wanglab/gogpt-training-data huggingface dataset:
Protein: Polyubiquitin 11 [Cleaved into: Ubiquitin] (P0CH33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- Protein NBR1 homolog
- E3 ubiquitin-protein ligase UPL3
- E3 ubiquitin-protein ligase PRT1
- Ubiquitin carboxyl-terminal hydrolase 14
- Large ribosomal subunit protein uL2x
- Ubiquitin-conjugating enzyme E2 13
- CCT motif family protein
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- Probable CCR4-associated factor 1 homolog 7
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGF
Protein: DNA polymerase epsilon subunit B (DNA polymerase II subunit 2) (AtDPB2) (Protein CYCLOPS 2) (Q500V9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: As accessory component of DNA polymerase II participates in chromosomal DNA replication. Required for the timing and determination of cell fate during plant embryogenesis and root pole development, by promoting cell cycle and cell type patterning. Necessary for proper shoot (SAM) and root apical meristem (RAM) functions (By similarity). Is essential to promote the first divisions of the zygote.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA polymerase epsilon catalytic subunit A
- Cell division cycle 45
- DNA replication licensing factor MCM4
- DNA polymerase II subunit B4
- DNA polymerase alpha catalytic subunit
- DNA replication licensing factor MCM5
- DNA polymerase epsilon catalytic subunit B
- DNA replication licensing factor MCM3
- DNA polymerase alpha subunit B
- DNA replication complex GINS protein SLD5
Sequence:
MSSTSQKRKKIQKKFKNRGYNLKFDALDEILVFADQFPDDDDGEAIDLLLDNLQETHKSSTVDAESVRGLINRLLGAHNAPEEPTTSASSLAIIDAFLVPKFGYDSVKKKFNEHTSSLPIHGEASAKTALYRERFMLLSQRVSRAEHFSRPAFDAEMSQFENNEISSIQSLISQRGRKWVMGVISQLEDGHFYLEDLSASVEIDLSKAKITTGFFTENTIILAEGEMQVNGIFQVITCGFPPLEDRDKTLKAHSEYDFFGGGTLTKEEMIKLADLERQAVNDTFVILSDIWLDDEEVMRKLETVLDGFESVETVPSLFVFMGNFCSRPCNLSFGSYSSLREQFGKLGRMIGNHPRLKENSRFLFIPGPEDAGPSTVLPRCALPKYLTEELRNIIPNAIFSSNPCRVKFYNQEIVFFRQDLLYRMRRSCLVTPSSEETNDPFKHLVYTITHQSHLCPLPLMVQPIIWNYDHALRLYPTPHTIVLGDKSEQEVCKFGGTTCFNPGSFSTDSTFVAYRPSTQEVELSAL
Protein: Cilia- and flagella-associated protein 206 (A2RV06)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Essential for sperm motility and is involved in the regulation of the beating frequency of motile cilia on the epithelial cells of the respiratory tract (By similarity). Required for the establishment of radial spokes in sperm flagella (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q6PE87}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6PE87}.
Interaction partners:
- Radial spoke head protein 9 homolog
Sequence:
MSSSQAEGVIRNIIREISQTCLSRGQTLSETLIAFMVKAVVLDPTNHFNVDRTLTKQDVQKLIELCVDRLMDQTSPTLQTIKMQVYFDMNYTPRREFLEMQQKLLQSRLQSLSREITDSRAKSREDLKKLYGTIVHYIIQSSNLSSSTDINTVRETTAALQSIFPPSQLGSFMSLLKSDKEQQLKENSLIVSGIRLFNKDNGEGGEAIQSLPSILNEKLPGVVSDLERELASCERLCWQYTGLLELISERDTAHSQSPVPPRLLTQALYNTRQHEAFLRLTLADVILCAQEVTRLQSDLMSRMTLLRDAIHTKTTVPTTHVFPHFSAVGRLWAGLEQEMLLLSMLTNVASGLRVFLTAESLLTPDQMELPVRTDADRCSGTAEERVLVSETSSCECCFPESTADFQHLPLQYNGFCGVALVDRNGLLLPGNTSIGVLKHKEKYYAFSSRSAAYEFSCRADEYTAAVLETASRTPELIQLLQLQQHFTSSTAYSQLPAGHQSLTAGMPSGQKLLLKSISKSDAGVQTEIHPLQSNICTSYEWNEWEMRRKAIKLANLHSKVTRSSQSDWSLMRRHNSSQTFLPKDASCQTKRDGESLVPKAQVYLSSLRGAAGFRKVDLSRAVDE
Protein: Complement component receptor 1-like protein (Antigen 5I2) (Complement regulatory protein Crry) (Q63135)
Organism: Rattus norvegicus (Rat)
Function: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. Also acts as a decay-accelerating factor, preventing the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Seems to act as a costimulatory factor for T-cells. May play a crucial role in early embryonic development by maintaining fetomaternal tolerance.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Complement C4
- Complement C3
- Complement C4A.
- Complement factor I
- CD59 glycoprotein
Sequence:
MEASSPLDPVGRLVAFCRGGVHLAVLLLFLSPSTLGQCPAPPLFPYAKPINPTDESTFPVGTSLKYECRPGYIKRQFSITCEVNSVWTSPQDVCIRKQCETPLDPQNGIVHVNTDIRFGSSITYTCNEGYRLIGSSSAMCIISDQSVAWDAEAPICESIPCEIPPSIPNGDFFSPNREDFHYGMVVTYQCNTDARGKKLFNLVGEPSIHCTSIDGQVGVWSGPPPQCIELNKCTPPHVENAVIVSKNKSLFSLRDMVEFRCQDGFMMKGDSSVYCRSLNRWEPQLPSCFKVKSCGAFLGELPNGHVFVPQNLQLGAKVTFVCNTGYQLKGNSSSHCVLDGVESIWNSSVPVCEQVICKLPQDMSGFQKGLQMKKDYYYGDNVALECEDGYTLEGSSQSQCQSDASWDPPLPKCVSQVICKLPQDMSGFQKGLQMKKDYYYGDNVALECEDGYTLEGSSQSQCQSDASWDPPLPKCVSRSNSGLIAGIFIGIIVLILFIIFSYWMIMKFKKRNSTNEKCKEVGIYLNSKEDSCVQPQSLLTSQENNSTSSPARNSLTQEV
Protein: Calcium-binding EF-hand domain-containing protein (Q86A78)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- EGF-like domain-containing protein
- BEACH domain-containing protein lvsD
- Chloride channel protein D
- Myb-like protein B
- Uncharacterized protein
Sequence:
MDWNQQTNQYQQPQQPQGGYNPYNNNNNNNNNMNQQRFGGGGGGNQGYNSNQGYNNNNNNNSNNMNNMGGGMGNMGMNNNNMGGNMGMNNNNNNMNNMNNMNNMNNMNNMNNNMGGGGGGNMGNQNFNNTMNMNNNMNNNNNMNNNNINNNMNNNMNNNNNMNNMGGGSSGGGNQNFNKYQNYNYNQYDPRMNQQNNNNNNNNINNNSNNNNNNTLVNRTSPNQQSSGGVVSGGGNRPMGNNMNNNNMNNNMNNNNMNNNMNSSMNSNMNSNMNSNMNNNNMNNMGGMSNNNMNNNNNNMNNNMNMGSGMNNMGMNNMNNMNNMNNNTTTMNNNNMGNDNRNSSNQNYNNQNNNQNNNQNNSGNTVMGINIKDFPRGSGSSWGKGSNNMNSNNNNNNSINRSKSYKSKDGYSGGGSRDYSGGGGGGGNRSGGDFTNKYRDKGSYSSSSTSSTSSSSTSSSKKDYEKESRKSTESSSSSSTSSGDKKYSTKIPSHQFTQENYDYSSLKNIFSRLQISPDFTRLVSSWIDSTGGEEPQQRIEVNQNIPFLIDIKDFGFEKVDIHKTSFSKQQQQQQQQQQLNKSTTHIKYNSKVMLYSFYSNIEDPSITKKIKFLVSKEDKDISCIGGTWLPDLDGEDVNDPQTLINTAIRTTKEYTQIDLSGCKKWYKFMEVHYYRPPTEEQSYYQEITVIYVPDITDIQPMDVDSLLKVPTVSETTPSAPVGVTTATTKTTEEEEEEDQAPKDHVSKDFDNDETSSNTEQNQPPKSSTTSNTTKPAAAVPTTTAATATTTHGSLHLPKASKFYNVITPSSEGNRYKAMMLSLDGLLDYDESDTHEGTFEASLFSELFYLMLCRDMGTNILTSIVNYRPTSQESDEITDTTLKRKRDDNHAFRGENSEINTSNNTNTNNNNNNNNNNNGTNQPTDSSSLDGNRKSTEKSPQQDVCGVTDKKVKLDGESSTDNTENGEIIGDNTLTNTNNEPVQIEGELNEGLNNNTNNINNNNNNNNEINNNDNNNNNQNENNNQNDNNNEYNIESNNYNNNDNSSNNTNTSNTSSSSINSPNLSNKDDSNRNSAENQRSSVTSNASSSTSTTIGTQVDESAKVLESFHFFDLNRVNYLREEDVETIIHNLGLFLSKSYVQNVVQKVSTNYTSKQGRVYYQEIVKKLIKPTQQQLSTIPSLPQTHSIVPSQSQPQPQQQPQQQEQQQQQQQQEQQQQQQEQELMSIEQPQQPTQQQDSMAIEQQSQELAIEQESNLDQPPKDQDLVQQEPIDQQIQQNITENI
Protein: Interferon C (C1IRY1)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPCQLQGQLVRITHNLLRDMGGNFPLECLQENVFMAFPATAFASSGAPQLGSSGAKAIYETLKNIDILFEADDLPTQWDQQKLKNFQNIVYRQIEEGKCMMGSVDTSDYLIRTEGLNTYFGNIAAVLKEKNFSYC
Protein: Amino acid transporter transmembrane domain-containing protein (Q54CB3)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAYNSRNSSSNSQGGGGMIIGNNNNNGVINRHSSESTPLINNETYEVEKKYAPIPSFWNTVKAFAGAGSFALPGAMTHAGLWIGSIGLVLISILSNYTMNILLKCSIQMTQDRIGPEKPSYADIAQRAFGRVGELFVCFMNFLVTMSICVSYLILIGQNIDYFTKIGYIPMIWIVLPFILLLTFLTDMKYLGFTSIFGALSLILAMFTIVIYGIKDNHVHPLSDYTFDFKQIPLWFGNAAFFFCNHIVVIPVSHASGDNKRYPNVLNFAMIFITVINVAFAVLCYLYYNFISGGIPSAIVDVLPNGIFANIVKVCVVLELSCSFPLIFAAGLNVVDSSIQIFHHHFNAFPELDGSSVKTPFFSRNWKFYLIRIVFCSMLAGIASAVTNFGNYTSLIGSLMLAVAGFVVPPLLSLRFFPQQAIPWKVFHITITIFGIMATILGTYLSIKAFVDPSN
Protein: Inner membrane protein YbcI (P45570)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YbcN
- Uncharacterized MFS-type transporter YdeE
- Inner membrane transport protein YdhP
- Uncharacterized protein YdhL
- Inner membrane protein YiaA
- Uncharacterized lipoprotein YjbF
- Purine ribonucleoside efflux pump NepI
- Peptidase B
Sequence:
MPTVITHAAVPLCIGLGLGSKVIPPRLLFAGIILAMLPDADVLSFKFGVAYGNVFGHRGFTHSLVFAFVVPLLCVFIGRRWFRAGLIRCWLFLTVSLLSHSLLDSVTTGGKGVGWLWPWSDERFFAPWQVIKVAPFALSRYTTPYGHQVIISELMWVWLPGMLLMGMLWWRRR
Protein: PRA1 family protein (Q389C4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363107}.
Interaction partners:
Sequence:
MTDKDGGTEMSFVDGATEGQTAGFADAPTSNPMGNAAMIDPQSFVSKAWGFVRFPAEAVRQQLNRVRPWSQFFDREQFASPEGFGDAVSRLRCNVVHFYHNYFVVALLGSLIVLIVNPMFSICMFLMLLMWAYTHKKQMEAAETNVNHLLIGNYEISFSKAYILISIFGIISFFLFNGSSVMFWMFFASLGVATVHAVLRKPHSENELAHFV
Protein: Zinc finger CCCH domain-containing protein 53 (AtC3H53) (Q9FL40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Tetratricopeptide repeat
- AT3G18790 protein
- Pre-mRNA-splicing factor SPF27 homolog
- Cell division cycle 5-like protein
- Zinc finger CCCH domain-containing protein 51
- Pre-mRNA-splicing factor SYF2
- Cwf15 / Cwc15 cell cycle control family protein
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- AT4g21110/F7J7_50
- Transcriptional regulator ATRX
Sequence:
MSHRDHGADGWESADFPITCESCFGDNPYMRMTRADYDKECKICSRPFTAFRWRPGRNARFKKTEICQTCSKLKNVCQVCLLDLGFGLPVQVRDSALNINSHYSVPMSHVNREYFADEHDPKTRAGLDYESSFGKMQPNDTILKLQRRTPSYEKNRPKICSFYTIGQCKRGAECSFRHEMPETGELSHQNIRDRYYSVNDPVAMKLLRKAGEMGTLEPPEDESIKTLYVGGLNSRIFEQDIHDHFYAYGEMESIRVMAEDGKYDQSGSNQQQQGSIAHTGLISQQQNQHSQMQQYYMQPPPPNEYSHYPSMDTQRMGAAFSTQESDGSSTSENNRAYSSYSYPMPPHQPYPTPPPYIDIYIYI
Protein: Stellate supressor protein (Q24542)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
NNNNNNSSWINWFLGIKANEFLCHMPTDYFQDTFNQMGLEYFSQTLDVILKPVFDSSSGLFYDDEKKWYGMIHASPIRSPIRSERGRTPCQWASAMCGTVNGEDLLPTL
Protein: SET and MYND domain-containing protein DDB_G0288495 (EC 2.1.1.-) (Q54IV4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable methyltransferase.
Interaction partners:
- Trishanku
Sequence:
MISYEYCDSSDSFYFNDIQDFDFNPWIEVKSVSEKGRCVFSKKFIPKGTMVFRDIPYAAIVDNQFKRNICTTCFKILLESNRHNFQTCPSCFQVNYCSNYCKQYSKIETKHTELECKWIQDFTVSFKHQMAEDDRNIVLLVLKILARRIHEKQSTIFHNKPLTTNTFETCTSNNNNIDLLPMIPNDIPDLIDHLDDYFINSKNNNEFENEEEEEEEQEQKGEGEQEENENNENNEKVKKKVIIIDDNEKEKEEIKKFNKIWKNDFKRLINIAKVIQIIIDDSIDSLENIKCDYGFVDNQGDTEMVDNSIDPKGLDKLVDNLSSSDLNILRLLCKIRANYFGLWNSAYKPIPLNSIDDDDDDNNNNKEKPNNDYLWCGSGVYLKLSLFNHSCFPNCTTLIEYNINKKNSNNNNGNNGNNNSYGDTNQLTISIITLRDIEENQELLITYIPLNQKINDRVKSLKSNWLFQCDCKRCHFEKINENQTEKIYKDSCCTNQKCSGGLLIPLEQNSTQGICRVCKNTYTLPTVFYPLK
Protein: Calcium-dependent lipid-binding protein (AtCLB) (CaLB protein) (Protein NTMC 2 TYPE 4) (NTMC2TYPE4) (Q9LEX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in membrane trafficking (By similarity). Acts as a repressor of abiotic stress (e.g. drought and salt) responses by binding specifically to the promoter of THAS1 to regulate its transcription. Binds to membrane lipid ceramides.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:21252258}; Single-pass membrane protein {ECO:0000255}. Note=Localized in the nucleus membrane of root tips cells. {ECO:0000269|PubMed:21252258}.
Interaction partners:
- Thalianol synthase 1
- CASP-like protein 2C1
- Protein ROOT HAIR DEFECTIVE 3
Sequence:
MGLISGILFGIIFGVALMAGWSRMMTHRSSKRVAKAVDMKLLGSLSRDDLKKICGDNFPQWISFPAFEQVKWLNKLLSKMWPYIAEAATMVIRDSVEPLLEDYRPPGITSLKFSKLTLGNVAPKIEGIRVQSFKEGQVTMDVDLRWGGDPNIVLGVTALVASIPIQLKDLQVFTVARVIFQLADEIPCISAVVVALLAEPKPRIDYTLKAVGGSLTAIPGLSDMIDDTVDTIVKDMLQWPHRIVVPIGGIPVDLSDLELKPQGKLIVTVVKATNLKNKELIGKSDPYATIYIRPVFKYKTKAIENNLNPVWDQTFELIAEDKETQSLTVEVFDKDVGQDERLGLVKLPLSSLEAGVTKELELNLLSSLDTLKVKDKKDRGSITLKVHYHEFNKEEQMAALEDEKKIMEERKRLKEAGVIGSTMDAVGMVGSGLGAGVGMVGTGIGTGVGLVGSGVSSGVGMVGSGFGAVGSGLSKAGRFMGRTITGQSSKRSGSSTPVNTVPENDGAKQQ
Protein: Antimicrobial peptide microplusin (Microplusin) (Q86LE5)
Organism: Rhipicephalus microplus (Cattle tick) (Boophilus microplus)
Function: Has bacteriostatic activity against the Gram-positive bacterium M.luteus, but not against Gram-negative bacterium E.coli SBS363. Has fungistatic activity against C.neoformans, but not C.albicans. Binds and sequesters copper and iron ions. Copper-chelating is crucial for antimicrobial activity against M.luteus.
Subcellular location: Secreted {ECO:0000269|PubMed:14642886}.
Interaction partners:
Sequence:
MKAIFVSALLVVALVASTSAHHQELCTKGDDALVTELECIRLRISPETNAAFDNAVQQLNCLNRACAYRKMCATNNLEQAMSVYFTNEQIKEIHDAATACDPEAHHEHDH
Protein: LysM domain receptor-like kinase 10 (OsLysM-RLK10) (EC 2.7.11.1) (LysM-containing receptor-like kinase 10) (Receptor-like cytoplasmic kinase 276) (OsRLCK276) (D7UPN3)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MFSLPALLIGACAFAAAAVAASGDGCRAGCSLAIAAYYFSEGSNLTFIATIFAIGGGGYQALLPYNPAITNPDYVVTGDRVLVPFPCSCLGLPAAPASTFLAGAIPYPLPLPRGGGDTYDAVAANYADLTTAAWLEATNAYPPGRIPGGDGRVNVTINCSCGDERVSPRYGLFLTYPLWDGETLESVAAQYGFSSPAEMELIRRYNPGMGGVSGKGIVFIPVKDPNGSYHPLKSGGMGNSLSGGAIAGIVIACIAIFIVAIWLIIMFYRWQKFRKATSRPSPEETSHLDDASQAEGIKVERSIEFSYEEIFNATQGFSMEHKIGQGGFGSVYYAELRGEKTAIKKMGMQATQEFLAELKVLTHVHHLNLVRLIGYCVENCLFLVYEFIDNGNLSQHLQRTGYAPLSWATRVQIALDSARGLEYLHEHVVPVYVHRDIKSANILLDKDFRAKIADFGLAKLTEVGSMSQSLSTRVAGTFGYMPPEARYGEVSPKVDVYAFGVVLYELLSAKQAIVRSSESVSESKGLVFLFEEALSAPNPTEALDELIDPSLQGDYPVDSALKIASLAKSCTHEEPGMRPTMRSVVVALMALTANTDLRDMDYHPF
Protein: Phosphatidic acid phosphatase, putative (Q585M9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 1
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- dolichyl-diphosphooligosaccharide--protein glycotransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase protein, putative
- Diacylglycerol kinase
Sequence:
MHANWITWAASTVVYDAGDTISFVFALSSLLPSIIVIFIAGLASSSTSHQRDAALLLLVGLCQNTALNTFLKAFIKGPRPISSMYIMVPMSSSSNYGMPSNHSQFMFFFITWLLRKASANHIPVSWGMWLFFLVSATVVACGRVYNSYHSTDQVIVGAAVGVINAYASTTPTLERVLRWLMFRLSPVRNFFTSWVTYVRL
Protein: 2,4-diacetylphloroglucinol hydrolase (DAPG hydrolase) (EC 3.7.1.24) (Q4K423)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Function: Hydrolase that specifically degrades the potent antimicrobial compound 2,4-diacetylphloroglucinol (DAPG) to equimolar amounts of mildly toxic monoacetylphloroglucinol (MAPG) and acetate.
Interaction partners:
- 2,4-diacetylphloroglucinol biosynthesis regulator PhlH
Sequence:
MEARNMTPFTYFSLPMQKLFLRNQAAVRNKPYAKYFRSEMRVPLSAVRKIQQGPMALEDTLTPSIEDINRLLEPDFVSEESGYALLPGPMAYVQSRKFFPGCTAQMFKWWFIWHPAESERYTLWFPYAHVSNPCVHHQRLRDESLSFEERLYGNTFCASEYVGDRLMHLHIDFQQPASLGLNTDLYREAKIDGSVSALMSLADHPEVPVSLMVHLFKEVPDGMYLTSRYWVGAHPSMARFPGAEKAASLLKENGFGEAELETLAYEFAVHDMCEFNHLASFLPDLYREFGTPAA
Protein: Phospholipid phosphatase 1 (EC 3.1.3.-) (EC 3.1.3.106) (EC 3.1.3.4) (EC 3.6.1.75) (35 kDa PAP) (mPAP) (Hydrogen peroxide-inducible protein 53) (Hic53) (Lipid phosphate phosphohydrolase 1) (PAP2-alpha) (Phosphatidate phosphohydrolase type 2a) (Phosphatidic acid phosphatase 2a) (PAP-2a) (PAP2a) (Q61469)
Organism: Mus musculus (Mouse)
Function: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (By similarity). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes. It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P. Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes. May also have an intracellular activity to regulate phospholipid-mediated signaling pathways.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:19215222}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000269|PubMed:11535125}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 3
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Sequence:
MFDKTRLPYVALDVICVLLAGLPFAILTSRHTPFQRGIFCNDDSIKYPYKEDTIPYALLGGIVIPFCIIVMSIGESLSVYFNVLHSNSFVGNPYIATIYKAVGAFLFGVSASQSLTDIAKYTIGSLRPHFLAICNPDWSKINCSDGYIEDYICQGNEEKVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPMLQFGLIAFSIYVGLSRVSDYKHHWSDVTVGLIQGAAMAILVALYVSDFFKDTHSYKERKEEDPHTTLHETASSRNYSTNHEP
Protein: GH10871p (Tartan, isoform A) (Q9VU51)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRNMMIAFVGIWCILASIGVEPAAGLANCPPGCQCDDNTLVVQCGEGQLDVLPIALNPSIQRLVIKSNKIKTIDSSIQFYAELTFLDLSSNHLMTIPQRTFAYQKKLQEVHLNHNKIGQISNKTFIGLSAVTVLNLRGNQISELHQGTFTPLLKIEELNLGENRIGYLDPKAFDGLSQLRILYLDDNALTTVPDPVIFQAMPSLAELFLGMNTLQSIQADAFQDLKGLTRLELKGASLRNISHDSFLGLQELRILDLSDNRLDRIPSVGLSKLVRLEQLSLGQNDFEVISEGAFMGLKQLKRLEVNGALRLKRVMTGAFSDNGNLEYLNLSSNKMLLEVQEGALSGLSQLKHVVLKANALTSLAEGLFPWKDLQTLDLSENPLSCDCRVMWLHNLLVAKNASQDDVSELLCEFPERLRGESLRHLNPAMMGCTHADPRKQALIGALLVGSAATITALALVLYRCRHKIRETIKGGLWGNSALGRKEREYQKTFCDEDYMSRHQHHPCSLGIHSTFPNTYTAPHHPGATHHYGMCPMPVNDLGAIDPQQKFQQLVVPTATMISEKKLNNNKALVSQGAIDDSASFVLHMKSATMGRDVHQQNPQLNHYTKPQFLSATATVGDSCYSYADVPMVHGAPLGGPNQPQLRLTQEHFKQRELYDQEMGSEILDHNYIYSNTHYSMPLEQLGRSKTPTPPPMPPALPLRNGLCATTGRRSFQQKSASQKQQQNNNTLRQFTH
Protein: Protein Mis18-beta (Cancer/testis antigen 86) (CT86) (Opa-interacting protein 5) (OIP-5) (O43482)
Organism: Homo sapiens (Human)
Function: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:17199038}. Chromosome {ECO:0000269|PubMed:17199038}. Chromosome, centromere {ECO:0000269|PubMed:17199038}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin.
Interaction partners:
- Protein Mis18-alpha
- Mis18-binding protein 1
- Histone H3-like centromeric protein A
- Holliday junction recognition protein
- Centromere protein C
- Hyaluronan mediated motility receptor
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- G2/mitotic-specific cyclin-B1
- Thyroid receptor-interacting protein 6
- Kinesin-like protein KIF11
Sequence:
MAAQPLRHRSRCATPPRGDFCGGTERAIDQASFTTSMEWDTQVVKGSSPLGPAGLGAEEPAAGPQLPSWLQPERCAVFQCAQCHAVLADSVHLAWDLSRSLGAVVFSRVTNNVVLEAPFLVGIEGSLKGSTYNLLFCGSCGIPVGFHLYSTHAALAALRGHFCLSSDKMVCYLLKTKAIVNASEMDIQNVPLSEKIAELKEKIVLTHNRLKSLMKILSEVTPDQSKPEN
Protein: SIN3-like 5 (F4IEM8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
Sequence:
MKRVREEVYVEPQMRGPTVSSRGETNGRPSTISGGGTTGGLTTVDALTYLKAVKDMFQDNKEKYETFLGVMKDFKAQRVDTNGVIARVKDLFKGYDDLLLGFNTFLPKGYKITLQPEDEKPKKPVDFQVAIEFVNRIKARFGGDDRAYKKFLDILNMYRKETKSINEVYQEVTLLFQDHEDLLGEFVHFLPDFRGSVSVNDPLFQRNTIPRDRNSTFPGMHPKHFEKKIKRSRHDEYTELSDQREDGDENLVAYSAGNSLGKSLANQGQWPGYPKVEDTEGIQIYESNGGHERDPDIGSQKNLLSTNHMAKAINELDLTDCAQCTPSYRRLPDDYPIQIPSYRNSLGEKVLNDHWVSVTSGSEDYSFKHMRKNQYEESLFRCEDDRFELDMLLESVSAAIKRVESLLEKINNNTISIETPICIREHLSELNLRCIERLYGDYGLDVMDFLKKNSHIALPVILTRLKQKQEEWARCRADFRKVWAEVYAKNHHKSLDHRSFYFKQQDSKNLSTKGLVAEIKDISERKHKEDLLRAIAVGTKPSFTPDVEFIYTDTKVHTDLYKLIKYYCEEICATEQSDKVMKLWVTFLEPMFGVPSRSETIETMKDVAKIEDNQEHHDASEAVKENTCDGSMASNLKPLTPPKMPNKENPMIQGSSFAQDLPVNTGESIQQDKLHDVAAITNEDSQPSKLVSTRNDLIMEGVENRSRVSDVSMGGHKVEREEGELSPTESCEQENFEVYKENGLEPVQKLPDNEISNTDREPKEGACGTEAVTRSNALPEDDDNKITQKLSEGDENASKFIVSASKFGGQVSSDEEHKGAESENEAGGMVNSNEGEDGSFFTFSERYLQPVKPLAKHVPGTLQASECDTRNDSRVFYGNDSLYVLFRLHQMLYERIQSAKIHSERKWKAPDSTSTDSYTRFMEALYNLLDGSSDNTKFEDECRAIIGAQSYVLFTLDKLVQKFVKHLHAVAADETDTKLLQLYAYENYRKPGRFFDIVYHENARALLHDQNIYRIEYSSAQTRLGIQLMNSWNDQPEVTAVTVEPGFANYLQNDFLSFVSDEEKPGLFLKRNKAKLSGPGEESLGMSRALEGLNIINEVECKIACSSFKVKYEPHTADLLYRRKQKKATLNPTGPENVKTSDSSELSRKKRISRFHMSLNRRLVALP
Protein: Ubiquitin-conjugating enzyme E2 2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 2) (RAD6 homolog) (Ubiquitin carrier protein 2) (Ubiquitin-protein ligase 2) (P23566)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Component of the histone H2B ubiquitin ligase complex (HULC) which plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation (By similarity). Required for obr1 ubiquitination, which regulates mating-type silencing. With cut8, regulates the nuclear accumulation of the proteasome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Postreplication repair E3 ubiquitin-protein ligase rad18
- E3 ubiquitin-protein ligase brl2
- E3 ubiquitin-protein ligase brl1
- Ubiquitin-activating enzyme E1 1
- E3 ubiquitin-protein ligase ubr1
- E3 ubiquitin-protein ligase ubr11
- Small histone ubiquitination factor 1
- Polyubiquitin
- Ubiquitin-conjugating enzyme spm2
- Proliferating cell nuclear antigen
Sequence:
MSTTARRRLMRDFKRMQQDPPAGVSASPVSDNVMLWNAVIIGPADTPFEDGTFKLVLSFDEQYPNKPPLVKFVSTMFHPNVYANGELCLDILQNRWSPTYDVAAILTSIQSLLNDPNNASPANAEAAQLHRENKKEYVRRVRKTVEDSWES