wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin enhancer-binding factor 3 (Q9Z1X4)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs. As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (By similarity). Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response. Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q12906}. Cytoplasm {ECO:0000269|PubMed:21123651}. Nucleus {ECO:0000269|PubMed:21123651}. Note=Localizes in the cytoplasm in response to viral infection. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000269|PubMed:21123651}.
Interaction partners:
- Interleukin enhancer-binding factor 2
- ATP-dependent RNA helicase A
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoprotein K
- Interferon-induced, double-stranded RNA-activated protein kinase
- RNA-binding protein FUS
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoprotein D0
Sequence:
MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGNSELSEAENMDTPPDDESKEGAGEQKAEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLTTVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKADPPQAMNALMRLNQLKPGLQYKLISQTGPVHAPIFTMSVEVDGSNFEASGPSKKTAKLHVAVKVLQDMGLPTGAEGRDSSKGEDSAEESDGKPAIVAPPPVVEAVSNPSSVFPSDATTEQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFPDTPLALEANKKKRTPVPVRGGPKFAAKPHNPGFGMGGPMHNEVPPPPNIRGRGRGGNIRGRGRGRGFGGANHGGGYMNAGAGYGSYGYSSNSATAGYSQFYSNGGHSGNAGGGGSGGGGGSSSYSSYYQGDSYNSPVPPKHAGKKPLHGGQQKASYSSGYQSHQGQQQPYNQSQYSSYGTPQGKQKGYGHGQGSYSSYSNSYNSPGGGGGSDYSYDSKFNYSGSGGRSGGNSYGSSGSSSYNTGSHGGYGTGSGGSSSYQGKQGGYSSQSNYSSPGSSQSYSGPASSYQSSQGGYSRNTEHSMNYQYR
Protein: SIN3-HDAC complex-associated factor (Protein FAM60A) (Tera protein) (Q8C8M1)
Organism: Mus musculus (Mouse)
Function: Subunit of the Sin3 deacetylase complex (Sin3/HDAC), this subunit is important for the repression of genes encoding components of the TGF-beta signaling pathway (By similarity). Core component of a SIN3A complex (composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1) present in embryonic stem (ES) cells. Promotes the stability of SIN3A and its presence on chromatin and is essential for maintaining the potential of ES cells to proliferate rapidly, while ensuring a short G1-phase of the cell cycle, thereby preventing premature lineage priming.
Subcellular location: Nucleus {ECO:0000269|PubMed:28554894}.
Interaction partners:
- Histone deacetylase complex subunit SAP30
- Paired amphipathic helix protein Sin3a
- Sin3 histone deacetylase corepressor complex component SDS3
- Inhibitor of growth protein 2
- Histone deacetylase 1
- Breast cancer metastasis-suppressor 1 homolog
- AT-rich interactive domain-containing protein 4B
- Breast cancer metastasis-suppressor 1-like protein
- Inhibitor of growth protein 1
- Mortality factor 4-like protein 1
Sequence:
MFGFHKPKMYRSIEGCCICRAKSSSSRFTDSKRYEKDFQSCFGLHETRSGDICNACVLLVKRWKKLPAGSKKNWNHVVDARAGPSLKTTLKPKKVKTLSGNRMKSNQISKLQKEFKRHNSDAHSTTSSASPAQSPCYSNQSDEGSDTEMASSSNRTPVFSFLDLTYWKRQKICCGIIYKGRFGEVLIDTHLFKPCCSSKKAAAEKPEEQGPAPLPISTQEW
Protein: eRF1 methyltransferase catalytic subunit mtq2 (eRF1 MTase catalytic subunit mtq2) (EC 2.1.1.297) (N(5)-glutamine methyltransferase catalytic subunit mtq2) (Q9UT94)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Methylates eRF1 on 'Gln-182' using S-adenosyl L-methionine as methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form to be efficiently methylated.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Multifunctional methyltransferase subunit trm112
- Putative peptide chain release factor 1, mitochondrial
- tRNA
- 18S rRNA
- Probable MRF1 mitochondrial N
- Eukaryotic peptide chain release factor subunit 1
- Protein arginine N-methyltransferase 2
- Protein arginine N-methyltransferase 1
Sequence:
MLSTPVTSQLRLKEFQDVYEPAEDTFALLDALEKDAKKLRQMAEMKNLLTAEIGCGSGCASSFLKSGILKNKPIVHFMSDISNSACRASKITALNNRELYKDDNGLFITVQTSFLDGIRLGNGVDILIFNPPYVPTEFEEIPSEAATIASAWAGGTDGMDVTSTLLNQLKDILSQDGVFYMVAVARNKLHSICEILQKDGFIVNETLKRKAGRETLSILRIYRIGNTIWDE
Protein: Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.-) (D3Z8Q6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Axin-2
- E3 ubiquitin-protein ligase RNF146
- Telomeric repeat-binding factor
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- SH3 domain-binding protein 2
- TERF1
- BRISC and BRCA1-A complex member 1
- Glycogen synthase kinase-3 beta
Sequence:
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGPTPASPTAGGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGAVCTVAATAAAPAASAAVGVAPSPAGGGGNNSASSTSSPTSSSSSSPSSPGSSIAESPEAAGVGSTATLGPGAAGLGPGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVAELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDSLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKAGDLETVKQLCSPQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLERGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGAERKEGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (Q386H6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MAEDAAPDTSHQSSNTSDEGGAKSEVIVHMNNREANEEYGYPNNFIKTSHYTALSFLPLGLIAQFMRVSNFYFLVCMCLTLIPGLSPVNPVTAILPLLFVIGVSLAKEGVEEFRRHTADRLANSVEVDVLINGVMQRVPSRDIRVGDIVRVSNGEEVRADLLCLSTSDEEDQVYIDMCNLDGETSLKNRKPHEHTASLRTPEQLQEAQVKIVTTQPDAELHSWSGCIESNGEAFAVDIGNFLCRGSVLRKTDWVWGVVVYAGVDTKMFRNLKGHPMKMSDLDRRLNVMIVALLLFKCVVLATLAFLLVWWNRNNKEHIWYLHWYMNQYGSTVLLLRSFVTIFLLLSYFIPISLFVTIEVCKVIQAYWMVADGKMTDVVNGRLCRCRPNTSNLNEQLAMVRFIFTDKTGTLTENVMKFKQGDFQGFRLDSACGTKPTDLLDRCNPAREAAYEYFLSIALCNTVQPTEDPNAEGGISYDGTSPDEVALVSMAAEHGFRLKKRTTREMVLDIEGVEHEYRILATLEFTPERKMMSIIVRDNVSHHIVLFTKGADSSLLPRTCTNRQAQNYVQKLRGTLQDMSVCGLRTLVIGRRFLLPEEYKNWEDSYKTASRTLIDRSAALDDVCMRIEGDLWPVGATAIEDKLQQEVPETISFFLEAGVVIWMLTGDKRETAVTVAATAKLCDPQKDSIIHIDIGSFDPKSAEAIRKVDSDLSKVRRTLESGGENGSKCTIVIDGLALGVAMSEHFLTFLDLSMRVNSAVCCRLTPLQKAEVVRMFQGSTGLTAIAIGDGANDVSMIQEGRVGVGIIGLEGSQAALSADYAIPRFRHLRRLCAVHGRYSLVRNSGCIMISFYKNAVLGMMMILFCFHSAFSGGTLFDGWLLTFFNILLTSIPPFFLGVFDKDLPEDALLRRPHLFTQLSHGLYFDVMTTVRWFGEALIHGTLIFYLFYLTIRNLDWSTHNISMIELGTMQIFIVVLVVLVRCGLAVRCWRSLQLLGLLASLAITLALTLTYSSFKSVGGSSIYWQMFDLALGPKFWLYMLLVLGSLIMINLSVLYFQKRRYPTLRDTADEENRVMCRGSLLDENVSQGDKAGYVTFGVESTQSSDREDKSIDIQDMRRREIEAGDTLHG
Protein: Uncharacterized ABC transporter ATP-binding protein C825.01 (Q9USH9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Translation initiation factor rli1
- mRNA export factor elf1
Sequence:
MARGKRSTQRDADLELESLQSEIESESPQPVTKSKAKKNKKKLNKASAFNSDNDSNYDLKPEDDEVDEEVVPVKKKPSKKSKKAKANAFEAFADEQSVEEEEEEDSEKPVRKNKKSSKKASPKNAFDALADDMDDLSLDEEESESSEKSKKKKKKSKSKDDGSEALDDGDIESSEKDKKKKKKSKENDDAPKKDRKTRKKEEKARKLASMLESENKDNDANAAPLNKTDAFKDGLPSGRLIFAYASGQKVAPDGSNPADGITVTGNLLSPPNSRDLQVEKLSVSAWGKLLIKDSELNLINGRRYGLIAPNGSGKSTLLHAIACGLIPTPSSLDFYLLDREYIPNELTCVEAVLDINEQERKHLEAMMEDLLDDPDKNAVELDTIQTRLTDLETENSDHRVYKILRGLQFTDEMIAKRTNELSGGWRMRIALARILFIKPTLMMLDEPTNHLDLEAVAWLEEYLTHEMEGHTLLITCHTQDTLNEVCTDIIHLYHQKLDYYSGNYDTFLKVRAERDVQLAKKARQQEKDMAKLQNKLNMTGSEQQKKAKAKVKAMNKKLEKDKQSGKVLDEEIIQEKQLVIRFEDCGGGIPSPAIKFQDVSFNYPGGPTIFSKLNFGLDLKSRVALVGPNGAGKTTLIKLILEKVQPSTGSVVRHHGLRLALFNQHMGDQLDMRLSAVEWLRTKFGNKPEGEMRRIVGRYGLTGKSQVIPMGQLSDGQRRRVLFAFLGMTQPHILLLDEPTNALDIDTIDALADALNNFDGGVVFITHDFRLIDQVAEEIWIVQNGTVKEFDGEIRDYKMMLKQQIAKEREEERRIELEKQKK
Protein: Neurotoxin (EC 3.4.24.69) (D/C mosaic neurotoxin) (Neurotoxin type DC) (A5JGM8)
Organism: Clostridium botulinum
Interaction partners:
Sequence:
MTWPVKDFNYSDPVNDNDILYLRIPQNKLITTPVKAFMITQNIWVIPERFSSDTNPSLSKPPRPTSKYQSYYDPSYLSTDEQKDTFLKGIIKLFKRINERDIGKKLINYLVVGSPFMGDSSTPEDTFDFTRHTTNIAVEKFENGSWKVTNIITPSVLIFGPLPNILDYTASLTLQGQQSNPSFEGFGTLSILKVAPEFLLTFSDVTSNQSSAVLGKSIFCMDPVIALMHELTHSLHQLYGINIPSDKRIRPQVSEGFFSQDGPNVQFEELYTFGGSDVEIIPQIERLQLREKALGHYKDIAKRLNNINKTIPSSWSSNIDKYKKIFSEKYNFDKDNTGNFVVNIDKFNSLYSDLTNVMSEVVYSSQYNVKNRTHYFSKHYLPVFANILDDNIYTIINGFNLTTKGFNIENSGQNIERNPALQKLSSESVVDLFTKVCLRLTRNSRDDSTCIQVKNNTLPYVADKDSISQEIFESQIITDETNVENYSDNFSLDESILDAKVPTNPEAVDPLLPNVNMEPLNVPGEEEVFYDDITKDVDYLNSYYYLEAQKLSNNVENITLTTSVEEALGYSNKIYTFLPSLAEKVNKGVQAGLFLNWANEVVEDFTTNIMKKDTLDKISDVSAIIPYIGPALNIGNSALRGNFKQAFATAGVAFLLEGFPEFTIPALGVFTFYSSIQEREKIIKTIENCLEQRVKRWKDSYQWMVSNWLSRITTQFNHISYQMYDSLSYQADAIKAKIDLEYKKYSGSDKENIKSQVENLKNSLDVKISEAMNNINKFIRECSVTYLFKNMLPKVIDELNKFDLKTKTELINLIDSHNIILVGEVDRLKAKVNESFENTIPFNIFSYTNNSLLKDMINEYFNSINDSKILSLQNKKNTLMDTSGYNAEVRVEGNVQLNPIFPFDFKLGSSGDDRGKVIVTQNENIVYNAMYESFSISFWIRINKWVSNLPGYTIIDSVKNNSGWSIGIISNFLVFTLKQNENSEQDINFSYDISKNAAGYNKWFFVTITTNMMGNMMIYINGKLIDTIKVKELTGINFSKTITFQMNKIPNTGLITSDSDNINMWIRDFYIFAKELDDKDINILFNSLQYTNVVKDYWGNDLRYDKEYYMINVNYMNRYMSKKGNGIVFNTRKNNNDFNEGYKIIIKRIRGNTNDTRVRGENVLYFNTTIDNKQYSLGMYKPSRNLGTDLVPLGALDQPMDEIRKYGSFIIQPCNTFDYYASQLFLSSNATTNRLGILSIGSYSFKLGDDYWFNHEYLIPVIKIEHYASLLESTSTHWVFVPASE
Protein: Medium-chain acyl-CoA ligase ACSF2, mitochondrial (EC 6.2.1.2) (Q96CM8)
Organism: Homo sapiens (Human)
Function: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein mS29
Sequence:
MAVYVGMLRLGRLCAGSSGVLGARAALSRSWQEARLQGVRFLSSREVDRMVSTPIGGLSYVQGCTKKHLNSKTVGQCLETTAQRVPEREALVVLHEDVRLTFAQLKEEVDKAASGLLSIGLCKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYVLKKVGCKALVFPKQFKTQQYYNVLKQICPEVENAQPGALKSQRLPDLTTVISVDAPLPGTLLLDEVVAAGSTRQHLDQLQYNQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNSNILGERLKLHEKTPEQLRMILPNPLYHCLGSVAGTMMCLMYGATLILASPIFNGKKALEAISRERGTFLYGTPTMFVDILNQPDFSSYDISTMCGGVIAGSPAPPELIRAIINKINMKDLVVAYGTTENSPVTFAHFPEDTVEQKAESVGRIMPHTEARIMNMEAGTLAKLNTPGELCIRGYCVMLGYWGEPQKTEEAVDQDKWYWTGDVATMNEQGFCKIVGRSKDMIIRGGENIYPAELEDFFHTHPKVQEVQVVGVKDDRMGEEICACIRLKDGEETTVEEIKAFCKGKISHFKIPKYIVFVTNYPLTISGKIQKFKLREQMERHLNL
Protein: Single-strand-selective monofunctional uracil-DNA glycosylase 1 isoform 2 (A0A024RAZ8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPQAFLLGSIHEPAGALMEPQPCPGSLAESFLEEELRLNAELSQLQFSEPVGIIYNPVEYAWEPHRNYVTRYCQGPKEVLFLGMNPGPFGMAQTGVPFGEVSMVRDWLGIVGPVLTPPQEHPKRPVLGLECPQSEVSGARFWGFFRNLCGQPEVFFHHCFVHNLCPLLFLAPSGRNLTPAELPAKQREQLLGICDAALCRQVQLLGVRLVVGVGRLAEQRARRALAGLMPEVQVEGLLHPSPRNPQANKGWEAVAKERLNELGLLPLLLK
Protein: Sulfite efflux pump SSU1 (Sulfite sensitivity protein SSU1) (P41930)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in efflux of free sulfite. Mutations in the SSU1 gene cause sensitivity to sulfite.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9294463}; Multi-pass membrane protein {ECO:0000269|PubMed:9294463}.
Interaction partners:
- Zinc finger protein FZF1
- Protein ECM34
- Uroporphyrinogen-III C-methyltransferase
Sequence:
MVANWVLALTRQFDPFMFMMVMGVGISSNILYSFPYPARWLRICSYIMFAIACLIFIAVQALQILHLIVYIKEKSFREYFNDFFRNMKHNLFWGTYPMGLVTIINFLGALSKANTTKSPTNARNLMIFVYVLWWYDLAVCLVIAWGISFLIWHDYYPLEGIGNYPSYNIKMASENMKSVLLLDIIPLVVVASSCGTFTMSEIFFHAFNRNIQLITLVICALTWLHAIIFVFILIAIYFWSLYINKIPPMTQVFTLFLLLGPMGQGSFGVLLLTDNIKKYAGKYYPTDNITREQEILTIAVPWCFKILGMVSAMALLAMGYFFTVISVVSILSYYNKKEIENETGKVKRVYTFHKGFWGMTFPMGTMSLGNEELYVQYNQYVPLYAFRVLGTIYGGVCVCWSILCLLCTLHEYSKKMLHAARKSSLFSESGTEKTTVSPYNSIESVEESNSALDFTRLA
Protein: Zinc finger protein 441 (Q8N8Z8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDSVAFEDVAINFTCEEWALLGPSQKSLYRDVMQETIRNLDCIGMIWQNHDIEEDQYKDLRRNLRCHMVERACEIKDNSQCGGPFTQTQDSIVNEKIPGVDPWESSECTDVLMGRSSLNCYVRVDSEHKPCEYQEYGEKPYTHTQCGTAFSYQPCFQIHERPQHGKKLYDCKECASFSSLENLQRHMAAHHGDGPRICKLCGNAFIWPSLFHMLRRTHTEEKPYEYEQCSTAFPAYSSTLRHERTHSGEKPYQCKQCGKAFSCSCYTQLYERTHTGEQSYECKQCGKAFYHLGSFQRHMIVHTGDGPHKCKICGKGFLSPSSVRRHKRTHTGEKPYECKYCGKAFSDCTGFRRHMITHTGDGPHKCKVCGKAFDSPSLCRRHETTHTGEKPYKCECGKAFSDFYYFRNHETTHTGEKPYKCKQCGKAFICCTYLQIHERIHTGERPYKCKQCGKAFRSSNYIRVHEKTHTGEKPYECKQCGKALSHLKSFQRHMIMHTGDGPHKCKICGKSFDSPSSFRRHERIHTGERPYKCKLCGKGFRSSSYIQLHERTHTGEKPYGCQQCGKALSDLSSFRRHMITHTGNGPHKCKICGKGFDYPSSVQRHERTHTGEKPYECKECGKAFSHSSYLRIHERVHTGEKPYKCKECGKPFHCPSAFHKHERTHSMEKPYKCKECGEAFHCISSFHKHEMTH
Protein: SLIT-ROBO Rho GTPase-activating protein 1 (srGAP1) (Rho GTPase-activating protein 13) (Q7Z6B7)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42.
Interaction partners:
- Roundabout homolog 1
- Cell division control protein 42 homolog
- Roundabout homolog 2
- SLIT-ROBO Rho GTPase-activating protein 2
- Slit homolog 3 protein
- SLIT-ROBO Rho GTPase-activating protein 3
- Slit homolog 1 protein
- Transforming protein RhoA
- Slit homolog 2 protein
- Actin-binding protein WASF1
Sequence:
MSTPSRFKKDKEIIAEYESQVKEIRAQLVEQQKCLEQQTEMRVQLLQDLQDFFRKKAEIETEYSRNLEKLAERFMAKTRSTKDHQQYKKDQNLLSPVNCWYLLLNQVRRESKDHATLSDIYLNNVIMRFMQISEDSTRMFKKSKEIAFQLHEDLMKVLNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQIGRSGDPVFHIRLEERHQRRSSVKKIEKMKEKRQAKYSENKLKSIKARNEYLLTLEATNASVFKYYIHDLSDLIDCCDLGYHASLNRALRTYLSAEYNLETSRHEGLDIIENAVDNLEPRSDKQRFMEMYPAAFCPPMKFEFQSHMGDEVCQVSAQQPVQAELMLRYQQLQSRLATLKIENEEVKKTTEATLQTIQDMVTIEDYDVSECFQHSRSTESVKSTVSETYLSKPSIAKRRANQQETEQFYFMKLREYLEGSNLITKLQAKHDLLQRTLGEGHRAEYMTTRPPNVPPKPQKHRKSRPRSQYNTKLFNGDLETFVKDSGQVIPLIVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNSFERGENPLADDQSNHDINSVAGVLKLYFRGLENPLFPKERFNDLISCIRIDNLYERALHIRKLLLTLPRSVLIVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMPVPEIQDQVSCQAHVNEIIKTIIIHHETIFPDAKELDGPVYEKCMAGDDYCDSPYSEHGTLEEVDQDAGTEPHTSEDECEPIEAIAKFDYVGRSARELSFKKGASLLLYHRASEDWWEGRHNGIDGLVPHQYIVVQDMDDTFSDTLSQKADSEASSGPVTEDKSSSKDMNSPTDRHPDGYLARQRKRGEPPPPVRRPGRTSDGHCPLHPPHALSNSSVDLGSPSLASHPRGLLQNRGLNNDSPERRRRPGHGSLTNISRHDSLKKIDSPPIRRSTSSGQYTGFNDHKPLDPETIAQDIEETMNTALNELRELERQSTAKHAPDVVLDTLEQVKNSPTPATSTESLSPLHNVALRSSEPQIRRSTSSSSDTMSTFKPMVAPRMGVQLKPPALRPKPAVLPKTNPTIGPAPPPQGPTDKSCTM
Protein: Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase (EC 2.4.3.7) (NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase) (ST6GalNAc IV) (ST6GalNAcIV) (Sialyltransferase 3C) (SIAT3-C) (Sialyltransferase 7D) (SIAT7-D) (Q9H4F1)
Organism: Homo sapiens (Human)
Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. Prefers O-glycans to glycoproteins or glycolipids.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Alpha-2-HS-glycoprotein
- Alpha-2,8-sialyltransferase 8B
Sequence:
MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYSSVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRSTLRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQVYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCREKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWRTE
Protein: Branched chain amino acid ABC transporter membrane protein (Q9HUQ1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
- Branched chain amino acid ABC transporter ATP binding protein
- Probable permease of ABC branched-chain amino acid transporter
- Amino acid binding protein
- High-affinity branched-chain amino acid transport ATP-binding protein
- High-affinity branched-chain amino acid transport ATP-binding protein BraF
- Leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein
- High-affinity branched-chain amino acid transport system permease protein BraE
- High-affinity branched-chain amino acid transport ATP-binding protein BraG
- High-affinity branched-chain amino acid transport system permease protein BraD
- Aliphatic amidase expression-regulating protein
Sequence:
MDGIFLQQMINGLTLGSVYGLIAIGYTMVYGIIGMINFAHGEVYMISAYLSAIALALLAFFGLQNFPLLILGTLLFTVLVTCTYGWVIERIAYKPLRNSTRLAPLISAIGMSLILQNYVQVAQGPRQQGIPTLLDGALKFHVGDGFVQLTYTKLFILIASLIGMAVLTYVIRYTKLGRMCRATQQDRKMASILGINTDRVISYVFVIGAAMAALAGVLITMNYGTFDFYAGFIIGIKAFTAAVLGGIGSLPGAMLGGLVLGVAEAQFSGMVNTDYKDVFAFSLLVLILIFRPQGLLGRPQIAKV
Protein: Epidermal growth factor receptor pathway substrate 15 (B1AUU8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAAQLSLTQLSSGNPVYEKYYRQVDTGNTGRVLASDAAAFLKKSGLPDLILGKIWDLADTDGKGILNKQEFFVALRLVACAQNGLEVSLSSLNLAVPPPRFHDTSSPLLISGTSAAELPWAVKPEDKAKYDAIFDSLSPVNGFLSGDKVKPVLLNSKLPVDILGRVWELSDIDHDGMLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTWVVSPAEKAKYDEIFLKTDKDMDGFVSGLEVREIFLKTGLPSTLLAHIWSLCDTKDCGKLSKDQFALAFHLISQKLIKGIDPPHVLTPEMIPPSDRASLQKNIIGSSPVADFSAIKELDTLNNEIVDLQREKNNVEQDLKEKEDTIKQRTSEVQDLQDEVQRENTNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLARSSPELLPSGVTDENEVTTAVTEKVCSELDNNRHSKEEDPFNVDSSSLTGPVADTNLDFFQSDPFVGSDPFKDDPFGKIDPFGGDPFKGSDPFASDCFFRQSTDPFATSSTDPFSAANNSSITSVETLKHNDPFAPGGTVVAASDSATDPFASVFGNESFGGGFADFSTLSKVNNEDPFRSATSSSVSNVVITKNVFEETSVKSEDEPPALPPKIGTPTRPCPLPPGKRSINKLDSPDPFKLNDPFQPFPGNDSPKEKDPEIFCDPFTSATTTTNKEADPSNFANFSAYPSEEDMIEWAKRESEREEEQRLARLNQQEQEDLELAIALSKSEISEA
Protein: Vacuolar protein sorting-associated protein 25 (AtVPS25) (ESCRT-II complex subunit VPS25) (Q8VZC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex (By similarity).
Subcellular location: Endosome {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 20 homolog 2
- Vacuolar protein sorting-associated protein 20 homolog 1
- Vacuolar protein sorting-associated protein 22 homolog 1
- Vacuolar protein sorting-associated protein 36
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- Protein ELC
- Protein FREE1
- LisH domain-like protein
- Vacuolar protein sorting-associated protein 28 homolog 2
Sequence:
MQKLADFKLPQFFNYPPYFTLQPVRDTREKQIQLWKELILDYCKSQKIFLIGVEEDFPLFSNSAIDRSLSHEARETFLSAIVGEGRAEWLDKGHRKCLILWHRIQDWADIVLQFVRDNGLEDSVMTVEEIRSGTESLGTELQGIDRTILMRALKLLENKGKLALFKGTSADDEGVKFSV
Protein: Uterine Lumin Expressed/locailized (Q18947)
Organism: Caenorhabditis elegans
Interaction partners:
- Secreted protein
- Chitinase-like protein C25A8.4
- Secreted protein
- DUF19 domain-containing protein
- Uterine Lumin Expressed/locailized
- TransThyretin-Related family domain
- DUF4362 domain-containing protein
- FIP
- DUF1525 domain-containing protein
- Candidate secreted effector protein
Sequence:
MLVVLAISLAVTAVCAQYGSGPANNPPASSYSSNVYYPPPVYGSVYWDYDSGSREHRHKQCPRLRAYVGEFPGIPEEAFYPPIIRYVKYNRKVTALVVCDRDEKNLNFLFARHNKTRDVRSASVVAIGSTAGVTLVCNRDDRRYEGFVIDMNATTNGFSKKIEITQLTCLGLDKTIIGLPVEHGVQQLAQKIQEILEDDFFVPVIPSRRKRQAGGATANSAESTTEAADTESTTEAAATETPAAESTTTEASATDAAATEASATDAAATEGAVTKAAAGVTEESATEVITVATTPASPDAALNNAINELGKILGQVF
Protein: Uric acid degradation bifunctional protein TTL (Transthyretin-like protein) [Includes: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97); 5-hydroxyisourate hydrolase (HIU hydrolase) (HIUHase) (EC 3.5.2.17)] (Q9LVM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the last two steps of the degradation of uric acid, i.e. the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) and its stereoselective decarboxylation to (S)-allantoin. Might function as a negative regulator to modulate brassinosteroid-mediated plant growth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15319482}; Peripheral membrane protein {ECO:0000269|PubMed:15319482}; Cytoplasmic side {ECO:0000269|PubMed:15319482}. Peroxisome {ECO:0000269|PubMed:17951448}.; SUBCELLULAR LOCATION: [Isoform 1]: Peroxisome {ECO:0000269|PubMed:20511299}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:20511299}.
Interaction partners:
- Uricase
- Allantoinase
- Protein BRASSINOSTEROID INSENSITIVE 1
- Peroxisomal nicotinamide adenine dinucleotide carrier
- TPR repeat-containing thioredoxin TTL4
- Xanthine dehydrogenase 2
- Eukaryotic translation initiation factor 3 subunit I
- Serine/threonine-protein kinase-like protein At3g51990
Sequence:
MAMEIGEDEWKVCCGSSEFAKQMSTSGPLTSQEAIYTARDIWFNQVNVTDWLEAFSAHPQIGNTPSPSINSDFARRSVSEQSTAFATTSASALQELAEWNVLYKKKFGFIFIICASGRTHAEMLHALKERYENRPIVELEIAAMEQMKITELRMAKLFSDKAKVISETDSSSSPVSTKPQDRLRIIGGHLNVAAEAKAPKRSRPPITTHVLDVSRGAPAAGVEVHLEVWSGTTGPSFVHGGGGVWSSVGTSATDRDGRSGPLMDLVDALNPGTYRISFDTAKYSPGCFFPYVSIVFQVTESQKWEHFHVPLLLAPFSFSTYRGS