ASB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ASB2_HUMAN
• UniProt AC: Q96Q27
• Protein Name: Ankyrin repeat and SOCS box protein 2
• Gene Name: ASB2
• Organism: Homo sapiens (Human).
• Sequence Length: 587
• Protein Description: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.; Isoform 1: Enhances adhesion of hematopoietic cells to fibronectin through targeting of filamins FLNA and FLNB for proteasomal degradation, it is transiantly expressed during hematopoietic cell differentiation.; Isoform 2: Involved in myogenic differentiation and targets filamin FLNB for proteasomal degradation but not filamin FLNA..
• Protein Sequence: MTRFSYAEYFSLFHSCSAPSRSTAPPESSPARAPMGLFQGVMQKYSSSLFKTSQLAPADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLAPERARLYEDRRSSALYFAVVNNNVYATELLLQHGADPNRDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFAMKCLSLLKFLMDLGCDGEPCFSCLYGNGPHPPAPQPSSRFNDAPAADKEPSVVQFCEFVSAPEVSRWAGPIIDVLLDYVGNVQLCSRLKEHIDSFEDWAVIKEKAEPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ

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
28	Phosphorylation	RSTAPPESSPARAPM CCCCCCCCCCCCCCC	47.60	-
29	Phosphorylation	STAPPESSPARAPMG CCCCCCCCCCCCCCH	22.40	-
45	Phosphorylation	FQGVMQKYSSSLFKT HHHHHHHHHHCHHCH	9.26	29978859
46	Phosphorylation	QGVMQKYSSSLFKTS HHHHHHHHHCHHCHH	22.08	29978859
47	Phosphorylation	GVMQKYSSSLFKTSQ HHHHHHHHCHHCHHC	28.15	29978859
48	Phosphorylation	VMQKYSSSLFKTSQL HHHHHHHCHHCHHCC	31.70	24719451
51	Ubiquitination	KYSSSLFKTSQLAPA HHHHCHHCHHCCCCC	53.19	-
52	Phosphorylation	YSSSLFKTSQLAPAD HHHCHHCHHCCCCCC	17.86	29978859
53	Phosphorylation	SSSLFKTSQLAPADP HHCHHCHHCCCCCCH	24.64	29978859
88	Ubiquitination	KNLAEPNKEGWLPLH CCCCCCCCCCCEEHH	69.21	-
107	Ubiquitination	YGQVGCLKVLQRAYP HHHHHHHHHHHHHCC	45.00	-
155	Ubiquitination	AEPDISNKSRETPLY CCCCCCCCCCCCHHH	44.06	-
162	Phosphorylation	KSRETPLYKACERKN CCCCCHHHHHHHHCC	9.57	-
168	Acetylation	LYKACERKNAEAVKI HHHHHHHCCHHHHEE	37.91	20167786
199	Phosphorylation	TALHESVSRNDLEVM HHHCHHCCCCCCCHH	34.35	28509920
219	Ubiquitination	GGAKVESKNAYGITP CCCEEECCCCCCCCH	31.90	-
312	Phosphorylation	VQMLLPVTSRTRIRR EEEEEECCCCCCHHH	15.56	28509920
313	Phosphorylation	QMLLPVTSRTRIRRS EEEEECCCCCCHHHC	31.71	28509920
323	Phosphorylation	RIRRSGVSPLHLAAE CHHHCCCCHHHHHHH	25.85	-
342	Phosphorylation	EVLEALLSARFDVNT HHHHHHHHCCCCCCC	20.46	24719451
442	Phosphorylation	MFAMKCLSLLKFLMD HHHHHHHHHHHHHHH	40.92	24719451
582	Ubiquitination	GRLIRYLKYENTQ-- HHHHHHHEECCCC--	41.40	-

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
323	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
323	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ASB2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ASB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CUL5_HUMAN	CUL5	physical	16325183
RBX2_HUMAN	RNF7	physical	16325183
JAK3_MOUSE	Jak3	physical	21969365
CUL1_HUMAN	CUL1	physical	21119685
CUL5_HUMAN	CUL5	physical	21119685
JAK2_HUMAN	JAK2	physical	21119685
ELOB_HUMAN	TCEB2	physical	21119685
SKP2_HUMAN	SKP2	physical	21119685
TFE2_HUMAN	TCF3	physical	21119685
RBX2_HUMAN	RNF7	physical	19300455
ELOB_HUMAN	TCEB2	physical	19300455
ELOC_HUMAN	TCEB1	physical	19300455
CUL5_HUMAN	CUL5	physical	19300455
UBC_HUMAN	UBC	physical	19300455
FLNB_HUMAN	FLNB	physical	19300455
FLNA_HUMAN	FLNA	physical	21737450
UB2D1_HUMAN	UBE2D1	physical	19300455
ELOB_HUMAN	TCEB2	physical	24044920
ELOC_HUMAN	TCEB1	physical	24044920
CUL5_HUMAN	CUL5	physical	24044920
RBX2_HUMAN	RNF7	physical	24044920
H33_HUMAN	H3F3A	physical	24337577
HMGB1_HUMAN	HMGB1	physical	24337577
ROA1_HUMAN	HNRNPA1	physical	24337577
RAN_HUMAN	RAN	physical	24337577
SSBP_HUMAN	SSBP1	physical	24337577
5NTC_HUMAN	NT5C2	physical	24337577
RL35A_HUMAN	RPL35A	physical	24337577
VIME_HUMAN	VIM	physical	24337577
HNRPD_HUMAN	HNRNPD	physical	24337577
PPM1A_HUMAN	PPM1A	physical	24337577
CAND1_HUMAN	CAND1	physical	24337577
PROF1_HUMAN	PFN1	physical	24337577
HNRH1_HUMAN	HNRNPH1	physical	24337577
HNRPK_HUMAN	HNRNPK	physical	24337577
ROA2_HUMAN	HNRNPA2B1	physical	24337577
SMD1_HUMAN	SNRPD1	physical	24337577
IF4B_HUMAN	EIF4B	physical	24337577
CK084_HUMAN	C11orf84	physical	24337577
UBC_HUMAN	UBC	physical	21737450
UBC_HUMAN	UBC	physical	18799729
FLNA_HUMAN	FLNA	physical	18799729
ASB2_HUMAN	ASB2	physical	24044920
DCNL3_HUMAN	DCUN1D3	physical	28514442
CUL5_HUMAN	CUL5	physical	28514442
NFKB2_HUMAN	NFKB2	physical	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.