wanglab/gogpt-training-data huggingface dataset:
Protein: Protein O-glucosyltransferase 3 (EC 2.4.1.-) (KDEL motif-containing protein 2) (Protein O-xylosyltransferase POGLUT3) (EC 2.4.2.-) (Q7Z4H8)
Organism: Homo sapiens (Human)
Function: Protein glucosyltransferase that catalyzes the transfer of glucose from UDP-glucose to a serine residue within the consensus sequence peptide C-X-N-T-X-G-S-F-X-C. Can also catalyze the transfer of xylose from UDP-xylose but less efficiently. Specifically targets extracellular EGF repeats of proteins such as NOTCH1, NOTCH3, FBN1, FBN2 and LTBP1. May regulate the transport of NOTCH1 and NOTCH3 to the plasma membrane and thereby the Notch signaling pathway.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
Sequence:
MRRLPRALLLQLRLALLVAAGAPEVLVSAPRSLVWGPGLQAAVVLPVRYFYLQAVNSEGQNLTRSPAGETPFKVVVKSLSPKELVRIHVPKPLDRNDGTFLMRYRMYETVDEGLKIEVLYGDEHVAQSPYILKGPVYHEYCECPEDPQAWQKTLSCPTKEPQIAKDFASFPSINLQQMLKEVPKRFGDERGAIVHYTILNNHVYRRSLGKYTDFKMFSDEILLSLTRKVLLPDLEFYVNLGDWPLEHRKVNGTPSPIPIISWCGSLDSRDVVLPTYDITHSMLEAMRGVTNDLLSIQGNTGPSWINKTERAFFRGRDSREERLQLVQLSKENPQLLDAGITGYFFFQEKEKELGKAKLMGFFDFFKYKYQVNVDGTVAAYRYPYLMLGDSLVLKQDSPYYEHFYMALEPWKHYVPIKRNLSDLLEKVKWAKENDEEAKKIAKEGQLMARDLLQPHRLYCYYYQVLQKYAERQSSKPEVRDGMELVPQPEDSTAICQCHRKKPSREEL
Protein: LDL receptor-related protein 6 (Q9DFH4)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
GFTECVDHSDEQNCPMCSDMQYQCTSGQCIDSSLRCNGEDNCQDKSDEKNCNEVCAPDQFHCGNGQCIGKHRRCDLSPDCSDSSDEQACYPTEEPPPPSTNTIGSIIGVILTVFVVGGVYFICQRVLCRRMKGDGETMTNDYVVHGPASVPLAYVPHPSSLTGSLPGMSRGKSVISTLSIMAGSSGPPYDRAHVTGASSSSSSSTKGTYFPPIL
Protein: Transcriptional regulator MET32 (Methionine-requiring protein 32) (Q12041)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Auxiliary transcriptional regulator of sulfur amino acid metabolism. Involved in the transcriptional activation of MET28.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcriptional activator of sulfur metabolism MET4
- Transcriptional activator of sulfur metabolism MET28
- Centromere-binding protein 1
- F-box protein MET30 subunit MET30)
- Sulfate adenylyltransferase
- Adenylyl-sulfate kinase
- Transcriptional regulator MET31
- Glutamate--cysteine ligase
- Phosphoadenosine phosphosulfate reductase
- General control transcription factor GCN4
Sequence:
MEDQDAAFIKQATEAIVDVSLNIDNIDPIIKELLERVRNRQNRLQNKKPALIPAENGVDINSQGGNIKVKKENALPKPPKSSKSKPQDRRNSTGEKRFKCAKCSLEFSRSSDLRRHEKTHFAILPNICPQCGKGFARKDALKRHYDTLTCRRNRTKLLTAGGEGINELLKKVKQSNIVHRQDNNHNGSSNG
Protein: Non-structural maintenance of chromosome element 3 (Non-SMC element 3) (Q9Y7U4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15331764, ECO:0000269|PubMed:15601840, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Non-structural maintenance of chromosomes element 1
- Structural maintenance of chromosomes protein 5
- E3 SUMO-protein ligase nse2
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosome element 4
- Non-structural maintenance of chromosome element 6
- Non-structural maintenance of chromosome element 5
- Structural maintenance of chromosomes protein 3
Sequence:
MSQLSFTGKSSSKGRSRLTQEVRPTASQIIADEEASDLDEYEEDLEGSGNEDDFGPSMSRSSRGRKRRKGDPLELQSQFEERNETDAINFQLLVRNVVRYAICSQTSHNTITRKDIVQKAFPEGTSRNLFQSVFEEADRQLQLSFGFRLVAVTQSNRKKDMAVSQLRRPATSNANSSNLHRYWVLRSTLPMELQKDSRLIVDSVLDTAYYGFLMTVIAFIAVSHCSVGHSELQSFLQELLTEEETTPLHLDITRSLSLLVRQGYLDRVKDDTHNQFVYYIGSRAVTEISIEGLKSFVTEFFPDSDIDMDALLTEYRQEYQNQSSSSAA
Protein: Type 1 encapsulin shell protein (Linocin M18) (M18 encapsulin) (Q45296)
Organism: Brevibacterium linens
Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous shells 23-24 nm in diameter with 2-2.5 nm thick walls. Cargo protein DyP (dye-decolorizing peroxidase) is targeted to the interior via its C-terminal extension; probably only 1 DyP hexamer is incorporated into each shell. Empty shells can be isolated in the absence of cargo.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:19172747, ECO:0000269|PubMed:27355101, ECO:0000269|PubMed:29166561, ECO:0000269|PubMed:7986050}.
Interaction partners:
Sequence:
MNNLYRELAPIPGPAWAEIEEEARRTFKRNIAGRRIVDVAGPTGFETSAVTTGHIRDVQSETSGLQVKQRIVQEYIELRTPFTVTRQAIDDVARGSGDSDWQPVKDAATTIAMAEDRAILHGLDAAGIGGIVPGSSNAAVAIPDAVEDFADAVAQALSVLRTVGVDGPYSLLLSSAEYTKVSESTDHGYPIREHLSRQLGAGEIIWAPALEGALLVSTRGGDYELHLGQDLSIGYYSHDSETVELYLQETFGFLALTDESSVPLSL
Protein: TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TGF-beta-activated kinase 1-binding protein 2) (Q5U303)
Organism: Rattus norvegicus (Rat)
Function: Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains. The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 (By similarity). Regulates the IL1-mediated translocation of NCOR1 out of the nucleus (By similarity). Involved in heart development (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9NYJ8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NYJ8}. Endosome membrane {ECO:0000250|UniProtKB:Q9NYJ8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NYJ8}. Lysosome membrane {ECO:0000250|UniProtKB:Q9NYJ8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NYJ8}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NYJ8}. Note=Following IL1 stimulation, translocation occurs from the membrane to cytosol. Interaction with TRIM38 promotes translocation from cytosol to endosome and lysosome. {ECO:0000250|UniProtKB:Q9NYJ8}.
Interaction partners:
- TGF-beta activated kinase 1
- NF-kappa-B essential modulator
- TNF receptor-associated factor 6
- Interleukin-1 receptor-associated kinase 1
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- Mitogen-activated protein kinase kinase kinase 7
- Receptor-interacting serine/threonine-protein kinase 1
- Toll-like receptor 3
- TNF receptor-associated factor
- Myeloid differentiation primary response protein MyD88
Sequence:
MAQGSHQIDFQVLHDLRQKFPEVPEVVVSRCMLQNNNNLDACCAVLSQESTRYLYGEGDLNFSDESGISGLRNHMTSLNLDLQSQNVYHHGREGSRVNGSRTLTHSVSDGQLQGGQSNNELFQQEPQTAPAQVPQGFNVFGMPSTSGASNSTPHLGFHLGSKGTSNLSQQTPRFNPIMVTLAPNIQTGRSTPTSLHIHGVPPPVLNSPQGNSIYIRPYITTPSGAARQTQQHSGWVSQFNPVNPQQAYQPSQPGPWTTYPASNPLPHTSTQQPNQQGHQTSHVYMPISSPTTPQPPTVHSSASSQSSAHSQYNIQNISTGPRKNQIEIKLEPPQRNSSSKLRSSGPRTASTSSLVNSQTLNRNQPTVYIAASPPSTDEMISRSQPKVYISANASTGDEQGMRNQPTLFISTNSGASAASRNMSGQVSMGPAFIHHHPPKSRVLGGNSAASPRVVVTQPNTKYTFKITVSPNKPPAVSPGVVSPTFELTNLLNHPDHYVETETIQHLTDPTLAHVDRVSEARKLSMGSDDAAYTQALLVHQKARMERLQRELEMQKKKLDKLKSEVNEMENSLTRRRLKRSNSMSQIPSLEEMQQLRSCNRQLQIDIDCLTKEIDLFQARGPHFNPSAIHNFYDNIGFVGPVPPKPKDQRSTIKAPKTQDTEDEEGAQWNCTACTFLNHPALIRCEQCEMPRHF
Protein: Ornithine decarboxylase antizyme (ODC-Az) (Q02803)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels. Binds to ODC/SPE1 monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Interaction partners:
- Ornithine decarboxylase
- Telomere replication protein EST3
Sequence:
MYEVIQKRKTKIINVLQSPELMRLIEDPSNLGISLHFPVSSLLKSNKCTPMPKLSTYSLASGGFKDWCADIPLDVPPEIDIIDFYWDVILCMESQFILDYNVPSKNKGNNQKSVAKLLKNKLVNDMKTTLKRLIYNENTKQYKNNNSHDGYNWRKLGSQYFILYLPLFTQELIWCKLNENYFHVVLPSLLNSRNVHDNHSTYINKDWLLALLELTSNLNQNFKFEYMKLRLYILRDDLINNGLDLLKNLNWVGGKLIKNEDREVLLNSTDLATDSISHLLGDENFVILEFEC
Protein: Beta-spectrin (Q28297)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Interaction partners:
Sequence:
LVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNHMADELINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIRDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKALLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDSRNDSFTTCIELGKSLLARKHYASEEIKENLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLDLLELRRQQEEEERKRRPPSPEPSTKASEDTESQQQWDTSKGEQVSQNGLPAEQGSPRMAETVDTGEMVNGAAEQRTSSKESSPIPSPTSDRKAKTALPAQSAATLPARTQETPSAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKTAASGIPYHSEVPVSLKEAICEVALDYKKKKHVFKLRLNDGNEYLFQAKDDEEMNTWIQAISSAISSDKHEVSASTQSTPASSRAQTLPTSVVTITSESSPGKREKDKEKDKEKRFSIFGKKK
Protein: Somatostatin receptor 1b (Somatostatin receptor type 1 subtype B) (Q5G546)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MENMATNRSGDYPEYPTGLPYNSSLDYEDYDQELDASKIIIPSIYALVCCVGLTGNAMVIYVILKYAKMKTATNIYILNLAIADELFMLSVPFLATSAAVRHWPFGSLMCRLVLSVDGINMFTSIFCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNVCVWGLSLLVILPIIIFADTVPAQDGGVDCNFLWPEAAWSVAFVVYTFLLGFLLPVGAICLCYCLMVARMRAVGLKAGWLQRRRSEKKITRMVLCIVAVFVLCWMPFYIVQLVSVFHRPPDAMVTQLFVILSYANSGANPILYGFVSDNFRRSFQRIVCFRWLESGLDGEQVDYRAVALKRQATNGQKDFPKECLASGMVFQNGTCTSRTTTL
Protein: Pectin methylesterase inhibitor 1 (Q9STH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At4g12382
- Cell wall / vacuolar inhibitor of fructosidase 1
Sequence:
MEPKLTHLCYCLLLFLPLLCQSTIAKPSSSPNPSSSINFIVSSCRVTRYQTLCVKCLAAFADKIRRNENQLAQTALAVTLVRVQSTTIYVGKLTKARRIKRREYLAVKDCVENLGDGLEMLAQSMRELKQVGRSGRDRDEFLWRLSNVETWVSAALTDETTCLDGFDGKVMDGVVKSAIRRRVVHVARVTSNALALVNRFAARHKS
Protein: CTP synthase 1 (EC 6.3.4.2) (CTP synthetase 1) (UTP--ammonia ligase 1) (P28274)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen.
Interaction partners:
- CTP synthase 2
- Nucleoside diphosphate kinase
- GMP synthase
- Golgi apyrase
- Asparagine synthetase 2
- Glutamine synthetase
- Glutamate synthase
- Amidophosphoribosyltransferase
- Large ribosomal subunit protein uL23
- Dihydroorotate dehydrogenase
Sequence:
MKYVVVSGGVISGIGKGVLASSTGMLMKTLGLKVTSIKIDPYMNIDAGTMSPLEHGECFVLDDGGETDLDLGNYERYLGVTLTKDHNITTGKIYSHVIAKERKGDYLGKTVQIVPHLTNAIQDWIERVAKIPVDDTGMEPDVCIIELGGTVGDIESAPFVEALRQFQFKVGKENFALIHVSLVPVIHGEQKTKPTQAAIKGLRSLGLVPDMIACRCSETLDKPTIDKIAMFCHVGPEQVVNVHDVNSTYHVPLLLLEQKMIDYLHARLKLDEISLTEEEKQRGLELLSKWKATTGNFDESMETVKIALVGKYTNLKDSYLSVIKALEHSSMKCRRKLDIKWVEATDLEPEAQESNKTKFHEAWNMVSTADGILIPGGFGVRGTEGMVLAARWARENHIPFLGVCLGLQIATIEFTRSVLGRKDSHSAEFYPDIDEKNHVVVFMPEIDKETMGGSMRLGLRPTFFQNETEWSQIKKLYGDVSEVHERHRHRYEINPKMVDELENNGLIFVGKDDTGKRCEILELKNHPYYIATQYHPEYTSKVLDPSKPFLGLVAASAGILQDVIEGKYDLEAGENKFNF
Protein: Cadmium-inducible lysosomal protein CDR-5 (GST C-terminal domain-containing protein) (G5EGC7)
Organism: Caenorhabditis elegans
Interaction partners:
- Heme Responsive protein
- Heme transporter hrg-4
- ShKT domain-containing protein
- Heme transporter hrg-1
Sequence:
MILEIIAGIIIILFIFNLLHTIYKTFLTTPTVNATPKIHKRDYQKDVVYLYQFPRIDTVPNLSSFCLKTETFLRAFKIPHEVIETGSLRSRNGTLPFVELNGEHIPDSDLIEVRLRKHFQIPNLSAEDESHATALCRLADNHLLSIIIKYKAAEDAWYSALLRGVPGPNCLKTILKPIVRKLFMKKVHERTGGAIGNFTEDEAEMLCHKDLQAIQDSIKGKYLFGDKITSADCTVFGEVASAYYPFPNKFSRIIDSHYPKLHEYCDRIIEELYPNDFSI
Protein: Erythropoietin induced cDNA-1 transcript variant 2 (Q8IX09)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKEKAAAFSLSGGHACGAVGSRDPNSREQGESLELCQHLASHKLSRQ
Protein: Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I)] (P04639)
Organism: Rattus norvegicus (Rat)
Function: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein B-100
- Phosphatidylcholine-sterol acyltransferase
- Apolipoprotein A-II
- Apolipoprotein C-I
- P-type phospholipid transporter
- Apolipoprotein E
- Apolipoprotein A-IV
- Apolipoprotein C-III
- Serum paraoxonase/arylesterase 1
- Scavenger receptor class B member 1
Sequence:
MKAAVLAVALVFLTGCQAWEFWQQDEPQSQWDRVKDFATVYVDAVKDSGRDYVSQFESSTLGKQLNLNLLDNWDTLGSTVGRLQEQLGPVTQEFWANLEKETDWLRNEMNKDLENVKQKMQPHLDEFQEKWNEEVEAYRQKLEPLGTELHKNAKEMQRHLKVVAEEFRDRMRVNADALRAKFGLYSDQMRENLAQRLTEIKNHPTLIEYHTKASDHLKTLGEKAKPALDDLGQGLMPVLEAWKAKIMSMIDEAKKKLNA
Protein: Meiotic driver wtf28 (A0A218N035)
Organism: Schizosaccharomyces kambucha (Fission yeast)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele.
Subcellular location: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
Interaction partners:
Sequence:
MKNKYYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGNTLPPYSENINLKDPKQMGQNITKLFNWNKSTTPPDYDENRLPITDEGNNPPNTHRENHSSGTADNSSPFLIKLIISFTPIFVLNVPAVCYLTYKDALFKDYGKDEWVYFGVWCAICLMSFISLWCFYETWTKAVKVTVIFLAQCVKVTVIFLAQCVKVTAIFSAQCIKVTVISLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTSSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIRNGIASFLGGIANAFGGIANAIRGANDNNDIPLGEMEVESEV
Protein: Anion exchange protein 3 (AE 3) (Anion exchanger 3) (Neuronal band 3-like protein) (Solute carrier family 4 member 3) (P16283)
Organism: Mus musculus (Mouse)
Function: Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:2686841}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MANGVIPPPGGASPLPQVRVPLEEPPLGPDVEEEDDDLGKTLAVSRFGDLISKTPAWDPEKPSRSYSERDFEFHRHTSHHTHHPLSARLPPPHKLRRPPPTSARHTRRKRKKEKTSAPPSEGTPPIQEEGGAGAEEEEEEEEEEEGESEAEPVEPLPPGPPQKAKFSIGSDEDDSPGLPVKAPCAKALPSVGLQSDQSPQRSGSSPSPRARASRISTEKSRPWSPSASYDLRERLCPGSALGNPGPEQRVPTDEAEAQMLGSADLDDMKSHRLEDNPGVRRHLVKKPSRIQGGRGSPSGLAPILRRKKKKKKLDRRPHEVFVELNELMLDRSQEPHWRETARWIKFEEDVEEETERWGKPHVASLSFRSLLELRRTIAQGAALLDLEQTTLPGIAHLVVETMIVSDQIRPEDRASVLRTLLLKHSHPNDDKDSGFFPRNPSSSSVNSVLGNHHPTPSHGPDGAVPTMADDQGEPAPLWPHDPDAKEKPLHMPGGDGHRGKSLKLLEKIPEDAEATVVLVGCVPFLEQPAAAFVRLSEAVLLESVLEVPVPVRFLFVMLGPSHTSTDYHELGRSIATLMSDKLFHEAAYQADDRQDLLGAISEFLDGSIVIPPSEVEGRDLLRSVAAFQRELLRKRREREQTKVEMTTRGGYAAPGKELSLEMGGSEATSEDDPLQRTGSVFGGLVRDVKRRYPHYPSDLRDALHSQCVAAVLFIYFAALSPAITFGGLLGEKTEGLMGVSELIVSTAVLGVLFSLLGAQPLLVVGFSGPLLVFEEAFFKFCRAQDLEYLTGRVWVGLWLVVFVLALVAAEGSFLVRYISPFTQEIFAFLISLIFIYETFHKLYKVFTEHPLLPFYPPDEALETGLELNSSALPPTEGPPGPRNQPNTALLSLILMLGTFLIAFFLRKFRNSRFLGGKARRIIGDFGIPISILVMVLVDYSITDTYTQKLTVPTGLSVTSPHKRTWFIPPLGSARPFPPWMMVAAAVPALLVLILIFMETQITALIVSQKARRLLKGSGFHLDLLLIGSLGGLCGLFGLPWLTAATVRSVTHVNALTVMRTAIAPGDKPQIQEVREQRVTGVLIASLVGLSIVMGAVLRRIPLAVLFGIFLYMGVTSLSGIQLSQRLLLIFMPAKHHPEQPYVTKVKTWRMHLFTCIQLGCIALLWVVKSTAASLAFPFLLLLTVPLRRCLLPRLFQDRELQALDSEDAEPNFDEDGQDEYNELHMPV
Protein: Tubulin beta-9 chain (Beta-9-tubulin) (P29517)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin alpha-6 chain
- Tubulin alpha-2 chain
- Tubulin alpha-5 chain
- Tubulin alpha-1 chain
- Gamma-tubulin complex component 4
- Tubulin-folding cofactor A
- Tubulin beta-4 chain
- Mitotic spindle checkpoint protein MAD2
- Tubulin beta-7 chain
- Tubulin beta-5 chain
Sequence:
MREILHIQGGQCGNQIGAKFWEVICGEHGIDQTGQSCGDTDLQLERINVYFNEASGGKYVPRAVLMDLEPGTMDSLRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLANPTFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYSALSVPELTQQMWDAKNMMCAADPRHGRYLTASAVFRGKMSTKEVDEQMMNVQNKNSSYFVEWIPNNVKSSVCDIAPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQYQDATVGEEEYEEDEEEEEA
Protein: Uncharacterized protein (Q383R2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
- Uncharacterized protein
- Large ribosomal subunit protein mL46
- Uncharacterized protein
- KOW domain-containing protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Large ribosomal subunit protein uL29m
Sequence:
MLRRTVCVQHYRAKLELDRIRSMLRGRARLERKVGLKRLFFLMRTQTRYRVEQQAHWERAIVRKNVDSAAREHGTGWQHLRNELGRQNVMLLPRSQQLLAQYEPLAFRAVVELCASRIPPPPPPVVASVPEESYTLWPPASHDNSECASTDGSDAPHGQQQSLSHPAARVELRCGVERVLRRGPSGLGNNVNELIDAWKEFDVSPLRKGEVNK
Protein: Flavonoid 3',5'-methyltransferase (EC 2.1.1.267) (Anthocyanin-O-methyltransferase) (VvAOMT) (C7AE94)
Organism: Vitis vinifera (Grape)
Function: Mediates O-methylation of anthocyanins. Anthocyanins are major pigments in grapes: at ripening initiation in red grapevine berries, the exocarp turns color from green to red and then to purple due to the accumulation and extent of methylation of anthocyanins. Catalyzes both 3' and 5' O-methylation of anthocyanins, with a preference for glycosylated substrates. Active on both anthocyanins and flavonols in vitro. Most active with delphinidin 3-glucoside but also acts on cyanidin 3-glucoside, cyanidin, myricetin, quercetin and quercetin 3-glucoside. Not able to methylate flavan type skeletons with chiral centers, such as catechins or dihydroquercetin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19525322}.
Interaction partners:
Sequence:
MSSSSHRGILKTEALTKYLLETSAYPREHEQLKGLREATVEKHKYWSLMNVPVDEGLFISMLLKIMNAKKTIELGVFTGYSLLATALALPQDGKIIAVDPDKEAYQTGVPFIKKAGVEHKINFIQSDAMSVLNDLIADGKEEGTLDFAMVDADKENYLNYHELLLKLVRVGGIIAYDNTLWFGSVARSEEEEMMDFERAGRVHLMKLNKFLASDPRVELSHLSIGDGVALCRRLY
Protein: Integrin alpha-D (ADB2) (CD11 antigen-like family member D) (Leukointegrin alpha D) (CD antigen CD11d) (Q13349)
Organism: Homo sapiens (Human)
Function: Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. May play a role in the atherosclerotic process such as clearing lipoproteins from plaques and in phagocytosis of blood-borne pathogens, particulate matter, and senescent erythrocytes from the blood.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-2
- Vascular cell adhesion protein 1
- Fibronectin
- Integrin beta-6
- Integrin alpha-X
- Integrin beta-7
- Integrin alpha-2
- Integrin beta-1
Sequence:
MTFGTVLLLSVLASYHGFNLDVEEPTIFQEDAGGFGQSVVQFGGSRLVVGAPLEVVAANQTGRLYDCAAATGMCQPIPLHIRPEAVNMSLGLTLAASTNGSRLLACGPTLHRVCGENSYSKGSCLLLGSRWEIIQTVPDATPECPHQEMDIVFLIDGSGSIDQNDFNQMKGFVQAVMGQFEGTDTLFALMQYSNLLKIHFTFTQFRTSPSQQSLVDPIVQLKGLTFTATGILTVVTQLFHHKNGARKSAKKILIVITDGQKYKDPLEYSDVIPQAEKAGIIRYAIGVGHAFQGPTARQELNTISSAPPQDHVFKVDNFAALGSIQKQLQEKIYAVEGTQSRASSSFQHEMSQEGFSTALTMDGLFLGAVGSFSWSGGAFLYPPNMSPTFINMSQENVDMRDSYLGYSTELALWKGVQNLVLGAPRYQHTGKAVIFTQVSRQWRKKAEVTGTQIGSYFGASLCSVDVDSDGSTDLILIGAPHYYEQTRGGQVSVCPLPRGRVQWQCDAVLRGEQGHPWGRFGAALTVLGDVNEDKLIDVAIGAPGEQENRGAVYLFHGASESGISPSHSQRIASSQLSPRLQYFGQALSGGQDLTQDGLMDLAVGARGQVLLLRSLPVLKVGVAMRFSPVEVAKAVYRCWEEKPSALEAGDATVCLTIQKSSLDQLGDIQSSVRFDLALDPGRLTSRAIFNETKNPTLTRRKTLGLGIHCETLKLLLPDCVEDVVSPIILHLNFSLVREPIPSPQNLRPVLAVGSQDLFTASLPFEKNCGQDGLCEGDLGVTLSFSGLQTLTVGSSLELNVIVTVWNAGEDSYGTVVSLYYPAGLSHRRVSGAQKQPHQSALRLACETVPTEDEGLRSSRCSVNHPIFHEGSNGTFIVTFDVSYKATLGDRMLMRASASSENNKASSSKATFQLELPVKYAVYTMISRQEESTKYFNFATSDEKKMKEAEHRYRVNNLSQRDLAISINFWVPVLLNGVAVWDVVMEAPSQSLPCVSERKPPQHSDFLTQISRSPMLDCSIADCLQFRCDVPSFSVQEELDFTLKGNLSFGWVRETLQKKVLVVSVAEITFDTSVYSQLPGQEAFMRAQMEMVLEEDEVYNAIPIIMGSSVGALLLLALITATLYKLGFFKRHYKEMLEDKPEDTATFSGDDFSCVAPNVPLS
Protein: Proline-rich protein 4 (Lacrimal proline-rich protein) (Nasopharyngeal carcinoma-associated proline-rich protein 4) (Q16378)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Statherin
- Lipocalin-1
Sequence:
MLLVLLSVVLLALSSAQSTDNDVNYEDFTFTIPDVEDSSQRPDQGPQRPPPEGLLPRPPGDSGNQDDGPQQRPPKPGGHHRHPPPPPFQNQQRPPRRGHRQLSLPRFPSVSLQEASSFFQRDRPARHPQEQPLW
Protein: Septin-12 (Q4V8G5)
Organism: Rattus norvegicus (Rat)
Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). Involved in spermatogenesis. Involved in the morphogenesis of sperm heads and the elongation of sperm tails probably implicating the association with alpha- and beta-tubulins. Forms a filamentous structure with SEPTIN7, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8IYM1, ECO:0000250|UniProtKB:Q9D451, ECO:0000269|PubMed:17685441}. Note=At interphase, forms a filamentous structure in the cytoplasm. During anaphase, translocates to the central spindle region and to the midbody during cytokinesis (By similarity). Found in the sperm annulus. {ECO:0000250, ECO:0000269|PubMed:17685441}.
Interaction partners:
- Septin-5
- Septin
- Septin
- Septin-2
- Septin-11
- Septin-8
- Neuronal-specific septin-3
- Septin-7
- Septin-10
- Septin-1
Sequence:
MDERRTPSPCSSRPSSPRTPPCEMFGPVGIEAVLDQLRIKAMKTGFEFNIMVVGQSGLGKSTMVNTLFKSKVWQSPAPNLDVPMPQTLELHSVTHVIEEKGLKLKLTVTDTPGFGDQINNDKCWDPILSYINQQYEQYLQEELLITRQRHIPDTRVHCCVYFVPPTGHCLRPLDIEFLRRLCRTVNVVPVIARADSLTIEERDAFRSRIQQNLKNHCIDVYPQQCFDEDINDRLLNSKIREQIPFAVVGADREHIVNGRCVLGRKTKWGIIEVENMAHCEFLLLRDLLIRSHLQDLKDITHNVHYENYRVLRLNESHVLPRGPGWVNLAPASPGQLMAPGPEKVRKRSKDPRDDEC