGTGNDKDDEEGKEGGASASAGGSDEEMKDLSKKDDDAKSKDNTKSDKTNTNTDSSSTSSSATGNTNNTDKKPKESSGSSPSGDKSAIKSDKSNKSSPTETAAAASGGEVDIKTEDSSGDGETKDGTEAKEGTGTGTGPLAVPKEGTFSENNMQTAAAAALASAAVKAKHLAALEERKIKSLVALLVETQMKKLEIKLRHFEELEATMEREREGLEYQRQQLITERQQFHLEQLKAAEFRARQQAHHRLQQELQGQAAAGSMILPQQQQLPQAQQPQQQQQTLPPHPHLAQQQQLPPHPHQLPPQSQPLAGPTAQHQPLPPHVVSSPNGAPFAAPPISLTGGLPPGAPTAIVTNPSDQTGPVAAGAAQSQAPTPMDTTPPSSGPVSDANAPPGSAMPPGGIPPANTAPIAGVAPSS
Protein: Ribosome-inactivating protein velutin (EC 3.2.2.22) (rRNA N-glycosidase) (P83324)
Organism: Flammulina velutipes (Agaricus velutipes)
Function: Inhibits protein synthesis but does not possess ribonuclease activity. Also inhibits HIV-1 reverse transcriptase, beta-glucosidase and beta-glucuronidase.
Interaction partners:
Sequence:
XHPDLFXXRPDNTASPKFEDPRLNP
Protein: CMP-N,N'-diacetyllegionaminic acid synthase (EC 2.7.7.82) (Q0P8S7)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into flagellin via O-linkage to Ser/Thr. Catalyzes the conversion of N,N'-diacetyllegionaminic acid (Leg5Ac7Ac) and CTP into CMP-N,N'-diacetyllegionaminic acid (CMP-Leg5Ac7Ac).
Interaction partners:
- N,N'-diacetyllegionaminic acid synthase
- GDP/UDP-N,N'-diacetylbacillosamine 2-epimerase
- Oxidoreductase
- Sugar-phosphate nucleotide transferase
- 6-hydroxymethylpterin diphosphokinase MptE-like domain-containing protein
- Uncharacterized protein
- PseD protein
- PseE protein
- Sialic acid synthase
- Nucleotide sugar dehydratase
Sequence:
MAEILCTICARGGSKGVKNKNIRKINKLEMIAYSIIQAQNSKLFKHIVISTDSDEIASVAQKYGAEVFFKREAHLANDRTAKLPVMRDALLRSEEHFKTCFETLIDLDASAPLRSSLDIKKAYESFVENDNSNLITAVPARRNPYFNLVEIQNNKVVKSKEGNFTTRQSAPKCYDMNASIYIFKRDYLLENDSVFGKNTGLFVMDESTAFDIDSELDFKIVEFLISLKNLSPKDF