dbPTM

SE1L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SE1L1_HUMAN
UniProt AC	Q9UBV2
Protein Name	Protein sel-1 homolog 1
Gene Name	SEL1L
Organism	Homo sapiens (Human).
Sequence Length	794
Subcellular Localization	Endoplasmic reticulum membrane Single-pass type I membrane protein .
Protein Description	Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. [PubMed: 16186509 Enhances SYVN1 stability. Plays a role in LPL maturation and secretion. Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells. May play a role in Notch signaling.]
Protein Sequence	MRVRIGLTLLLCAVLLSLASASSDEEGSQDESLDSKTTLTSDESVKDHTTAGRVVAGQIFLDSEESELESSIQEEEDSLKSQEGESVTEDISFLESPNPENKDYEEPKKVRKPALTAIEGTAHGEPCHFPFLFLDKEYDECTSDGREDGRLWCATTYDYKADEKWGFCETEEEAAKRRQMQEAEMMYQTGMKILNGSNKKSQKREAYRYLQKAASMNHTKALERVSYALLFGDYLPQNIQAAREMFEKLTEEGSPKGQTALGFLYASGLGVNSSQAKALVYYTFGALGGNLIAHMVLGYRYWAGIGVLQSCESALTHYRLVANHVASDISLTGGSVVQRIRLPDEVENPGMNSGMLEEDLIQYYQFLAEKGDVQAQVGLGQLHLHGGRGVEQNHQRAFDYFNLAANAGNSHAMAFLGKMYSEGSDIVPQSNETALHYFKKAADMGNPVGQSGLGMAYLYGRGVQVNYDLALKYFQKAAEQGWVDGQLQLGSMYYNGIGVKRDYKQALKYFNLASQGGHILAFYNLAQMHASGTGVMRSCHTAVELFKNVCERGRWSERLMTAYNSYKDGDYNAAVIQYLLLAEQGYEVAQSNAAFILDQREASIVGENETYPRALLHWNRAASQGYTVARIKLGDYHFYGFGTDVDYETAFIHYRLASEQQHSAQAMFNLGYMHEKGLGIKQDIHLAKRFYDMAAEASPDAQVPVFLALCKLGVVYFLQYIRETNIRDMFTQLDMDQLLGPEWDLYLMTIIALLLGTVIAYRQRQHQDMPAPRPPGPRPAPPQQEGPPEQQPPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MRVRIGLTLLLCAVL CCHHHHHHHHHHHHH	15.33	22210691
28	Phosphorylation	ASSDEEGSQDESLDS CCCCCCCCCCCCCCC	37.42	22210691
32	Phosphorylation	EEGSQDESLDSKTTL CCCCCCCCCCCCCEE	45.85	-
37	O-linked_Glycosylation	DESLDSKTTLTSDES CCCCCCCCEECCCHH	30.87	55835871
37	Phosphorylation	DESLDSKTTLTSDES CCCCCCCCEECCCHH	30.87	26699800
38	O-linked_Glycosylation	ESLDSKTTLTSDESV CCCCCCCEECCCHHH	31.60	55835875
38	Phosphorylation	ESLDSKTTLTSDESV CCCCCCCEECCCHHH	31.60	26699800
40	Phosphorylation	LDSKTTLTSDESVKD CCCCCEECCCHHHCC	31.85	26657352
40	O-linked_Glycosylation	LDSKTTLTSDESVKD CCCCCEECCCHHHCC	31.85	OGP
41	Phosphorylation	DSKTTLTSDESVKDH CCCCEECCCHHHCCC	42.36	29255136
41	O-linked_Glycosylation	DSKTTLTSDESVKDH CCCCEECCCHHHCCC	42.36	69003355
44	Phosphorylation	TTLTSDESVKDHTTA CEECCCHHHCCCCCC	39.18	29255136
44	O-linked_Glycosylation	TTLTSDESVKDHTTA CEECCCHHHCCCCCC	39.18	55835883
46	Ubiquitination	LTSDESVKDHTTAGR ECCCHHHCCCCCCCE	53.74	-
49	Phosphorylation	DESVKDHTTAGRVVA CHHHCCCCCCCEEEE	28.60	23312004
49	O-linked_Glycosylation	DESVKDHTTAGRVVA CHHHCCCCCCCEEEE	28.60	55835889
50	Phosphorylation	ESVKDHTTAGRVVAG HHHCCCCCCCEEEEE	24.56	23312004
50	O-linked_Glycosylation	ESVKDHTTAGRVVAG HHHCCCCCCCEEEEE	24.56	55835895
63	Phosphorylation	AGQIFLDSEESELES EEEEEECCCHHHHHH	45.47	28192239
66	Phosphorylation	IFLDSEESELESSIQ EEECCCHHHHHHHHH	43.35	20639409
70	Phosphorylation	SEESELESSIQEEED CCHHHHHHHHHHHHH	45.42	20639409
71	Phosphorylation	EESELESSIQEEEDS CHHHHHHHHHHHHHH	20.93	20639409
78	Phosphorylation	SIQEEEDSLKSQEGE HHHHHHHHHHHCCCC	40.76	20639409
81	Phosphorylation	EEEDSLKSQEGESVT HHHHHHHHCCCCCHH	38.46	29759185
88	O-linked_Glycosylation	SQEGESVTEDISFLE HCCCCCHHHHHHHHC	36.90	OGP
96	O-linked_Glycosylation	EDISFLESPNPENKD HHHHHHCCCCCCCCC	31.93	OGP
160	Ubiquitination	CATTYDYKADEKWGF EEEECEECCCCCCCC	46.60	-
176	Ubiquitination	ETEEEAAKRRQMQEA CCHHHHHHHHHHHHH	55.98	-
189	Phosphorylation	EAEMMYQTGMKILNG HHHHHHHHHHHHHCC	23.04	28258704
195	N-linked_Glycosylation	QTGMKILNGSNKKSQ HHHHHHHCCCCCHHH	56.15	UniProtKB CARBOHYD
197	Phosphorylation	GMKILNGSNKKSQKR HHHHHCCCCCHHHHH	44.39	28258704
212	Ubiquitination	EAYRYLQKAASMNHT HHHHHHHHHHHCCCH	43.24	-
217	N-linked_Glycosylation	LQKAASMNHTKALER HHHHHHCCCHHHHHH	36.86	UniProtKB CARBOHYD
248	Ubiquitination	AAREMFEKLTEEGSP HHHHHHHHHHHCCCC	49.82	-
272	N-linked_Glycosylation	YASGLGVNSSQAKAL HHCCCCCCHHHHHHH	33.86	12754519
272	N-linked_Glycosylation	YASGLGVNSSQAKAL HHCCCCCCHHHHHHH	33.86	12754519
431	N-linked_Glycosylation	SDIVPQSNETALHYF CCCCCCCCHHHHHHH	45.45	19159218
440	Ubiquitination	TALHYFKKAADMGNP HHHHHHHHHHHCCCC	38.62	-
457	Phosphorylation	QSGLGMAYLYGRGVQ CCCCCHHHHHCCCEE	7.49	-
472	Ubiquitination	VNYDLALKYFQKAAE ECHHHHHHHHHHHHH	38.11	-
503	Phosphorylation	GIGVKRDYKQALKYF CCCCCCCHHHHHHHH	14.72	29083192
504	Ubiquitination	IGVKRDYKQALKYFN CCCCCCHHHHHHHHC	33.12	-
571	Phosphorylation	NSYKDGDYNAAVIQY HHCCCCCCHHHHHHH	16.54	26074081
578	Phosphorylation	YNAAVIQYLLLAEQG CHHHHHHHHHHHHCC	6.54	26074081
586	Phosphorylation	LLLAEQGYEVAQSNA HHHHHCCHHHHHHCC	13.61	26074081
591	Phosphorylation	QGYEVAQSNAAFILD CCHHHHHHCCEEEEC	20.78	26074081
603	Phosphorylation	ILDQREASIVGENET EECCHHHCCCCCCCC	17.04	26074081
608	N-linked_Glycosylation	EASIVGENETYPRAL HHCCCCCCCCCCHHH	40.77	19159218
610	O-linked_Glycosylation	SIVGENETYPRALLH CCCCCCCCCCHHHHH	50.86	30059200
632	Ubiquitination	GYTVARIKLGDYHFY CCEEEEEEECCEEEE	40.64	-
639	Phosphorylation	KLGDYHFYGFGTDVD EECCEEEECCCCCCC	9.76	30387612
663	Phosphorylation	LASEQQHSAQAMFNL HHHCCHHHHHHHHHH	20.10	30387612
676	Ubiquitination	NLGYMHEKGLGIKQD HHHHHHHCCCCCCHH	44.77	-
681	Ubiquitination	HEKGLGIKQDIHLAK HHCCCCCCHHHHHHH	39.87	-
688	Ubiquitination	KQDIHLAKRFYDMAA CHHHHHHHHHHHHHH	49.77	-

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 SE1L1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SE1L1_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 SE1L1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYVN1_HUMAN	SYVN1	physical	16186509
DERL2_HUMAN	DERL2	physical	16186509
DERL1_HUMAN	DERL1	physical	16186509
FXRD2_HUMAN	FOXRED2	physical	19706418
RPN1_HUMAN	RPN1	physical	19706418
OS9_HUMAN	OS9	physical	18711132
SYVN1_HUMAN	SYVN1	physical	18711132
UBXN4_HUMAN	UBXN4	physical	18711132
FAF2_HUMAN	FAF2	physical	18711132
AUP1_HUMAN	AUP1	physical	18711132
UB2J1_HUMAN	UBE2J1	physical	18711132
OS9_HUMAN	OS9	physical	18264092
ERLEC_HUMAN	ERLEC1	physical	18264092
SYVN1_HUMAN	SYVN1	physical	18264092
EDEM1_MOUSE	Edem1	physical	22905195
OS9_HUMAN	OS9	physical	19346256
EDEM1_HUMAN	EDEM1	physical	21632540
SYJ2B_HUMAN	SYNJ2BP	physical	22939629
ERLEC_HUMAN	ERLEC1	physical	23356641
SYVN1_HUMAN	SYVN1	physical	23867461
DERL2_HUMAN	DERL2	physical	23867461
OS9_HUMAN	OS9	physical	23867461
DERL1_HUMAN	DERL1	physical	23867461
SHH_HUMAN	SHH	physical	24366871
SYVN1_HUMAN	SYVN1	physical	24366871
DERL2_HUMAN	DERL2	physical	24366871
SYVN1_HUMAN	SYVN1	physical	23356641
OS9_HUMAN	OS9	physical	23356641
OS9_HUMAN	OS9	physical	21454652
SYVN1_HUMAN	SYVN1	physical	21454652
ITB4_HUMAN	ITGB4	physical	24324549
OS9_HUMAN	OS9	physical	22119785
UB2J1_HUMAN	UBE2J1	physical	22119785
ERLEC_HUMAN	ERLEC1	physical	22119785
SYVN1_HUMAN	SYVN1	physical	22119785
HYOU1_HUMAN	HYOU1	physical	26344197
SYVN1_HUMAN	SYVN1	physical	26471130
HYOU1_HUMAN	HYOU1	physical	27030672

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 SE1L1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-431 AND ASN-608, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-272.	12754519 [Abstract]