wanglab/gogpt-training-data huggingface dataset:
Protein: HAT C-terminal dimerisation domain-containing protein (H2L033)
Organism: Caenorhabditis elegans
Interaction partners:
- Phosphatidylinositol-4,5-bisphosphate 4-phosphatase
- RING-type domain-containing protein
- Zinc finger protein zfp-2
- GON-4-like protein
- U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein
- Retinoblastoma-like protein homolog lin-35
Sequence:
MLYKCCKCLALLNKNSMVIVPKDPENLKNWMEKYDFQIKTIMAGSVHFLCKTHLSEDKSVERIPSSSVESATEQYMLEIKEEEPYSQAGSSSESWPEVKEEVIEPVEEIDYDHMPFEIEQNSYETFDESKSYHNSYESDHHQPTTSTSATRAIRRPTTKSLEFTNLPTYLQELSDGEILSFCVKTSSNLSGATSLECGMCEEQYFNSTDTRPIRHHLISRHEATMKKYKNHFPITAAPKIYAPIQQVTIDRADQALTKFFIKSGIPLRAVQDRNLNMLAFNMNSEYSLPTVETMHSFLEKIADAKANAKLNFDDSPVTITFDTTTFNNRHYLAFTVHYYHIRSRMRRCIFLREYDMTGPIVPSVMTAIQKTIEESGSRLKITTVVAGKAEFEDALEDMHSFKQVMICFSQNINKFAETLIEHPVFAGPLQKLRDFITKFPTHRNSWGKFKSYIVKKRTYGEYPEVDNGHWITTLDFITKCLHMHRLFSEFVSTSAQLQYIDVEDNVNIVYLHSLLNLCKSALKEMVDVKATIADVIPAIADISFSLIVTTSKQTVVDAVSTIFNQLLLPFVEQSDIHRFALFLHPLRHGSDLLASADWMKIKTDLSSHLSLREAAEATLAHPSSFDNTITADKEVNAFSQYVCRVTGVETGIMDWWARHAGRFPRLYKYARELFIIPAFSIDAAYYLGEYGILTHSINESDISKRKMLLRAASELVEYRSKGSLMCKPICVKRRKDANSPEDAWYHAIDVRALQIVDVPSDEPPKRMIPQRTPFVYQNPNPLPPHRILQSFPTIRTNREAPHGRSLKDEIAKIAANRQKIQRVYTVASSSPYARPVVVKTESKEGIVEQLTPSAPPPKRYYAVRPAAGNGTSVIRGKDGQVLRVIRNTPSVSFNLNTPLTASKKMYFIRTKTGVTHQLHQPPQ
Protein: TOX high mobility group box family member 3 (Trinucleotide repeat-containing gene 9 protein) (B7SBD2)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional coactivator of the p300/CBP-mediated transcription complex. Activates transactivation through cAMP response element (CRE) sites. Protects against cell death by inducing antiapoptotic and repressing pro-apoptotic transcripts. Stimulates transcription from the estrogen-responsive or BCL-2 promoters. Required for depolarization-induced transcription activation of the C-FOS promoter in neurons. Associates with chromatin to the estrogen-responsive C3 promoter region.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DENN domain containing 1A
- KRR1 small subunit processome component
- BTB/POZ domain-containing protein 9
Sequence:
MDVRFYPAAAGDPAGLDFAQCLGYYGYSKLGNNNYMNMAEANNAFFAASEQTFHTPSLGDEEFEIPPITPPPESDPTLGMPDVLLPFQTLSDPLPSQGNEFTPQFPPQSLDLPSITISRNLVEQDGVLHSNGLHMDQSHTQVSQYRQDPSLVMRSIVHMTDAARSGIMPPAQLTTINQSQLSAQLGLNLGGASVPHTSPSPPASKSATPSPSSSINEEDADETNRAVGEKRTAPDSGKKPKTPKKKKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYRASLVSKAAAESAEAQTIRSVQQTLASTNLTSSLLLNTSLSQHGTVPASPQTLPQSLPRSIAPKPLTMRLPMSQIVTSVTIAANMPSNIGAPLISSMGTTMVGSVSSTQVSPSVQTQQHQLQLQQQQQQQQQQMQQMQHQQLQQHQMHQQIQQQMQQQHFQHHMQQHLQQQQQQHLQQQISQQQLQQQLQQHLQLQQQLQHMQHQSQPSPRQHSPVTSQITSPIPAIGSPQPASQQHQPQIQSQTQTQVLPQVSIF
Protein: CD177 antigen (Human neutrophil alloantigen 2a) (HNA-2a) (NB1 glycoprotein) (NB1 GP) (Polycythemia rubra vera protein 1) (PRV-1) (CD antigen CD177) (Q8N6Q3)
Organism: Homo sapiens (Human)
Function: In association with beta-2 integrin heterodimer ITGAM/CD11b and ITGB2/CD18, mediates activation of TNF-alpha primed neutrophils including degranulation and superoxide production. In addition, by preventing beta-2 integrin internalization and attenuating chemokine signaling favors adhesion over migration. Heterophilic interaction with PECAM1 on endothelial cells plays a role in neutrophil transendothelial migration in vitro. However, appears to be dispensable for neutrophil recruitment caused by bacterial infection in vivo. Acts as a receptor for the mature form of protease PRTN3 allowing its display at the cell surface of neutrophils. By displaying PRTN3 at the neutrophil cell surface, may play a role in enhancing endothelial cell junctional integrity and thus vascular integrity during neutrophil diapedesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:12675722, ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:24926686, ECO:0000269|PubMed:27227454, ECO:0000269|PubMed:28240246, ECO:0000269|PubMed:28807980}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:17244676}. Membrane raft {ECO:0000269|PubMed:21193407}; Lipid-anchor, GPI-like-anchor {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:17244676}. Secreted {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:18462208}. Cytoplasmic granule membrane {ECO:0000269|PubMed:18462208}. Cell projection, lamellipodium {ECO:0000269|PubMed:28807980}. Note=Cell surface expression on neutrophils is increased upon TNF-alpha, fMLP or CXCL8/IL8-mediated stimulation (PubMed:17244676, PubMed:17580308). In neutrophils, stored predominantly in secondary and tertiary granules (PubMed:18462208). Can also be shedded from the cell membrane (PubMed:12239154, PubMed:18462208). Localizes to lamellar protrusions in spreading neutrophils (PubMed:28807980). {ECO:0000269|PubMed:12239154, ECO:0000269|PubMed:17244676, ECO:0000269|PubMed:17580308, ECO:0000269|PubMed:18462208, ECO:0000269|PubMed:28807980}.
Interaction partners:
- Platelet endothelial cell adhesion molecule
- Myeloblastin
- Contactin-5
- Contactin-6
- Integrin alpha-M
- Urokinase plasminogen activator surface receptor
Sequence:
MSAVLLLALLGFILPLPGVQALLCQFGTVQHVWKVSDLPRQWTPKNTSCDSGLGCQDTLMLIESGPQVSLVLSKGCTEAKDQEPRVTEHRMGPGLSLISYTFVCRQEDFCNNLVNSLPLWAPQPPADPGSLRCPVCLSMEGCLEGTTEEICPKGTTHCYDGLLRLRGGGIFSNLRVQGCMPQPGCNLLNGTQEIGPVGMTENCNRKDFLTCHRGTTIMTHGNLAQEPTDWTTSNTEMCEVGQVCQETLLLLDVGLTSTLVGTKGCSTVGAQNSQKTTIHSAPPGVLVASYTHFCSSDLCNSASSSSVLLNSLPPQAAPVPGDRQCPTCVQPLGTCSSGSPRMTCPRGATHCYDGYIHLSGGGLSTKMSIQGCVAQPSSFLLNHTRQIGIFSAREKRDVQPPASQHEGGGAEGLESLTWGVGLALAPALWWGVVCPSC
Protein: Cofilin (Actin-depolymerizing factor 1) (Q03048)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10231390}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10231390}. Nucleus matrix {ECO:0000269|PubMed:10231390}. Note=Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton.
Interaction partners:
- Actin
- Profilin
- Actin-interacting protein 1
- Actin-related protein 2
- Actin-related protein 3
- Adenylyl cyclase-associated protein
- Twinfilin-1
- Coronin-like protein
- Fimbrin
- F-actin-capping protein subunit beta
Sequence:
MSRSGVAVADESLTAFNDLKLGKKYKFILFGLNDAKTEIVVKETSTDPSYDAFLEKLPENDCLYAIYDFEYEINGNEGKRSKIVFFTWSPDTAPVRSKMVYASSKDALRRALNGVSTDVQGTDFSEVSYDSVLERVSRGAGSH
Protein: Nuclear receptor (Q21804)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Glycosyltransferase family 92 protein R07B7.12
Sequence:
MTSEESTSDYILPDIEITDEETKCDPNTKNILPKQCRICRNPAVGYHYDVASCNGCKAFFRRTVITGRLPNCKFGDKCLEDHKIPKPGTRLCGSCRFSKCEQMGMNPMAIKSEIISKKGNILKMELVKKHNRQLIAVTKEIAIDDEFSKVLSKLKAVENKLDNLFNSRLPKNYVDYRQFTDILAEKPTFAVEQIPNLSFIPDQVFHEYGGLAHNSFLAVVEFAKFLDFFPKLDSETQLKVVRHGALMVRGMMNTERSIRKFHSDCVRRADGSIAGKPMRNYNGIWVEQRKIVQKGLHAFLRNKIDETEYLLLKGIVLCNPAICGLPESAQQILEDERRRYVRSLLTYCLKQYGIRYGPDRLSSILSIMPIMENQQKEEKSFNVILRSFYSNVSILVSPLYDEIMSS
Protein: Platelet derived growth factor receptor beta (E5RJ14)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQEPPQEMAKAQDGTFSSVLTLTNLTGLDTGEYFCTHNDSRGLETDERKRLYIFVPDPTVGFLPNDAEELFIFLTEITEITIPCRVTDPQLVVTLHEKKGDVALPVPYDHQRGFSGIFEDRSYICKTTIGDREVDSDAYYVYRLQ
Protein: Protein YIG1 (Q08956)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the regulation of anaerobiotic glycerol metabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16358322}. Nucleus {ECO:0000269|PubMed:16358322}.
Interaction partners:
- Glycerol-1-phosphate phosphohydrolase 2
- V-type proton ATPase subunit G
- Respiratory growth induced protein 2
- Glycerol-1-phosphate phosphohydrolase 1
Sequence:
MGIPMQIYQDGKGVQFYHTRYQNVFDERASKYGNYTVNNDYPQLPDTIKEHIDQLTFSNVGEDGGDVGNYSEEDDDGDEEKELEDVFRSNRGLEFVRINNYFTTHDLQSFKSFRNFNSKYWIFYSNQAEDKKLLLYDFNGQHLIFIKQQFYGQLNLLLSDAIICMDCNFGYNSNTIQILVGFQNGKLLKLNCDLNGNVNNHLLLKDPSTSSHQSHLSILNVWAGLLPHFVVSFSLKDGLLITSLDHQQSNGSFQSFHTNIDLPVDLRTTTNVKSVLNFPQFTLYKGNDMIFHCKNLLGSDASTLNKEINFMLKIDEDVQKIDYLLKTNHILLETNMRYLSIPTRDPIENSNSSPPVSDSEVYPIFYKTQELHVHASGTGRQIANNGKYIFITEQHLYGTALSVYKYSISFKRWLFVGYSDIRAKYGIRSVKDLFVGNCPSVNSPVLTILTDDNNIQTILLK
Protein: Ficolin-2 (37 kDa elastin-binding protein) (Collagen/fibrinogen domain-containing protein 2) (EBP-37) (Ficolin-B) (Ficolin-beta) (Hucolin) (L-ficolin) (Serum lectin p35) (Q15485)
Organism: Homo sapiens (Human)
Function: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region.
Subcellular location: Secreted.
Interaction partners:
- MBL associated serine protease 1
- Mannan-binding lectin serine protease 2
- Mannose-binding protein C
- Ficolin-3
- Pentraxin-related protein PTX3
- Collectin-10
- Ficolin-1
- Calreticulin
- Collectin-11
- Complement C3
Sequence:
MELDRAVGVLGAATLLLSFLGMAWALQAADTCPEVKMVGLEGSDKLTILRGCPGLPGAPGPKGEAGTNGKRGERGPPGPPGKAGPPGPNGAPGEPQPCLTGPRTCKDLLDRGHFLSGWHTIYLPDCRPLTVLCDMDTDGGGWTVFQRRVDGSVDFYRDWATYKQGFGSRLGEFWLGNDNIHALTAQGTSELRVDLVDFEDNYQFAKYRSFKVADEAEKYNLVLGAFVEGSAGDSLTFHNNQSFSTKDQDNDLNTGNCAVMFQGAWWYKNCHVSNLNGRYLRGTHGSFANGINWKSGKGYNYSYKVSEMKVRPA
Protein: Ras GTPase-activating-like protein IQG1 (Cytokinesis protein 1) (IQGAP-related protein 1) (Q12280)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the assembly and the contraction of the actomyosin ring at the bud neck during cytokinesis. Seems to be involved in additional tasks during cell division like axial bud-site selection and targeted secretion by recruiting the spatial landmark BUD4, the septin CDC12 and the secretion landmark SEC3 to the bud neck. May be regulated by calcium ions.
Subcellular location: Bud neck {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18344988, ECO:0000269|PubMed:9442111}. Note=Forms a ring at the bud neck in a MLC1-dependent manner, which contracts at the end of cytokinesis.
Interaction partners:
- Cytokinesis protein 2
- Myosin light chain 1
- Myosin-1
- Myosin light chain 2
- Cell division control protein 42
- Cytokinesis protein 3
- Actin
- Ingression protein 1
- Calmodulin
- Chitin synthase 2
Sequence:
MTAYSGSPSKPGNNNSYLNRYVENLGTNVTPPLRPQSSSKINSSLNIASPSHLKTKTSASNSSATILSKKVESSVSKLKPSLPNKLVGKYTVDLSNYSKIELRYYEFLCRVSEVKIWIEAVIEEALPSEIELCVGDSLRNGVFLAKLTQRINPDLTTVIFPAGDKLQFKHTQNINAFFGLVEHVGVPDSFRFELQDLYNKKNIPQVFETLHILISMINKKWPGKTPALTNVSGQISFTKEEIAACKKAWPRIRDFKSLGTNINTAPASPEEPKEKRSGLIKDFNKFERPNIPVEEILITPRKNITDANCSDFSNTPSPYNEAPKMSNLDVVVEKRKFTPIEPSLLGPTPSLEYSPIKNKSLSYYSPTISKYLTYDTEFYTRRSRAREEDLNYYQTFKYSPSHYSPMRRERMTEEQFLEKVVQLQNICRGVNTRFNLYIQKRLLNLFEQDILRFQACLRGNKFRVLSSMYLPIRRAKIDVPHVEAIQSRIKGSRIRYKYDKLKFTLSRFSCTVELLQAYCRSKLLKTTVNTKLNDIEISHYPLTKLQSYMRASYVRKKVMSLNTKLNDERESIMKFSAIIRGNVVRCSEDAILSAVHDVHKENISKLQSLIRGIFTRSCLASIIYSLGKENCNIIQLSACIRGNAVRHKVQSLFAPENNLSETVHDLQGLVRGILVRYTLDLVDDIVEYNNLALFQAFSRGALVRESLDQKSSFYKRNVRSVIMIQSWIRKSLQRSAYLELLDCPNPSLWAVKKFVHLLNGTATIEEVQNQLESCQASLDSENMKKERLLKSIRQQLNINGVLDKFGLLKDKDHELGISDSTIPKSKYQKYEKLFYMLQVDPSYWKLLYLKEPEFVAKNVYMTFGTVNQRMNDRERSYFTRFVCEMLQNAINEAPSIESFLDNRSQFWQTILQDFLRRESPEFFSIIVPVLDYLSDPVVDFESDPYKIYQEIHGFSSPQHCSPVDDASTKNKFIDNLRCLWHAIEMVAEIYTRKVHTIPVEIRYLCTKIFCYAADKNIEEIDSLRAISSILVNVFVSEYLVNREYYGYKDSNVQKNNQKIDILMKSLATVFEIKNFDGFLDPLNQYANEIKPHIKDVLYNVLVDPEYEQEGDRLIYLDMVSPSPKLELLTEKVLEISGKFEEYLNEFPEADILHDILEKNLDNSSFPRSGRVTLELDASAYRFLVSDDKMRKIYDQVKRAFVYMMQIEDVDTNLYDLSISTILPQDEPNFANFLEQNPKIRDDPMIQKLKPLKYFTLKNVTLKKIHELESTGTFCSSDNKLQNFLNDIANTIKNPNYAIDYVTQEIYITKETLTKISEMNHSLDIELSRLKKHVDHTIKDFQKAKDFSPVHKSKFGNFKNAVKKVQGRERSELQGMKFKWNTKQLYERGVLKTIRGEKLAELTVKVFGSSGPKFPDIIFKISTSDGSRFGIQMIDKRKGPDKRYSDDVDSFSFKDLIKTQVEPKIETWKLFHSNVVVNNSQLLHLIVSFFYKRNAL
Protein: Protease Rv3090 (EC 3.4.-.-) (O05769)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000269|PubMed:36402348}; Multi-pass membrane protein {ECO:0000255}. Secreted, cell wall {ECO:0000269|PubMed:36402348}.
Interaction partners:
- ATP-dependent zinc metalloprotease FtsH
- Uncharacterized zinc protease Rv2782c
- Conserved protein
Sequence:
MTWQIVFVVICVIVAGVAALFWRLPSDDTTRSRAKTVTIAAVAAAAVFFFLGCFTIVGTRQFAIMTTFGRPTGVSLNNGFHGKWPWQMTHPMDGAVQIDKYVKEGNTDQRITVRLGNQSTALADVSIRWQLKQAAAPELFQQYKTFDNVRVNLIERNLSVALNEVFAGFNPLDPRNLDVSPLPSLAKRAADILRQDVGGQVDIFDVNVPTIQYDQSTEDKINQLNQQRAQTSIALEAQRTAEAQAKANEILSRSISDDPNVVVQNCITAAINKGISPLGCWPGSSALPTIAVPGR
Protein: Glucokinase (EC 2.7.1.2) (Glucose kinase) (P0A6V8)
Organism: Escherichia coli (strain K12)
Function: An ATP-dependent kinase that phosphorylates glucose to make glucose-6-phosphate, not active on fructose, galactose or mannose. Not highly important in wild-type E.coli as glucose is transported into the cell by the PTS system as glucose 6-phosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9023215}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- PTS system glucose-specific EIICB component
- Glucose-6-phosphate isomerase
- KHG/KDPG aldolase
- PTS system glucose-specific EIIA component
- Phosphoglucomutase
- HTH-type transcriptional regulator HexR
- Transketolase 1
- Phosphogluconate dehydratase
- Transketolase 2
Sequence:
MTKYALVGDVGGTNARLALCDIASGEISQAKTYSGLDYPSLEAVIRVYLEEHKVEVKDGCIAIACPITGDWVAMTNHTWAFSIAEMKKNLGFSHLEIINDFTAVSMAIPMLKKEHLIQFGGAEPVEGKPIAVYGAGTGLGVAHLVHVDKRWVSLPGEGGHVDFAPNSEEEAIILEILRAEIGHVSAERVLSGPGLVNLYRAIVKADNRLPENLKPKDITERALADSCTDCRRALSLFCVIMGRFGGNLALNLGTFGGVFIAGGIVPRFLEFFKASGFRAAFEDKGRFKEYVHDIPVYLIVHDNPGLLGSGAHLRQTLGHIL
Protein: ISG12a protein (Interferon, alpha-inducible protein 27) (Q70LM9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAFSGTGTLVASIVSKMTSSAAMVKAGGAVSGTILAGSKAMTVAAVPPALSAVGFTASGIAASSLAAKMMSLSAIANGGGVPAGGLVAILQSAGAAGLSVPSTVIVGSAGSAVVASVMNICESFYPFLMGSEVADMATEVADMAIEVADISTEEALPNLSNTEKD
Protein: DASH complex subunit SPC19 (19 kDa spindle pole component protein) (Outer kinetochore protein SPC19) (Q03954)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095}. Chromosome {ECO:0000269|PubMed:36701236}. Note=Associates with the mitotic spindle and the kinetochore (PubMed:14562095). Associates with origin of replication (ORI) sites during interphase (PubMed:36701236). {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:36701236}.
Interaction partners:
- DASH complex subunit DAD4
- DASH complex subunit DAD2
- DASH complex subunit ASK1
- DASH complex subunit SPC34
- DASH complex subunit DUO1
- DASH complex subunit DAM1
- DASH complex subunit DAD3
- DASH complex subunit DAD1
- DASH complex subunit HSK3
- Inner kinetochore subunit IML3
Sequence:
MTDALEQSVLALEGTVSVLKDSVESLKCANEPSTNLASTMLQTKRVFRLVPEYDVERSKLDLIEEVEPLVRTLGDKLRKSMGRMQRELDTLQQTYELNDLRLKKNISMDDDDALNSPDMGQEYEGRDADDVVMMASSTNEELEELKKLKEKKKQLENKLEILKQK
Protein: IP07030p (Q4V5L1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- AT19071p
- AT16150p
- IP07034p
- AT25465p
- MIP06038p
- CG5565 protein
- IP11711p
- GEO12020p1
- IP04645p
- FI08034p
Sequence:
MDNDNMLDFTDLISCKDLPNITLHNIRPIYSIKVFMSEPKNSNVSIAELIKRQEVSAEQCRKALKVIKDRLLLKMAALQELKKYLLDLHSEIKKPGAGTRFVTNQEKVKLHFLDETEIREVELSDAVERCNIKLSSLYCEILALDSDMGSVAYLERVAQINKDFIMDWHKTQRQNKTSNIHCSGQGVKKTF
Protein: Collagen type V alpha 3 chain (F7EVZ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRSCRRLDQLQAGLCLLLASLQLVSWTLAEPVDVLETLGVHRDKAGVTKGPGFCPQRIPQGDRAFRVGKSSLLSVPTWQLFPDGHFPENFSVLLTLRAQPANQSVLLSIYDENGVRQMGLALGPALGLLGDSFRSLPKQINLMDGRWHRVAVSISGDKVTLVVDCEPQPPMFGQGPRVISTAGLTVMGTQELGEESFEGDIQELLLIPDPQAALQACELYLPDCETPDSTTTGVTKEEPETPAPRRRKGKGKKKDRGRKGKGRKKNKTSRLSPTPGAPENQTSLHTPETEKPSPHLPPTPTPLAITTTVTMGGNATVLQGLDSSTETEQMTPEMDATEESEGGGPTMGPEFRAAEQSLQTEFQIFPGAGEKGAKGEPATIEQGQQFEGPAGAPGPRGISGPSGPPGPPGFPGDRGLPGPAGLPGIPGIDGVRGLPGTVIMMPFHFASGSMKGPPVSFQQAQAQAVLQQAQLSMKGPPGPVGLTGRPGPVGLPGYPGLKGELGEAGPQGPRGLQGPPGPPGREGKTGRAGADGARGLPGDTGPKGDRGFDGLPGLPGEKGQRGDFGPVGQPGPPGEDGIKGLQGPPGPTGQAGEPGPRGLIGPRGPPGPLGRPGVTGSDGAPGAKGNVGPPGEPGPPGQQGNHGSQGIPGPQGPIGTPGEKGPPGNPGIPGVPGSEGPPGHPGHEGPTGEKGAQGPPGSAGPQGYPGPRGVKGTSGNRGLQGEKGERGEDGFPGFKGDEGPKGDRGNPGLPGPRGEDGPEGQKGPEGLPGDEGPPGAAGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPLGEKGKRGKAGQPGEEGERGTPGTRGDRGQPGATGQPGPKGDVGQNGSPGAPGEKGLPGLQGPPGFPGPKGPPGPQGKDGIPGHPGQRGELGFQGQTGPPGPAGVLGPQGKVGDVGPLGERGPPGPPGPPGEPGLPGIEGREGAKGELGPLGSLGKEGPPGPMGFPGPQGAPGDPGPIGLKGDKGPPGPLGANGSPGERGPVGPSGGIGLPGQSGGQGPIGPAGEKGSPGERGVPGPTGKDGIPGPPGLQGPPGAAGPSGEEGDKGEVGMPGHKGSKGDKGDAGPPGPTGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGFVGVIGPPGLQGLPGPPGEKGEVGDVGSMGPHGAPGPRGPPGPSGSAGSPGLPGGVGQPGAVGEKGEPGNAGDAGPPGVPGIPGPKGEIGEKGDSGPSGAAGPPGKKGPPGEDGAKGNMGPTGLPGDLGPPGDPGVPGTDGIPGEKGNAGDIGGPGPPGASGEPGARGLPGKRGSPGRMGPEGKEGEKGAKGDAGPDGPPGRTGPIGARGPPGRVGPDGLPGIPGPVGEPGLLGPPGLIGPPGPLGPPGLPGLKGDAGLKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGLQGDPGLPGPVGSLGHPGPPGVVGPLGQKGSKGSPGSLGPRGDPGPAGPPGPPGSPAEVHGLRRRRSVLDTPEGGLEEVMASLNSLSLELEQLQRPPGTAESPGLICHELHRNHPHLPDGEYWIDPNQGCARDAFKVFCNFTAGGETCLYPDKKFETVKLASWSREKPGGWYSTFRRGKKFSYVDADGSPVNVVQLTFLKLLSAAAHQRFTYTCQNSAAWLDEASGDHRHSIRFQGTNWEELSFNQTTAATIKVPHDGCRVRKGQAKTLFEFSSSVGFLPLWDVAAVDFGQTNQKFGFELGSVCFSS
Protein: UV excision repair protein RAD23 homolog B (Q4KMA2)
Organism: Rattus norvegicus (Rat)
Function: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Peptide-N
- Centrin 2
- p125
- 26S proteasome regulatory subunit 4
- DNA excision repair protein ERCC-1
- DNA repair protein complementing XP-A cells homolog
- RAD23 homolog A, nucleotide excision repair protein.
- Proteasome
- Ubiquitin-ribosomal protein eL40 fusion protein
- UBX domain-containing protein 1
Sequence:
MQVTLKTLQQQTFKIDIDPEETVKALKEKIESEKGKDAFPVAGQKLIYAGKILSDDTALKEYKIDEKNFVVVMVTKPKAVTSAVPATTQQSSSPSTTTVSSSPAAAVAQAPAPTPALAPTSTPASTTPASTTASSEPAPTGATQPEKPAEKPAQTPVLTSPAPADSTPGDSSRSNLFEDATSALVTGQSYENMVTEIMSMGYEREQVIAALRASFNNPDRAVEYLLMGIPGDRESQAVVDPPPQAVSTGTPQSPAVAAAAATTTATTTTTSGGHPLEFLRNQPQFQQMRQIIQQNPSLLPALLQQIGRENPQLLQQISQHQEHFIQMLNEPVQEAGGQGGGGGGGGGGGGGGGGIAEAGSGHMNYIQVTPQEKEAIERLKALGFPEGLVIQAYFACEKNENLAANFLLQQNFDED
Protein: Zinc finger protein 317 (Q96PQ6)
Organism: Homo sapiens (Human)
Function: May function as a transcription factor. May play an important role in erythroid maturation and lymphoid proliferation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- RNA-binding motif protein, Y chromosome, family 1 member A1
Sequence:
MAALSPTFATSTQDSTCLQDSEFPVSSKDHSCPQNLDLFVCSGLEPHTPSVGSQESVTFQDVAVDFTEKEWPLLDSSQRKLYKDVMLENYSNLTSLGYQVGKPSLISHLEQEEEPRTEERGAHQGACADWETPSKTKWSLLMEDIFGKETPSGVTMERAGLGEKSTEYAHLFEVFGMDPHLTQPMGRHAGKRPYHRRDYGVAFKGRPHLTQHMSMYDGRKMHECHQCQKAFTTSASLTRHRRIHTGEKPYECSDCGKAFNDPSALRSHARTHLKEKPFDCSQCGNAFRTLSALKIHMRVHTGERPYKCDQCGKAYGRSCHLIAHKRTHTGERPYECHDCGKAFQHPSHLKEHVRNHTGEKPYACTQCGKAFRWKSNFNLHKKNHMVEKTYECKECGKSFGDLVSRRKHMRIHIVKKPVECRQCGKTFRNQSILKTHMNSHTGEKPYGCDLCGKAFSASSNLTAHRKIHTQERRYECAACGKVFGDYLSRRRHMSVHLVKKRVECRQCGKAFRNQSTLKTHMRSHTGEKPYECDHCGKAFSIGSNLNVHRRIHTGEKPYECLVCGKAFSDHSSLRSHVKTHRGEKLFVSSVWKRLQ
Protein: Mannose-1-phosphate guanylyltransferase regulatory subunit alpha (GDP-mannose pyrophosphorylase A) (GMPP-alpha) (GTP-mannose-1-phosphate guanylyltransferase alpha) (Q96IJ6)
Organism: Homo sapiens (Human)
Function: May serve as a regulatory subunit and allow allosteric feedback inhibition of GMPPB by GDP-mannose.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24035193}. Note=Myc-tagged GMPPA shows a diffuse cytoplasmic and nuclear pattern in transfected COS-7 cells.
Interaction partners:
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Phosphomannomutase 2
- Phosphomannomutase 1
- GDP-mannose 4,6 dehydratase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- dTDP-D-glucose 4,6-dehydratase
- Golgi phosphoprotein 3
- Phosphoacetylglucosamine mutase
Sequence:
MLKAVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQPDEPLTQFLEAAQQEFNLPVRYLQEFAPLGTGGGLYHFRDQILAGSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEDSPGLWPGAGTIRLEQDVFSALAGQGQIYVHLTDGIWSQIKSAGSALYASRLYLSRYQDTHPERLAKHTPGGPWIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEGTPSDPNPNDPRARMDSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKELSRSFTNQIIL