wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-conjugating enzyme E2 2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 2) (Radiation sensitivity protein 6) (Ubiquitin carrier protein UBC2) (Ubiquitin-protein ligase UBC2) (P06104)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In association with the E3 enzyme RAD18, it catalyzes the monoubiquitination of POL30 'Lys-164', involved in postreplication repair of UV-damaged DNA. The RAD6/UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. In association with the E3 enzyme UBR1, is involved in N-end rule-dependent protein degradation. Also involved in sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8436296}. Nucleus {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8436296}.
Interaction partners:
- E3 ubiquitin-protein ligase UBR1
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- E3 ubiquitin-protein ligase BRE1
- E3 ubiquitin-protein ligase UBR2
- Ubiquitin-conjugating enzyme variant MMS2
- ATP-dependent DNA helicase SRS2
- DNA repair protein RAD5
- DNA polymerase zeta catalytic subunit
- Ubiquitin-activating enzyme E1 1
- MYND-type zinc finger protein MUB1
Sequence:
MSTPARRRLMRDFKRMKEDAPPGVSASPLPDNVMVWNAMIIGPADTPYEDGTFRLLLEFDEEYPNKPPHVKFLSEMFHPNVYANGEICLDILQNRWTPTYDVASILTSIQSLFNDPNPASPANVEAATLFKDHKSQYVKRVKETVEKSWEDDMDDMDDDDDDDDDDDDDEAD
Protein: GDP-mannose 6-dehydrogenase (GMD) (EC 1.1.1.132) (Guanosine diphospho-D-mannose dehydrogenase) (P11759)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the oxidation of guanosine diphospho-D-mannose (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics (Probable). Other sugars are not used as substrates.
Interaction partners:
- Alginate biosynthesis protein AlgA
- Mannuronan synthase
- Mannuronan synthase
- Mannuronan C5-epimerase
- Alginate biosynthesis protein AlgX
- Alginate lyase
- Alginate biosynthesis protein AlgK
- Probable alginate O-acetylase AlgJ
- Alginate production protein AlgE
- Alginate biosynthesis protein AlgA
Sequence:
MRISIFGLGYVGAVCAGCLSARGHEVIGVDVSSTKIDLINQGKSPIVEPGLEALLQQGRQTGRLSGTTDFKKAVLDSDVSFICVGTPSKKNGDLDLGYIETVCREIGFAIREKSERHTVVVRSTVLPGTVNNVVIPLIEDCSGKKAGVDFGVGTNPEFLRESTAIKDYDFPPMTVIGELDKQTGDLLEEIYRELDAPIIRKTVEVAEMIKYTCNVWHAAKVTFANEIGNIAKAVGVDGREVMDVICQDHKLNLSRYYMRPGFAFGGSCLPKDVRALTYRASQLDVEHPMLGSLMRSNSNQVQKAFDLITSHDTRKVGLLGLSFKAGTDDLRESPLVELAEMLIGKGYELRIFDRNVEYARVHGANKEYIESKIPHVSSLLVSDLDEVVASSDVLVLGNGDELFVDLVNKTPSGKKLVDLVGFMPHTTTAQAEGICW
Protein: Apoptosis-stimulating of p53 protein 2b isoform X1 (Tumor protein p53-binding protein, 2b) (F1QWN1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMPMFLTVYLSNSDKHFTELPITPETLCRDVLDMCKEPGEVDCYLAEMWRGSERVIGDSERIIEVLQRWGQQRAEVRFFLRHDRAPGHDTGGHRTPESLAKRSNAVKDRLMENGMAAPHMDITLSELQEMASRQQQQINAQQQLLATKEQRLRFLKLQDQRQQQQQVSEQEKLRQLRENAENQEAKLRRVRALKGQVEQKRISNSKLVEEIEQMNGLFQQKQRELVVAVSRVEELSRQLDVLRSGKMDMPHEAGPSSSGELERLYKELQLRNKLNQEQSAKLQQQRENLNKRNVEMAAMDKRVAELRERLWKKKAALQQKENLPQPSEGQNPQSVGPSRVAAVGPYIQTTPAPPLPPKQEILVKPAYPDGTATLPKPLPKPTTGGFLTGKISKISDLFSSTETSKSSHVHSSTLPRMTSHGSQEKDPEVDLRPPPLPLRKNQSSEDLLRDSQSAGRTFEKVPPPVPSKPKPALSGQSTFSKLPYSTGTFPGKARSANQKPPMPLPSHNNTLPLPLPPKPDTLPAATVRPFTSDTLAGKDTSTPTTLHKPQTVAASSIYSMYTQQSTLGKGYQGQSTLTRSQPRLYGKPVIPSSVGQQSFIQDFSHIEKICGLDGDQVDQGSSNTAPASSSVEGQEAERVPRPLSPTKLLPFLSNSHRLQSDVDLEALRKRLHNAPRPLKKRGSITESEGPGGPNIQKLLYQKTTLAAMETIAPAAFFPAEGEDGCRPVPNESTRPQEGHHDNTIPECEREEEELTPPPLPPRSPILDDNSNFSTGLNEPQLKEEQEVYGPAAPEPYVEEYPPYPPPPYPSMTEQEGPGEDSINMKAPEVTGQVMLPPGKRTNLRKTGSERINHGMRVRFNPLALLLDSSLEGEYDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQYGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVYAMTYSDLQTAADKCEEMEEGYAQCSQFLYGVQEKMGIMNRGVVYALWDYDGESPDELSFKEGDCLTVLRREDGEETEWWWARCADNEGYIPRNLLGLYPRIKPRQRSLA
Protein: Hyperpolarization-activated ion channel variant DMIH-A1B1C1 (Q56JI0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MHVKHTQRRVSGPGAFGTFTNDQRASRDNLCPDNQQQQQQRHSHSHQHLVRQSLVSLSNGQPAASAAPDSVSLLRAGDDQQQHPQQPHLQQQQQQQQHLQQQQQRHRSSSSRLSTSGISKQNSSDSRSGLRILDSSHSPVSCGTQSVSSTGGQSALYDACHEYSRSLSAAAAEGAASLLKSHYSDQQLAQTEPDPEPDPERDRDRDRDRDRDRERERRHLTNLNLNLSSEYDYSGSDKQQLVNETYIFKCIANSPSFLRTNKIKEQSKKLRNLSLKTRTAKKKGQIISKSNAVSDNSLHPGDKYLNLYLVEKKHSLQPQVASTSSSINTTHPQASSAPASSSSTCTKAPQARQQQLLLNGSLKGKGQSQSQGQSRQTLPGHRASVRSESGSGSSHTIPATGKSPPVPHSLAAKISSSASGSKNCNLLSASSNSCHKLNAHAQGSGAGSGSGSGSGSGPPGHSHYAAASPKSSVSSNGHLNKYCLTDLTRRKAEFNRQLSAPTDYTHHSSSNGSQQEGSSEANEGHEPVGESTITVASAGVSYPHPYSYPYHYAHHASSATAPANLKASLQLHSFGSHHPCPYPARPTSTSCTNSFNRRHIRRHKGKLGDRLLSGDSEESVRCSYCSVLNVNDNDLRISFENTCTDSLVTAFDDEALLICDQGTEMVHFDDVSLYGTPKEEPMPNIPIVSEKVSANFLKSQLQSWFQPTDNRLAMKLFGSRKALVKERIRQKTSGHWVIHPCSSFRFYWDLCMLLLLVANLIILPVAISFFNDDLSTRWIAFNCLSDTIFLIDIVVNFRTGIMQQDNAEQVILDPKLIAKHYLRTWFFLDLISSIPLDYIFLIFNQDFSDSFQILHAGRALRILRLAKLLSLVRLLRLSRLVRYVSQWEEVYFLNMASVFMRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVSINELQESYWLEQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIQSLDSSRRQYREKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGEVATSLSDGSYFGEICLLTNARRVASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTMETVAAERLNKIGKNPNIMHQKDEQLSNPESNTITAVVNALAAEADDCKDDDMDLKENLLHGSESSIAEPVQTIREGLPRPRSGEFRALFEGNTP
Protein: AT-rich interactive domain-containing protein 4A (ARID domain-containing protein 4A) (Retinoblastoma-binding protein 1) (RBBP-1) (P29374)
Organism: Homo sapiens (Human)
Function: DNA-binding protein which modulates activity of several transcription factors including RB1 (retinoblastoma-associated protein) and AR (androgen receptor) (By similarity). May function as part of an mSin3A repressor complex. Has no intrinsic transcriptional activity (By similarity). Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4B (By similarity). Involved in spermatogenesis, together with ARID4B, where it acts as a transcriptional coactivator for AR and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier (By similarity). Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:8414517, ECO:0000269|PubMed:8455946}.
Interaction partners:
- Breast cancer metastasis-suppressor 1
- Breast cancer metastasis-suppressor 1-like protein
- Paired amphipathic helix protein Sin3a
- Histone deacetylase complex subunit SAP30
- Paired amphipathic helix protein Sin3b
- Sin3 histone deacetylase corepressor complex component SDS3
- Histone deacetylase 1
- Inhibitor of growth protein 2
- Retinoblastoma-associated protein
- Inhibitor of growth protein 1
Sequence:
MKAADEPAYLTVGTDVSAKYRGAFCEAKIKTVKRLVKVKVLLKQDNTTQLVQDDQVKGPLRVGAIVETRTSDGSFQEAIISKLTDASWYTVVFDDGDERTLRRTSLCLKGERHFAESETLDQLPLTNPEHFGTPVIAKKTNRGRRSSLPVTEDEKEEESSEEEDEDKRRLNDELLGKVVSVVSATERTEWYPALVISPSCNDDITVKKDQCLVRSFIDSKFYSIARKDIKEVDILNLPESELSTKPGLQKASIFLKTRVVPDNWKMDISEILESSSSDDEDGPAEENDEEKEKEAKKTEEEVPEEELDPEERDNFLQQLYKFMEDRGTPINKPPVLGYKDLNLFKLFRLVYHQGGCDNIDSGAVWKQIYMDLGIPILNSAASYNVKTAYRKYLYGFEEYCRSANIQFRTVHHHEPKVKEEKKDLEESMEEALKLDQEMPLTEVKSEPEENIDSNSESEREEIELKSPRGRRRIARDVNSIKKEIEEEKTEDKLKDNDTENKDVDDDYETAEKKENELLLGRKNTPKQKEKKIKKQEDSDKDSDEEEEKSQEREETESKCDSEGEEDEEDMEPCLTGTKVKVKYGRGKTQKIYEASIKSTEIDDGEVLYLVHYYGWNVRYDEWVKADRIIWPLDKGGPKKKQKKKAKNKEDSEKDEKRDEERQKSKRGRPPLKSTLSSNMPYGLSKTANSEGKSDSCSSDSETEDALEKNLINEELSLKDELEKNENLNDDKLDEENPKISAHILKENDRTQMQPLETLKLEVGENEQIVQIFGNKMEKTEEVKKEAEKSPKGKGRRSKTKDLSLEIIKISSFGQNEAGSEPHIEAHSLELSSLDNKNFSSATEDEIDQCVKEKKLKRKILGQSSPEKKIRIENGMEMTNTVSQERTSDCIGSEGMKNLNFEQHFERENEGMPSLIAESNQCIQQLTSERFDSPAEETVNIPLKEDEDAMPLIGPETLVCHEVDLDDLDEKDKTSIEDVAVESSESNSLVSIPPALPPVVQHNFSVASPLTLSQDESRSVKSESDITIEVDSIAEESQEGLCERESANGFETNVASGTCSIIVQERESREKGQKRPSDGNSGLMAKKQKRTPKRTSAAAKNEKNGTGQSSDSEDLPVLDNSSKCTPVKHLNVSKPQKLARSPARISPHIKDGEKDKHREKHPNSSPRTYKWSFQLNELDNMNSTERISFLQEKLQEIRKYYMSLKSEVATIDRRRKRLKKKDREVSHAGASMSSASSDTGMSPSSSSPPQNVLAVECR
Protein: UPF0231 protein YacL (P0A8E5)
Organism: Escherichia coli (strain K12)
Interaction partners:
- DNA-binding transcriptional dual regulator CRP
- Uncharacterized protein YhfK
- RNA polymerase-associated protein RapA
- Chaperone protein YcdY
Sequence:
MDYEFLRDITGVVKVRMSMGHEVVGHWFNEEVKENLALLDEVEQAAHALKGSERSWQRAGHEYTLWMDGEEVMVRANQLEFAGDEMEEGMNYYDEESLSLCGVEDFLQVVAAYRNFVQQK
Protein: Small ribosomal subunit protein uS12 (40S ribosomal protein S23) (D6RD47)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKCRGLRTARKLRSHRRDQKWHDKQYKKAHLGTALKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKSFHGYSGMVEMKL
Protein: Lymphotoxin-alpha (LT-alpha) (TNF-beta) (Tumor necrosis factor ligand superfamily member 1) (Q06332)
Organism: Rattus norvegicus (Rat)
Function: Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM (By similarity). In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo.
Subcellular location: Secreted {ECO:0000250}. Membrane {ECO:0000250}. Note=The homotrimer is secreted. The heterotrimer is membrane-associated. {ECO:0000250}.
Interaction partners:
- Lymphotoxin-beta
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor receptor superfamily member 1B
- Lymphotoxin B receptor)
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily, member 14
- CD40 ligand
- Tumor necrosis factor ligand superfamily member 11
- T-cell surface glycoprotein CD4
- Tumor necrosis factor receptor superfamily, member 5, isoform CRA_a.
Sequence:
MTPLGRLHLLRVLSTPPVFLLGLLLALPLGAQGLSGVRFSASRTAHQPPQKHLTHGLLKPAAHLVGYPSKQNSLLWRANTDRAFLRHGFSLNNNSLLIPTSGLYFVYSQVVFSGESCSPRAIPTPIYLAHEVQLFSSQYPFHVPLLSAQKSVYPGLQGPWVRSMYQGAVFLLSKGDQLSTHTDGISHLHFSPSTVFFGAFAL
Protein: Porphobilinogen deaminase (PBG) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase) (P06983)
Organism: Escherichia coli (strain K12)
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Interaction partners:
- Delta-aminolevulinic acid dehydratase
- Uroporphyrinogen-III synthase
- Glutamyl-tRNA reductase
- Uroporphyrinogen decarboxylase
- Siroheme synthase
- Glutamate-1-semialdehyde 2,1-aminomutase
- Protein HemX
- Protein HemY
- Ferrochelatase
- Succinate dehydrogenase flavoprotein subunit
Sequence:
MLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDTPLAKVGGKGLFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALPAGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLESRIRAALPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERAMNTRLEGGCQVPIGSYAELIDGEIWLRALVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAREILAEVYNGDAPA
Protein: Modulator of macroautophagy TMEM150B (Protein DRAM-3) (Transmembrane protein 150B) (Transmembrane protein 224) (A6NC51)
Organism: Homo sapiens (Human)
Function: Modulator of macroautophagy that causes accumulation of autophagosomes under basal conditions and enhances autophagic flux. Represses cell death and promotes long-term clonogenic survival of cells grown in the absence of glucose in a macroautophagy-independent manner. May have some role in extracellular matrix engulfment or growth factor receptor recycling, both of which can modulate cell survival.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25608530, ECO:0000269|PubMed:25929859}; Multi-pass membrane protein {ECO:0000269|PubMed:25608530}. Endosome membrane {ECO:0000269|PubMed:25929859}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:25929859}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes mainly at the plasma membrane where it concentrates at actin-rich focal adhesions (PubMed:25608530, PubMed:25929859). {ECO:0000269|PubMed:25608530, ECO:0000269|PubMed:25929859}.
Interaction partners:
Sequence:
MWGYLSLMPVFLAVWAISGVWIVFAIAVTNRTVDLSKGFPYISICGSFPPQSCIFSQVLNMGAALAAWICIVRYHQLRDWGVRRWPNQLILWTGLLCALGTSVVGNFQEKNQRPTHLAGAFLAFILGNVYFWLQLLLWRLKRLPQPGAAWIGPLRLGLCSVCTILIVAMIVLHACSLRSVSAACEWVVAMLLFALFGLLAVDFSALESCTLCVQPWPSLSPPPASPISLPVQL
Protein: External alternative NAD(P)H-ubiquinone oxidoreductase B4, mitochondrial (EC 1.6.5.9) (External alternative NADH dehydrogenase NDB4) (NADH:ubiquinone reductase (non-electrogenic) NDB4) (Q9SKT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane (By similarity). NAD(P)H dehydrogenase; more efficient on NADH.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side {ECO:0000269|PubMed:21841088}. Peroxisome {ECO:0000250}.
Interaction partners:
- Ubiquinol oxidase 1a, mitochondrial
- Ubiquinol oxidase 1b, mitochondrial
- Ubiquinol oxidase 3, mitochondrial
- Ubiquinol oxidase 1c, mitochondrial
- Alternative NAD
- Ribosomal L18p/L5e family protein
- F14B2.25/F14B2.25
- Uncharacterized mitochondrial protein AtMg00010
- Uncharacterized mitochondrial protein AtMg01410
Sequence:
MSFHSFYQRASSLFKAYPSTSKILLLSTFSGGGGVLVYSDSNPLKRILHADATLDSDGNPIRKKKVVVLGSGWSGYSFLSYLNNPNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVKIDASNKKIHCRSKEGSSLKGTTEFDMDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERASLPNLTEEERKKILHFVVVGGGPTGVEFSAELHDFLVQDVAKIYPKVQEFTKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADEISTKERETGKIVSEPYGMVVWSTGIGSRPVIKDFMQQIGQGQRRVLATDEWLRVEGCDGVYALGDTATINQRRVMEDIAAIFNKADKGNTGTLKKKDFNSVVKDICQRYPQVELYLKKNKLKNIANLLKSANGEDTQVNIEKFKQALSEVDSQMKNLPATAQVASQQGKYLAKCFNKMEKCEKKPEGPLRFRGEGRHRFQPFRYRHFGSFAPLGGEQTAAELPGDWVSIGHSSQWLWYSVYASKLVSWRTRMLVISDWTRRFVFGRDSSSI
Protein: Prokineticin receptor (Prokineticin receptor 1a isoform X1) (D3TZW3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Prokineticin-1
- Prokineticin
- Prokineticin receptor 1b
Sequence:
MTENNTSTETWTLIHPSGSPHDLIYDIPVDYEVPVDEIPDTTQGRAFFVATIVIAMVLVCIMLVCGVGNCVFIASLARYKKLRNLTNLLIANLAISDFLVATVCCPFLVDYYVVKRLSWDHGIVLCVSINYLRTVSLYVSTNALLAIAVDRYMAIVHPLKPRMKYQTAYWLIFGVWIIPVLIAVPSAYFATEHEYPHSTLHHDKKIFCAQIWSADQQLMYRSYFLFIFIVEFLGPVATMSVCYARISKELWFKNVPGYPTEQLRKRLRRRRRTVVALIAVLVAYVLCWAPYYSFTLLRDFYPALITRGRNSLVVFYIIECIAMSNGVINTLCFVSVRNNAVKWLRAVKFAKWRSLTRVIVGKMAEDDIRTSSLRVTEDVECTRIK
Protein: Chromosome partition protein Smc (Q8TZY2)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01894}.
Interaction partners:
- Segregation/condensation protein A
- SMC-Scp complex subunit ScpB
- Cell division inhibitor minD homolog
Sequence:
MPYIEKLELKGFKSYGNKKVVIPFSKGFTAIVGANGSGKSNIGDAILFVLGGLSAKAMRASRISDLIFAGSKNEPPAKYAEVAIYFNNEDRGFPIDEDEVVIRRRVYPDGRSSYWLNGRRATRSEILDILTAAMISPDGYNIVLQGDITKFIKMSPLERRLLIDDISGIAEYDSKKEKALEELKQAEENLARVDLLIKEVKKQLDKLEKERNDALRYLDLKDKLEKAKVSLLLGEIKILETQIKEGEKRRAEIEEEIQKIEKEIEKIGKEIVEKVKVLREIEERIEKESGEEAIQITKKIGEVTSKIELTKRNIEVAKEELEDAQRRLAKTKEELRKVLSEIEKSKGAITRWKKRRDALINEIKKKEEERNVLVVKLGEIDKTFGAAREEFDSVVKELEETTRKMYEIEGNIRRLQEEKEKLHSRILFLRAKLPGIKEKINEFKAVVEDKRAEISEIEGKLSTIQAKRIKVEKEIEAKSNELEKVSKELESSERELIAAEAQREVRGNRAAEELKRSGIGGIYGTLAELIKVKDEAYALAIEVALGNRADNVVVEDELVAEKAIKYLKEHKLGRLTFLPLNKIKPKHVDSSVGLPAVDVIEYDQKIENAVKFALGDTVIVNSMEEARPHIGKVRMVTIEGELYERSGAITGGHFRARGLAVDTTKLREKVESLRRRKEALEGELNSLKIELRSLENASFELRIKLSDEKKELELASKDLNRLLEEENAVKEEIEESERKIQEIEQKIENEKSELAKLRGRIQRLERKKEKLKKALENPEARELMEKIRIIDGEISSLKEELSRIESRIESLESRLNEELLPRKASLEEEIEGLVNKINALKNNISENEKALELLNKELEKLKSIEENIKGEIRTLREKRKKLEEDISKLREKKEVLQRKLQELEIEANTLKVRDAQLNAQLEEKKYQLTHYDKNLIKSIKEIPLDLEKVKKEIEKMEEEIRSLEPVNMKAIEDFEIVERRYLELKSKREKLEAEKESIIEFINEIEKEKKNVFMRTFEAISRNFSEIFAKLSPGGSARLILENPEDPFSGGLEIEAKPAGKDVKRIEAMSGGEKALTALAFVFAIQKFKPAPFYLFDEIDAHLDDANVKRVADLIKESSKESQFIVITLRDVMMANADKIIGVSMRDGVSKVVSLSLEKAMKILEEIRKKQGWEHGN
Protein: Sister chromatid cohesion protein 1 (Q12158)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate.
Subcellular location: Nucleus {ECO:0000269|PubMed:9335333, ECO:0000269|PubMed:9335334, ECO:0000269|PubMed:9990856}. Chromosome {ECO:0000269|PubMed:9335333, ECO:0000269|PubMed:9990856}. Chromosome, centromere {ECO:0000269|PubMed:9990856}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved by ESP1, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. {ECO:0000269|PubMed:9990856}.
Interaction partners:
- Sister chromatid cohesion protein PDS5
- Separin
- Structural maintenance of chromosomes protein 3
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Sister chromatid cohesion protein 2
- Structural maintenance of chromosomes protein 1
- Cohesin subunit SCC3
- G2/mitotic-specific cyclin-2
- Mitosis inhibitor protein kinase SWE1
- S-phase entry cyclin-6
Sequence:
MVTENPQRLTVLRLATNKGPLAQIWLASNMSNIPRGSVIQTHIAESAKEIAKASGCDDESGDNEYITLRTSGELLQGIVRVYSKQATFLLTDIKDTLTKISMLFKTSQKMTSTVNRLNTVTRVHQLMLEDAVTEREVLVTPGLEFLDDTTIPVGLMAQENSMERKVQGAAPWDTSLEVGRRFSPDEDFEHNNLSSMNLDFDIEEGPITSKSWEEGTRQSSRNFDTHENYIQDDDFPLDDAGTIGWDLGITEKNDQNNDDDDNSVEQGRRLGESIMSEEPTDFGFDLDIEKEAPAGNIDTITDAMTESQPKQTGTRRNSKLLNTKSIQIDEETENSESIASSNTYKEERSNNLLTPQPTNFTTKRLWSEITESMSYLPDPILKNFLSYESLKKRKIHNGREGSIEEPELNVSLNLTDDVISNAGTNDNSFNELTDNMSDFVPIDAGLNEAPFPEENIIDAKTRNEQTTIQTEKVRPTPGEVASKAIVQMAKILRKELSEEKEVIFTDVLKSQANTEPENITKREASRGFFDILSLATEGCIGLSQTEAFGNIKIDAKPALFERFINA
Protein: N-terminal EF-hand calcium-binding protein 1 (EF-hand calcium-binding protein 1) (Neuronal calcium-binding protein 1) (Synaptotagmin-interacting protein 1) (Stip-1) (Q9ESB5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- WD repeat-containing protein 90
Sequence:
MEDSRETSPSSNNSSEELSSALQLSKGMSIFLDILRRADKNDDGKLSFEEFKAYFADGVLSGEELHELFHTIDTHNTNNLDTEELCEYFSQHLGEYENVLAALEDLNLSILKAMGKTKKDYQEASNLEQFVTRFLLKETLNQLQSLQNSLECAMETTEEQTRQERQGPSKPEVLSIQWPGKRSSRRVQRHNSFSPNSPQFNVSSPALLEEDNQWMTQINRLQKLIDRLEKKDLKLEPLEEEVIEENTKPHIMLVQRQMSVTEEDLEEFQLALKHYVESASAQSGCLRISIQKLSNESRYMIYEFWENSSVWNRHLQTNYSKTFQRSNVDFLETPELTSTMLVPASWWILKNN
Protein: OCEL domain-containing protein (Q9N554)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ell-associated factor Eaf
- Probable cyclin-dependent kinase 9
- C3H1-type domain-containing protein
- Putative transcription elongation factor S-II
- Cyclin-T1.1
- Cyclin-T1.2
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- RNA polymerase II subunit A C-terminal domain phosphatase
- Suppressor of Ty 6 homolog
- Transcription elongation factor SPT5
Sequence:
MLKSSSGNMHHFSTGSSSAIIASSSSSSSSSNGYGHSPRDLLTGAAVANGGGGGFGGVAGVAFATTSPPTPVNLDVQRIDCTDETTVVMVKLTDEMFAALQESQRSGKPLRINVNDKEGRVEIGDGTASSKTNNTFYFQKQTVPEQTDTLVHSGGGVRNVGTYKTKYQIQATDRSFQETKKRAELRAEVEKSRGTKQMKKSGVTSSSSRYHNSSNSTPRSMNSAPNSSRVSPSFMSSSSSKASTSHVTTNNSKGTPNNGSESKKIDMTPQLMKHSIKKRIIHLIVTQKYSNWEEVYKKLKSDGLPEEKDEIEKIRSCVEEVSETRPEMSVMSLRTSFLSEVDQRWMFFNQEEKSHVRRLCNSGSRVGPTDNNFAPLRKKGMERITASSKTEKDKVKEKLEEAAKIPSPPKDQKSLPSIVEEDDYYTAPPEPANKRRAHNLAPPPPPPVQVVTPQTTSSQTETGPLPPKRTKRPESSSPQLERSSQPASKLNPIKLAATIAMQPIPKCDPPPPPPSRDTYHHNVASVAVNGGGSTASSRVSSPASSLSSPSQPSCNWEKQFGDIKTLSEAEAYFKQFHKEYPLYMECHEMLTKVSSEFRGLEVKLLTAVALSKTSPSPQNMQNVKQIEKNIQNRYAHFEKDPEFMKARQRHTDLRSKLNVLKTRIGSWEKMRRQSSTNV
Protein: Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (EC 3.2.2.6) (Oligophrenin-4) (Three immunoglobulin domain-containing IL-1 receptor-related 2) (TIGIRR-2) (X-linked interleukin-1 receptor accessory protein-like 1) (Q9NZN1)
Organism: Homo sapiens (Human)
Function: May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in neurite outgrowth (By similarity). During dendritic spine formation can bidirectionally induce pre- and post-synaptic differentiation of neurons by trans-synaptically binding to PTPRD (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12783849}; Single-pass type I membrane protein {ECO:0000269|PubMed:12783849}. Cytoplasm {ECO:0000269|PubMed:12783849}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=May localize to the cell body and growth cones of dendrite-like processes. {ECO:0000250}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Neuronal calcium sensor 1
- Interleukin-1 family member 10
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Receptor-type tyrosine-protein phosphatase S
- Mitogen-activated protein kinase 8
- Leucine-rich repeat and fibronectin type-III domain-containing protein 4
- SLIT and NTRK-like protein 3
- Disks large homolog 4
- SLIT and NTRK-like protein 2
Sequence:
MKAPIPHLILLYATFTQSLKVVTKRGSADGCTDWSIDIKKYQVLVGEPVRIKCALFYGYIRTNYSLAQSAGLSLMWYKSSGPGDFEEPIAFDGSRMSKEEDSIWFRPTLLQDSGLYACVIRNSTYCMKVSISLTVGENDTGLCYNSKMKYFEKAELSKSKEISCRDIEDFLLPTREPEILWYKECRTKTWRPSIVFKRDTLLIREVREDDIGNYTCELKYGGFVVRRTTELTVTAPLTDKPPKLLYPMESKLTIQETQLGDSANLTCRAFFGYSGDVSPLIYWMKGEKFIEDLDENRVWESDIRILKEHLGEQEVSISLIVDSVEEGDLGNYSCYVENGNGRRHASVLLHKRELMYTVELAGGLGAILLLLVCLVTIYKCYKIEIMLFYRNHFGAEELDGDNKDYDAYLSYTKVDPDQWNQETGEEERFALEILPDMLEKHYGYKLFIPDRDLIPTGTYIEDVARCVDQSKRLIIVMTPNYVVRRGWSIFELETRLRNMLVTGEIKVILIECSELRGIMNYQEVEALKHTIKLLTVIKWHGPKCNKLNSKFWKRLQYEMPFKRIEPITHEQALDVSEQGPFGELQTVSAISMAAATSTALATAHPDLRSTFHNTYHSQMRQKHYYRSYEYDVPPTGTLPLTSIGNQHTYCNIPMTLINGQRPQTKSSREQNPDEAHTNSAILPLLPRETSISSVIW