wanglab/gogpt-training-data huggingface dataset:
Protein: Exosome complex component MTR3 (Exosome component 6) (mRNA transport regulator 3 homolog) (Q8BTW3)
Organism: Mus musculus (Mouse)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Exosome complex exonuclease RRP42
- Exosome complex component RRP41
- Exosome complex component RRP46
- Exosome complex component RRP45
- Exosome complex component RRP40
- Exosome complex component RRP43
- Exosome complex component RRP4
- Exosome complex component CSL4
- Exosome complex component 10
- DIS3-like exonuclease 1
Sequence:
MPGDHRRIRGPEESQPPQLYAAEDDETPAARDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGSGPAGAGGEAPAALRGRLLCDFRRAPFSGRRRRAPQGGGGEDRELGLALQEALEPAVRLGRYPRAQLEVSALLLEDGGCALAAALTAAALALADAGVEMYDLVVGCGLSLTPGPSPTWLLDPTRLEEEHSAAGLTVALMPVLNQVAGLLGSGEGGQTESWTDAVRLGLEGCQRLYPVLQQCLVRAARRRGAAAPP
Protein: Low affinity immunoglobulin gamma Fc region receptor II (Fc gamma receptor IIB) (Fc-gamma RII) (Fc-gamma-RIIB) (FcRII) (IgG Fc receptor II beta) (Lymphocyte antigen 17) (Ly-17) (CD antigen CD32) (P08101)
Organism: Mus musculus (Mouse)
Function: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of antigen-antibody complexes from the circulation and modulation of antibody production by B-cells. Isoform IIB1 and isoform IIB1' form caps but fail to mediate endocytosis or phagocytosis. Isoform IIB2 can mediate the endocytosis of soluble immune complexes via clathrin-coated pits. Isoform IIB1 and isoform IIB2 can down-regulate B-cell, T-cell, and mast cell activation when coaggregated to B-cell receptors for AG (BCR), T-cell receptors for AG (TCR), and Fc receptors, respectively.
Subcellular location: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform IIB1]: Cytoplasm, cytoskeleton. Note=Binds the cytoskeleton and is not localized in endocytotic pits.; SUBCELLULAR LOCATION: [Isoform IIB3]: Secreted. Note=Released as a soluble molecule.
Interaction partners:
- Galectin-3
- B-lymphocyte antigen CD19
- Tyrosine-protein kinase Lyn
- High affinity immunoglobulin gamma Fc receptor I
- Receptor-type tyrosine-protein phosphatase C
- Tyrosine-protein kinase SYK
- Integrin alpha-M
- T-cell surface glycoprotein CD4
- Adhesion G protein-coupled receptor E1
- C-reactive protein
Sequence:
MESNWTVHVFSRTLCHMLLWTAVLNLAAGTHDLPKAVVKLEPPWIQVLKEDTVTLTCEGTHNPGNSSTQWFHNGRSIRSQVQASYTFKATVNDSGEYRCQMEQTRLSDPVDLGVISDWLLLQTPQLVFLEGETITLRCHSWRNKLLNRISFFHNEKSVRYHHYSSNFSIPKANHSHSGDYYCKGSLGRTLHQSKPVTITVQGPKSSRSLPVLTIVAAVTGIAVAAIVIILVSLVYLKKKQVPALPGNPDHREMGETLPEEVGEYRQPSGGSVPVSPGPPSGLEPTSSSPYNPPDLEEAAKTEAENTITYSLLKHPEALDEETEHDYQNHI
Protein: Probable multidrug resistance-associated protein lethal(2)03659 (Wunen region A protein) (P91660)
Organism: Drosophila melanogaster (Fruit fly)
Function: Vital for development.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- RING-type E3 ubiquitin transferase
Sequence:
MDKQPVLEPTFDSVSERENTSIEESSLLENNGFDHRNKDESLSVNTSPPLVCRKCFELGHQTENCKQKLTVNSENNSAQNEKEKVLPENPRARSNFISSLCFWYTIPIFRKGYRKTLDSTDLYRPLEEQKSDILGNRLCASWERELKNDGRSPSLVRALLRVFGWQLGFPGLAIFVVELGLRTLQPIFLVKLISYFSGEPDAANAGFYYAVAQIVISALTVMILTPTTFGIHHVCFKMRVAMGSMIFRKALRLTKGALGDTTSGHVVNLISNDIPRLDSAPYTVHYLWVGPLQVLVITYLMYQEIGISAVFGVLFMLLFMPIQMYLGTRTSAIQLKAAERTDNRIRMVNEIISAIQVLKMYAWEQPFEQMVTHAREKEMNTIRQGQYIRGFDFARRIVLSRVAIFLSLVGYVILGKVFTPEIAFMITAYYNVLLAAMSIYVPSAIIQTAQFLTSIRRVEQFMQSEELGSSDKSEGPSKDTVPGNPPSNNNEADLLKSAISIRDLKAKWDPNSPDYTLSGINLEIKPGSVVAVIGLTGSGKSSLIQAILGELKANSGQLQVNGSLSYTSQESWLFSGTVRQNILFGQPMDSQRYEEVVKKCALERDFDLLPLRDNTIVGERGATLSGGQKARISLARSVYRKASIYLLDDPLSAVDASVARHLFDQCVRGHLRGSTVVLVTHQEQFLPHVDQIVILANGQIKALGDYESLLKTGLITGLGSLSKTDKAKTEEQEPLNLNSPDNKNEVTPIKENSEQTVGGSSSGKEHVERQESGGISLALYRKYFQAGGGLVAFLVMLSSSVLAQVAVTGGDYFLTYWVKKESTAAGHGEMEDMESKSMDVYKYTLIIILSVIMNLSSSFLLFNIAKKASIRLHNTIFNRVTRADMHFFSINKHGSILNRFTKDMSQVDEVLPVVLVDVMQIALWLAGIIIVIANVNPLLLVPTLMLSVIFYHLRNLYLKTSRDLKRVEAINRSPVYSHLAASLNGLTTIRALDAQRVLEKEFDSYQDAHSSAFFMYISTSQAFGYCMNCICVIYISIITLSFFAFPPGNGADVGLVITQAMGLIDMVQWGVRQTAELENTMTAVERVVEYESIEPEGMLEAPDDKKPPKTWPEQGEIIFKELNLRYTPNAKAENVLKSLSFVIQPREKVGIVGRTGAGKSSLINALFRLSYTDGSVLIDTRDTRQMGLHDLRRQISIIPQEPVLFSGTMRYNLDPFDEYSDEKLWGCLEEVKLKEVVSDLPDGLASKISEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQATIRSKFRDCTVLTIAHRLHTIIDSDKVMVMDAGRVVEFGSPYELMTKSDSKVFHNLVNQSGRASYEGLLKIAQETFESS
Protein: Uncharacterized ABC transporter permease YbbP (P77504)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Thioesterase 1/protease 1/lysophospholipase L1
- Uncharacterized ABC transporter ATP-binding protein YbbA
- Uncharacterized protein YaiL
Sequence:
MIARWFWREWRSPSLLIVWLALSLAVACVLALGNISDRMEKGLSQQSREFMAGDRALRSSREVPQAWLEEAQKRGLKVGKQLTFATMTFAGDTPQLANVKAVDDIYPMYGDLQTNPPGLKPQAGSVLLAPRLMALLNLKTGDTIDVGDATLRIAGEVIQEPDSGFNPFQMAPRLMMNLADVDKTGAVQPGSRVTWRYKFGGNENQLDGYEKWLLPQLKPEQRWYGLEQDEGALGRSMERSQQFLLLSALLTLLLAVAAVAVAMNHYCRSRYDLVAILKTLGAGRAQLRKLIVGQWLMVLTLSAVTGGAIGLLFENVLMVLLKPVLPAALPPASLWPWLWALGTMTVISLLVGLRPYRLLLATQPLRVLRNDVVANVWPLKFYLPIVSVVVVLLLAGLMGGSMLLWAVLAGAVVLALLCGVLGWMLLNVLRRMTLKSLPLRLAVSRLLRQPWSTLSQLSAFSLSFMLLALLLVLRGDLLDRWQQQLPPESPNYFLINIATEQVAPLKAFLAEHQIVPESFYPVVRARLTAINDKPTEGNEDEALNRELNLTWQNTRPDHNPIVAGNWPPKADEVSMEEGLAKRLNVALGDTVTFMGDTQEFRAKVTSLRKVDWESLRPNFYFIFPEGALDGQPQSWLTSFRWENGNGMLTQLNRQFPTISLLDIGAILKQVGQVLEQVSRALEVMVVLVTACGMLLLLAQVQVGMRQRHQELVVWRTLGAGKKLLRTTLWCEFAMLGFVSGLVAAIGAETALAVLQAKVFDFPWEPDWRLWIVLPCSGALLLSLFGGWLGARLVKGKALFRQFAG
Protein: Putative ferric-chelate reductase 1 homolog (DmSDR2) (EC 1.-.-.-) (Q8MSU3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Putative ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Large ribosomal subunit protein uL23m
- Fe2OG dioxygenase domain-containing protein
- Cytochrome c oxidase subunit 7C, mitochondrial
- Uncharacterized protein
- Uncharacterized protein, isoform B
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS15m
Sequence:
MMQALTMRSWLATLVTALLAVAIWPDPGQSLPQGAPETVCDTMLPFHSGGSVLPQNSVSPFSVETSSSTLGQGQTLRVDLTGVPAGLSFGGYMIQARNRNPPHQIIGQFGPARDGTIKLMNCENSVNNSATHSNAGPKQQVILEWQSPVDFLGQVVFNATIAQSYNEFWVGVPSQPVQIVRRDLSAAPPLPTQSPSAPAGTTRAPYVPPSYVAPNNVVAVSSDPIYNGCGQSKNCFGFPDGCVATKSCTSITVVTVRGDVFEFEIQSGKGTNAAYVAVGLSDDAKMGDDLTTECVPENGRVNLYSSLTSASPYSAVRSNVNQNSARLLDASIVDGVIYCRVQRDAVTNVQGRTFDLRNGKYHLLVASGSSLKENSVGYHDIGRLPSAQPINLAEVQDLSGSSRLLIQLHGAFMIAAWIGTTSLGIIFARYFKQTWVGSQSCGTDQWFAWHRLLMVTTWSLTVAAYVLIWVELKQAVWHAHSIIGLITVILCFIQPIGALFRPGPNDKKRPYFNWGHWLGGNLAHILGIVTIFFSVKLPKAELPEWMDWILVSFVVVHVLVHLIFSIGGMASERHLSQRANTFQMGDMSHHQQHAMRNGMSMERKMDAPYAGMRKGLLGVYGVVLILFVTVLILLVVLAPIEQFLGKS
Protein: SUppressor of activated let-60 Ras (H2KZM3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKCTTRFILRYTNHTLYLSTADLVIKAIFSVIYNALSIHFVPNFIALVAPPVLTILIFFYNVNELDYFFGWLNHHLEPVTSILLTIVCISIAIYSLIRKKQFLLAEGPREFKIDDISSSVKAKNSRLEKVDHVHASCEWPQGFTVSLKAYIKVEKTNKDWVAQAASDFYELKALLHHEIKAQGAKEVVVEPVFVDQTELTTDFMDPICISRSCHNEDVGCCTIPKSTGDV
Protein: TCF19 (Transcription factor 19) (Transcription factor 19 isoform 2) (D2IYK5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLPCFQLLRIGGGRGGDLYTFHPPAGAGCTYRLGHRADLCDVALRPQQEPGLISGIHAELHAEPRGDDWRVSLEDHSSQGTLVNNVRLPRGHRLELSDGDLLTFGPEGPPGTSPSEFYFMFQQVRVKPQDFAAITIPRSRGEARVGAGFRPMLPSQGAPQRPLSTFSPAPKATLILNSIGSLSKLRPQPLTFSPSWGGPKSLPVPAPPGEVGTTPSAPPQRNRRKSVHRVLAELDDESEPPENPPPVLMEPRKKLRVDKAPLTPTGNRRGRPRKYPVSAPMAPPAVGGGEPCAAPCCCLPQEETVAWVQCDGCDVWFHVACVGCSIQAAREADFRCPGCRAGIQT
Protein: Protein-methionine methyltransferase laeA (EC 2.1.1.-) (Secondary metabolism regulator laeA) (Velvet complex subunit laeA) (C8VQG9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Methyltransferase that performs automethylation at Met-207. No other methyl-accepting substrate has been identified yet. Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Controls the expression of the sterigmatocystin, penicillin, and lovastatin gene clusters. Controls light-dependent formation of the velB-vosA complex, veA protein modification, and is required for light-mediated inhibition of sexual development. Within the velvet complex, controls light-dependent secondary metabolism. Involved in the defense response against Drosophila melanogaster larval grazing.
Subcellular location: Nucleus {ECO:0000269|PubMed:18556559}.
Interaction partners:
- Developmental and secondary metabolism regulator veA
- Velvet complex subunit B
- C2H2 type master regulator of conidiophore development brlA
- Spore development regulator vosA
- Sexual development regulator velC
- pH-response transcription factor pacC/RIM101
- Sterigmatocystin biosynthesis regulatory protein
- Conidiophore development regulator abaA
- Orotidine 5'-phosphate decarboxylase
- DNA-binding protein creA
Sequence:
MFEMGPVGTRLPAMTSPAHNHYSYHSPTSSDRGRSRQNSDAMDIQSITEREPATRYAVAGGPAPWNRNGSPSMSPMYSNNSERNQFHEENGRTYHGFRRGMYFLPCDEQEQDRLDIFHKLFTVARVSESLIYAPHPTNGRFLDLGCGTGIWAIEVANKYPDAFVAGVDLAPIQPPNHPKNCEFYAPFDFEAPWAMGEDSWDLIHLQMGCGSVMGWPNLYRRIFAHLRPGAWFEQVEIDFEPRCDDRSLDGTALRHWYDCLKQATAETMRPIAHSSRDTIKDLQDAGFTEIDHQIVGLPLNPWHQDEHERKVARWYNLAVSESIENLSLAPFSRVYRWPLERIQQLAADVKSEAFNKEIHAYNILHIYQARKPLR
Protein: Chondroitin proteoglycan 1 (Cell junction protein 1) (Cytokinesis protein cej-1) (Q17802)
Organism: Caenorhabditis elegans
Function: Required for polar body extrusion during cytokinesis in embryo development. Affects cortical granule size. Has roles in meiotic chromosome segregation, osmotic barrier function and polarization in conjunction with cpg-2. Binds chitin.
Interaction partners:
- Chondroitin proteoglycan 3
- MEiotic SPindle
- CCCH-type zinc finger protein oma-1
- Uncharacterized protein C05C10.5
- Tetratricopeptide SHNi-TPR domain-containing protein
- EGF-like domain-containing protein
- Pumilio domain-containing protein 7
- Inactive protein-tyrosine phosphatase egg-5
- RNA-binding protein pos-1
- PUM-HD domain-containing protein
Sequence:
MTLKPVLLAFLVASAYAQYGVAGMYENLPLETTTLDGSGDGSGADNGFVSGADAVAIDTDCSTKEDGLYAIGGCSPQFLTCSGGISRIMDCPADLIYDPRIVACEYSYNVPQCGGVPQDVTSTQEAYPSEETTVNPYAPVEEATTTPAEDVTVPEETTTEAYAPVDDYSTTTPAEDVPVPVETTASPYAPIVPYTTGAPAADEPVTRSAVTKSCVGKADGFYSFGECSDHYTACSNGYLIPMQCPARLAFDEARVICDYVMNVPECTNGSGNDEGSADETTPESSGEMPYSNGYGYEETTTVAEDVPSTKDYAEPIAAAYVARYPSEKTTAENVPTTTIGYEPEVVETTAPYVEETTTTVGYKPEVEETTTEAEVPTTTVGYEPEIVETTAPYVEETTTAADVPSTTAVYEPEVVETTTEAEVPTTTTVGYEPEVVETTVPYVEETTTAADVPTTTVGYEPEVEETTTEAEVPTTTVGYESEVVETTAADIPTTTIGYAPIVVESTTAADVPTTTVPAETTTEVPACVEGATAIEPCSQHYKNCVNGQEAIFICENGLFFSPEQARCAPADQIAECHQTTVQYY
Protein: Interleukin-23 receptor (IL-23 receptor) (IL-23R) (Q5VWK5)
Organism: Homo sapiens (Human)
Function: Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12023369}; Single-pass type I membrane protein {ECO:0000269|PubMed:12023369}.
Interaction partners:
- Interleukin-23 subunit alpha
- Interleukin-12 receptor subunit beta-1
- Tyrosine-protein kinase JAK2
- Interleukin-12 subunit beta
- Signal transducer and activator of transcription 3
- Non-receptor tyrosine-protein kinase TYK2
- Interleukin-10
- Interferon gamma
- Interleukin-22
- Interleukin-6
Sequence:
MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYKNFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYINISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVPQVTSKAFQHDTWNSGLTVASISTGHLTSDNRGDIGLLLGMIVFAVMLSILSLIGIFNRSFRTGIKRRILLLIPKWLYEDIPNMKNSNVVKMLQENSELMNNNSSEQVLYVDPMITEIKEIFIPEHKPTDYKKENTGPLETRDYPQNSLFDNTTVVYIPDLNTGYKPQISNFLPEGSHLSNNNEITSLTLKPPVDSLDSGNNPRLQKHPNFAFSVSSVNSLSNTIFLGELSLILNQGECSSPDIQNSVEEETTMLLENDSPSETIPEQTLLPDEFVSCLGIVNEELPSINTYFPQNILESHFNRISLLEK
Protein: Protein NCA1 (NO CATALASE ACTIVITY 1) (Q9M2V1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has holdase chaperone activity that may fold catalase to a functional structure. Not required for the peroxisome import of catalases. Required for the activity of catalases and acts mainly at the post-transcriptional level.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24285797, ECO:0000269|PubMed:25700484}. Nucleus {ECO:0000269|PubMed:24285797}.
Interaction partners:
- Catalase-2
- At4g19200
Sequence:
MTTTSVCPFSKAARPDDGSTRKQGEITASGCPFSKAARPDDASARKQGETTASGCPFSKSARPDENGSKGCPEQEGNLNKDSTDSATVPAKCPFGYDSQTFKLGPFSCMLCQALLYESSRCVPCTHVFCKVCLTRFKDCPLCGADIESIEVDENLQKMVDQFIEGHARIKRSVVNGTEKEEVENDNKKVIYADVSMERGSFLVQQAMRAFSAQNYESAKSRLAMCTEDIRDQLGREGNTPELCSQLGAVLGMLGDCSRAMGDSSSAVKHFEESVEFLMKLPLNDLEITHTLSVSLNKIGDLKYYDEDLQAARSYYDRALNVRRDAMKHHPNAPSQILDVAVSLAKVADIDRTLQNEVAATDGFKEGMRLLESLKLDSEDSALEQRRLSVLEFLKKQVETDAETAL
Protein: SERTA domain-containing protein 4 (Q9NUC0)
Organism: Homo sapiens (Human)
Interaction partners:
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- E3 ubiquitin-protein ligase CBLL2
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- SERTA domain-containing protein 1
Sequence:
MTLVLSMNRFCEPIVSEGAAEIAGYQTLWEADSYGGPSPPGPAQAPLQGDRGAGPPLAGSHYRGISNPITTSKITYFKRKYVEEEDFHPPLSSCSHKTISIFEERAHILYMSLEKLKFIDDPEVYLRRSVLINNLMKRIHGEIIMQNNWCFPACSFNGTSAQEWFMAQDCPYRKRPRMAKEECEKFHACCFYQECGGHYLNLPLSVNANVGSASTAASSPSASSSSSSSSSSPPLPLPSCSRQVDFDVGSASIYKSDGQIPANEIFVTNVRSLGVQEKAKLNDEKANDDTNRDGGPLSHEPVGNDLAFECKGQFYDYFETGYNERNNVNESWKKSLRKKEASPPSNKLCCSKGSKI
Protein: Protein TRANSPARENT TESTA GLABRA 1 (WD-repeat protein GhTTG3) (Q8LJT0)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- DNA damage-binding protein 1a-like
- DNA damage-binding protein 1
- DNA excision repair protein ERCC-8-like
- DNA excision repair protein ERCC-8-like
- ADP-ribosylation factor
Sequence:
MENSTQESHLRSDNSVTYESAYTVYAMALSSTPSSTNINHQRIALGSFLEDYTNRVDIISFDPETLSFKTHPKLAFDHPYPPTKLMFQPNRKSASSSSSCSDLLASTGDFLRLWEVRESSIEPVTVLNNSKTSEFCAPLTSFDWNDVEPKRIGTSSIDTTCTIWDIEKCVVETQLIAHDKEVYDIAWGEARVFASVSADGSVRIFDLRDKEHSTIIYESPQPDTPLLRLAWNKQDLKYMATIQMDSNKVVILDIRSPTTPVAELERHHASVNAIAWAPQSCKHICSAGDDTQALIWELPTVAGPNGIDPLCVYSAGYEINQLQWSAAQPDWIAIAFSNKLQLLKV
Protein: Sperm microtubule inner protein 6 (Ciliated bronchial epithelial protein 1) (Spermatid-specific manchette-related protein 1) (Testis development protein NYD-SP22) (Q8NCR6)
Organism: Homo sapiens (Human)
Function: May play a role in spermatogenesis (By similarity). May be involved in differentiation or function of ciliated cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q2MH31}. Nucleus {ECO:0000269|PubMed:15242845}. Cytoplasm {ECO:0000269|PubMed:15242845}. Mitochondrion {ECO:0000250|UniProtKB:Q2MH31}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:28601408}. Note=During spermatid elongation (step 10), localizes along the length of the manchette and later during the elongation process only at the distal ends of spermatid manchette (step 12). In late elongated spermatids (step 16), in the final steps of spermiogenesis, localization is restricted to the midpiece of the flagellum. Localizes at the contractile ring in dividing cells (By similarity). Predominantly perinuclear in bronchial epithelial cells but also detected in the nucleus in some primary epithelial cells and in a number of cell lines (PubMed:15242845). {ECO:0000250|UniProtKB:Q2MH31, ECO:0000269|PubMed:15242845}.
Interaction partners:
Sequence:
MFLFSRKTRTPISTYSDSYRAPTSIKEVYKDPPLCAWEANKFLTPGLTHTMERHVDPEALQKMAKCAVQDYTYRGSISGHPYLPEKYWLSQEEADKCSPNYLGSDWYNTWRMEPYNSSCCNKYTTYLPRLPKEARMETAVRGMPLECPPRPERLNAYEREVMVNMLNSLSRNQQLPRITPRCGCVDPLPGRLPFHGYESACSGRHYCLRGMDYYASGAPCTDRRLRPWCREQPTMCTSLRAPARNAVCCYNSPAVILPISEP
Protein: Uncharacterized methyltransferase C1348.04 (EC 2.1.1.-) (Q9P3V6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable methyltransferase.
Interaction partners:
Sequence:
MNLVQLGKLHENVLDAGCEPNRNARYLASLGYKVVGIDISERAISKAIDKTSSEKSNVNFNQRDFSRLNEFKGHFDTVIDIGCFHSILNSDHEPYTASLSHICHSDSSVFLRAFSETNKSRYRRWQGHKRYSLALKRNNVKKLSL
Protein: E3 ubiquitin-protein ligase PEP5 (EC 2.3.2.27) (A0A1D8PMF6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}. Vacuole membrane {ECO:0000256|PIRNR:PIRNR007860}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR007860}; Cytoplasmic side {ECO:0000256|PIRNR:PIRNR007860}.
Interaction partners:
- Vacuolar protein sorting-associated protein 41
- Tethering complex ATP-binding subunit
- Probable vacuolar protein sorting-associated protein 16 homolog
- CORVET complex membrane-binding subunit
- CNH domain-containing protein
- CORVET complex subunit
- CCZ1/INTU/HSP4 first Longin domain-containing protein
- V-SNARE protein
- Vam7p
- Ypt7p
Sequence:
MSSPTYSPSRTISSPLLSLSSWRQFQLFDYTPIRDPNYHSSHALYSDPTLSCITATTTSYLIIAINHCTIKLINLSDLTCQLTFDAYNIDYRITFIEPIHNSNNLFVTLAEKQGMPSIIKLWDISKLLNLANNENNDSSKNSKLDQSEYRFEFQTQVLVNDHSSGTTGIGDNSYPISCFKFNYDLTCLAIGYTNGKVILVRGDLLRDRGAKQRLIYNSGNNDPITGVQFNETEQVLYVTTTEKLLTVATTGRNHEKPLKILSNKYGANLNCTDIDESNQNLIVGLNDSIQFYDCFTKISTINFKLAKSRIIKCKQYLLIVSPEERNKAGVSETDHGIDKSLMSRIVILDLVNNHISFNLLISDSSISHAFSLSNGTFLLLTTDGVLYKINEKSINQQIEIVLQRELFSVAFNLGQQYKLPNETLLRIQILHGDYLYDQNKFDEAIDVYIKCLELFKKSGKIVEQKQRNNRQDNQTEVEEEEDIDEFIINIITKFKEATNISNLTKFLIRLYEKSLANIDHITLLLCCYCKLKKIDNLNEFIDELDLSIENLQELNYELIINLFKECGFYDQVLKLLYKLNQPNLIVDIQLNDLHKPKLALNYMKTLTIDDLLLILIDHSTNLLDSCPLETTELLINVFTGKYQPNKPNAKYVFDVSNNGNTSTMNQPQKNPEKESSEREKSVDISNYRAFLNYLSLQSEETDNSDNYTESKTSQENPTLLSNKEPTYLPPKPNLIYASFTNHPKEFVIFLEASLEAFNKYDGNIVDKRETLLTLLEIYLSLNKSTGDKEWLDKAETLTRDYNQLLDNQALLLLSHIYNFKPGEVIAQEKSGNEIDLFMSCQLNQDVEGCFEILEKYGDTKPQLYELMLKFIISSKTIFDQIKYEDIQVILEQIKIYKLLTPIELVDILTENPDNEFITLGLVKDYFIDYFQQQTKEISNNTKLIEKYEQESTKNSFKLSELSKPFVIQNNKCSGCNLKLDFPVIHFKCKHSFHQKCLSTNLIATSTESSTSSTPTSMSTSMLNPNNNAVINHNDDDKFTCPICIHKFNDIKNAKLNQYKLGDAANQNKENFDVFINSLHSSNDKFKFVSDYIGKGVMEDQ
Protein: Succinate dehydrogenase cytochrome b556 subunit (Cytochrome b-556) (P69054)
Organism: Escherichia coli (strain K12)
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Succinate--CoA ligase subunit beta
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Succinate dehydrogenase iron-sulfur subunit
- Fumarate reductase iron-sulfur subunit
- Fumarate reductase flavoprotein subunit
- Succinate--CoA ligase subunit alpha
- 2-oxoglutarate dehydrogenase E1 component
- Fumarate hydratase class I, aerobic
- Cytochrome bo
Sequence:
MIRNVKKQRPVNLDLQTIRFPITAIASILHRVSGVITFVAVGILLWLLGTSLSSPEGFEQASAIMGSFFVKFIMWGILTALAYHVVVGIRHMMMDFGYLEETFEAGKRSAKISFVITVVLSLLAGVLVW
Protein: Glycerol-3-phosphate O-acyltransferase 1 (G-3-P acyltransferase 1) (GPAT 1) (EC 2.3.1.15) (Dihydroxyacetone phosphate acyltransferase 1) (DHAP-AT 1) (EC 2.3.1.42) (Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 1) (Suppressor of choline-transport mutants 1) (P32784)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone phosphate sn-1 acyltransferase, catalyzing the first and committed reaction in the de novo synthesis of glycerophospholipids and triacylglycerols (TAGs). Prefers Gly-3-P over dihydroxyacetone phosphate and has a marked preference for 16-carbon fatty acyl chains. Transfers a fatty acid from fatty acyl-CoA to the sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid (LysoPA). These lipids not only are precursors of glycerolipids, but also are dynamic components of signal transduction systems that control cell physiology. SCT1 is the primary supplier of diacylglycerols (DAG), used mainly in TAG synthesis and phosphatidylcholine (PC) synthesis through the CDP-choline pathway. Regulates fatty acid desaturation, that is, the ratio of unsaturated versus saturated fatty acyl chains, by competing with the desaturase OLE1 for the common substrate C16:0-CoA. Sequesters C16:0-CoA into lipids, thereby shielding it from desaturation by OLE1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19525420}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to both perinuclear and cortical endoplasmic reticulum. {ECO:0000269|PubMed:19525420}.
Interaction partners:
- Lysophospholipid acyltransferase
- Phosphatidic acid phosphohydrolase 1
- Glycerol-3-phosphate O-acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Lysophosphatidic acid:oleoyl-CoA acyltransferase 1
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Triacylglycerol lipase 4
- Triacylglycerol lipase 5
- Lipid phosphate phosphatase 1
- Glycerol-3-phosphate dehydrogenase, mitochondrial
Sequence:
MPAPKLTEKFASSKSTQKTTNYSSIEAKSVKTSADQAYIYQEPSATKKILYSIATWLLYNIFHCFFREIRGRGSFKVPQQGPVIFVAAPHANQFVDPVILMGEVKKSVNRRVSFLIAESSLKQPPIGFLASFFMAIGVVRPQDNLKPAEGTIRVDPTDYKRVIGHDTHFLTDCMPKGLIGLPKSMGFGEIQSIESDTSLTLRKEFKMAKPEIKTALLTGTTYKYAAKVDQSCVYHRVFEHLAHNNCIGIFPEGGSHDRTNLLPLKAGVAIMALGCMDKHPDVNVKIVPCGMNYFHPHKFRSRAVVEFGDPIEIPKELVAKYHNPETNRDAVKELLDTISKGLQSVTVTCSDYETLMVVQTIRRLYMTQFSTKLPLPLIVEMNRRMVKGYEFYRNDPKIADLTKDIMAYNAALRHYNLPDHLVEEAKVNFAKNLGLVFFRSIGLCILFSLAMPGIIMFSPVFILAKRISQEKARTALSKSTVKIKANDVIATWKILIGMGFAPLLYIFWSVLITYYLRHKPWNKIYVFSGSYISCVIVTYSALIVGDIGMDGFKSLRPLVLSLTSPKGLQKLQKDRRNLAERIIEVVNNFGSELFPDFDSAALREEFDVIDEEEEDRKTSELNRRKMLRKQKIKRQEKDSSSPIISQRDNHDAYEHHNQDSDGVSLVNSDNSLSNIPLFSSTFHRKSESSLASTSVAPSSSSEFEVENEILEEKNGLASKIAQAVLNKRIGENTAREEEEEEEEEEEEEEEEEEGKEGDA