wanglab/gogpt-training-data huggingface dataset:
Protein: Prelamin-A/C [Cleaved into: Lamin-A/C (70 kDa lamin) (Renal carcinoma antigen NY-REN-32)] (P02545)
Organism: Homo sapiens (Human)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Required for cardiac homeostasis.
Subcellular location: Nucleus lamina {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547, ECO:0000305|PubMed:10080180}. Nucleus envelope {ECO:0000269|PubMed:29599122, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:31548606}. Nucleus matrix {ECO:0000269|PubMed:31548606}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina (PubMed:15317753). EMD is required for proper localization of non-farnesylated prelamin-A/C (PubMed:19323649). Also localizes to the micronuclear envelope in response to response to genome instability (PubMed:37788673). {ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:37788673}.; SUBCELLULAR LOCATION: [Isoform C]: Nucleus speckle {ECO:0000269|PubMed:16061563}.
Interaction partners:
- Emerin
- SUN domain-containing protein 2
- SUN domain-containing protein 1
- Nesprin-1
- Lamin-B1
- Barrier-to-autointegration factor
- Nesprin-2
- Lamin-B2
- Lamina-associated polypeptide 2, isoform alpha
- CAAX prenyl protease 1 homolog
Sequence:
METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM
Protein: Biotin--protein ligase (EC 6.3.4.-) (Biotin apo-protein ligase) [Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9); Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC 6.3.4.10) (Holocarboxylase synthetase) (HCS); Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)] (Q920N2)
Organism: Mus musculus (Mouse)
Function: Biotin--protein ligase catalyzing the biotinylation of the 4 biotin-dependent carboxylases acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, and methylcrotonyl-CoA carboxylase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P50747}. Mitochondrion {ECO:0000250|UniProtKB:P50747}.
Interaction partners:
- Biotinidase
- Pyruvate carboxylase, mitochondrial
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Acetyl-CoA carboxylase 1
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Acetyl-CoA carboxylase 2
- CCA tRNA nucleotidyltransferase 1, mitochondrial
Sequence:
MEDRLQMDNGLIAQKIVSVHLKDPALKELGKASDKQVQGPPPGPEASPEAQPAQGVMEHAGQGDCKAAGEGPSPRRRGCAPESEPAADGDPGLSSPELCQLHLSICHECLELENSTIDSVRSASAENIPDLPCDHSGVEGAAGELCPERKGKRVNISGKAPNILLYVGSGSEEALGRLQQVRSVLTDCVDTDSYTLYHLLEDSALRDPWSDNCLLLVIASRDPIPKDIQHKFMAYLSQGGKVLGLSSPFTLGGFRVTRRDVLRNTVQNLVFSKADGTEVRLSVLSSGYVYEEGPSLGRLQGHLENEDKDKMIVHVPFGTLGGEAVLCQVHLELPPGASLVQTADDFNVLKSSNVRRHEVLKEILTALGLSCDAPQVPALTPLYLLLAAEETQDPFMQWLGRHTDPEGIIKSSKLSLQFVSSYTSEAEITPSSMPVVTDPEAFSSEHFSLETYRQNLQTTRLGKVILFAEVTSTTMSLLDGLMFEMPQEMGLIAIAVRQTQGKGRGPNAWLSPVGCALSTLLVFIPLRSQLGQRIPFVQHLMSLAVVEAVRSIPGYEDINLRVKWPNDIYYSDLMKIGGVLVNSTLMGETFYILIGCGFNVTNSNPTICINDLIEEHNKQHGAGLKPLRADCLIARAVTVLEKLIDRFQDQGPDGVLPLYYKYWVHGGQQVRLGSTEGPQASIVGLDDSGFLQVHQEDGGVVTVHPDGNSFDMLRNLIVPKRQ
Protein: Seripauperin-16 (P35994)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Seripauperin-20
- Seripauperin-3
- Seripauperin-10
- Seripauperin-18
- Seripauperin-14
- Seripauperin-15
- Seripauperin-12
- Seripauperin-2
- Seripauperin-13
- Seripauperin-11
Sequence:
MVKLTSIAAGVAAIAAGVAAAPATTTLSPSDERVNLVELGVYVSDIRAHLAQYYLFQAAHPSETYPVEIAEAVFNYGDFTTMLTGIPAEQVTRVITGVPWYSTRLRPAISSALSKDGIYTIAN
Protein: Protein IRL10 (TRL10) (F5HI32)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Subcellular location: Virion membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MYPRVMHAVCFLALGLISYVAVCAENTVTTNCLVKAENTHLTCKCNPNTTSNTNNGSKCHAMCKCRVTEPITMLGAYSAWGAGSFVATLIVLLVVFFVIYAREEEKNNTGTEVDQCLAYRSLTRKKLEQHAAKKQNIYERIPYRPSRQNDNSPLIEPTGTDDEEDEDDDV
Protein: N-acetyllactosaminide alpha-1,3-galactosyltransferase (EC 2.4.1.87) (UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase) (Galactosyltransferase) (Q3L7M0)
Organism: Rattus norvegicus (Rat)
Function: Synthesizes the galactose-alpha(1,3)-galactose group by catalyzing the transfer of a galactose residue, with an alpha-1,3 linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide borne by a glycoprotein or a glycolipid. Preferentially glycosylates proteins, can synthesize galactose-alpha(1,3)-galactose on glycoproteins but cannot synthesize the glycosphingolipid isoglobotrihexosylceramide or isogloboside 3 (iGb3).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:17206613}; Single-pass type II membrane protein {ECO:0000269|PubMed:17206613}. Note=Membrane-bound form in trans cisternae of Golgi.
Interaction partners:
- Alpha-lactalbumin
- Beta-1,4-galactosyltransferase
- Beta-1,4-galactosyltransferase
- Cytidine monophospho-N-acetylneuraminic acid hydroxylase, pseudogene
Sequence:
MVTMPQDLHVKVSMSRSKSETSLLSSRSGSQEKIMNVKGKIILSVLMVSTVLVVFWEYVNRTHSYQEEDIERAREKGRNGDSIVEPQLWDWFNPKNRPEVLTVTPWKAPIVWEGTYDTALLEKYYARQKITVGLTVFAVGKYIEHYLEDFLESANKYFMVGHRVIFYVMMDDTSRMPAVHLSPLHSLQVFEIRSEKRWQDISMMRMKTIGEHILDHIQHEVDFLFCMDVDQVFQDNFGVETLGQLVAQLQAWWYKASPDEFTYERRELSAAYIPFGEGDFYYHAAVFGGTPVHILNLTRECFKGILQDKKHDIEAQWHDESHLNKYFLFNKPTKILSPEYCWDYHIGLPSDIKNVKIAWQTKEYNLVRSNV
Protein: Uncharacterized protein Rv0940c (P9WKP1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Putative coenzyme F420-dependent oxidoreductase Rv3520c
- ChsH2 C-terminal OB-fold domain-containing protein
- Possible lipid transfer protein or keto acyl-CoA thiolase Ltp4
- Luciferase-like domain-containing protein
Sequence:
MRFSYAEAMTDFTFYIPLAKAAEAAGYSSMTIPDSIAYPFESDSKYPYTPDGNREFMDGKPFIETFVLTAALGAVTTRLRFNFFVLKLPIRPPALVAKQAGSLAALIGNRVGLGVGTSPWPEDYELMGVPFAKRGKRIDECIEIVRGLTTGDYFEFHGEFYDIPKTKMTPAPTQPIPILVGGHADAALRRAARADGWMHGGGDPDELDRLIARVKRLREEAGKTSPFEIHVISLDGFTVDGVKRLEDKGVTDVIVGFRVPYTMGPDTEPLQTKIRNLEMFAENVIAKV
Protein: Nuclear receptor coactivator 2 (NCoA-2) (Glucocorticoid receptor-interacting protein 1) (GRIP-1) (Steroid receptor coactivator 2) (SRC-2) (Transcriptional intermediary factor 2) (Q61026)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC1 expression. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK-BMAL1 heterodimer.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15596}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Estrogen receptor
- Retinoic acid receptor RXR-alpha
- Nuclear receptor coactivator 1
- Nuclear receptor coactivator 3
- Glucocorticoid receptor
- Bile acid receptor
- Peroxisome proliferator-activated receptor gamma
- Estrogen receptor beta
- Androgen receptor
Sequence:
MSGMGENTSDPSRAETRKRKECPDQLGPSPKRSTEKRNREQENKYIEELAELIFANFNDIDNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMMLEALDGFFFVVNLEGSVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSMVNGGSWSGEPPRRSSHTFNCRMLVKPLPDSEEEGHDSQEAHQKYEAMQCFAVSQPKSIKEEGEDLQSCLICVARRVPMKERPTLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLVRRCIQKFHTQHEGESLSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQTTNEPQLVISLHMLHREQNVCVMNPDLTGQAMGKPLNPISSSSPAHQALCSGNPGQDMTLGSNINFPMNGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPGQASSVLSPRQRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQALSEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQAEASCHPEEQKGPNDSSMPQAASGDRAEGHSRLHDSKGQTKLLQLLTTKSDQMEPSPLPSSLSDTNKDSTGSLPGPGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKELSQESSSTAPGSEVTVKQEPASPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTKLIAMKTVKEEVSFEPSDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPTGSVDKQAIINDLMQLTADSSPVPPAGAQKAALRMSQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAGPFPPIRNSSPYSVIPQPGMMGNQGMLGSQGNLGNNSTGMIGSSTSRPSMPSGEWAPQSPAVRVTCAATTGAMNRPVQGGMIRNPTASIPMRANSQPGQRQMLQSQVMNIGPSELEMNMGGPQYNQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALLDQLYLALRNFDGLEEIDRALGIPELVSQSQAVDAEQFSSQESSIMLEQKPPVFPQQYASQAQMAQGGYNPMQDPNFHTMGQRPNYTTLRMQPRPGLRPTGIVQNQPNQLRLQLQHRLQAQQNRQPLMNQISSVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMQQQVQQRTLMMRGQGLNVTPSMVAPAGLPAAMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATTPQSPLMSPRMAHTQSPMMQQSQANPAYQPTSDMNGWAQGSMGGNSMFSQQSPPHFGQQANTSMYSNNMNISVSMATNTGGLSSMNQMTGQMSMTSVTSVPTSGLPSMGPEQVNDPALRGGNLFPNQLPGMDMIKQEGDASRKYC
Protein: Telomeric repeat binding factor 2 (H3BR06)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSLPALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTMAKKALKSESAASSTGKEDKQPAPGPVEKPPREPARQLRNPPTTIGMMTLKAAFKTLSGAQDSEAAFAKLDQKDLVLPTQALPASPALKNKRPRKDENESSAPADGEGGSELQPKNKRMTISRL
Protein: Nectin cell adhesion molecule 3 (A0A8I5ZU75)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MARTPGPALLCPGGGKAQLSSASPPAAGLLLPAPTPPPLLLLLIPLLLFSRLCGALAGSIIVEPHVTAVWGKNVSLKCLIEVNETITQISWEKIHGKSTQTVAVHHPQYGFSVQGEYQGRILFKNYSLNDATITLHNIGFSDSGKYICKAVTFPLGNAQSSTTVTVLVEPTVSLMKGPDSLIDGGNETVAAVCIAATGKPVARIDWEGDLGEMESTITSFPNETATIISQYKLFPTRFARGRRITCVVKHPALEKDIRYSFILDIQYAPEVSVTGYDGNWFVGRKGVNLKCNADANPPPFKSVWSRLDGEWPDGLLASDNTLHFVHPLTFNYSGVYVCKVTNSLGQRSDQKVIYISDPPTTTTLQPTVQWRSSTADVQDLATEHKKLPFPLSTLATLKDDTIGTIIASVVGGALFVVLVSILAGVFCYRRRRTFRGDYFAKNYIPPSDMQKESQIDVLQHDEHDSYPDSVKKENKAPVNNLIRKDYLEEPEKTQWNNVENLTRFERPMDYYEDLKMGMKFVSDERYNENEDDLVSHVDGSVISRREWYV
Protein: Basic leucine zipper transcriptional factor ATF-like 3 (B-ATF-3) (21 kDa small nuclear factor isolated from T-cells) (Jun dimerization protein p21SNFT) (Q9NR55)
Organism: Homo sapiens (Human)
Function: AP-1 family transcription factor that controls the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Required for development of CD8-alpha(+) classical dendritic cells (cDCs) and related CD103(+) dendritic cells that cross-present antigens to CD8 T-cells and produce interleukin-12 (IL12) in response to pathogens (By similarity). Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:12087103}.
Interaction partners:
- Transcription factor Jun
- Basic leucine zipper transcriptional factor ATF-like
- Transcription factor JunB
- Basic leucine zipper transcriptional factor ATF-like 2
- Metallophosphoesterase 1
- Transcription factor JunD
- Interferon regulatory factor 8
- Integrin alpha-X
- Integrin alpha-E
- Cyclic AMP-dependent transcription factor ATF-2
Sequence:
MSQGLPAAGSVLQRSVAAPGNQPQPQPQQQSPEDDDRKVRRREKNRVAAQRSRKKQTQKADKLHEEYESLEQENTMLRREIGKLTEELKHLTEALKEHEKMCPLLLCPMNFVPVPPRPDPVAGCLPR
Protein: Helicase-like transcription factor (EC 2.3.2.27) (EC 3.6.4.-) (RING-type E3 ubiquitin transferase HLTF) (RUSH-1) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3) (Sucrose nonfermenting protein 2-like 3) (Q95216)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity. This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1, to which this protein can bind directly. Mediates repression by c-Rel through a DNA-looping mechanism. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA (By similarity). Transcriptional regulator that mediates the ability of prolactin to augment progesterone-dependent transcription of the SCGB1A1/uteroglobin gene through a bipartite progesterone receptor half-site/overlapping Y-box combination (-38/-26) where progesterone activation is attenuated by nuclear factor Y binding. Regulation also involves two GC-rich sequences in the proximal promoter (positions -162/+90) and a RUSH/SMARCA3 site (positions -616/-611) in the 5'-untranslated region.
Subcellular location: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Cytoplasmic and nuclear localization in the presence of prolactin. Nuclear localization is stimulated by progesterone.
Interaction partners:
- RING-type E3 ubiquitin transferase
- Proliferating cell nuclear antigen
- DNA repair protein RAD51 homolog 1
- Protein S100-A10
- DNA polymerase zeta catalytic subunit
- Exonuclease 1
- RNA helicase
- DNA repair protein RAD52 homolog
- UBC core domain-containing protein
- UBC core domain-containing protein
Sequence:
MSWMFKRDPVWKYLQTVQYGVHGNFSRLSYPTFFPRFEFQDIIPPDDFLTSDEELDSVLFGTLRGHVVGLRYYTGVVNNNEMVALQREPNNPYDKNAIKVNNVNGNQVGYLKKELAAALAYIMDNKLAQIEGVVPYGANNAFTMPLQMTFWGKEENRKAVLDQLKKHGFKLGPAPKTLGFSLESGWGSGRAGPSYSMPVHAAIQMTTEQLKTEFDKLFEDLKEDDKTQEMEPAEAVETPLLPHQKQALAWMVSRENSRELPPFWELRNDLYYNTITNFSEKDQPENVHGGILADDMGLGKTLTAIAVILTNFHDGKPLPVERMKKNQVKKECNSSESDKPGRKDTIKKTDGLSKEGSRYSEEPSISDVKKNKYSMSELSSSQPKRKKIAVQYIESSDSEEIEISELPQKMKGKLKNVQSETKRVKVGPSKIKEDTAFACALTSSASTTTKKILKKGASAQRVQRKLMFEERPRTTLIICPLSVLSNWIDQFGQHIKSDVHLNFYVYYGPDRIRDPALLSKQDIVLTTYNILTHDYGTKGDSPLHSIRWLRVILDEGHAIRNPNAQQTKAVLDLEAERRWVLTGTPIQNSLKDLWSLLSFLKLKPFVDREWWHRTIQRPVTMGDEGGLRRLQSLIKNITLRRTKTSKIKGKPVLELPERPVFIQHITLSDEERKIYQSVKSEGKATIGRYFNEGTVLAHYADVLGLLLRLRQICCHTHLLTNTVSSSGPSGNDTPEELRKKLIKKMKLILSSGSDEECAICLDSLTVPVITHCAHVFCKPCICQCIQNEQPHAKCPLCRNDIHGDNLLECPPEELACDSEKKSNMEWTSSSKINALMHALIDLRTKNPNIKSLVVSQFTTFLSLIETPLKASGFVFTRLDGSMAQKKRVESIQCFQNTEAGSPTIMLLSLKAGGVGLNLCAASRVFLMDPAWNPAAEDQRFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNTKRELAAGAFGTKKNANEMKQAKINEIRTLIDL
Protein: Alpha-actinin, sarcomeric (Q9XVU8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVDYYQQPPSYHQPGYDYTQQEEEWDREGLLDPAWEKQQKKTFTAWCNSHLRKAGTSIDTIEEDFRNGLKLMLLLEVISGEPLPKPDRGKMRFHKIANVNKALEYIESKGVKLVSIGAEEIVDGNVKMTLGLIWTIILRFAIQDINVEELSARDGLLLWCQRKTAPYNNVNVQNFHNSWKDGLAFCALIHRHRPDLLDYSQLHKGDPIHNLNLAFDIAEKHLDIPKMLDAEDMANSQPDEKAVMTYVSCYYHYFSGMRKAETAANRICRVLKVNQENEKMMEDYENLASDLLAWINRWMPWLANRSTDDTLQQAQQKLEDYRNYRRREKPPRIEDKGRLETLFNTLQTRLRLSNRPAFLPRDGHLIKDINAAWAGLEDSEKGFEEWLLSEIMRLERLEHLAEKFRRKCALHEEWAHGKEDALRSNDWRSCGLYKIKALRKRHEAFESDLGAHQDRVEQIAAIARELNNLRYPDIGPINARCQAICSQWDRLGQLSSKRRETLEDAERIAERLDSLYLDFAKRAAPFNNWLDGAREDLADLVIVHEMREIEELVNAHDQFKSTLGDADREFSSINQIEHEVEHLVTSHGLDRELLRNPYTDLSASDIRRKWGEVQNSVPRRDSQLQAELKRQQNNERLRTIFAEKANQVGPWLERELEQVLAIGLGGRGRLEDAIQQLRSIQRNVLGYKPNLDELERVHQEMQENFVFENRKSRYSMESLRVGWETLLTSINKTINEFENQVLLRDSKGISEEQIAEFRASFSHFDKERAGLDPEQLRSCLISVGYTIRPGREGDAELHRVLAHVDPNRMGRVPFEAFLDFMTKENSDQDTVEQMIDSFRILASGKTFITADELERELPRDQAAYCMARMAPSREPGAPPRSFDYVTFSRSLYSQ
Protein: alpha-1,2-Mannosidase (EC 3.2.1.-) (Q57W82)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- UDP-glucose:glycoprotein glucosyltransferase, putative
- Calreticulin
- Endoplasmic reticulum oxidoreductin, putative
Sequence:
MPWVRALLVLVTVFFVRLPSVMREERFHQYGNGESRKLHNVSDMHPIQAEMLPYVRDMIDHAFGSYIKYAFPKDELCPVSGTGKNTMGGYGWTLIDSLDTLAIAGFHKEFRRHAKWVEEHLTFDIDESVSVFETTIRALGGLLAAHFMYEEGIVPIIPSEHDYNGGFLRLAVDLADRLMPCFDTPTGIPYGAINLRRGVSGGESQLANTAGAGTLLMEMTVLSRITGDEKYERAARRASEALFAARDSQTELMGNHIHTHTGIWRHGESSVGGNIDSVIEYFIKSHSMSGDIGDWERFERTARAVNRYVRKGGMLLAASMYSGRRLQTSQESLSSFFPGNLVLGGHLHEAVESSWPIHTFFKHFGVLPEIFSLESGEPSWMSHDYVGRPEHIESLYMLYRATRDPTYLLMGKELALAINLRMRTPYGFSSVSDVRYPHHDGVHRDSMESFMIAETLKYLYLLFDECNAVHMQGRMGGRASPHCVMDSGSGSSVSHVGWVFNTEAHLFPNSAEWWAPTSLETLDKEAEDPAAALRRQRLEVIDGLLASFEEVDGEVVGANDKGGAALYQFHCANHALSDIGRLSKSVFR
Protein: Uncharacterized protein FAM120AOS (FAM120A opposite strand protein) (Q5T036)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKTKDIGDDDTVASEFWSGALSQPSSVPTRPRTPNRDSWRRAWAARGLHPRPSILQPGPARLSRARAGGTRCPQRRHGRATFCALGRGIGVRRGPGPRPARIPGLTLTWKRMSARRMQWAMQTGGRNQTFGGGVPLFWTWLTICCAVWRSLPCRLTHSCSRAFSSAPLKKTKSSMLPPKQALASAARNLCRGAGCNRQAVAGQLLPSTWSLHAHGLAKEAPILPVKKISRSCSVNNKVSKKTTKPPTLRSFLSPI
Protein: 12-oxophytodienoate reductase 1 (EC 1.3.1.42) (12-oxophytodienoate-10,11-reductase 1) (OPDA-reductase 1) (OsOPR1) (Q84QK0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probably involved in the biosynthesis or metabolism of oxylipin signaling molecules. In vitro, reduces cis(-)-12-oxophytodienoic acid (cis(-)-OPDA) and to cis(-)-OPC-8:0.
Interaction partners:
- Allene oxide cyclase, chloroplastic
- 4-coumarate--CoA ligase-like 4
- Os10g0190800 protein
- Electron transfer flavoprotein subunit beta, mitochondrial
Sequence:
MVHAPAKVAAAAAIPLLTPYKMGQLELSHRVVLAPLTRCRSYGNVPQPHAAVYYSQRATRGGLLIAEATDISPTAQGYPETPGIYTQQQIEAWKPIVDAVHRKGALFFLQIWHVGRVSTTDFQPNGQAPISSTDKQITPDDSGMVYSKPRRLRTDEIPQIIDDFRRAARNAIEAGFDGVEIHGAHGYLLEQFMKDSANDRTDEYGGSLENRCRFAVEVIDAVVAEVGAHRVGIRLSPFVDFMDCFDSDPVALGSYMVQQLNKHPGFLYCHMVEPRMAIIEGRRKIAHGLLPFRKQFNGTFIAAGGYDREEGNKVVADGYADLVAYGRLFLANPDLPRRFELDAPLNRYDRSTFYTQDPVVGYTDYPFLEEIDEESRTTYA
Protein: Small ribosomal subunit protein uS12A (40S ribosomal protein S23-A) (RP37) (S28) (YS14) (P0CX29)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS17A
- Small ribosomal subunit protein eS7A
- Small ribosomal subunit protein uS8A
- Small ribosomal subunit protein uS4A
- Small ribosomal subunit protein eS27B
- Small ribosomal subunit protein uS19
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein uS14A
- Small ribosomal subunit protein eS30A
- Small ribosomal subunit protein uS8B
Sequence:
MGKGKPRGLNSARKLRVHRRNNRWAENNYKKRLLGTAFKSSPFGGSSHAKGIVLEKLGIESKQPNSAIRKCVRVQLIKNGKKVTAFVPNDGCLNFVDENDEVLLAGFGRKGKAKGDIPGVRFKVVKVSGVSLLALWKEKKEKPRS
Protein: Tapasin-related protein (TAPASIN-R) (TAP-binding protein-like) (TAP-binding protein-related protein) (TAPBP-R) (Tapasin-like) (Q9BX59)
Organism: Homo sapiens (Human)
Function: Component of the antigen processing and presentation pathway, which binds to MHC class I coupled with beta2-microglobulin/B2M. Association between TAPBPR and MHC class I occurs in the absence of a functional peptide-loading complex (PLC).
Subcellular location: Cell membrane {ECO:0000305|PubMed:11920573}; Single-pass type I membrane protein {ECO:0000305|PubMed:11920573}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:11920573}; Single-pass type I membrane protein {ECO:0000305|PubMed:11920573}. Microsome membrane {ECO:0000305|PubMed:11920573}; Single-pass type I membrane protein {ECO:0000305|PubMed:11920573}. Golgi apparatus membrane {ECO:0000269|PubMed:23401559}; Single-pass type I membrane protein {ECO:0000269|PubMed:23401559}. Note=Mainly found in endoplasmic reticulum but a minority is found on the cell surface (PubMed:11920573).
Interaction partners:
- Beta-2-microglobulin
- Major histocompatibility complex class I-related protein 1
- HLA class I histocompatibility antigen, A alpha chain
- Vesicle-associated membrane protein 1
Sequence:
MGTQEGWCLLLCLALSGAAETKPHPAEGQWRAVDVVLDCFLAKDGAHRGALASSEDRARASLVLKQVPVLDDGSLEDFTDFQGGTLAQDDPPIIFEASVDLVQIPQAEALLHADCSGKEVTCEISRYFLQMTETTVKTAAWFMANMQVSGGGPSISLVMKTPRVTKNEALWHPTLNLPLSPQGTVRTAVEFQVMTQTQSLSFLLGSSASLDCGFSMAPGLDLISVEWRLQHKGRGQLVYSWTAGQGQAVRKGATLEPAQLGMARDASLTLPGLTIQDEGTYICQITTSLYRAQQIIQLNIQASPKVRLSLANEALLPTLICDIAGYYPLDVVVTWTREELGGSPAQVSGASFSSLRQSVAGTYSISSSLTAEPGSAGATYTCQVTHISLEEPLGASTQVVPPERRTALGVIFASSLFLLALMFLGLQRRQAPTGLGLLQAERWETTSCADTQSSHLHEDRTARVSQPS
Protein: Interferon alpha-5 (IFN-alpha-5) (Interferon alpha-61) (Interferon alpha-G) (LeIF G) (P01569)
Organism: Homo sapiens (Human)
Function: Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase.
Subcellular location: Secreted.
Interaction partners:
- Interferon alpha/beta receptor 1
- Interferon alpha-14
- Ubiquitin-like protein ISG15
- Interferon alpha-2
- Interferon alpha-6
- Interferon alpha/beta receptor 2
- Interferon alpha-4
- Interferon alpha-16
- Interleukin-2
- Antiviral innate immune response effector IFIT1
Sequence:
MALPFVLLMALVVLNCKSICSLGCDLPQTHSLSNRRTLMIMAQMGRISPFSCLKDRHDFGFPQEEFDGNQFQKAQAISVLHEMIQQTFNLFSTKDSSATWDETLLDKFYTELYQQLNDLEACMMQEVGVEDTPLMNVDSILTVRKYFQRITLYLTEKKYSPCAWEVVRAEIMRSFSLSANLQERLRRKE