dbPTM

SAHH2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SAHH2_HUMAN
UniProt AC	O43865
Protein Name	S-adenosylhomocysteine hydrolase-like protein 1 {ECO:0000312\|HGNC:HGNC:344}
Gene Name	AHCYL1 {ECO:0000312\|HGNC:HGNC:344}
Organism	Homo sapiens (Human).
Sequence Length	530
Subcellular Localization	Endoplasmic reticulum . Cytoplasm, cytosol . Microsome . Apical cell membrane . Associates with membranes when phosphorylated, probably through interaction with ITPR1.
Protein Description	Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1. [PubMed: 16793548 When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates of ITPR1 to interact with CFTR and SLC26A6 mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion]
Protein Sequence	MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGRRSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREIEIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIYSTQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKKYPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRSQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1 (in isoform 2)	Acetylation	-	7.55	22814378
2	Acetylation	------MSMPDAMPL ------CCCCCCCCC	38.74	20068231
2	Phosphorylation	------MSMPDAMPL ------CCCCCCCCC	38.74	29255136
3	Sulfoxidation	-----MSMPDAMPLP -----CCCCCCCCCC	3.17	28183972
7	Sulfoxidation	-MSMPDAMPLPGVGE -CCCCCCCCCCCCCH	4.58	28183972
27	Acetylation	KEIEDAEKYSFMATV HCHHHHHHHCEEEEE	48.17	26051181
28	Phosphorylation	EIEDAEKYSFMATVT CHHHHHHHCEEEEEC	9.92	25159151
29	Phosphorylation	IEDAEKYSFMATVTK HHHHHHHCEEEEECC	21.44	18707149
31	Sulfoxidation	DAEKYSFMATVTKAP HHHHHCEEEEECCCC	2.22	30846556
33	Phosphorylation	EKYSFMATVTKAPKK HHHCEEEEECCCCHH	19.54	26356563
35	Phosphorylation	YSFMATVTKAPKKQI HCEEEEECCCCHHHC	19.68	46160637
36	Acetylation	SFMATVTKAPKKQIQ CEEEEECCCCHHHCC	59.35	25953088
40	Acetylation	TVTKAPKKQIQFADD EECCCCHHHCCCCHH	52.12	26051181
40	Ubiquitination	TVTKAPKKQIQFADD EECCCCHHHCCCCHH	52.12	-
48	Sulfoxidation	QIQFADDMQEFTKFP HCCCCHHHHHHHCCC	4.18	21406390
53	Ubiquitination	DDMQEFTKFPTKTGR HHHHHHHCCCCHHCC	55.45	-
57	Ubiquitination	EFTKFPTKTGRRSLS HHHCCCCHHCCHHHH	49.58	-
58	Phosphorylation	FTKFPTKTGRRSLSR HHCCCCHHCCHHHHH	38.10	28102081
62	Phosphorylation	PTKTGRRSLSRSISQ CCHHCCHHHHHHHCC	29.36	28102081
64	Phosphorylation	KTGRRSLSRSISQSS HHCCHHHHHHHCCCC	25.81	28102081
66	Phosphorylation	GRRSLSRSISQSSTD CCHHHHHHHCCCCCC	24.18	23090842
68	Phosphorylation	RSLSRSISQSSTDSY HHHHHHHCCCCCCCC	25.84	16793548
70	Phosphorylation	LSRSISQSSTDSYSS HHHHHCCCCCCCCCC	28.54	68737123
71	Phosphorylation	SRSISQSSTDSYSSA HHHHCCCCCCCCCCC	28.70	16793548
72	Phosphorylation	RSISQSSTDSYSSAA HHHCCCCCCCCCCCC	33.92	30576142
74	Phosphorylation	ISQSSTDSYSSAASY HCCCCCCCCCCCCCC	27.31	26657352
75	Phosphorylation	SQSSTDSYSSAASYT CCCCCCCCCCCCCCC	14.95	26434776
76	Phosphorylation	QSSTDSYSSAASYTD CCCCCCCCCCCCCCC	19.90	23090842
77	Phosphorylation	SSTDSYSSAASYTDS CCCCCCCCCCCCCCC	21.44	19220705
80	Phosphorylation	DSYSSAASYTDSSDD CCCCCCCCCCCCCCC	28.43	23090842
81	Phosphorylation	SYSSAASYTDSSDDE CCCCCCCCCCCCCCC	15.16	23090842
82	Phosphorylation	YSSAASYTDSSDDEV CCCCCCCCCCCCCCC	27.23	28857561
84	Phosphorylation	SAASYTDSSDDEVSP CCCCCCCCCCCCCCH	28.06	28857561
85	Phosphorylation	AASYTDSSDDEVSPR CCCCCCCCCCCCCHH	52.47	28857561
90	Phosphorylation	DSSDDEVSPREKQQT CCCCCCCCHHHHHCC	19.05	110736801
100	Acetylation	EKQQTNSKGSSNFCV HHHCCCCCCCCCCCH	65.95	26051181
100	Ubiquitination	EKQQTNSKGSSNFCV HHHCCCCCCCCCCCH	65.95	-
102	Phosphorylation	QQTNSKGSSNFCVKN HCCCCCCCCCCCHHC	26.33	28102081
103	Phosphorylation	QTNSKGSSNFCVKNI CCCCCCCCCCCHHCH	42.46	28102081
108	Acetylation	GSSNFCVKNIKQAEF CCCCCCHHCHHHHHH	54.88	25953088
108	Ubiquitination	GSSNFCVKNIKQAEF CCCCCCHHCHHHHHH	54.88	-
111	2-Hydroxyisobutyrylation	NFCVKNIKQAEFGRR CCCHHCHHHHHHCCC	53.50	-
111	Acetylation	NFCVKNIKQAEFGRR CCCHHCHHHHHHCCC	53.50	25953088
111	Ubiquitination	NFCVKNIKQAEFGRR CCCHHCHHHHHHCCC	53.50	-
127	Sulfoxidation	IEIAEQDMSALISLR EEEHHHHHHHHHHHH	2.23	30846556
141	Acetylation	RKRAQGEKPLAGAKI HHHHCCCCCCCCCEE	52.75	25953088
141	Ubiquitination	RKRAQGEKPLAGAKI HHHHCCCCCCCCCEE	52.75	-
239	Acetylation	DLTHWVYKKYPNVFK CHHHHHHHHCCCHHH	35.89	26051181
240	Acetylation	LTHWVYKKYPNVFKK HHHHHHHHCCCHHHH	48.53	27452117
240	Ubiquitination	LTHWVYKKYPNVFKK HHHHHHHHCCCHHHH	48.53	-
246	Acetylation	KKYPNVFKKIRGIVE HHCCCHHHHHHHHHH	42.90	25953088
249	Methylation	PNVFKKIRGIVEESV CCHHHHHHHHHHHHC	37.35	-
255 (in isoform 2)	Ubiquitination	-	16.09	21906983
257	Phosphorylation	GIVEESVTGVHRLYQ HHHHHHCCHHHHHHH	42.64	-
263	Phosphorylation	VTGVHRLYQLSKAGK CCHHHHHHHHHHCCC	13.83	6831211
267	2-Hydroxyisobutyrylation	HRLYQLSKAGKLCVP HHHHHHHHCCCEEEE	70.52	-
267	Acetylation	HRLYQLSKAGKLCVP HHHHHHHHCCCEEEE	70.52	25953088
267	Malonylation	HRLYQLSKAGKLCVP HHHHHHHHCCCEEEE	70.52	26320211
267	Ubiquitination	HRLYQLSKAGKLCVP HHHHHHHHCCCEEEE	70.52	-
270	Acetylation	YQLSKAGKLCVPAMN HHHHHCCCEEEEECC	43.50	25953088
270	Malonylation	YQLSKAGKLCVPAMN HHHHHCCCEEEEECC	43.50	26320211
270	Ubiquitination	YQLSKAGKLCVPAMN HHHHHCCCEEEEECC	43.50	-
272	S-nitrosylation	LSKAGKLCVPAMNVN HHHCCCEEEEECCCC	3.82	24105792
276	Sulfoxidation	GKLCVPAMNVNDSVT CCEEEEECCCCCHHH	4.75	21406390
281	Phosphorylation	PAMNVNDSVTKQKFD EECCCCCHHHHHHCC	26.87	20068231
283	Phosphorylation	MNVNDSVTKQKFDNL CCCCCHHHHHHCCCE	31.54	20068231
284	Ubiquitination	NVNDSVTKQKFDNLY CCCCHHHHHHCCCEE	49.70	-
286	2-Hydroxyisobutyrylation	NDSVTKQKFDNLYCC CCHHHHHHCCCEEEH	57.13	-
286	Acetylation	NDSVTKQKFDNLYCC CCHHHHHHCCCEEEH	57.13	26051181
286	Ubiquitination	NDSVTKQKFDNLYCC CCHHHHHHCCCEEEH	57.13	-
302	Ubiquitination	ESILDGLKRTTDVMF HHHHHHHCCCCCEEE	53.91	21906983
302 (in isoform 1)	Ubiquitination	-	53.91	21906983
308	Sulfoxidation	LKRTTDVMFGGKQVV HCCCCCEEECCEEEE	2.62	21406390
359	2-Hydroxyisobutyrylation	MDGFRVVKLNEVIRQ HCCCEEEEHHHHHHC	42.62	-
359	Acetylation	MDGFRVVKLNEVIRQ HCCCEEEEHHHHHHC	42.62	25953088
359	Ubiquitination	MDGFRVVKLNEVIRQ HCCCEEEEHHHHHHC	42.62	-
372	Phosphorylation	RQVDVVITCTGNKNV HCCCEEEECCCCCCE	7.75	68726059
374	Phosphorylation	VDVVITCTGNKNVVT CCEEEECCCCCCEEC	34.83	68726065
385 (in isoform 2)	Ubiquitination	-	3.70	21906983
389	Ubiquitination	REHLDRMKNSCIVCN HHHHHHHCCCEEEEE	46.75	-
391	Phosphorylation	HLDRMKNSCIVCNMG HHHHHCCCEEEEECC	10.33	19224921
400	Phosphorylation	IVCNMGHSNTEIDVT EEEECCCCCCEEEEC	39.45	18669648
402	Phosphorylation	CNMGHSNTEIDVTSL EECCCCCCEEEECCC	37.01	18669648
407	Phosphorylation	SNTEIDVTSLRTPEL CCCEEEECCCCCCCC	20.49	18669648
411	Phosphorylation	IDVTSLRTPELTWER EEECCCCCCCCCHHH	26.80	21406692
415	Phosphorylation	SLRTPELTWERVRSQ CCCCCCCCHHHHHHH	24.50	21406692
418	Methylation	TPELTWERVRSQVDH CCCCCHHHHHHHCCE	22.25	-
421	Phosphorylation	LTWERVRSQVDHVIW CCHHHHHHHCCEEEC	31.53	24719451
432	2-Hydroxyisobutyrylation	HVIWPDGKRVVLLAE EEECCCCCEEEEEEC	49.77	-
432	Ubiquitination	HVIWPDGKRVVLLAE EEECCCCCEEEEEEC	49.77	21906983
432 (in isoform 1)	Ubiquitination	-	49.77	21906983
452	Phosphorylation	LSCSTVPTFVLSITA EECCCCCEEEEEHHH	23.26	22210691
456	Phosphorylation	TVPTFVLSITATTQA CCCEEEEEHHHHHHH	16.76	22210691
461	Phosphorylation	VLSITATTQALALIE EEEHHHHHHHHHHHH	14.91	22210691
478	Acetylation	NAPEGRYKQDVYLLP CCCCCCCCCEEEECC	38.37	26051181
478	Ubiquitination	NAPEGRYKQDVYLLP CCCCCCCCCEEEECC	38.37	-
482	Phosphorylation	GRYKQDVYLLPKKMD CCCCCEEEECCHHHH	15.71	110736809
486	2-Hydroxyisobutyrylation	QDVYLLPKKMDEYVA CEEEECCHHHHHHHH	61.78	-
486	Ubiquitination	QDVYLLPKKMDEYVA CEEEECCHHHHHHHH	61.78	-
487	Ubiquitination	DVYLLPKKMDEYVAS EEEECCHHHHHHHHH	50.04	-
513	Ubiquitination	ELTDDQAKYLGLNKN ECCHHHHHHCCCCCC	35.06	-
524	Ubiquitination	LNKNGPFKPNYYRY- CCCCCCCCCCCCCC-	35.17	-
527	Phosphorylation	NGPFKPNYYRY---- CCCCCCCCCCC----	9.61	21945579
528	Phosphorylation	GPFKPNYYRY----- CCCCCCCCCC-----	15.29	21945579
529	Methylation	PFKPNYYRY------ CCCCCCCCC------	21.96	-

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 SAHH2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
68	S	Phosphorylation	16793548
Phosphorylated at Ser/Thr residues between Ser-68 and Thr-72 in the PEST region: required for interaction with dATP-bound RRM1 and ITPR1.
68	S	Phosphorylation	16793548
Phosphorylation at Ser-68 by PRKD1 and CAMK4 is required for further phosphorylations by CSNK1A1.
68	S	Phosphorylation	16793548
Probably phosphorylated by CAMK2A; phosphorylation at Ser-68 may be required for interaction with SLC9A3.
72	T	Phosphorylation	16793548
Phosphorylated at Ser/Thr residues between Ser-68 and Thr-72 in the PEST region: required for interaction with dATP-bound RRM1 and ITPR1.

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 SAHH2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBCA_HUMAN	TBCA	physical	22939629
TRIP6_HUMAN	TRIP6	physical	22939629
UBE2C_HUMAN	UBE2C	physical	22939629
UBQL1_HUMAN	UBQLN1	physical	22939629
UCHL3_HUMAN	UCHL3	physical	22939629
ZPR1_HUMAN	ZPR1	physical	22939629
STAM1_HUMAN	STAM	physical	22939629
SMAP_HUMAN	C11orf58	physical	22939629
TEBP_HUMAN	PTGES3	physical	22939629
SGTA_HUMAN	SGTA	physical	22939629
STIP1_HUMAN	STIP1	physical	22939629
SGT1_HUMAN	SUGT1	physical	22939629
TACC3_HUMAN	TACC3	physical	22939629
TADBP_HUMAN	TARDBP	physical	22939629
THADA_HUMAN	THADA	physical	22939629
TKT_HUMAN	TKT	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
ZRAB2_HUMAN	ZRANB2	physical	22939629
TM1L2_HUMAN	TOM1L2	physical	22939629
SC24C_HUMAN	SEC24C	physical	22939629
ST1A1_HUMAN	SULT1A1	physical	22939629
TTL12_HUMAN	TTLL12	physical	22939629
UB2D2_HUMAN	UBE2D2	physical	22939629
UB2L3_HUMAN	UBE2L3	physical	22939629
UBP34_HUMAN	USP34	physical	22939629
SC24A_HUMAN	SEC24A	physical	22939629
SHOT1_HUMAN	KIAA1598	physical	22939629
SODC_HUMAN	SOD1	physical	22939629
STMN1_HUMAN	STMN1	physical	22939629
TAGL2_HUMAN	TAGLN2	physical	22939629
TLE3_HUMAN	TLE3	physical	22939629
TMOD3_HUMAN	TMOD3	physical	22939629
TPM2_HUMAN	TPM2	physical	22939629
TTC1_HUMAN	TTC1	physical	22939629
UB2V1_HUMAN	UBE2V1	physical	22939629
UBE2B_HUMAN	UBE2B	physical	22939629
UBQL4_HUMAN	UBQLN4	physical	22939629
RL40_HUMAN	UBA52	physical	22939629
SLD5_HUMAN	GINS4	physical	22939629
SPS1_HUMAN	SEPHS1	physical	22939629
CHIP_HUMAN	STUB1	physical	22939629
SUMO2_HUMAN	SUMO2	physical	22939629
SYUG_HUMAN	SNCG	physical	22939629
TCPE_HUMAN	CCT5	physical	22939629
UBL7_HUMAN	UBL7	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22939629
SP100_HUMAN	SP100	physical	22939629
SRXN1_HUMAN	SRXN1	physical	22939629
TPD54_HUMAN	TPD52L2	physical	22939629
TTC9C_HUMAN	TTC9C	physical	22939629
UB2D1_HUMAN	UBE2D1	physical	22939629
UBE4B_HUMAN	UBE4B	physical	22939629
UFC1_HUMAN	UFC1	physical	22939629
ZYX_HUMAN	ZYX	physical	22939629
SPRE_HUMAN	SPR	physical	22939629
THIO_HUMAN	TXN	physical	22939629
USP9X_HUMAN	USP9X	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
VPS4B_HUMAN	VPS4B	physical	22939629
SERC_HUMAN	PSAT1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
SKP1_HUMAN	SKP1	physical	22939629
SNX12_HUMAN	SNX12	physical	22939629
STAT6_HUMAN	STAT6	physical	22939629
UBXN1_HUMAN	UBXN1	physical	22939629
TBB6_HUMAN	TUBB6	physical	22939629
SERPH_HUMAN	SERPINH1	physical	22939629
SH3L3_HUMAN	SH3BGRL3	physical	22939629
SNX3_HUMAN	SNX3	physical	22939629
STMN2_HUMAN	STMN2	physical	22939629
TES_HUMAN	TES	physical	22939629
TPM1_HUMAN	TPM1	physical	22939629
TYSY_HUMAN	TYMS	physical	22939629
UFM1_HUMAN	UFM1	physical	22939629
VP26A_HUMAN	VPS26A	physical	22939629
ANCHR_HUMAN	ZFYVE19	physical	22939629
SIN3A_HUMAN	SIN3A	physical	22939629
PDC6I_HUMAN	PDCD6IP	physical	22863883
PP2AA_HUMAN	PPP2CA	physical	22863883
UBA6_HUMAN	UBA6	physical	22863883
SAHH2_HUMAN	AHCYL1	physical	25416956
SOX30_HUMAN	SOX30	physical	25416956
PSD12_HUMAN	PSMD12	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197

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 SAHH2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-400; THR-402AND THR-407, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28, AND MASSSPECTROMETRY.	15951569 [Abstract]

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