NSE4A_HUMAN - dbPTM
NSE4A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSE4A_HUMAN
UniProt AC Q9NXX6
Protein Name Non-structural maintenance of chromosomes element 4 homolog A
Gene Name NSMCE4A
Organism Homo sapiens (Human).
Sequence Length 385
Subcellular Localization Nucleus . Chromosome, telomere .
Protein Description Component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Is involved in positive regulation of response to DNA damage stimulus..
Protein Sequence MSGDSSGRGPEGRGRGRDPHRDRTRSRSRSRSPLSPRSRRGSARERREAPERPSLEDTEPSDSGDEMMDPASLEAEADQGLCRQIRHQYRALINSVQQNREDILNAGDKLTEVLEEANTLFNEVSRAREAVLDAHFLVLASDLGKEKAKQLRSDLSSFDMLRYVETLLTHMGVNPLEAEELIRDEDSPDFEFIVYDSWKITGRTAENTFNKTHTFHFLLGSIYGECPVPKPRVDRPRKVPVIQEERAMPAQLRRMEESHQEATEKEVERILGLLQTYFREDPDTPMSFFDFVVDPHSFPRTVENIFHVSFIIRDGFARIRLDQDRLPVIEPVSINEENEGFEHNTQVRNQGIIALSYRDWEEIVKTFEISEPVITPSQRQQKPSA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSGDSSGRG
------CCCCCCCCC
51.8424043423
5Phosphorylation---MSGDSSGRGPEG
---CCCCCCCCCCCC
37.9124043423
6Phosphorylation--MSGDSSGRGPEGR
--CCCCCCCCCCCCC
36.9324043423
26PhosphorylationPHRDRTRSRSRSRSP
CCCCCCCCCCCCCCC
33.7124719451
28PhosphorylationRDRTRSRSRSRSPLS
CCCCCCCCCCCCCCC
35.5420363803
30PhosphorylationRTRSRSRSRSPLSPR
CCCCCCCCCCCCCCC
38.0523401153
32PhosphorylationRSRSRSRSPLSPRSR
CCCCCCCCCCCCCCC
31.2923401153
35PhosphorylationSRSRSPLSPRSRRGS
CCCCCCCCCCCCCCC
22.9626055452
38PhosphorylationRSPLSPRSRRGSARE
CCCCCCCCCCCCHHH
29.7024275569
38O-linked_GlycosylationRSPLSPRSRRGSARE
CCCCCCCCCCCCHHH
29.7030379171
54PhosphorylationREAPERPSLEDTEPS
HCCCCCCCCCCCCCC
51.0822115753
58PhosphorylationERPSLEDTEPSDSGD
CCCCCCCCCCCCCCC
40.1822115753
61PhosphorylationSLEDTEPSDSGDEMM
CCCCCCCCCCCCCCC
37.8722617229
63PhosphorylationEDTEPSDSGDEMMDP
CCCCCCCCCCCCCCH
53.1022617229
72PhosphorylationDEMMDPASLEAEADQ
CCCCCHHHHHHHHHH
31.9325072903
79UbiquitinationSLEAEADQGLCRQIR
HHHHHHHHHHHHHHH
54.5322817900
95PhosphorylationQYRALINSVQQNRED
HHHHHHHHHHHCHHH
17.8228555341
106UbiquitinationNREDILNAGDKLTEV
CHHHHHHHHHHHHHH
24.9022817900
111PhosphorylationLNAGDKLTEVLEEAN
HHHHHHHHHHHHHHH
29.7726074081
125PhosphorylationNTLFNEVSRAREAVL
HHHHHHHHHHHHHHH
17.6526074081
145UbiquitinationVLASDLGKEKAKQLR
HHHHHHCHHHHHHHH
64.4433845483
147UbiquitinationASDLGKEKAKQLRSD
HHHHCHHHHHHHHHH
65.45-
204PhosphorylationSWKITGRTAENTFNK
CEEEECCCHHHCCCC
39.4020068231
206UbiquitinationKITGRTAENTFNKTH
EEECCCHHHCCCCCE
57.0722817900
238 (in isoform 2)Ubiquitination-54.2821906983
238 (in isoform 1)Ubiquitination-54.2821906983
238UbiquitinationPRVDRPRKVPVIQEE
CCCCCCCCCCCCCHH
54.2821906983
258PhosphorylationQLRRMEESHQEATEK
HHHHHHHHHHHHHHH
19.71-
263PhosphorylationEESHQEATEKEVERI
HHHHHHHHHHHHHHH
47.00-
265UbiquitinationSHQEATEKEVERILG
HHHHHHHHHHHHHHH
63.8121906983
265 (in isoform 2)Ubiquitination-63.8121906983
265 (in isoform 1)Ubiquitination-63.8121906983
301PhosphorylationDPHSFPRTVENIFHV
CCCCCCCHHHHHHEE
32.2024719451
333PhosphorylationLPVIEPVSINEENEG
CCEEECEECCCCCCC
30.3429255136
345PhosphorylationNEGFEHNTQVRNQGI
CCCCCCCHHHHCCCE
30.2817525332
365UbiquitinationRDWEEIVKTFEISEP
CCHHHHHHHCEECCC
53.8322817900
365 (in isoform 1)Ubiquitination-53.8321906983
370PhosphorylationIVKTFEISEPVITPS
HHHHCEECCCCCCHH
28.7530266825
375PhosphorylationEISEPVITPSQRQQK
EECCCCCCHHHHCCC
19.6830266825
377PhosphorylationSEPVITPSQRQQKPS
CCCCCCHHHHCCCCC
29.3717525332
381UbiquitinationITPSQRQQKPSA---
CCHHHHCCCCCC---
62.9129967540
382UbiquitinationTPSQRQQKPSA----
CHHHHCCCCCC----
32.3829967540
384PhosphorylationSQRQQKPSA------
HHHCCCCCC------
54.3622067460

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of NSE4A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSE4A_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of NSE4A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSE1_HUMANNSMCE1physical
18086888
SMC6_HUMANSMC6physical
18086888
SMC6_HUMANSMC6physical
26186194
NSE3_HUMANNDNL2physical
26186194
SMC5_HUMANSMC5physical
26186194
BRCA2_HUMANBRCA2physical
26186194
DNJB2_HUMANDNAJB2physical
26186194
NSE3_HUMANNDNL2physical
28514442
SMC6_HUMANSMC6physical
28514442
DNJB2_HUMANDNAJB2physical
28514442
SMC5_HUMANSMC5physical
28514442
BRCA2_HUMANBRCA2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSE4A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345 AND SER-377, ANDMASS SPECTROMETRY.

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