wanglab/gogpt-training-data huggingface dataset:
Protein: Mediator of RNA polymerase II transcription subunit 7 (Cofactor required for Sp1 transcriptional activation subunit 9) (CRSP complex subunit 9) (Mediator complex subunit 7) (Q9CZB6)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 6
Sequence:
MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKAEPMDTDDNSNCPGQNEQQRESSGHRRDQIIEKDAALCVLIDEMNERP
Protein: Hook microtubule-tethering protein 1 (D3ZB48)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- AKT-interacting protein
- FHF complex subunit HOOK-interacting protein 1B
- Hook microtubule-tethering protein 2
- RIMS binding protein 3
- FHF complex subunit HOOK interacting protein 2A
- Ac1288
- Cytoplasmic dynein 1 light intermediate chain 1
- BICD cargo adaptor 2)
Sequence:
MEDPQPLPQPELPLCDSLIIWLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESECKVAKFRDYEEKLIVSAWYNKSLAFQKLGMESRLVSGASACKDSVAAAPARSFLAQQRHITSTRRNLSVKVPAAASD
Protein: Serine/threonine-protein kinase SRK2E (EC 2.7.11.1) (Protein OPEN STOMATA 1) (SNF1-related kinase 2.6) (SnRK2.6) (Serine/threonine-protein kinase OST1) (Q940H6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activator of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomata closure in response to drought, darkness, high CO(2), plant pathogens, or decreases in atmospheric relative humidity (RH). Involved in the resistance to drought by avoiding water loss. Required for the stomata closure mediated by pathogen-associated molecular pattern (PAMPs) (e.g. flg22 and LPS) of pathogenic bacteria such as P.syringae pv. tomato (Pst) and E.coli O157:H7. As a plant defense process, stomata are closed transiently in order to limit invaders, but actively reopened by bacteria after a few hours; virulent strains (e.g. Pst DC3000) are more efficient than avirulent strains (e.g. Pst DC3000 AvrRpt2) in reopening stomata. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1, and thus promotes stomata closure. Essential for stomatal closure in response to reactive oxygen species (ROS). Promotes MAPKKK18 activity upon abscisic acid (ABA) treatment.
Subcellular location: Nucleus {ECO:0000269|PubMed:26852793}.
Interaction partners:
- Protein phosphatase 2C 77
- Protein phosphatase 2C 16
- Protein phosphatase 2C 56
- Protein phosphatase 2C 37
- Guard cell S-type anion channel SLAC1
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
- Transcription factor ICE1
- Probable protein phosphatase 2C 78
- Abscisic acid receptor PYR1
- ABSCISIC ACID-INSENSITIVE 5-like protein 4
Sequence:
MDRPAVSGPMDLPIMHDSDRYELVKDIGSGNFGVARLMRDKQSNELVAVKYIERGEKIDENVKREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYASGGELFERICNAGRFSEDEARFFFQQLISGVSYCHAMQVCHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLKKEYDGKVADVWSCGVTLYVMLVGAYPFEDPEEPKNFRKTIHRILNVQYAIPDYVHISPECRHLISRIFVADPAKRISIPEIRNHEWFLKNLPADLMNDNTMTTQFDESDQPGQSIEEIMQIIAEATVPPAGTQNLNHYLTGSLDIDDDMEEDLESDLDDLDIDSSGEIVYAM
Protein: Natural killer cell receptor 2B4 (NK cell type I receptor protein 2B4) (NKR2B4) (Non-MHC restricted killing associated) (SLAM family member 4) (SLAMF4) (Signaling lymphocytic activation molecule 4) (CD antigen CD244) (Q07763)
Organism: Mus musculus (Mouse)
Function: Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor. Activating function implicates association with SH2D1A and FYN. Downstreaming signaling involves predominantly VAV1, and, to a lesser degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of SH2D1A is proposed to be dependent on INPP5D and to a lesser extent PTPN6/SHP-1 and PTPN11/SHP-2. Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis. Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells. Regulation of NK cell activity by adapters Sh2d1b and Sh2d1b2 is reported conflictingly. Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1. At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self-tolerance of developing NK cells (By similarity). Involved in the regulation of CD8(+) T-cell proliferation; expression on activated T-cells and binding to CD488 provides costimulatory-like function for neighboring T-cells. Inhibits inflammatory responses in dendritic cells (DCs).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9BZW8}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BZW8}. Cell membrane {ECO:0000250|UniProtKB:Q9BZW8}. Membrane raft {ECO:0000250|UniProtKB:Q9BZW8}. Note=Receptor engagement results in a recruitment to lipid drafts essential for the subsequent tyrosine phosphorylation of the ITSMs. {ECO:0000250|UniProtKB:Q9BZW8}.
Interaction partners:
- CD48 antigen
- SH2 domain-containing protein 1A
- SH2 domain-containing protein 1B
- Tyrosine-protein kinase Fyn
- SH2 domain-containing protein 1B2
- Linker for activation of T-cells family member 1
- Histone-lysine N-methyltransferase EZH2
- SLAM family member 6
- Natural cytotoxicity triggering receptor 1
- CD160 antigen
Sequence:
MLGQAVLFTTFLLLRAHQGQDCPDSSEEVVGVSGKPVQLRPSNIQTKDVSVQWKKTEQGSHRKIEILNWYNDGPSWSNVSFSDIYGFDYGDFALSIKSAKLQDSGHYLLEITNTGGKVCNKNFQLLILDHVETPNLKAQWKPWTNGTCQLFLSCLVTKDDNVSYALYRGSTLISNQRNSTHWENQIDASSLHTYTCNVSNRASWANHTLNFTHGCQSVPSNFRFLPFGVIIVILVTLFLGAIICFCVWTKKRKQLQFSPKEPLTIYEYVKDSRASRDQQGCSRASGSPSAVQEDGRGQRELDRRVSEVLEQLPQQTFPGDRGTMYSMIQCKPSDSTSQEKCTVYSVVQPSRKSGSKKRNQNSSLSCTVYEEVGNPWLKAHNPARLSRRELENFDVYS
Protein: PepSY domain-containing protein (Q9I178)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Thiamine pyrophosphate-binding protein
- Periplasmic protein
- Secreted protein
- High-affinity zinc uptake system protein ZnuA
- Metal ABC transporter substrate-binding protein
- Probable permease of ABC transporter
- Probable ATP-binding component of ABC transporter
- Ferripyoverdine receptor
- Uncharacterized protein PA4219
- L-ornithine N
Sequence:
MSKKSRSRLWFLVHSWLALPIWFFVLIVCVTGTLAVVSQEIVWLANPDVRASKPYEDAEPLSFSQVLKAINEAQPDLLVESIQRPDEEHFALTAEVSYPGGSEATLYINPYTGAIQGESPSFDFRQFTRALHGWWLVPFNNGYSWGWYMVSLLGLPMLASLITGLVVYKRFWKGFLKPRLRINQGARIFWGDFHRLSGIWSIWFIALISITGTWFLIQAILADNHVTLTNDGIPPVIARADVPRAAPGQKVPYIELDEAVRLVTGRIPSLEASAVFLPGNAYSPMFVAGRGWYPLMFQSAALNPYTGKIETTRLLSDRTPLQFVTESMRPLHTGDFGGIWVKLIWFVFGLLLSMMVLSGLLIWSKRTAQATAALVKRGKRPARQPKPAKPAPVMANQTAEGQP
Protein: Inversin (Q8UVC1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled for degradation by the ubiquitin-proteasome. This suggests that it is required in renal development to oppose the repression of terminal differentiation of tubular epithelial cells by Wnt signaling.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associates with the cytoskeleton. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase Nek8
- Nephronophthisis 1.
- Nephrocystin-3
- Si:dkey-202c5.1 protein.
- Abelson helper integration site 1.
- Centrosomal protein of 290 kDa
- IQ calmodulin-binding motif-containing protein 1
- Intraflagellar transport 88 homolog.
- Prickle homolog 2b
- Prickle homolog 2a.
Sequence:
MAMLLPQNPSQVHAAAVNGDKNTLHKLITESALRDSEDQFGRTPLMYCVLADRLDCAEVLLKAGAGINKTDHSQRTALHLAAQKGNVRFMKLLLSRHADWRLKDLEEMTPLHLASRHSSSKPLSLLLKHMAPGEVDTQDRNKQTALHWSAFYNHPEHVKLLIKHDSNIGIPDSEGKIPLHWAAHNKHPNATRTVRCILEAAPTESLLNWQDYEGRTPLHFAVADGNEAVVEVLTSYEGCSVTAYDNLFRTPLHWAALLGHAKIVHLLLERNKSGMIPSDSQGATPLHYGAQSNFADTVAVFLKHHSVRDEPDLEGRTAFMWAAGKGSNDVIKIMLDLKKDIDINMTDKYGGTALHAAALSGHVSTVRLLLEQGGMVDPLDVMKHTPLFRACEMGHRDVILTLIKGGARVDLVDIDGHSALHWAALGGNAEVCEVLMENGISPNLQDQAGRTPLQCAAYAGYINCMALLIQHDADPNIQDKEGRTALHWSCNNGYLDAVKLLLGCGAFPNHMEHTEERYTPLDYALLGEHQELTQFLLEHGALSIAAIQDIAASSIQALYKGYKVRRAFRERKKLLMRHEQLRKDAAKKREEERRREAEQQLSFAEAGQKQRVLLAAVGVEKLSLDEAEQRVKDSVAAKGHKHKKSSSAHNSQSRREKPSRAERRTREPETSDAPSIRSLPPVTPMSTKKCPVTREEVCVRETFGPDTGISLNCGSANERRSPAGSSRPGSAKPVHTGTHVAPGHMETTPTPKPRPSTTGAHSKNASQDTPQHNETQTTSKGNKPISEHKPTGSQPSNNTSVTRQKEKRQEKETHREKDKRSRTEGDKQTVREKQKGTGIERAKERLMGRTRKKLAEKEKEKKKDGTCSKNQAAVVIQRAWRRSCVRGRIRKVLCRSLKGVESAEATALLIQLLWEWPVLHDHTHRKPSDVQAPPTRIAGKKSSVLQNIYGAAPSKRGTSLRAAALKTQSQSQSQVLLDLSLRTHKQLSAVECVNLVDSVSQAKQFSYHLRPSSGASQSSQN
Protein: V-set domain containing T-cell activation inhibitor 1 (B7 homolog 4) (B7-H4) (Immune costimulatory protein B7-H4) (Protein B7S1) (T cell costimulatory molecule B7x) (Q7TSP5)
Organism: Mus musculus (Mouse)
Function: Negatively regulates T-cell-mediated immune response by inhibiting T-cell activation, proliferation, cytokine production and development of cytotoxicity. When expressed on the cell surface of tumor macrophages, plays an important role, together with regulatory T-cells (Treg), in the suppression of tumor-associated antigen-specific T-cell immunity. Involved in promoting epithelial cell transformation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}. Note=Expressed at the cell surface. A soluble form has also been detected. {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}.
Interaction partners:
- B- and T-lymphocyte attenuator
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death 1 ligand 2
- Programmed cell death protein 1
Sequence:
MASLGQIIFWSIINIIIILAGAIALIIGFGISGKHFITVTTFTSAGNIGEDGTLSCTFEPDIKLNGIVIQWLKEGIKGLVHEFKEGKDDLSQQHEMFRGRTAVFADQVVVGNASLRLKNVQLTDAGTYTCYIRTSKGKGNANLEYKTGAFSMPEINVDYNASSESLRCEAPRWFPQPTVAWASQVDQGANFSEVSNTSFELNSENVTMKVVSVLYNVTINNTYSCMIENDIAKATGDIKVTDSEVKRRSQLQLLNSGPSPCVFSSAFVAGWALLSLSCCLMLR
Protein: Putative BCL-10 protein (Q2HQX3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MDSWCITDEDMAEVKKEALERLRPYLCEKLVADRHLDYLRSRRVLTRDDAEDICCRVGNSKKTGRMLDYLAENPRGLDYLVESICRVRTKDFVIGKITNEVEVVKMERREAAILSAAGSSSPVCICKERTPFVSLQSGSSEAQSIQTSLSNSEDKWGQNEASFSWSALPEGVSVSSLHSLPKPGEQGAPSVPLEDNEPGTLRV
Protein: Sal-like protein 2 (Spalt-like protein 2) (Zinc finger protein Spalt-2) (Sal-2) (mSal-2) (Q9QX96)
Organism: Mus musculus (Mouse)
Function: Probable transcription factor that plays a role in eye development before, during, and after optic fissure closure.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- POU domain, class 3, transcription factor 2
- Transcription factor SOX-2
Sequence:
MSRRKQRRPQQLISDCEGPSASENGDASEEDHPQVCAKCCAQFSDPTEFLAHQNSCCTDPPVMVIIGGQENPSNSSASSAPRPEGHSRSQVMDTEHSNPPDSGSSGAPDPTWGPERRGEESSGQFLVAATGTAAGGGGGLILASPKLGATPLPPESTPAPPPPPPPPPPPGVGSGHLNIPLILEELRVLQQRQIHQMQMTEQICRQVLLLGSLGQTVGAPASPSELPGTGAASSTKPLLPLFSPIKPAQTGKTLASSSSSSSSSGAEPPKQAFFHLYHPLGSQHPFSVGGVGRSHKPTPAPSPALPGSTDQLIASPHLAFPGTTGLLAAQCLGAARGLEAAASPGLLKPKNGSGELGYGEVISSLEKPGGRHKCRFCAKVFGSDSALQIHLRSHTGERPYKCNVCGNRFTTRGNLKVHFHRHREKYPHVQMNPHPVPEHLDYVITSSGLPYGMSVPPEKAEEEAGTPGGGVERKPLVASTTALSATESLTLLSTGTSTAVAPGLPTFNKFVLMKAVEPKSKADENTPPGSEGSAIAGVADSGSATRMQLSKLVTSLPSWALLTNHLKSTGSFPFPYVLEPLGASPSETSKLQQLVEKIDRQGAVAVASTASGAPTTSAPAPSSSASGPNQCVICLRVLSCPRALRLHYGQHGGERPFKCKVCGRAFSTRGNLRAHFVGHKTSPAARAQNSCPICQKKFTNAVTLQQHVRMHLGGQIPNGGSALSEGGGAAQENSSEQSTASGPGSFPQPQSQQPSPEEEMSEEEEEDEEEEEDVTDEDSLAGRGSESGGEKAISVRGDSEEVSGAEEEVATSVAAPTTVKEMDSNEKAPQHTLPPPPPPPDNLDHPQPMEQGTSDVSGAMEEEAKLEGTSSPMAALTQEGEGTSTPLVEELNLPEAMKKDPGESSGRKACEVCGQSFPTQTALEEHQKTHPKDGPLFTCVFCRQGFLDRATLKKHMLLAHHQVPPFAPHGPQNIATLSLVPGCSSSIPSPGLSPFPRKDDPTMP
Protein: Enoyl-CoA delta isomerase 2 (EC 5.3.3.8) (DRS-1) (Delta(3),delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Diazepam-binding inhibitor-related protein 1) (DBI-related protein 1) (Dodecenoyl-CoA isomerase) (Hepatocellular carcinoma-associated antigen 88) (Peroxisomal 3,2-trans-enoyl-CoA isomerase) (pECI) (Renal carcinoma antigen NY-REN-1) (O75521)
Organism: Homo sapiens (Human)
Function: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:Q5XIC0}.; SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome matrix {ECO:0000269|PubMed:10419495}.
Interaction partners:
- Enoyl-CoA delta isomerase 1, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Acetyl-CoA acetyltransferase, cytosolic
- Cocaine- and amphetamine-regulated transcript protein
- Acetyl-CoA acetyltransferase, mitochondrial
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Sterol carrier protein 2
Sequence:
MAMAYLAWRLARRSCPSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEVWTRLKAFAKLPPNALRISKEVIRKREREKLHAVNAEECNVLQGRWLSDECTNAVVNFLSRKSKL
Protein: Ribokinase (AtRBSK) (RK) (EC 2.7.1.15) (A1A6H3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway (By similarity). Can also use xylose and fructose as carbohydrate substrates with a low efficiency. Can use GTP, and, to a lower extent, CTP and UTP as alternative phosphoryl donors.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000269|PubMed:27601466}.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1, chloroplastic
- Ribose-phosphate pyrophosphokinase 5, chloroplastic
- Ribose-phosphate pyrophosphokinase 2, chloroplastic
- Transketolase-2, chloroplastic
- Transketolase-1, chloroplastic
- Probable ribose-5-phosphate isomerase 4, chloroplastic
- Probable ribose-5-phosphate isomerase 3, chloroplastic
- Probable ribose-5-phosphate isomerase 1
- Probable ribose-5-phosphate isomerase 2
- Probable phosphoglucomutase, cytoplasmic 2
Sequence:
MMKGISSVSQSINYNPYIEFNRPQLQISTVNPNPAQSRFSRPRSLRVLSLSADPSANRNPKSAVDAHAPPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDRKSVLKLLKFSI
Protein: Protein FimG (P08190)
Organism: Escherichia coli (strain K12)
Function: Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.
Subcellular location: Fimbrium.
Interaction partners:
- Type 1 fimbrin D-mannose specific adhesin
- Chaperone protein FimC
- Protein FimF
- Outer membrane usher protein FimD
- Type-1 fimbrial protein, A chain
- Fimbrin-like protein FimI
Sequence:
MKWCKRGYVLAAILALASATIQAADVTITVNGKVVAKPCTVSTTNATVDLGDLYSFSLMSAGAASAWHDVALELTNCPVGTSRVTASFSGAADSTGYYKNQGTAQNIQLELQDDSGNTLNTGATKTVQVDDSSQSAHFPLQVRALTVNGGATQGTIQAVISITYTYS
Protein: Systemic RNA interference defective protein 5 (Q19443)
Organism: Caenorhabditis elegans
Function: Plays a role in RNA-mediated gene silencing by mediating transport of both ingested and endogenous dsRNA between cells. Not required for the uptake of dsRNA from the intestinal lumen.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:22981770}; Single-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:22981770}.
Interaction partners:
- Tyrosine-protein kinase sid-3
- Systemic RNA interference defective protein 2
- Systemic RNA interference defective protein 1
- Vesicle-trafficking protein SEC22b
Sequence:
MPSKNCAKNLHACQWERDIALVFLGLMVLFNIGQVVYMNRARLYRLIRRGAEQIPADDEEPIIGIRD
Protein: Kinetochore protein NDC80 homolog (Highly expressed in cancer protein) (Kinetochore protein Hec1) (HsHec1) (Kinetochore-associated protein 2) (Retinoblastoma-associated protein HEC) (O14777)
Organism: Homo sapiens (Human)
Function: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules. Plays a role in chromosome congression and is essential for the end-on attachment of the kinetochores to spindle microtubules.
Subcellular location: Nucleus {ECO:0000269|PubMed:9315664}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14699129}. Note=Localizes to kinetochores from late prophase to anaphase (PubMed:14699129). Localizes specifically to the outer plate of the kinetochore (PubMed:14699129). {ECO:0000269|PubMed:14699129}.
Interaction partners:
- Kinetochore protein Spc24
- Kinetochore protein Nuf2
- Kinetochore protein Spc25
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Outer kinetochore KNL1 complex subunit KNL1
- Cytoskeleton-associated protein 5
- Dual specificity protein kinase TTK
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Protein MIS12 homolog
- Outer kinetochore KNL1 complex subunit ZWINT
Sequence:
MKRSSVSSGGAGRLSMQELRSQDVNKQGLYTPQTKEKPTFGKLSINKPTSERKVSLFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQEREKEPNRLESLRKLKASLQGDVQKYQAYMSNLESHSAILDQKLNGLNEEIARVELECETIKQENTRLQNIIDNQKYSVADIERINHERNELQQTINKLTKDLEAEQQKLWNEELKYARGKEAIETQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRAQVYVPLKELLNETEEEINKALNKKMGLEDTLEQLNAMITESKRSVRTLKEEVQKLDDLYQQKIKEAEEEDEKCASELESLEKHKHLLESTVNQGLSEAMNELDAVQREYQLVVQTTTEERRKVGNNLQRLLEMVATHVGSVEKHLEEQIAKVDREYEECMSEDLSENIKEIRDKYEKKATLIKSSEE
Protein: Nodulin-like protein (Putative nodulin protein) (T1N24.3 protein) (Q9XGZ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Early nodulin-like protein 13
- Histone H4
- Early nodulin-like protein 6
- Cyclin-dependent kinase C-2 C
- Early nodulin-like protein 10
- WAT1-related protein At5g07050
- Early nodulin-like protein 15
- GPI-anchored protein LORELEI
Sequence:
MENRSEMGNRRQQNLFVIASPDEIAKIHRAETSKQAGAIAGAKAAAVAAVASAIPTVAAVRMFPWAKANLNYTAQALIISSASIAAFFITADKTILQGARRNTEAQLKKVQQDSK
Protein: 60S ribosomal protein L34, putative (Q383V6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L35, putative
- 60S ribosomal protein L13a, putative
- 60S ribosomal protein L19, putative
- 60S ribosomal protein L2, putative
- Large ribosomal subunit protein uL5
- Ribosomal protein L37
- 60S ribosomal protein L27a
- 60S ribosomal protein L29
Sequence:
MSCPRVQYRRRMHYATRGNRMRLVRTPGNRLVMQKRGKRSQGPHTPWVLGHKRLAGTKALRHTKARLAPRHQKTTSRPYGGVLSHEQVRDRIVRAFLIEEQRIVKRALKAHAKVQKEKKRRAAKRKSKEEKVAAVAKKVAAKVGAKSVIAKKEAPKRKAGKAPVGAKLKK
Protein: Nuclear factor 1 (Q5VW26)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQPNGSGQVVGKVPGHFTPVLAPSPHPSAVRPVTLSMTDTKPITTSTEGEAASPTATTYTASGTSQANRYVGLSPRDPSFLHQQQLRICDWTMNQNGRHLYPSTSEDTLGITWQSPGTWASLVPFQVSNRTPILPANVQNYGLNIIGEPFLQAETSN
Protein: L-cysteine S-thiosulfotransferase subunit SoxA (EC 2.8.5.2) (Cytochrome c551 subunit monoheme) (Protein SoxA) (SoxAX cytochrome complex subunit A) (Sulfur oxidizing protein A) (Thiosulfate-oxidizing multienzyme system protein SoxA) (TOMES protein SoxA) (Q08IS0)
Organism: Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila)
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.
Subcellular location: Periplasm {ECO:0000269|PubMed:17516047}.
Interaction partners:
Sequence:
MKKTVTAVALLCALSSTAIAPTFAADDDEAARLKAIEEYRKQIADGNPSDLLAMEGEELWRTPYGPKNQSLEQCDLGLGPGVVKGAAAKLPRYFPDTGKVEDLESRLMTCMERLQGVERQKVIDSPWRKGEKLRMDKIVAYIVTESNGEKIDVDMSHPKMKEMYELGKRMFFYRTGPFDFSCATCHGKDGQRIRLQELPNLTKHEGAAAGWGSWPAYRVSNSQFWTMQMRLNDCFRQQRTAEPIYGSDATIALSVYMAANGNGGVMLTPGIKR