wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-arabinopyranose mutase (EC 5.4.99.30) (Q8VWN8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555, ECO:0000256|PIRNR:PIRNR016429}.
Interaction partners:
Sequence:
MATVSPTPLLKDELDIVIPTIRNLDFLEMWRPFFQPYHLIIVQDGDPTKTIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPSGKDINALEQHIQNLLSPSTPFFFNTLYDPYRSGADFVRGYPFSLREGVTTAVSHGLWLNIPDYDAPTQLVKPLERNTRYVDAIMTIPKGTLFPMCGMNLAFNRELIGPAMYFGLMGDGQPIGRYDDMWAGWCTKVICDHLGWGVKTGLPYIWHSKASNPFVNLKKEYKGIYWQEELIPFFQSVALPKDCTTVQKCYIEISKQVKAKLGKVDDYFNKLADAMVTWIEAWDELNPSGDISAKIPNGASK
Protein: TAR DNA-binding protein 43 (A0A8I6GLU8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDEADASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKDYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSPDEPLRSRKVFVGRCTEDMTAEELQQFFCQYGEVVDVFIPKPFRAFAFVTFADDKVAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRGGGAGLGNNQGGNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQSQGSMQREPNQAFGSGNNSYSGSNSGAPLGWGSASNAGSGSGFNGGFGSSMDSKSSGWGM
Protein: Dual specificity protein phosphatase CDC14A (EC 3.1.3.16) (EC 3.1.3.48) (CDC14 cell division cycle 14 homolog A) (Q9UNH5)
Organism: Homo sapiens (Human)
Function: Dual-specificity phosphatase. Required for centrosome separation and productive cytokinesis during cell division. Dephosphorylates SIRT2 around early anaphase. May dephosphorylate the APC subunit FZR1/CDH1, thereby promoting APC-FZR1 dependent degradation of mitotic cyclins and subsequent exit from mitosis. Required for normal hearing.
Subcellular location: Nucleus {ECO:0000269|PubMed:9367992}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:12134069}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:15263015}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15263015}. Cell projection, kinocilium {ECO:0000250|UniProtKB:Q6GQT0}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q6GQT0}. Note=Centrosomal during interphase, released into the cytoplasm at the onset of mitosis. Subsequently localizes to the mitotic spindle pole and at the central spindle (PubMed:11901424, PubMed:12134069, PubMed:15263015). Present along both the transient kinocilia of developing cochlear hair cells and the persistent kinocilia of vestibular hair cells (By similarity). {ECO:0000250|UniProtKB:Q6GQT0, ECO:0000269|PubMed:11901424, ECO:0000269|PubMed:12134069, ECO:0000269|PubMed:15263015}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-1
- NAD-dependent protein deacetylase sirtuin-2
- Separin
- Fizzy-related protein homolog
- Cyclin-dependent kinase 1
- Dual specificity protein phosphatase CDC14B
- Inner centromere protein
- Wee1-like protein kinase
- Cell division cycle protein 16 homolog
- Cell division cycle 7-related protein kinase
Sequence:
MAAESGELIGACEFMKDRLYFATLRNRPKSTVNTHYFSIDEELVYENFYADFGPLNLAMVYRYCCKLNKKLKSYSLSRKKIVHYTCFDQRKRANAAFLIGAYAVIYLKKTPEEAYRALLSGSNPPYLPFRDASFGNCTYNLTILDCLQGIRKGLQHGFFDFETFDVDEYEHYERVENGDFNWIVPGKFLAFSGPHPKSKIENGYPLHAPEAYFPYFKKHNVTAVVRLNKKIYEAKRFTDAGFEHYDLFFIDGSTPSDNIVRRFLNICENTEGAIAVHCKAGLGRTGTLIACYVMKHYRFTHAEIIAWIRICRPGSIIGPQQHFLEEKQASLWVQGDIFRSKLKNRPSSEGSINKILSGLDDMSIGGNLSKTQNMERFGEDNLEDDDVEMKNGITQGDKLRALKSQRQPRTSPSCAFRSDDTKGHPRAVSQPFRLSSSLQGSAVTLKTSKMALSPSATAKRINRTSLSSGATVRSFSINSRLASSLGNLNAATDDPENKKTSSSSKAGFTASPFTNLLNGSSQPTTRNYPELNNNQYNRSSNSNGGNLNSPPGPHSAKTEEHTTILRPSYTGLSSSSARFLSRSIPSLQSEYVHY
Protein: Toxic protein HokE (P77091)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system; if it expressed it could be neutralized by antisense antitoxin RNA SokE.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P0ACG4}; Single-pass membrane protein {ECO:0000250|UniProtKB:P0ACG4}.
Interaction partners:
- Protein HokA
- Toxic protein HokD
- Toxic protein HokB
- mRNA interferase toxin YafO
- Antitoxin YafN
Sequence:
MLTKYALAAVIVLCLTVLGFTLLVGDSLCEFTVKERNIEFKAVLAYEPKK
Protein: Spermatogenesis-associated protein 2 (Q8K004)
Organism: Mus musculus (Mouse)
Function: Bridging factor that mediates the recruitment of CYLD to the LUBAC complex, thereby regulating TNF-alpha-induced necroptosis (By similarity). Acts as a direct binding intermediate that bridges RNF31/HOIP, the catalytic subunit of the LUBAC complex, and the deubiquitinase (CYLD), thereby recruiting CYLD to the TNF-R1 signaling complex (TNF-RSC) (By similarity). Required to activate the 'Met-1'- (linear) and 'Lys-63'-linked deubiquitinase activities of CYLD. Controls the kinase activity of RIPK1 and TNF-alpha-induced necroptosis by promoting 'Met-1'-linked deubiquitination of RIPK1 by CYLD.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29025062}. Nucleus {ECO:0000250|UniProtKB:Q66HP6}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF31
- Sharpin
- Ubiquitin carboxyl-terminal hydrolase CYLD
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Spermatogenesis-associated protein 2-like protein
Sequence:
MDTKYKDDLFRKYVQFHEGKVDTTPGNQQPGSDEYLRVAAATLLSLHKVDPLYRFRLIQFYEVVESSLRSLSSSSLSALHCAFSMLETMAINLFLFPWKKEFRSIKTYTGPFVYYVKSTLLEKDIRAILRFMGYEPELGTVYKLKELVESLQVKMVSFELFLAKVECEQMLGIHSQVKDKGYSELDVVAERKGSTEDARGCSDALRRRAESREHLTTSMARVALQKSASERAAKDYYKPRVTKPSRSVDAYDSYWESRKPPSKASLSLRKEPLAMDVGEDLKDEIIRPSPSLLAMSSSPHGSPDDLSSISSINGLGLLRSTYFSTQDDVDLYTDSEPRATYRRQDALRPDVWLVKNDTHPIYHKRSPPTKESALSKCQNCGLSCSSSLCQRCDSVLVCPSASKPSAFPSKASVHDSLAHGAPMREKYVGHQTQGLDRLAPVHSKPKPSTTATSRCGFCNRAGATNTCTQCSKVSCDACLGAYHYDPCCRKSELHKFLPNSQLNYKSAPFSQLVYR
Protein: HL02328p (Q95S10)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKGIYADH
Protein: Transcription factor SPT20 (P50875)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription regulator. May recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex/transcription factor TFIID complex subunit TAF10
- SAGA complex subunit SGF73
- SAGA complex subunit SPT7
- Histone acetyltransferase GCN5
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit SPT3
- SAGA complex/transcription factor TFIID complex subunit TAF6
- SAGA complex/transcription factor TFIID complex subunit TAF5
Sequence:
MSANSPTGNDPHVFGIPVNATPSNMGSPGSPVNVPPPMNPAVANVNHPVMRTNSNSNANEGTRTLTREQIQQLQQRQRLLLQQRLLEQQRKQQALQNYEAQFYQMLMTLNKRPKRLYNFVEDADSILKKYEQYLHSFEFHIYENNYKICAPANSRLQQQQKQPELTSDGLILTKNNETLKEFLEYVARGRIPDAIMEVLRDCNIQFYEGNLILQVYDHTNTVDVTPKENKPNLNSSSSPSNNNSTQDNSKIQQPSEPNSGVANTGANTANKKASFKRPRVYRTLLKPNDLTTYYDMMSYADNARFSDSIYQQFESEILTLTKRNLSLSVPLNPYEHRDMLEETAFSEPHWDSEKKSFIHEHRAESTREGTKGVVGHIEERDEFPQHSSNYEQLMLIMNERTTTITNSTFAVSLTKNAMEIASSSSNGVRGASSSTSNSASNTRNNSLANGNQVALAAAAAAAAVGSTMGNDNNQFSRLKFIEQWRINKEKRKQQALSANINPTPFNARISMTAPLTPQQQLLQRQQQALEQQQNGGAMKNANKRSGNNATSNNNNNNNNLDKPKVKRPRKNAKKSESGTPAPKKKRMTKKKQSASSTPSSTTMS
Protein: Transient receptor potential cation channel subfamily V member 6 (TrpV6) (CaT-like) (CaT-L) (Calcium transport protein 1) (CaT1) (Epithelial calcium channel 2) (ECaC2) (Q9H1D0)
Organism: Homo sapiens (Human)
Function: Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine. Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11097838, ECO:0000269|PubMed:11248124, ECO:0000269|PubMed:11278579, ECO:0000269|PubMed:15184369, ECO:0000269|PubMed:23612980, ECO:0000269|PubMed:29258289, ECO:0000269|PubMed:29861107}; Multi-pass membrane protein {ECO:0000269|PubMed:29258289}.
Interaction partners:
- Calmodulin-1
- Protein S100-A10
- Protein S100-G
- Plasma membrane calcium-transporting ATPase 1
- Protein NipSnap homolog 1
- Short transient receptor potential channel 1
- Transient receptor potential cation channel subfamily M member 8
- Transient receptor potential cation channel subfamily M member 4
- Transient receptor potential cation channel subfamily M member 7
- Transient receptor potential cation channel subfamily M member 6
Sequence:
MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI
Protein: Flagellar FliJ protein (P0A1K1)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Flagellar protein that affects chemotactic events.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Flagellum-specific ATP synthase
- Flagellar protein FliO
- Flagellar assembly protein FliH
- Flagellar M-ring protein
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliG
- Flagellar hook-length control protein
- Flagellar protein FliL
- Flagellar biosynthesis protein FlhA
- Flagellar biosynthetic protein FliP
Sequence:
MAQHGALETLKDLAEKEVDDAARLLGEMRRGCQQAEEQLKMLIDYQNEYRSNLNTDMGNGIASNRWINYQQFIQTLEKAIEQHRLQLTQWTQKVDLALKSWREKKQRLQAWQTLQDRQTAAALLAENRMDQKKMDEFAQRAAMRKPE
Protein: 5-aminolevulinate synthase, mitochondrial (EC 2.3.1.37) (5-aminolevulinic acid synthase) (Delta-ALA synthase) (Delta-aminolevulinate synthase) (P09950)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:3023841, ECO:0000269|PubMed:6381051}.
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Porphobilinogen deaminase
- Uroporphyrinogen-III synthase
- Lanosterol synthase ERG7
- Serine hydroxymethyltransferase, mitochondrial
- Low specificity L-threonine aldolase
- Sterol-4-alpha-carboxylate 3-dehydrogenase ERG26, decarboxylating
- Glycine dehydrogenase
- Serine hydroxymethyltransferase, cytosolic
- Alanine--glyoxylate aminotransferase 1
Sequence:
MQRSIFARFGNSSAAVSTLNRLSTTAAPHAKNGYATATGAGAAAATATASSTHAAAAAAAAANHSTQESGFDYEGLIDSELQKKRLDKSYRYFNNINRLAKEFPLAHRQREADKVTVWCSNDYLALSKHPEVLDAMHKTIDKYGCGAGGTRNIAGHNIPTLNLEAELATLHKKEGALVFSSCYVANDAVLSLLGQKMKDLVIFSDELNHASMIVGIKHANVKKHIFKHNDLNELEQLLQSYPKSVPKLIAFESVYSMAGSVADIEKICDLADKYGALTFLDEVHAVGLYGPHGAGVAEHCDFESHRASGIATPKTNDKGGAKTVMDRVDMITGTLGKSFGSVGGYVAASRKLIDWFRSFAPGFIFTTTLPPSVMAGATAAIRYQRCHIDLRTSQQKHTMYVKKAFHELGIPVIPNPSHIVPVLIGNADLAKQASDILINKHQIYVQAINFPTVARGTERLRITPTPGHTNDLSDILINAVDDVFNELQLPRVRDWESQGGLLGVGESGFVEESNLWTSSQLSLTNDDLNPNVRDPIVKQLEVSSGIKQ
Protein: Protein FAM200A (Q8TCP9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTPESRDTTDLSPGGTQEMEGIVIVKVEEEDEEDHFQKERNKVESSPQVLSRSTTMNERALLSSYLVAYRVAKEKMAHTAAEKIILPACMDMVRTIFDDKSADKLRTIPLSDNTISRRICTIAKHLEAMLITRLQSGIDFAIQLDESTDIASCPTLLVYVRYVWQDDFVEDLLCCLNLNSHITGLDLFTELENCLLGQYKLNWKHCKGISSDGTANMTGKHSRLTEKLLEATHNNAVWNHCFIHREALVSKEISPSLMDVLKNAVKTVNFIKGSSLNSRLLEIFCSEIGVNHTHLLFHTEVRWLSQGKVLSRVYELRNEIYIFLVEKQSHLANIFEDDIWVTKLAYLSDIFGILNELSLKMQGKNNDIFQYLEHILGFQKTLLLWQARLKSNRPSYYMFPTLLQHIEENIINEDCLKEIKLEILLHLTSLSQTFNYYFPEEKFESLKENIWMKDPFAFQNPESIIELNLEPEEENELLQLSSSFTLKNYYKILSLSAFWIKIKDDFPLLSRKSILLLLPFTTTYLCELGFSILTRLKTKKRNRLNSAPDMRVALSSCVPDWKELMNRQAHPSH
Protein: HTH arsR-type domain-containing protein (Q9HW47)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
Sequence:
MPLDIDEIIKALSHPVRRDMLRWLKEPEKYFVEQDHPFEIGVCAGKFDQRTGLSQSTVSVHLATLQRAGLVTSRRVGQWNFFKRNEETIQAFLDQLGDEL
Protein: Histidine-rich calcium binding protein (Q80W59)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGFQEPWLYSCLLWATVAILLVPPVVTQELRGTGLGLGNWNNNAGIPGSSEDLSTEYGHHIHSHGAYQGEKDRHHREEDEDFSREYGHQVQDHRYPGHEVGEENVSEEVFRGHVRQLHGHHKPNSEDLGDSAESHFPRQQSHNREEEDGVVSGEDHRHIPRHDHHGNEEEDDDGEEEERVGVMENSDDKHQAHGHHSHSKERDGLHHAHSHRHQGHHDEDDDDEDGVSTEGEHQAHRYQDHDEEDDDDSDEESHAHRLQGQEDENDDEDGDSSENGHQTQDHQGHKEQDDDDDEEEEEEEEEEEEEEEEEEEEEEEDDDDDSTEHRHRHQTQGHRKGKDEDESDEDDHVTRHGRRGHEDEDDDDDDDDDDDDDNDGGSTENVHQAHRHRGHEHEDDGDDSEEDYHHVPSHGHQSHQNEEEEDEAVSTEHWHQSPRHAHHDLGRENQEEATVKYSRHVASHRPQGHSAEEDSLEDSTNEVPGHHHHRVSRDGDEDISTEFGHKAPRHRLQDQDEWTRQGHGKSVQEDIGHQPLQPTGPGSGESRKEDDHSSQEGDEDLKQRQEAHSEEEEEEEEGHGLPMSLEDEEEEEKDKKESKGDRAAVSAPLSHHRKHDDDDDGDGDDDDDDNDDDDEILEENLLPFTIIPNPLAGREVAREGSSEEESREVTGQQDAQEYENYQPGSLCGYCSFCNRCSECESCHCDEENMGEHCDQCQHCQFCYLCPLVCDTLCTPGSYVDYFSSSVYQAVADMLETQEP
Protein: Microtubule associated protein 7 (A0A087WZ40)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGSATALRHERLKKTNARPIPLGLFTINEEDEQQKNGNSRRPKAPDSYKVQDKKNASSRPASAISGQNNNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNRWSWGGSLHGSPSIHSADPDRRSVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVNRLLTPTHSFLARSKSTAALSGEAVIPICPRSASCSPIIMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTASYKKERERENVLFLTSGTRRAVSPSNPKARQPARSRLWLPSKSLPHLPGTPRPTSSLPPGSVKAAPAQVRPPSPGNIRPVKREVKVEPEKKDPEKEPQKVANEPSLKGRAPLVKVEEATVEERTPAEPEVGPAAPAMAPAPASAPAPASAPAPAPVPTPAMVSAPSSTVNASASVKTSAGTTDPEEATRLLAEKRRLAREQREKEERERREQEELERQKREELAQRVAEERTTRREEESRRLEAEQAREKEEQLQRQAEERALREREEAERAQRQKEEEARVREEAERVRQEREKHFQREEQERLERKKRLEEIMKRTRRTEATDKKTSDQRNGDIAKGALTGGTEVSALPCTTNAPGNGKPVGSPHVVTSHQSKVTVESTPDLEKQPNENGVSVQNENFEEIINLPIGSKPSRLDVTNSESPEIPLNPILAFDDEGTLGPLPQVDGVQTQQTAEVI
Protein: Uncharacterized protein C140.04 (Q9P7B7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein NRDE2 homolog
- Uncharacterized protein C17A2.08c
- Uncharacterized helicase C17H9.02
- Copper transport protein ctr5
- Copper transport protein ctr4
- Metal homeostasis factor atx1
- Uncharacterized protein C20H4.06c
- Pre-mRNA-splicing factor cwf4
- Membrane-anchored protein 1
- Ribosome quality control complex subunit 2
Sequence:
MNVGKKSEIQVSAKSNLNFLNELIEEKKRYEDEKRKISHQKYTDKLLEANDNETTKRKLLVKQKRKSNKEFQSNIIKKRKDEERKGTLKTEQANEEELLQRSRLELERKAKKYDQYAAGELEIKETEDDGILVDFTRKWAEEAPENETVEITDEFGRTRSVSIYETGNTLLSQKEEYKPEKPIYGDYMPSFEVDEEKVQKLWKEDEQQAVHYDSTKEVRNKGTAFYQFSFDEKEREEQLLSLKEIHAKVTQQQRKNTEDVLTLRDKKLEERRKFLERDYAIKLGERWMSEHFSNN
Protein: Transforming growth factor beta-1-induced transcript 1 protein (Androgen receptor-associated protein of 55 kDa) (Hydrogen peroxide-inducible clone 5 protein) (Hic-5) (Q99PD6)
Organism: Rattus norvegicus (Rat)
Function: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity.
Subcellular location: Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Associated with the actin cytoskeleton, colocalizes with stress fibers.
Interaction partners:
- Vinculin
- Protein-tyrosine kinase 2-beta
- Androgen receptor
- Breast cancer anti-estrogen resistance protein 1
- Tyrosine-protein phosphatase non-receptor type 12
- Focal adhesion kinase 1
- Talin 1
- Talin 2
- PRKCA-binding protein
- Alpha-parvin
Sequence:
MEDLDALLSDLETTTSHMSRLGAPKERPPETLTPPPPYGHQPQTGSGESSGASGDKDHLYSTVCKPRSPKSVAPVAPPFSSSSGVLGNGLCELDRLLQELNATQFNITDEIMSQFPSSKMAEGEGKEDQSEDKSITTVPSSTFPAPSKPSATSATQELDRLMASLSDFRVQNHLPASGPPQPPAVSPTREGCPSPPGQTNKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFLCRGCSTTLGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGEEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECLAPFSGGSFFEHEGRPLCENHFHAQRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERASKPYCQPCFLKLFG
Protein: Serine/threonine-protein kinase pef1 (EC 2.7.11.22) (Cyclin-dependent kinase pef1) (PHO85 homolog) (O74456)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Glycerophosphocholine phosphodiesterase gde1
- Meiotically up-regulated gene 80 protein
- Cyclin-dependent kinases regulatory subunit
- G1/S-specific cyclin pas1
- Cell division control protein 18
- PHO85 cyclin-like protein psl1
- Protein kinase rad3
- Anaphase-promoting complex subunit 3
- Mitosis inhibitor protein kinase wee1
- Protein phosphatase PP2A regulatory subunit B
Sequence:
MNYQRLEKLGEGTYAHVYKGQNRVTGEIVALKVIRIDADEGTPSTAIREISLMKELRHPNIMSLSDVLQTENKLMLVFEYMEKDLKKYMDTYGNQGALPPSQVKNFTQQLLKGISFCHENRVLHRDLKPQNLLINSRGELKLADFGLARSIGIPVNTFSNEVVTLWYRAPDVLLGSRVYSTSIDIWSVGCIMAEMATGRPLFAGSNNEDQLLKIFRLLGTPTEQSWPGISLLPEYKPTFPIYKAQDLAYLFPTFDPLGLDLLRRMLRLQPELRTTGQDALQHAWFLTA
Protein: Myb family transcription factor 109 (Transcription factor WER-like protein) (Q6GVK7)
Organism: Gossypium arboreum (Tree cotton) (Gossypium nanking)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSMKKEGEILYKKGLWAMEEDKLLIDYVNVHGKGQWNKIANRTGLKRSGKSCRLRWMNYLSPNVKKGDFSEEEEDLVIRLHKLLGNRWSLIAKRVPGRTDNQVKNYWNSHLRKKLGIIDQNKTRIDFCQSSKQVKVCHVDEAATDPSPGHGTTTETTGITVDQSNQQEVIDHRVLNNTTQESMTTESYINTFWIPDHDYELSTLAMIDHFHECSSFHLS
Protein: Immunoglobulin lambda variable 3-21 (Ig lambda chain V-III region LOI) (Ig lambda chain V-V region DEL) (Ig lambda chain V-VII region MOT) (P80748)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWTVLLLGLLSHCTGSVTSYVLTQPPSVSVAPGQTARITCGGNNIGSKSVHWYQQKPGQAPVLVVYDDSDRPSGIPERFSGSNSGNTATLTISRVEAGDEADYYCQVWDSSSDHPT
Protein: Endothelial protein C receptor (Activated protein C receptor) (APC receptor) (Centrocyclin) (Centrosomal protein CCD41) (Endothelial cell protein C receptor) (CD antigen CD201) (Q64695)
Organism: Mus musculus (Mouse)
Function: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Vitamin K-dependent protein C
- Thrombomodulin
- Prothrombin
- Proteinase-activated receptor 1
- Platelet factor 4
- COX assembly mitochondrial protein 2 homolog
- Coagulation factor VII
- Myeloblastin
- Integrin alpha-M
- Tissue factor pathway inhibitor
Sequence:
MLTKFLPLLLLLLPGCALCNSDGSQSLHMLQISYFQDNHHVRHQGNASLGKLLTHTLEGPSQNVTILQLQPWQDPESWERTESGLQIYLTQFESLVKLVYRERKENVFFPLTVSCSLGCELPEEEEEGSEPHVFFDVAVNGSAFVSFRPKTAVWVSGSQEPSKAANFTLKQLNAYNRTRYELQEFLQDTCVEFLENHITTQNMKGSQTGRSYTSLVLGILMGCFIIAGVAVGIFMCTSGRRC