wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor Sox-2 (XSox2) (XlSox-2) (SRY (sex determining region Y)-box 2) (O42569)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional activator (By similarity). Functions as a switch in neuronal development, participating in the differentiation of embryonic neuroectodermal cells into neural tissues by making the ectodermal cells responsive to FGF-neuralizing signals. Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
Sequence:
MYSMMETELKPPAPQQPSGGNSNSASNNQNKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGANAMTSGVGGSLGAGVNQRMDTYAHMNGWTNGGYGMMQEQLGYPQHPGLNAHNAPQMQPMHRYDVSALQYNSMSSSQTYMNGSPTYSMSYSQQGAPGMSLGSMGSVVKSESSSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPESAAQSRLHMSQHYQSASVAGTGINGTLPLSHM
Protein: Mitochondrial genome maintenance exonuclease 1 (EC 3.1.-.-) (Q9BQP7)
Organism: Homo sapiens (Human)
Function: Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance. Has preference for 5'-3' exonuclease activity but is also capable of endoduclease activity on linear substrates. Necessary for maintenance of proper 7S DNA levels. Probably involved in mitochondrial DNA (mtDNA) repair, possibly via the processing of displaced DNA containing Okazaki fragments during RNA-primed DNA synthesis on the lagging strand or via processing of DNA flaps during long-patch base excision repair. Specifically binds 5-hydroxymethylcytosine (5hmC)-containing DNA in stem cells.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03030, ECO:0000269|PubMed:23313956, ECO:0000269|PubMed:23358826}.
Interaction partners:
- Twinkle mtDNA helicase
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA polymerase subunit gamma-2
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- DNA-directed RNA polymerase, mitochondrial
- DNA polymerase subunit gamma-1
- Deoxyguanosine kinase, mitochondrial
Sequence:
MKMKLFQTICRQLRSSKFSVESAALVAFSTSSYSCGRKKKVNPYEEVDQEKYSNLVQSVLSSRGVAQTPGSVEEDALLCGPVSKHKLPNQGEDRRVPQNWFPIFNPERSDKPNASDPSVPLKIPLQRNVIPSVTRVLQQTMTKQQVFLLERWKQRMILELGEDGFKEYTSNVFLQGKRFHEALESILSPQETLKERDENLLKSGYIESVQHILKDVSGVRALESAVQHETLNYIGLLDCVAEYQGKLCVIDWKTSEKPKPFIQSTFDNPLQVVAYMGAMNHDTNYSFQVQCGLIVVAYKDGSPAHPHFMDAELCSQYWTKWLLRLEEYTEKKKNQNIQKPEYSE
Protein: Photosystem II reaction center protein L (PSII-L) (Q2LIJ1)
Organism: Oryza australiensis
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01317}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01317}.
Interaction partners:
Sequence:
MTQSNPNEQNVELNRTSLYWGLLLIFVLAVLFSNYFFN
Protein: Slc30a10 protein (A8WFU0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGRYSGKTCRLILMLVITVIFFVAEIVAGYMGNSVALVSDSFNMLSDILSLCVGLTAARVSRRAGSGRFSFGLGRAEVVGALANAVFLIALCFSISMESLKRLAMPQAIDDAPLVLIVGSLGLAVNLVGLVIFQDCGRLCGRRGKEKKREEHREDREQELEQVETGLQEEKTEKDGAPLNIRGVLLHVLNDALGSVVVVVASALFYVWPLEPDQPCNWQCYVDPSLTLVMVIIILSSAAPLLKETTTILLQMSPEDLPVSAILESVCRLPGVSSVHEAHVWELAKGRNVASLHVKLQAPAGALWAQVSLQQQITQIFHRAGVHSLTLQLELADSDADSSCSAPCLSSSCQKLSCCPAGPVCVCAPPRDSSTEKHTPEACTHSSKL
Protein: Zinc finger protein 578 (Q96N58)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLHEEAAQKRKGKEPGMALPQGRLTFRDVAIEFSLAEWKFLNPAQRALYREVMLENYRNLEAVDISSKRMMKEVLSTGQGNTEVIHTGMLQRHESYHTGDFCFQEIEKDIHDFEFQSQKDERNGHEASMPKIKELMGSTDRHDQRHAGNKPIKDQLGLSFHLHLPELHIFQPEEKIANQVEKSVNDASSISTSQRISCRPETHTPNNYGNNFFHSSLLTQKQEVHMREKSFQCNETGEAFNCSSFVRKHQIIHLGEKQYKFDICGKVFNEKRYLARHRRCHTSEKPYKCNECGKSFSYKSSLTCHRRCHTGEKPYKCNECGKSFSYKSSLTCHHRCHTGEKPYKCNECGKSFSYKSSLRCHRRLHTGIKPYKCNECGKMFGQNSTLVIHKAIHTGEKPYKCNECGKAFNQQSHLSRHHRLHTGEKPYKCNDCGKAFIHQSSLARHHRLHTGEKSYKCEECDRVFSQKSNLERHKIIHTGEKPYKCNECHKTFSHRSSLPCHRRLHSGEKPYKCNECGKTFNVQSHLSRHHRLHTGEKPYKCKVCDKAFMCHSYLANHTRIHSGEKPYKCNECGKAHNHLIDSSIKPCMSS
Protein: Probable fimbrial chaperone YadV (P33128)
Organism: Escherichia coli (strain K12)
Function: Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches.
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
- Outer membrane usher protein HtrE
- Outer membrane usher protein YehB
- Probable outer membrane usher protein ElfC
- Outer membrane usher protein SfmD
- Outer membrane usher protein FimD
- Uncharacterized outer membrane usher protein YbgQ
- Outer membrane usher protein YraJ
- Uncharacterized outer membrane usher protein YhcD
- Uncharacterized fimbrial-like protein YadM
- Type-1 fimbrial protein, A chain
Sequence:
MFFNTKHTTALCFVTCMAFSSSSIADIVISGTRVIYKSDQKSVNVRLENKGNNPLLVQSWLDTGDDNAEPGSITVPFTATPPVSRIDAKRGQTIKLMYTASTSLPKDRESVFWFNVLEVPPKPDAEKVANQSLLQLAFRTRIKLFYRPDGLKGNPSEAPLALKWFWSGSEGKASLRVTNPTPYYVSFSSGDLEASGKRYPIDVKMIAPFSDEVMKVNGLNGKANSAKVHFYAINDFGGAIEGNARL
Protein: Myb domain protein 100 (Putative MYB family transcription factor) (Putative transcription factor) (Q9S754)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Coiled-coil domain-containing protein 86
- AT4g02720/T10P11_1
- AT5g28150/T24G3_80
Sequence:
MKKNYQKKNIKVVSTSKYLKKSDIDKVNWTESEDIKLKEIMALGPKNKWTKVAKKFEGRTGKQCRERWYNHARPNIKKTAWSEEEDQILIEAHKVLGTKWVEIAQQLPGRSDNNIKNHWNTTKRRVQNKRGGTVNPVGNNILENYIRCITINNEDFLKTDGSYGEPTNIESDDDSKDMLYGEMNLSLETITTQTTKPLTNASTTSPYVQMPEDNYTMEDCESLEDILELLRWWE
Protein: Phytochrome E (P42498)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
Interaction partners:
- Cryptochrome-1
- Cryptochrome-2
- Phototropin-2
- Phototropin-1
- Transcription factor PIF3
- E3 ubiquitin-protein ligase COP1
- Cryptochrome DASH, chloroplastic/mitochondrial
- Transcription factor PIF6
- Adagio protein 2
- Adagio protein 1
Sequence:
MGFESSSSAASNMKPQPQKSNTAQYSVDAALFADFAQSIYTGKSFNYSKSVISPPNHVPDEHITAYLSNIQRGGLVQPFGCLIAVEEPSFRILGLSDNSSDFLGLLSLPSTSHSGEFDKVKGLIGIDARTLFTPSSGASLSKAASFTEISLLNPVLVHSRTTQKPFYAILHRIDAGIVMDLEPAKSGDPALTLAGAVQSQKLAVRAISRLQSLPGGDIGALCDTVVEDVQRLTGYDRVMVYQFHEDDHGEVVSEIRRSDLEPYLGLHYPATDIPQAARFLFKQNRVRMICDCNATPVKVVQSEELKRPLCLVNSTLRAPHGCHTQYMANMGSVASLALAIVVKGKDSSKLWGLVVGHHCSPRYVPFPLRYACEFLMQAFGLQLQMELQLASQLAEKKAMRTQTLLCDMLLRDTVSAIVTQSPGIMDLVKCDGAALYYKGKCWLVGVTPNESQVKDLVNWLVENHGDDSTGLTTDSLVDAGYPGAISLGDAVCGVAAAGFSSKDYLLWFRSNTASAIKWGGAKHHPKDKDDAGRMHPRSSFTAFLEVAKSRSLPWEISEIDAIHSLRLIMRESFTSSRPVLSGNGVARDANELTSFVCEMVRVIETATAPIFGVDSSGCINGWNKKTAEMTGLLASEAMGKSLADEIVQEESRAALESLLCKALQGEEEKSVMLKLRKFGQNNHPDYSSDVCVLVNSCTSRDYTENIIGVCFVGQDITSEKAITDRFIRLQGDYKTIVQSLNPLIPPIFASDENACCSEWNAAMEKLTGWSKHEVIGKMLPGEVFGVFCKVKCQDSLTKFLISLYQGIAGDNVPESSLVEFFNKEGKYIEASLTANKSTNIEGKVIRCFFFLQIINKESGLSCPELKESAQSLNELTYVRQEIKNPLNGIRFAHKLLESSEISASQRQFLETSDACEKQITTIIESTDLKSIEEGKLQLETEEFRLENILDTIISQVMIILRERNSQLRVEVAEEIKTLPLNGDRVKLQLILADLLRNIVNHAPFPNSWVGISISPGQELSRDNGRYIHLQFRMIHPGKGLPSEMLSDMFETRDGWVTPDGLGLKLSRKLLEQMNGRVSYVREDERCFFQVDLQVKTMLGVESRGTEGSSSIK
Protein: Cellular tumor antigen p53 (Tumor suppressor p53) (Q29537)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P04637}.
Interaction partners:
- E3 ubiquitin-protein ligase Mdm2
- MDM4 regulator of p53.
- Serine-protein kinase ATM
- CREB binding protein.
- E1A binding protein p300.
- Sirtuin 1.
- Ubiquitin specific peptidase 7
- Cyclin dependent kinase inhibitor 1A.
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
Sequence:
MEESQSELNIDPPLSQETFSELWNLLPENNVLSSELCPAVDELLLPESVVNWLDEDSDDAPRMPATSAPTAPGPAPSWPLSSSVPSPKTYPGTYGFRLGFLHSGTAKSVTWTYSPLLNKLFCQLAKTCPVQLWVSSPPPPNTCVRAMAIYKKSEFVTEVVRRCPHHERCSDSSDGLAPPQHLIRVEGNLRAKYLDDRNTFRHSVVVPYEPPEVGSDYTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNVLGRNSFEVRVCACPGRDRRTEEENFHKKGEPCPEPPPGSTKRALPPSTSSSPPQKKKPLDGEYFTLQIRGRERYEMFRNLNEALELKDAQSGKEPGGSRAHSSHLKAKKGQSTSRHKKLMFKREGLDSD
Protein: Mitochondrial substrate carrier family protein ancA (ADP,ATP carrier protein) (ADP/ATP translocase) (Adenine nucleotide translocator) (ANT) (O97470)
Organism: Dictyostelium discoideum (Social amoeba)
Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell. Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02722}.
Interaction partners:
- Cysteine proteinase 4
- Mitochondrial substrate carrier family protein Z
- Developmentally-regulated GTP-binding protein 1 homolog
- UPF0235 protein
- DNA polymerase epsilon subunit 2
- Large ribosomal subunit protein eL18
- ATP synthase subunit alpha
- Cytochrome c
- Cytochrome c1, heme protein, mitochondrial
- Developmentally-regulated GTP-binding protein 2 homolog
Sequence:
MSNQKKNDVSSFVKDSLIGGTAGGVSKTIVAPIERVKLLLQVQSASTQIAADKQYKGIVDCFVRVSKEQGVISLWRGNLANVIRYFPTQALNFAFKDKYKKFFVRHTAKENPTKFFIGNLLSGGAAGATSLLFVYPLDFARTRLAADVGTGSARQFTGLGNCISSIYKRDGLIGLYRGFGVSVGGIFVYRAAFFGGYDTAKGILLGENNKKASFWASWGIAQVVTTIAGVVSYPFDTVRRRMMMQAGRADILYSSTWDCWVKIATREGPTAFFKGALSNAIRGSGGALVLVIYDEIQKLMGFEGGVGSE
Protein: Ahnak protein (Q8R2L7)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEKEEETTRELLLPNWQGSGSHGLTIAQRDDGVFVQEVMQNSPAARTGVVKEGDQIVGATIYFDNLQSGEVTQLLNTMGHHTVGLKLHRKGDRSPEPGQTWTHEVFSSRSSEVVLNTVQPSSLDCNDQNKPKEAINKAGAASDSTPDAGIGDNLHDGPEIKADSIRNEKVTSP
Protein: Probable membrane protein KdpF (Q79FT7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Potassium-transporting ATPase ATP-binding subunit
- Potassium-transporting ATPase potassium-binding subunit
- Potassium-transporting ATPase KdpC subunit
- Sensor protein KdpD
- Uncharacterized membrane protein ArfB
Sequence:
MTTVDNIVGLVIAVALMAFLFAALLFPEKF
Protein: YjeF N-terminal domain-containing 3 (ApoA-I-binding protein 2) (Q1LVI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis. Orchestrates hematopoietic stem and progenitor cell emergence from the hemogenic endothelium, a type of specialized endothelium manifesting hematopoietic potential. YJEFN3-mediated cholesterol efflux activates endothelial SREBF2, the master transcription factor for cholesterol biosynthesis, which in turn transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence.
Interaction partners:
- ATP-dependent
- m7GpppN-mRNA hydrolase
- RNA helicase
- RNA helicase
- Decapping mRNA 1B.
- Decapping mRNA 1A.
Sequence:
MNHSSNEKEPETIEPLRYLSKTEVATVETELLRDYRFGQQQLIEIWGHACAIAITKAFPLSSLSKKQPTLLVVCGPEQNGSIGLVCARHLRMFEYEPTIFYPKRSTLGLHQDFTVQCEKMDIPFLSYLPTEVQLLNDAYNLVIDAILGPETDHKDVKEPYAGMLVTLKQVKIPIVSVDVPSGWDADEPAKDGINPEVLISLTAPKKCATGFSGKHFLAGRFLPYDIQKKYELNLPEFPGTECIIEL
Protein: Splicing factor 1 (CW17) (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (mZFM) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162) (Q64213)
Organism: Mus musculus (Mouse)
Function: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 1
- Splicing factor 3A subunit 3
- Probable ATP-dependent RNA helicase DDX46
- RNA-binding protein 25
- Splicing factor U2AF 35 kDa subunit
- Pre-mRNA-processing factor 40 homolog A
- Serine/arginine repetitive matrix protein 2
- RNA-binding protein 39
Sequence:
MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHTLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPASNPPPPSLMSTTQSRPPWMNSGPSENRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGTPQMQGNPTMVPLPPGVQPPLPPGAPPPPPCSIECLLCLLSSPNSLCLSPNRAARIPPRGSDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B4DR80)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAHSPVQSGLPGMQNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDSSSEDSDAETDGQASGGSDSGDWIFTIREKDPKNLENGALQPSDLDRNKMKDIPKRPFSQCLSTIISPLFAELKEKSQACGGNLGSIEELRGAIYLAEEACPGISDTMVAQLVQRLQRYSLSGGGTSSH
Protein: Large ribosomal subunit protein uL11m (39S ribosomal protein L11, mitochondrial) (L11mt) (MRP-L11) (Q9VFJ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9Y3B7}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Ribosomal protein
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL13m
- Small ribosomal subunit protein bS16m
Sequence:
MSKAAGKLKSLKKTVERVTHTSKLKTNIPAGMAAAGPPLGPMLGQRAINIAAFCKDFNAKTAEMKEGVPLPCRISVNSDRSYDLAIHHPPATFFLKQAAGIQRGTMTPGKEVAGMITLKHLYEIAAIKIQDPPNVLLTMQQMCEMLISIARTCGIKVVREIDPAAYGEFLEERKLIVEQQRRELQEKREAKMLRTG
Protein: 17.7 kDa class II heat shock protein (17.7 kDa heat shock protein) (AtHsp17.7) (O81822)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Chaperone protein ClpB1
- 23.6 kDa heat shock protein, mitochondrial
- 26.5 kDa heat shock protein, mitochondrial
- 23.5 kDa heat shock protein, mitochondrial
- Heat shock protein 90-1
- Heat shock 70 kDa protein 5
- Heat shock 70 kDa protein 4
- 18.5 kDa class IV heat shock protein
- Heat stress transcription factor A-2
- Protein HEAT-STRESS-ASSOCIATED 32
Sequence:
MDLEFGRFPIFSILEDMLEAPEEQTEKTRNNPSRAYMRDAKAMAATPADVIEHPDAYVFAVDMPGIKGDEIQVQIENENVLVVSGKRQRDNKENEGVKFVRMERRMGKFMRKFQLPDNADLEKISAACNDGVLKVTIPKLPPPEPKKPKTIQVQVA
Protein: Protein FAM98B (Q52LJ0)
Organism: Homo sapiens (Human)
Function: Positively stimulates PRMT1-induced protein arginine dimethylated arginine methylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:24608264}. Cytoplasm {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:24608264}.
Interaction partners:
- ATP-dependent RNA helicase DDX1
- RNA transcription, translation and transport factor protein
- RNA-splicing ligase RtcB homolog
- Ashwin
- Protein archease
Sequence:
MRGPEPGPQPTMEGDVLDTLEALGYKGPLLEEQALTKAAEGGLSSPEFSELCIWLGSQIKSLCNLEESITSAGRDDLESFQLEISGFLKEMACPYSVLISGDIKDRLKKKEDCLKLLLFLSTELQASQILQNKKHKNSQLDKNSEVYQEVQAMFDTLGIPKSTTSDIPHMLNQVESKVKDILSKVQKNHVGKPLLKMDLNSEQAEQLERINDALSCEYECRRRMLMKRLDVTVQSFGWSDRAKVKTDDIARIYQPKRYALSPKTTITMAHLLAAREDLSKIIRTSSGTSREKTACAINKVLMGRVPDRGGRPNEIEPPPPEMPPWQKRQEGGGGRGGWGGGGGGGGRGGGGGGGGRGGWGGGGGGWGGGGGGGGGWGGGGGGGRGGFQGRGDYGGRGGYGGRGGYGGRGYGDPYGGGGGGGGGGGGGGGYRRY
Protein: HAUS augmin-like complex subunit 4 (Q9H6D7)
Organism: Homo sapiens (Human)
Function: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
Interaction partners:
- HAUS augmin-like complex subunit 6
- HAUS augmin-like complex subunit 5
- HAUS augmin-like complex subunit 1
- HAUS augmin-like complex subunit 3
- HAUS augmin-like complex subunit 2
- HAUS augmin-like complex subunit 8
- HAUS augmin-like complex subunit 7
- Tubulin gamma-1 chain
- Pericentriolar material 1 protein
Sequence:
MASGDFCSPGEGMEILQQVCSKQLPPCNLSKEDLLQNPYFSKLLLNLSQHVDESGLSLTLAKEQAQAWKEVRLHKTTWLRSEILHRVIQELLVDYYVKIQDTNVTSEDKKFHETLEQRLLVTELMRLLGPSQEREIPPLLGLEKADLLELMPLSEDFVWMRARLQQEVEEQLKKKCFTLLCYYDPNSDADSETVKAAKVWKLAEVLVGEQQQCQDAKSQQKEQMLLLEKKSAAYSQVLLRCLTLLQRLLQEHRLKTQSELDRINAQYLEVKCGAMILKLRMEELKILSDTYTVEKVEVHRLIRDRLEGAIHLQEQDMENSRQVLNSYEVLGEEFDRLVKEYTVLKQATENKRWALQEFSKVYR
Protein: Glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH 2) (EC 1.2.1.12) (Triose-phosphate dehydrogenase 1) (P00358)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00360}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase 3
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Uncharacterized protein YML053C
- Glucose-6-phosphate isomerase
- Phosphoglycerate mutase 1
- Actin
- Enolase 1
Sequence:
MVRVAINGFGRIGRLVMRIALQRKNVEVVALNDPFISNDYSAYMFKYDSTHGRYAGEVSHDDKHIIVDGHKIATFQERDPANLPWASLNIDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSNSSIFDAAAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA
Protein: Kinesin-like protein KIF21A (Kinesin-like protein KIF2) (Renal carcinoma antigen NY-REN-62) (Q7Z4S6)
Organism: Homo sapiens (Human)
Function: Microtubule-binding motor protein probably involved in neuronal axonal transport. In vitro, has a plus-end directed motor activity.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXL2}. Cytoplasm, cell cortex {ECO:0000269|PubMed:24120883, ECO:0000269|PubMed:27410476}. Cell projection, axon {ECO:0000269|PubMed:24120883}. Cell projection, dendrite {ECO:0000269|PubMed:24120883}. Cell projection, growth cone {ECO:0000269|PubMed:24120883}.
Interaction partners:
- KN motif and ankyrin repeat domain-containing protein 1
- KN motif and ankyrin repeat domain-containing protein 2
- Paired mesoderm homeobox protein 2A
- Tubulin beta-3 chain
- Kinesin-like protein KIF22
- Kinesin-like protein KIF11
- Kinesin-like protein KIF23
- Kinesin-associated protein 3
- Kinesin-like protein KIF20B
- Kinesin light chain 1
Sequence:
MLGAPDESSVRVAVRIRPQLAKEKIEGCHICTSVTPGEPQVFLGKDKAFTFDYVFDIDSQQEQIYIQCIEKLIEGCFEGYNATVFAYGQTGAGKTYTMGTGFDVNIVEEELGIISRAVKHLFKSIEEKKHIAIKNGLPAPDFKVNAQFLELYNEEVLDLFDTTRDIDAKSKKSNIRIHEDSTGGIYTVGVTTRTVNTESEMMQCLKLGALSRTTASTQMNVQSSRSHAIFTIHVCQTRVCPQIDADNATDNKIISESAQMNEFETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDKSKRATHVPYRDSKLTRLLQDSLGGNSQTIMIACVSPSDRDFMETLNTLKYANRARNIKNKVMVNQDRASQQINALRSEITRLQMELMEYKTGKRIIDEEGVESINDMFHENAMLQTENNNLRVRIKAMQETVDALRSRITQLVSDQANHVLARAGEGNEEISNMIHSYIKEIEDLRAKLLESEAVNENLRKNLTRATARAPYFSGSSTFSPTILSSDKETIEIIDLAKKDLEKLKRKEKRKKKRLQKLEESNREERSVAGKEDNTDTDQEKKEEKGVSERENNELEVEESQEVSDHEDEEEEEEEEEDDIDGGESSDESDSESDEKANYQADLANITCEIAIKQKLIDELENSQKRLQTLKKQYEEKLMMLQHKIRDTQLERDQVLQNLGSVESYSEEKAKKVRSEYEKKLQAMNKELQRLQAAQKEHARLLKNQSQYEKQLKKLQQDVMEMKKTKVRLMKQMKEEQEKARLTESRRNREIAQLKKDQRKRDHQLRLLEAQKRNQEVVLRRKTEEVTALRRQVRPMSDKVAGKVTRKLSSSDAPAQDTGSSAAAVETDASRTGAQQKMRIPVARVQALPTPATNGNRKKYQRKGLTGRVFISKTARMKWQLLERRVTDIIMQKMTISNMEADMNRLLKQREELTKRREKLSKRREKIVKENGEGDKNVANINEEMESLTANIDYINDSISDCQANIMQMEEAKEEGETLDVTAVINACTLTEARYLLDHFLSMGINKGLQAAQKEAQIKVLEGRLKQTEITSATQNQLLFHMLKEKAELNPELDALLGHALQDLDSVPLENVEDSTDEDAPLNSPGSEGSTLSSDLMKLCGEVKPKNKARRRTTTQMELLYADSSELASDTSTGDASLPGPLTPVAEGQEIGMNTETSGTSAREKELSPPPGLPSKIGSISRQSSLSEKKIPEPSPVTRRKAYEKAEKSKAKEQKHSDSGTSEASLSPPSSPPSRPRNELNVFNRLTVSQGNTSVQQDKSDESDSSLSEVHRSSRRGIINPFPASKGIRAFPLQCIHIAEGHTKAVLCVDSTDDLLFTGSKDRTCKVWNLVTGQEIMSLGGHPNNVVSVKYCNYTSLVFTVSTSYIKVWDIRDSAKCIRTLTSSGQVTLGDACSASTSRTVAIPSGENQINQIALNPTGTFLYAASGNAVRMWDLKRFQSTGKLTGHLGPVMCLTVDQISSGQDLIITGSKDHYIKMFDVTEGALGTVSPTHNFEPPHYDGIEALTIQGDNLFSGSRDNGIKKWDLTQKDLLQQVPNAHKDWVCALGVVPDHPVLLSGCRGGILKVWNMDTFMPVGEMKGHDSPINAICVNSTHIFTAADDRTVRIWKARNLQDGQISDTGDLGEDIASN