CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008957
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nck-associated protein 1-like 
Protein Synonyms/Alias
 Hematopoietic protein 1; Membrane-associated protein HEM-1 
Gene Name
 NCKAP1L 
Gene Synonyms/Alias
 HEM1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10LTSAYQHKLAEKLTIubiquitination[1]
14YQHKLAEKLTILNDRubiquitination[1, 2]
33LIRMYNIKKTCSDPKubiquitination[1]
40KKTCSDPKSKPPFLLubiquitination[1]
42TCSDPKSKPPFLLEKubiquitination[1]
49KPPFLLEKSMEPSLKubiquitination[1]
56KSMEPSLKYINKKFPubiquitination[1, 3]
60PSLKYINKKFPNIDVubiquitination[1, 3, 4, 5]
61SLKYINKKFPNIDVRubiquitination[1, 3, 4, 5]
81LGPVHREKAEIIRFLubiquitination[1]
188LEYDHPLKKLTEEFGubiquitination[1]
189EYDHPLKKLTEEFGPubiquitination[1]
313EDLFSSLKGYGKRVAubiquitination[1]
323GKRVADIKESKEHVIubiquitination[1]
326VADIKESKEHVIANSubiquitination[1]
349QFLRMAVKELETVLAubiquitination[1]
500QAYTSVAKAPLHLHEubiquitination[1, 6]
630LSEQLLPKHCATTISubiquitination[1, 6]
887QIRSNFSKPDLMASLubiquitination[1]
1035NNIHCLTKAIIQVSAacetylation[7]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
  
Sequence Annotation
  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Membrane; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1127 AA 
Protein Sequence
MSLTSAYQHK LAEKLTILND RGQGVLIRMY NIKKTCSDPK SKPPFLLEKS MEPSLKYINK 60
KFPNIDVRNS TQHLGPVHRE KAEIIRFLTN YYQSFVDVME FRDHVYELLN TIDACQCHFD 120
INLNFDFTRS YLDLIVTYTS VILLLSRIED RRILIGMYNC AHEMLHGHGD PSFARLGQMV 180
LEYDHPLKKL TEEFGPHTKA VSGALLSLHF LFVRRNQGAE QWRSAQLLSL ISNPPAMINP 240
ANSDTMACEY LSVEVMERWI IIGFLLCHGC LNSNSQCQKL WKLCLQGSLY ITLIREDVLQ 300
VHKVTEDLFS SLKGYGKRVA DIKESKEHVI ANSGQFHCQR RQFLRMAVKE LETVLADEPG 360
LLGPKALFAF MALSFIRDEV TWLVRHTENV TKTKTPEDYA DSSIAELLFL LEGIRSLVRR 420
HIKVIQQYHL QYLARFDALV LSDIIQNLSV CPEEESIIMS SFVSILSSLN LKQVDNGEKF 480
EFSGLRLDWF RLQAYTSVAK APLHLHENPD LAKVMNLIVF HSRMLDSVEK LLVETSDLST 540
FCFHLRIFEK MFAMTLEESA MLRYAIAFPL ICAHFVHCTH EMCPEEYPHL KNHGLHHCNS 600
FLEELAKQTS NCVLEICAEQ RNLSEQLLPK HCATTISKAK NKKTRKQRQT PRKGEPERDK 660
PGAESHRKNR SIVTNMDKLH LNLTELALTM NHVYSFSVFE HTIFPSEYLS SHLEARLNRA 720
IVWLAGYNAT TQEIVRPSEL LAGVKAYIGF IQSLAQFLGA DASRVIRNAL LQQTQPLDSC 780
GEQTITTLYT NWYLESLLRQ ASSGTIILSP AMQAFVSLPR EGEQNFSAEE FSDISEMRAL 840
AELLGPYGMK FLSENLMWHV TSQIVELKKL VVENMDILVQ IRSNFSKPDL MASLLPQLTG 900
AENVLKRMTI IGVILSFRAM AQEGLREVFS SHCPFLMGPI ECLKEFVTPD TDIKVTLSIF 960
ELASAAGVGC DIDPALVAAI ANLKADTSSP EEEYKVACLL LIFLAVSLPL LATDPSSFYS 1020
IEKDGYNNNI HCLTKAIIQV SAALFTLYNK NIETHLKEFL VVASVSLLQL GQETDKLKTR 1080
NRESISLLMR LVVEESSFLT LDMLESCFPY VLLRNAYREV SRAFHLN 1127 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
 GO:0031209; C:SCAR complex; IDA:UniProtKB.
 GO:0032403; F:protein complex binding; IDA:UniProtKB.
 GO:0030295; F:protein kinase activator activity; IMP:UniProtKB.
 GO:0030675; F:Rac GTPase activator activity; IMP:UniProtKB.
 GO:0070358; P:actin polymerization-dependent cell motility; IMP:UniProtKB.
 GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
 GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
 GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
 GO:0048821; P:erythrocyte development; IEP:UniProtKB.
 GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0032700; P:negative regulation of interleukin-17 production; ISS:UniProtKB.
 GO:0032715; P:negative regulation of interleukin-6 production; ISS:UniProtKB.
 GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IMP:UniProtKB.
 GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
 GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
 GO:0045579; P:positive regulation of B cell differentiation; ISS:UniProtKB.
 GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
 GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
 GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
 GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
 GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
 GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISS:UniProtKB.
 GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:UniProtKB.
 GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:UniProtKB.
 GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
 GO:0006461; P:protein complex assembly; ISS:UniProtKB.
 GO:0042493; P:response to drug; IMP:UniProtKB.
 GO:0043029; P:T cell homeostasis; ISS:UniProtKB. 
Interpro
 IPR019137; Nck-associated_protein-1. 
Pfam
 PF09735; Nckap1 
SMART
  
PROSITE
  
PRINTS