wanglab/gogpt-training-data huggingface dataset:
Protein: Crimpy, isoform B (GEO12523p1) (RE39205p) (Q9VPC5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGGSARGVGRRGVVLEQDVRTRSSQGERKRGLAGKQQHNNAKLPLRMRSNGSYFGRLNVSALLIYLWCYLLLVMAASGGSNHVVNGLKCYCNPKECDVIRSPDCPGKGLMLWDPCK
Protein: Transcription initiation factor TFIID subunit 10 (TBP-associated transcription factor family member taf-10) (Q95ZS0)
Organism: Caenorhabditis elegans
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-10 (By similarity). Essential for early embryonic development, but not required for transcription of some genes; probably acts via activating transcription initiation by RNA Pol II, as part of the TFIID complex.
Subcellular location: Nucleus {ECO:0000255|PIRNR:PIRNR017246, ECO:0000269|PubMed:11566890}.
Interaction partners:
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 1
- PHD-type domain-containing protein
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 8
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 13
Sequence:
MNDPEQYEPSSSTESVLMPPPALPQYFQRPAAAPQVYSTLEPSVQNLRSSLHKPLTGNQQQFVQKTLENVQKNPSQDDTHEFINQLADYPPTIPDSVTLHFLKSAGVDGSDPRVTRMISLAAQKHVSDIILDAMTSARMKGLGQTKKGTKDTKYTLTEELLDEILKEYGHQNTRPPYHT
Protein: Cell adhesion molecule 3 (Zgc:136589) (B0CLV6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSGMRARQTLAFPSFQRAALRALAAFTMILATSVRSNYVYDDDPFQPVTQDETVAVGGVVTLTCGVKENDNSSLQWSNTAQQTLYFGEKRALRDNRIQLVKSTATELIITIGDVQLSDDGEYTCSIFTMPVRTARATVTVLGVPGKPVITGFEGAVQEGGKVTLTCTSSGSKPPAKLHWYRDHVEIQGRPDVVESNPNEPTYTVTSELTLSVSRDDNDALIACAVDHPSIANGDKRTEQPLNVLFSPRVSIHPESDLPREGEKFYLQCVGNGNPEPNAFVWRRKEGELPPLAKVDGAFLRFESLNKSDNGVYECQADNGIGMGDVAHTLLVQEAGENAADPTAMSTGSGVDHAVIGGVVAVIVFIMLCLLLVLGRYLIRHKGTYLTHEAKGSDDAPDADTAIINAEGGHSGVDDKKEYFI
Protein: Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (UBA domain-containing protein 2) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) (Q11119)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 15
- Polyubiquitin
- Probable ubiquitin carboxyl-terminal hydrolase 2
- Ubiquitin carboxyl-terminal hydrolase 5
- Probable ubiquitin carboxyl-terminal hydrolase 7
- Ubiquitin carboxyl-terminal hydrolase 6
- Probable ubiquitin carboxyl-terminal hydrolase 9
- Putative ubiquitin thioesterase otu1
- Ubiquitin thioesterase otu2
- Probable mRNA-splicing protein ubp10
Sequence:
MSCPHLTETNVVIPDNSQVIYREECVRCFNSQDEEGGIDLCLTCFQSGCGETGLKHSLVHFEQTLHPIVVTIARQPKQKINDEPPQKITKLEIREDSDEDLYDYFYVPKCLVCNIILDIQDPLLSLSLEAMKNATKASNKSQLTAWENELTTCDHIINLPENETYVTNLDNATCSKCDLAENLWMCLTCGALSCGRKQYGGGGGNGHALSHYDDTGHPLAVKLKSISPDGQADIYCYSCDEERIDPNIKTHMLNFGIDIAKLNKTEKSLAELQLEQNLNWDFGASEEDDASKRLFGPGLTGLKNLGNSCYLASTMQSLFSIKEFAIHELNLFNTYNSVCQTPTTDLQCQLGKLADGLVSGKFSKPSKIGLLNNPSSSILPYQDGLRPFMFKDVVGQGHSEFGTSQQQDAYEFLLYLLGKIRKSSIAKTDITKIFDFETEQKLSCLSCKRVRYSSFSSQGLTLTVPRVKIGEIEGEQIYEEVSIDQCLDATIQPDQMEYTCEACKSKLGATTTTAMKSFPKVLILQANRFDLQGYQVKKLSIPIIVNEDGIYNFDRLMAKDHPNDEDYLPEKTETIEWNQSAIEQLQAMGFPLVRCQRALLATGNSDTETAMNWLFEHMEDPEIDKPIEVSELLPKADSSVSEENVQSLCEFGFTVAQARKGLLESNNNIERAVDWILNHPDESFEEPPLEGSDSSIKNENMGSWESTNVPVNYNLKAIISHKGSSAHAGHYVAFIRKEIDGKQQWVLFNDEKVLQVASLEEAKTTGYVYLFERLD
Protein: Glycine hydroxymethyltransferase (Serine methylase) (G3V4X0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
Protein: Without children, isoform E (A0A0B4KHZ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEEISSLDSFGADSNARPESATPRSEEQQDQDRQQTAPAASETLDTPASPPAEDAAAQESKPPPSKEADDDFEQISEGSLDADDNQSRDKAASTPADPVDAEEPAEEPTPNEEPQGGEDEQPQTEAVRVDPQEEPEEAEEETDALQATAEEVEAAAAEADAVDGGPASPEAMDVDEGEVDAEGEAEQEAEDDAALDREATDDVDMQSVGADSHQAEDAEPPEGRDEVDTSLEEQENGQDPDEREKDAAADEDDPDAEGDAESEQVDENAEETGEAEHGDDTVENVLEPEESDVCLIPDDQETEVTEAEKELARENAEKAAEEEEAEERQAKTPDNDRKSPADAAADPEDDSAAAVDATDVSPTTPTDAQAGAKSAATGIAEDGVAAAANEEEAGGDVPDPDEPTAEESSSAGAGEPGSTPKIIISWIVGSVQKCKQCGDEKNCGFRYRSPEESEEMDKEKENDKAEENAEEGEEEEARQKPAAPSGFEYICDTACVDALLEDQPGKYFVRRKKFLVEEVVREEGAAEAEASADGEGGDAEEEATPANTQDCLQCKDKTRCKYFIKQDQDCFYICNDDCFNLLNAEEPDKFKLKRHSIRVRNIGATTLQPPQNSPTKRTDGSVVARTVEEAETARLDRIESFRRRCADCEADINTDEKQLMWETMDFCNEVCLGSYQRTIGSTCETCKQEVSSIALGKYCVRFGFDVRQFCCAGCLNTFKKGLKTCSCCQKDISGGQEGFLAPVGDKDQFKDFCSQSCLRRYESMCNPRRKLRTDVCGVCNNQKPVRVEMLLEDREHYFCSNPCFSAFKFVSNVNADPCAMCSKYFERRSAESYTIYNEQQSPKVFCSRVCINVYIIVNRHIVSCQWCKVKKYNFDMIYQIGGPHDQETLTCSINCLTMHGVSCNISARAVTKCDNCSNFNTPQYHLTMSDASMRNFCTYQCVMQFQNQFARAPLTLDSDLPPSSAGSSKSQQQSNRGNKNAAPFPTGLPKRVKLKLSHTGKGGVGGKKSGSGTMLPVISTVQSLASGETEARIGNLTVRRKRGRPRESGTSSPPLSMPGVHPPAQRGRPRKHAVDYSARSPSPTMSGGSSHMGIPVRRNTTTTMDFGPATVTETKIITVPPYPKAVRNVNISCKPLTVTQGEQCSPDVRDCATQTEKDYSNKVLIPVPVPIFVPQPMYMYSAPFPVPVPIPLPIPVPIFIPTTRNTAQGILKEIKKIQDKMPEDPLEAELLMMAEMVAEEKHESDSDSDNEIKPDPGLVALQYQNSLESVAQQQQQQQVVDVSGAGHNPYGDDMLQIALKMATGDYDNHHQTSTVDLETSMTANTISSQSPMGHDGMGQMGVHHLDQQHHMLDATQRTARGRKRGVGVVMDPPNRNSRSPVKRQRGGEMDHSALQQQSQQAQQPQEKPDAQMFLKYTFGVNAWKQWVMTKNADIEKSSMRRRPFKTELLQMTADELNYSLCLFVKEVRKPNGTEYAPDTIYYLVLGIQQYLYVNGRIDNIFYDPYYERFTECLDEVARKFSVLYNDSQYIVTRVEEEHLWECKQLGAHSPHVLLSTLMFFNTKHFNLTTVEEHMQLSFSHIMKHWKRSSQNSKVPGSRNVLLRFYPPQAGLDANPRKKKVYEQQENEENPLRCPVRLYEFYLSKCPESVKTRNDVFYLQPERSCVPDSPVWYSTQALGQDALQRMLHRVKMVKEINIALLTT
Protein: Endonuclease 1 (AtENDO1) (EC 3.1.30.1) (Bifunctional nuclease I) (AtBFN1) (Deoxyribonuclease ENDO1) (Single-stranded-nucleate endonuclease ENDO1) (Q9SXA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Endonuclease that can use RNA, single-stranded and double-stranded DNA as substrates. Hydrolyzes single-stranded DNA and RNA without apparent specificity for bases during senescence. Endonuclease that recognizes and cleaves all types of mismatches with high efficiency, including heteroduplex double-stranded DNA. Maybe involved in programmed cell death (PCD) and senescence.
Interaction partners:
- Bifunctional nuclease 1
- Metacaspase-9
- Ribonuclease 3
- Expansin-B1
- Expansin-B3
- NAC domain-containing protein 92
- Endoglucanase 8
- Expressed protein
- Endoglucanase 21
Sequence:
MASAFRSSTRLILVLGILILCSVSSVRSWSKEGHILTCRIAQNLLEAGPAHVVENLLPDYVKGDLSALCVWPDQIRHWYKYRWTSHLHYIDTPDQACSYEYSRDCHDQHGLKDMCVDGAIQNFTSQLQHYGEGTSDRRYNMTEALLFLSHFMGDIHQPMHVGFTSDEGGNTIDLRWYKHKSNLHHVWDREIILTALKENYDKNLDLLQEDLEKNITNGLWHDDLSSWTECNDLIACPHKYASESIKLACKWGYKGVKSGETLSEEYFNTRLPIVMKRIVQGGVRLAMILNRVFSDDHAIAGVAAT
Protein: 12S seed storage protein CRD (Cruciferin D) (Legumin-type globulin storage protein CRD) [Cleaved into: 12S seed storage protein CRD alpha chain (12S seed storage protein CRD acidic chain); 12S seed storage protein CRD beta chain (12S seed storage protein CRD basic chain)] (Q9ZWA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Seed storage protein.
Subcellular location: Protein storage vacuole {ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At2g45350, chloroplastic
- 2S seed storage protein 5
- 2S seed storage protein 2
- DNA repair protein XRCC3 homolog
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 8
- DNA repair protein RAD51 homolog 3
- Meiotic recombination protein DMC1 homolog
- Protein DETOXIFICATION 37
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A
Sequence:
MHKLLFSLLSVVSLSFLLFFHGAEARQREAPFPNACHFSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVARITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFAEVEGSSGRGGGGDPGRRFEDMHQKLENFRRGDVFASLAGVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAGSRTQEEEQPLTWPSGNNAFSGFDPNIIAEAFKINIETAKQLQNQKDNRGNIIRANGPLHFVIPPPREWQQDGIANGIEETYCTAKIHENIDDPERSDHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQGQIIVIPQGFAVSKTAGETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAKRIKFSQQETMLSMTPSSSS
Protein: T-cell acute lymphocytic leukemia 2 (T-cell acute lymphocytic leukemia protein 2) (F1QUD8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Rhombotin-2
- Rhombotin-1
Sequence:
MTRKVFTNTRERWRQHNVNTAFAELRKLIPTHPPEKKLSKNEILRLAMRYINFLVTLLESQGGEPSAHSQAALLTLLTGNMQNLRTDRTWTSDTDPPSPGSSCDSSEAW
Protein: T-box transcription factor T (Brachyury protein) (Protein T) (P79777)
Organism: Gallus gallus (Chicken)
Function: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic site (called T site) and activates gene transcription when bound to such a site.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15178}.
Interaction partners:
Sequence:
MGSPEDAGKAPAYRVDHLLSAVESELQAGSEKGDPTERELRVALEDGELWLRFKELTNEMIVTKNGRRMFPVLKVSVSGLDPNAMYSFLLDFVAADGHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHSFPETQFTAVTAYQNEEITALKIKYNPFAKAFLDAKERNDHKDMMEEAGDNQQSGYSQLGSWLIPGAGALCPPANPHSQFGAPLSLSPAHSCERYSPLRNHRSAPYPNPYTHRNNSPTAYTDNSSACLPMLQSHDNWSSLGVPTHTTMLPMSHSTGTATSSSQYPNLWSVSNSTITPAPQSSGMSNGLSSQFLRGSPVHYTALPHPVTATTSTSPLYDGGAPADLPDSQYDASAHTRLASMWTPITPPSM
Protein: Mitofissin (Autophagy-related protein 44) (Mitochondrial fission factor atg44) (Q10167)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:37192628}.
Interaction partners:
Sequence:
MPFLSRLFHYGVDLALVSTCVAGIRRSSGISFEVEKIHNEDVKTAVEKYLNFGEWAFDQSSAFLGSSTWFKKV
Protein: Poly A polymerase head domain-containing protein (Q54BQ2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Strictosidine synthase family protein
Sequence:
MYTRPISKIEKSQDGYDRLYFHKQTNNEKEKLSPMQTSTPTSLKKDQPHENIKVSIYYSNERESESVDIRLTECEIQLFKELMHVIRDSGCGTTLRVAGGWVRDKLRGDDSNDIDITLDNMMGEAFAELVNKHLSSKHHQTHRIGVIQSNPEQSKHLETATVKVFDMWIDFVNLRSESYTDTSRIPVISIGTPLQDALRRDLTINSLFFNINENRIEDFTGQGINDLRDGIIRTPLPSLTTFLDDPLRVFRSIRFASRLNFKIDEELFKAGSDPVVKDAIKSKISHERIAKEFDGMLSAEEPYLSIELINKFGLFDCLFSLPTVGLDETYIEQLKNSNKDSEKYCEIADSWIGMGKQYEEIDTKRQLILSALMIPFYGIKFKNANKKNKEMSIIHYMFIEYIKFSNKDYDDVSLILECSEQLMEHIIKFVSAGIFNRKEIGLIIHKSAQLWIVVIIISFIKIQYRPNKLQTLFSRYDKPENEKYTIFHKFVGEIKEHDLIGIWNIKRLLNGKQVQDLLNRKPGTWLAPVIQLILEWQLENPSKTEQDCKDWLLTLDIK
Protein: Cystatin-SA (Cystatin-2) (Cystatin-S5) (P09228)
Organism: Homo sapiens (Human)
Function: Thiol protease inhibitor.
Subcellular location: Secreted {ECO:0000269|PubMed:20189825}.
Interaction partners:
- Cystatin-SN
- Serine/threonine-protein phosphatase CPPED1
- Cystatin-S
- Cystatin-B
Sequence:
MAWPLCTLLLLLATQAVALAWSPQEEDRIIEGGIYDADLNDERVQRALHFVISEYNKATEDEYYRRLLRVLRAREQIVGGVNYFFDIEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFQIYEVPWEDRMSLVNSRCQEA
Protein: Ionotropic receptor 100a (Q9V9T2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ionotropic receptor 11a
- IP13856p
Sequence:
MATTLQLIMLALVGGTLGQANNTDHKQVLTSIVKQLEGGLELHLRTSEDGGNDLVQFLMQEKSSIIISAKQEEVPSRAKIMRHHFFIFDGVHQMQEIRTSLFNTDGFYILALENNTIEDDVLLMEFAADVWLQHGHSRIYYVQLSKKSVLLFNPFLQRLVVVQDSKTYSRIYKDLEGYHLRIYIFDSVYSSVIGDGENKVLSVTGADAKLAKTVARQLNFTADFVWPDDEFFGGRLANGEYSGGVGRAHRGEVDIIFAGFFIKDYLTTHIQFSAAVYMDELCLYVKKAQRIPQSILPLFAVHMDVWLCFLLVGLLGALVWLILRAVNLILGIEGVPDGSRATRISYFGAARRIFVDTWVIWVRVNVGRFPPFHSERIFVASLCLVSVIFGALLESSLATVYIRPLYYRDVNTLRELDESGQPIYIKHPAFKDDLFYGHNSEVYRRLDAKMMLVAEGEERLIEMVSKRGGFAGVTRSASLQLSDIRYVMTKKVHKIPECPKNYHIAYVLPRPSPYLEEVNRIVLRLVAGGIVGLWTGEAKERAKWSIQRFPEYLAELDVGRWKVLTLSDVQLAFYALTIGCLLSAIVCMAEILLGRQRRLHSPK
Protein: C-X-C motif chemokine 6 (Granulocyte chemotactic protein 2) (GCP-2) (Small-inducible cytokine B6) (P80221)
Organism: Bos taurus (Bovine)
Function: Chemotactic for neutrophil granulocytes. Signals through binding and activation of its receptors (CXCR1 and CXCR2). In addition to its chemotactic and angiogenic properties, it has strong antibacterial activity against Gram-positive and Gram-negative bacteria (90-fold-higher when compared to CXCL5 and CXCL7) (By similarity).
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 2
- C-X-C motif chemokine 14
- Growth-regulated protein homolog gamma
- Interleukin-8
- C-X-C chemokine receptor type 4
- C-C motif chemokine 2
- C-X-C motif chemokine 11
- C-C motif chemokine 5
- Stromal cell-derived factor 1
Sequence:
MRLLSSRAARVSGPSGSLCALLALLLLTPPGPLASAGPVAAVVRELRCVCLTTTPGIHPKTVSDLQVIAAGPQCSKVEVIATLKNGREVCLDPEAPLIKKIVQKILDSGKNN
Protein: tRNA-splicing endonuclease subunit Sen54 (SEN54 homolog) (HsSEN54) (tRNA-intron endonuclease Sen54) (Q7Z6J9)
Organism: Homo sapiens (Human)
Function: Non-catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events.
Subcellular location: Nucleus {ECO:0000305}. Nucleus, nucleolus {ECO:0000305}. Note=May be transiently localized in the nucleolus. {ECO:0000305}.
Interaction partners:
- tRNA-splicing endonuclease subunit Sen2
- tRNA-splicing endonuclease subunit Sen15
- tRNA-splicing endonuclease subunit Sen34
- Polyribonucleotide 5'-hydroxyl-kinase Clp1
- Probable arginine--tRNA ligase, mitochondrial
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage stimulation factor subunit 2
- Serine/threonine-protein kinase VRK1
- Target of EGR1 protein 1
Sequence:
MEPEPEPAAVEVPAGRVLSARELFAARSRSQKLPQRSHGPKDFLPDGSAAQAERLRRCREELWQLLAEQRVERLGSLVAAEWRPEEGFVELKSPAGKFWQTMGFSEQGRQRLHPEEALYLLECGSIHLFHQDLPLSIQEAYQLLLTDHTVTFLQYQVFSHLKRLGYVVRRFQPSSVLSPYERQLNLDASVQHLEDGDGKRKRSSSSPRSINKKAKALDNSLQPKSLAASSPPPCSQPSQCPEEKPQESSPMKGPGGPFQLLGSLGPSPGPAREGVGCSWESGRAENGVTGAGKRRWNFEQISFPNMASDSRHTLLRAPAPELLPANVAGRETDAESWCQKLNQRKEKLSRREREHHAEAAQFQEDVNADPEVQRCSSWREYKELLQRRQVQRSQRRAPHLWGQPVTPLLSPGQASSPAVVLQHISVLQTTHLPDGGARLLEKSGGLEIIFDVYQADAVATFRKNNPGKPYARMCISGFDEPVPDLCSLKRLSYQSGDVPLIFALVDHGDISFYSFRDFTLPQDVGH
Protein: E3 ubiquitin-protein ligase TRIM33 (EC 2.3.2.27) (Ectodermin homolog) (RET-fused gene 7 protein) (Protein Rfg7) (RING-type E3 ubiquitin transferase TRIM33) (Transcription intermediary factor 1-gamma) (TIF1-gamma) (Tripartite motif-containing protein 33) (Q9UPN9)
Organism: Homo sapiens (Human)
Function: Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).
Subcellular location: Nucleus {ECO:0000269|PubMed:15820681, ECO:0000269|PubMed:16751102, ECO:0000269|PubMed:19135894, ECO:0000269|PubMed:25593309}. Note=In discrete nuclear dots resembling nuclear bodies (By similarity). Localizes to sites of DNA damage (PubMed:25593309). {ECO:0000250|UniProtKB:Q99PP7, ECO:0000269|PubMed:25593309}.
Interaction partners:
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Cell division cycle protein 20 homolog
- Cell division cycle protein 16 homolog
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Cell division cycle protein 23 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 27 homolog
- Cyclin-A2
Sequence:
MAENKGGGEAESGGGGSGSAPVTAGAAGPAAQEAEPPLTAVLVEEEEEEGGRAGAEGGAAGPDDGGVAAASSGSAQAASSPAASVGTGVAGGAVSTPAPAPASAPAPGPSAGPPPGPPASLLDTCAVCQQSLQSRREAEPKLLPCLHSFCLRCLPEPERQLSVPIPGGSNGDIQQVGVIRCPVCRQECRQIDLVDNYFVKDTSEAPSSSDEKSEQVCTSCEDNASAVGFCVECGEWLCKTCIEAHQRVKFTKDHLIRKKEDVSESVGASGQRPVFCPVHKQEQLKLFCETCDRLTCRDCQLLEHKEHRYQFLEEAFQNQKGAIENLLAKLLEKKNYVHFAATQVQNRIKEVNETNKRVEQEIKVAIFTLINEINKKGKSLLQQLENVTKERQMKLLQQQNDITGLSRQVKHVMNFTNWAIASGSSTALLYSKRLITFQLRHILKARCDPVPAANGAIRFHCDPTFWAKNVVNLGNLVIESKPAPGYTPNVVVGQVPPGTNHISKTPGQINLAQLRLQHMQQQVYAQKHQQLQQMRMQQPPAPVPTTTTTTQQHPRQAAPQMLQQQPPRLISVQTMQRGNMNCGAFQAHQMRLAQNAARIPGIPRHSGPQYSMMQPHLQRQHSNPGHAGPFPVVSVHNTTINPTSPTTATMANANRGPTSPSVTAIELIPSVTNPENLPSLPDIPPIQLEDAGSSSLDNLLSRYISGSHLPPQPTSTMNPSPGPSALSPGSSGLSNSHTPVRPPSTSSTGSRGSCGSSGRTAEKTSLSFKSDQVKVKQEPGTEDEICSFSGGVKQEKTEDGRRSACMLSSPESSLTPPLSTNLHLESELDALASLENHVKIEPADMNESCKQSGLSSLVNGKSPIRSLMHRSARIGGDGNNKDDDPNEDWCAVCQNGGDLLCCEKCPKVFHLTCHVPTLLSFPSGDWICTFCRDIGKPEVEYDCDNLQHSKKGKTAQGLSPVDQRKCERLLLYLYCHELSIEFQEPVPASIPNYYKIIKKPMDLSTVKKKLQKKHSQHYQIPDDFVADVRLIFKNCERFNEMMKVVQVYADTQEINLKADSEVAQAGKAVALYFEDKLTEIYSDRTFAPLPEFEQEEDDGEVTEDSDEDFIQPRRKRLKSDERPVHIK
Protein: LexA repressor (EC 3.4.21.88) (P61611)
Organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
Sequence:
MKDLTDKQQAVLAFITAIIKERGFPPTIREIGDEFGITAKGAYDHLKAIEKKGYLKTAKNQSRAIELIRQSPMESLPVQATSIPVIGQVAAGLPIFAEENIESYIPVPDEMAKGNVPMYALRVQGDSMIEVGINDGDIAIIEKRDIARNGEIVVALIEDEATLKVYYKEQDQIRLEARNPKYKPIKTKKATVMGKLIGLYRIY
Protein: Corneodesmosin (A0A8I5ZKH8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGSSRAPRMGRVGGHGLMALLMAGFILPGTLAKSIGPFSDPCKDPTRITSPNDPCLIGKTGSNSISSHGGTSSISSQGGSSSISSHGGTSSISSQGGSSSSQGSSSGSLIFKPGTGYSQSSYSFGSGGSQTGSSGSQTGSSGSQTGSSGYQSGNSGYQSGSSGSQSGRWVSSSSQWVSSSSQSGSSGSSREGPGNGSALPTDDNSSRLTSGTVQSGGSYTSKSSSSNQRPCSSNVPDSPCSGGPVITHSGPYISGSHTVSGGQRPVVVVVEQHGSGGPGGFQGMPCSNGGPSGKPCPPITSVQKPYGGYEVVGGSADSYLVPGMTYSGGKIYPVGYFTKDNPIRGSPGSPSFAAGPPISEGKYFSSNPIIPSRSSNAYPSGIVFQPVGSGGVQPCGTGSIGSKGPCSGTRIQITSSGSSTSYHPCSGGASQGPCSSPGTNSISGGSSSVSTGKIVLQPCGSKSSSSGYPCLSVPSSTLNGGLNGSPQPVPSVVLKPCGPNSPGRVPCRSIRDILTQVKPLGPQLMDPQVFLPQGEPLDKS
Protein: Uncharacterized protein (Q38CI1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSRNPPDSVCVTPTRHIVTDALAESTVTMYFSVFPCNCEPIFCSNRIPLLREAPPYCDGNVVYIGPAREVAQQKLQQLAFPRGFGCKNMEVRSGPSYSARFEQVRKRGVLRYHRIKIASTFVALVVSENGELRTIQAKHTAVAVVITCPPNTPHYDTLLQNFDSVLRYALHVSLDFAMWATQRFFLKLSRTAAFKELVAELEQHDRALETYSVVGAILANALTYTSPIPRLYSGASVTVASSASERLQSSSHDPAVSPVRNSGVFSSNPNVLVYEALRKLRGINERFTSRVVAGFLSVSCWEGYGLSYRNGTGICVCNGIAEAQQQKGQQLNLSDGRSVGKAAGFKCDADDIYADYWRFMEEEERQREKEAHESLRNVSGGTNSDEHEPGGGESDVWKSEPNADIPESQAAVTEERNSSPHATESATSGTSALSCPLSLSRVGRVVIFCTDPEIAKCLMILAAFFMRDRRVIASTTTPDMTPFAGRVESCAHSSLPVQWLMEDYNPRRFERLLCSPFTVENIVLVIDPRSLVCQRLRVHKTFSVSPILVERFGERHPVVRPFQKLLLGNVRVASDAVITSALRLACKLHKLGDPSSSCTKFLEWFVVCLVGRCHAIRFEKGLNSQLIKEVSPSPSQFPHSVDERSRIGKVESPSRINDGDVSFLDLISNVFGNDGATSAGGPLPHRSTHEMIESIFSGPKEGSQLLQYLPYDE
Protein: Kinesin heavy chain isoform 5C (EC 3.6.4.-) (Kinesin heavy chain neuron-specific 2) (Kinesin-1) (P56536)
Organism: Rattus norvegicus (Rat)
Function: Microtubule-associated force-producing protein that may play a role in organelle transport (By similarity). Has ATPase activity. Involved in synaptic transmission (By similarity). Mediates dendritic trafficking of mRNAs (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:O60282}. Note=Abundant in distal regions of dendrites. {ECO:0000250|UniProtKB:O60282}.
Interaction partners:
- Kinesin light chain
- Kinesin light chain 4
- Kinesin light chain 1
- Kinesin light chain 3
- Kinesin heavy chain isoform 5A
- Kinesin-1 heavy chain
- Neurofilament light polypeptide
- Neurofilament medium polypeptide
- E3 SUMO-protein ligase RanBP2
- Neurofilament heavy polypeptide
Sequence:
MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVIQHLEVELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQTDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGSSNSTHYQK
Protein: Cathepsin K (EC 3.4.22.38) (P55097)
Organism: Mus musculus (Mouse)
Function: Thiol protease involved in osteoclastic bone resorption. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation (By similarity). Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen.
Subcellular location: Lysosome {ECO:0000269|PubMed:12782676}. Secreted {ECO:0000269|PubMed:12782676}. Apical cell membrane {ECO:0000269|PubMed:12782676}; Peripheral membrane protein {ECO:0000269|PubMed:12782676}; Extracellular side {ECO:0000269|PubMed:12782676}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000269|PubMed:12782676}.
Interaction partners:
- Collagenase 3
- Apoptosis regulator Bcl-2
- Serpin B13
- Nuclear factor of activated T-cells, cytoplasmic 1
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Tumor necrosis factor ligand superfamily member 11
- Matrix metalloproteinase-9
- Dendritic cell-specific transmembrane protein
- Matrilysin
Sequence:
MWVFKFLLLPMVSFALSPEEMLDTQWELWKKTHQKQYNSKVDEISRRLIWEKNLKQISAHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLRIPPSRSYSNDTLYTPEWEGRVPDSIDYRKKGYVTPVKNQGQCGSCWAFSSAGALEGQLKKKTGKLLALSPQNLVDCVTENYGCGGGYMTTAFQYVQQNGGIDSEDAYPYVGQDESCMYNATAKAAKCRGYREIPVGNEKALKRAVARVGPISVSIDASLASFQFYSRGVYYDENCDRDNVNHAVLVVGYGTQKGSKHWIIKNSWGESWGNKGYALLARNKNNACGITNMASFPKM