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Protein

Adenosylhomocysteinase 3

Gene

AHCYL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 acitivity and Mg2+-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate (PubMed:19220705).By similarity1 Publication

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactori

NAD(+)Note: Binds 1 NAD(+) per subunit.

Pathway:iL-homocysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine.
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosylhomocysteinase (AHCYL1), Adenosylhomocysteinase (AHCYL2), Adenosylhomocysteinase (AHCYL1), Adenosylhomocysteinase (AHCY), Adenosylhomocysteinase (AHCY), Adenosylhomocysteinase, Adenosylhomocysteinase 2 (AHCYL1), Adenosylhomocysteinase (FGFR2-AHCYL1), Adenosylhomocysteinase 3 (AHCYL2)
This subpathway is part of the pathway L-homocysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homocysteine from S-adenosyl-L-homocysteine, the pathway L-homocysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei236 – 2361SubstrateBy similarity
Binding sitei310 – 3101SubstrateBy similarity
Binding sitei335 – 3351SubstrateBy similarity
Binding sitei365 – 3651SubstrateBy similarity
Binding sitei369 – 3691SubstrateBy similarity
Binding sitei370 – 3701NADBy similarity
Binding sitei422 – 4221NAD1 Publication
Binding sitei457 – 4571NAD1 Publication
Binding sitei525 – 5251NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi336 – 3383NADBy similarity
Nucleotide bindingi401 – 4066NAD1 Publication
Nucleotide bindingi478 – 4792NAD1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosylhomocysteinase 3 (EC:3.3.1.1)
Short name:
AdoHcyase 3
Alternative name(s):
IP(3)Rs binding protein released with IP(3) 2
Short name:
IRBIT2
Long-IRBIT1 Publication
S-adenosyl-L-homocysteine hydrolase 3
S-adenosylhomocysteine hydrolase-like protein 2
Gene namesi
Name:AHCYL2
Synonyms:KIAA0828
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:22204. AHCYL2.

Subcellular locationi

  • Cytoplasm By similarity
  • Microsome By similarity

  • Note: Associates with membranes when phosphorylated, probably through interaction with ITPR1.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162376046.

Polymorphism and mutation databases

BioMutaiAHCYL2.
DMDMi21759427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 611610Adenosylhomocysteinase 3PRO_0000116909Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei107 – 1071Phosphoserine2 Publications
Modified residuei121 – 1211N6-acetyllysineBy similarity
Modified residuei149 – 1491Phosphoserine1 Publication
Modified residuei152 – 1521Phosphoserine1 Publication
Modified residuei155 – 1551Phosphoserine1 Publication
Modified residuei158 – 1581Phosphoserine1 Publication
Modified residuei472 – 4721PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated during neuronal diffrentiation at the LISN domain.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96HN2.
PaxDbiQ96HN2.
PRIDEiQ96HN2.

PTM databases

PhosphoSiteiQ96HN2.

Expressioni

Gene expression databases

BgeeiQ96HN2.
CleanExiHS_AHCYL2.
ExpressionAtlasiQ96HN2. baseline and differential.
GenevisibleiQ96HN2. HS.

Organism-specific databases

HPAiHPA053128.

Interactioni

Subunit structurei

Homotetramer (Probable). Forms heteromultimers with AHCYL1 (via the C-terminal region) (PubMed:19220705). Interacts with ITPR1; with lower affinity than AHCYL1 and maybe via ITPR1 (PubMed:19220705). Interacts with SLC4A4 (By similarity).By similarity1 Publication1 Publication

Protein-protein interaction databases

BioGridi116958. 46 interactions.
IntActiQ96HN2. 7 interactions.
MINTiMINT-5005542.
STRINGi9606.ENSP00000315931.

Structurei

Secondary structure

1
611
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi191 – 1933Combined sources
Helixi194 – 20613Combined sources
Helixi209 – 21810Combined sources
Turni223 – 2264Combined sources
Beta strandi228 – 2336Combined sources
Helixi237 – 24812Combined sources
Beta strandi252 – 26110Combined sources
Helixi265 – 27410Combined sources
Helixi286 – 29712Combined sources
Beta strandi305 – 3128Combined sources
Helixi313 – 3219Combined sources
Helixi323 – 3275Combined sources
Beta strandi331 – 3344Combined sources
Helixi337 – 3437Combined sources
Beta strandi356 – 3583Combined sources
Helixi363 – 3697Combined sources
Helixi371 – 38616Combined sources
Beta strandi394 – 3985Combined sources
Helixi402 – 41312Combined sources
Beta strandi417 – 4215Combined sources
Helixi425 – 4339Combined sources
Helixi441 – 4444Combined sources
Turni445 – 4473Combined sources
Beta strandi449 – 4535Combined sources
Helixi463 – 4686Combined sources
Beta strandi473 – 4775Combined sources
Turni481 – 4844Combined sources
Helixi487 – 4904Combined sources
Beta strandi496 – 5016Combined sources
Beta strandi504 – 5085Combined sources
Beta strandi514 – 5185Combined sources
Helixi519 – 5213Combined sources
Helixi524 – 5285Combined sources
Helixi533 – 55220Combined sources
Turni555 – 5573Combined sources
Beta strandi560 – 5645Combined sources
Helixi567 – 57711Combined sources
Helixi578 – 5814Combined sources
Helixi590 – 5967Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVPX-ray2.25A/B/C/D175-607[»]
ProteinModelPortaliQ96HN2.
SMRiQ96HN2. Positions 176-607.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96HN2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 109108LISN domain, inhibits interaction with ITPR11 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

eggNOGiCOG0499.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227986.
HOVERGENiHBG005041.
InParanoidiQ96HN2.
KOiK01251.
OMAiAENWQPN.
OrthoDBiEOG76739S.
PhylomeDBiQ96HN2.
TreeFamiTF300415.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96HN2-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSVQVVSAAA AAKVPEVELK DLSPSEAESQ LGLSTAAVGA MAPPAGGGDP
60 70 80 90 100
EAPAPAAERP PVPGPGSGPA AALSPAAGKV PQASAMKRSD PHHQHQRHRD
110 120 130 140 150
GGEALVSPDG TVTEAPRTVK KQIQFADQKQ EFNKRPTKIG RRSLSRSISQ
160 170 180 190 200
SSTDSYSSAA SYTDSSDDET SPRDKQQKNS KGSSDFCVKN IKQAEFGRRE
210 220 230 240 250
IEIAEQEMPA LMALRKRAQG EKPLAGAKIV GCTHITAQTA VLMETLGALG
260 270 280 290 300
AQCRWAACNI YSTLNEVAAA LAESGFPVFA WKGESEDDFW WCIDRCVNVE
310 320 330 340 350
GWQPNMILDD GGDLTHWIYK KYPNMFKKIK GIVEESVTGV HRLYQLSKAG
360 370 380 390 400
KLCVPAMNVN DSVTKQKFDN LYCCRESILD GLKRTTDMMF GGKQVVVCGY
410 420 430 440 450
GEVGKGCCAA LKAMGSIVYV TEIDPICALQ ACMDGFRLVK LNEVIRQVDI
460 470 480 490 500
VITCTGNKNV VTREHLDRMK NSCIVCNMGH SNTEIDVASL RTPELTWERV
510 520 530 540 550
RSQVDHVIWP DGKRIVLLAE GRLLNLSCST VPTFVLSITA TTQALALIEL
560 570 580 590 600
YNAPEGRYKQ DVYLLPKKMD EYVASLHLPT FDAHLTELTD EQAKYLGLNK
610
NGPFKPNYYR Y
Length:611
Mass (Da):66,721
Last modified:December 1, 2001 - v1
Checksum:iA76B1275FC0D891D
GO
Isoform 2 (identifier: Q96HN2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-122: Missing.

Note: No experimental confirmation available.
Show »
Length:610
Mass (Da):66,593
Checksum:iD54ED0745D3A286B
GO
Isoform 3 (identifier: Q96HN2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MSVQVVSAAAAAKVPEVE → MLGSKKKYIVNGNSGIKA
     19-121: Missing.

Note: No experimental confirmation available.
Show »
Length:508
Mass (Da):56,697
Checksum:i1198694128CB2301
GO
Isoform 4 (identifier: Q96HN2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MSVQVVSAAAAAKVPEVEL → MEKWDGNEGTSAFHMPEWM
     20-122: Missing.

Note: No experimental confirmation available.
Show »
Length:508
Mass (Da):56,944
Checksum:i197CA80AF2940465
GO

Sequence cautioni

The sequence BAA74851.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1919MSVQV…PEVEL → MEKWDGNEGTSAFHMPEWM in isoform 4. 1 PublicationVSP_046278Add
BLAST
Alternative sequencei1 – 1818MSVQV…VPEVE → MLGSKKKYIVNGNSGIKA in isoform 3. 1 PublicationVSP_043185Add
BLAST
Alternative sequencei19 – 121103Missing in isoform 3. 1 PublicationVSP_043186Add
BLAST
Alternative sequencei20 – 122103Missing in isoform 4. 1 PublicationVSP_046279Add
BLAST
Alternative sequencei122 – 1221Missing in isoform 2. 1 PublicationVSP_040095

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020635 mRNA. Translation: BAA74851.1. Different initiation.
AK025372 mRNA. No translation available.
AK295851 mRNA. Translation: BAG58657.1.
AK316073 mRNA. Translation: BAH14444.1.
AC009244 Genomic DNA. No translation available.
AC011005 Genomic DNA. No translation available.
AC083866 Genomic DNA. No translation available.
AC093149 Genomic DNA. No translation available.
BC008349 mRNA. Translation: AAH08349.1.
BC024325 mRNA. Translation: AAH24325.1.
CCDSiCCDS47706.1. [Q96HN2-2]
CCDS47707.2. [Q96HN2-3]
CCDS47708.1. [Q96HN2-4]
CCDS5812.1. [Q96HN2-1]
RefSeqiNP_001124192.1. NM_001130720.2. [Q96HN2-2]
NP_001124194.2. NM_001130722.2. [Q96HN2-3]
NP_001124195.1. NM_001130723.2. [Q96HN2-4]
NP_056143.1. NM_015328.3. [Q96HN2-1]
UniGeneiHs.600789.

Genome annotation databases

EnsembliENST00000325006; ENSP00000315931; ENSG00000158467.
ENST00000446544; ENSP00000413639; ENSG00000158467. [Q96HN2-2]
ENST00000474594; ENSP00000420459; ENSG00000158467. [Q96HN2-4]
ENST00000490911; ENSP00000420801; ENSG00000158467. [Q96HN2-3]
GeneIDi23382.
KEGGihsa:23382.
UCSCiuc003vot.3. human. [Q96HN2-2]
uc011kov.2. human. [Q96HN2-1]
uc011kox.2. human. [Q96HN2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB020635 mRNA. Translation: BAA74851.1. Different initiation.
AK025372 mRNA. No translation available.
AK295851 mRNA. Translation: BAG58657.1.
AK316073 mRNA. Translation: BAH14444.1.
AC009244 Genomic DNA. No translation available.
AC011005 Genomic DNA. No translation available.
AC083866 Genomic DNA. No translation available.
AC093149 Genomic DNA. No translation available.
BC008349 mRNA. Translation: AAH08349.1.
BC024325 mRNA. Translation: AAH24325.1.
CCDSiCCDS47706.1. [Q96HN2-2]
CCDS47707.2. [Q96HN2-3]
CCDS47708.1. [Q96HN2-4]
CCDS5812.1. [Q96HN2-1]
RefSeqiNP_001124192.1. NM_001130720.2. [Q96HN2-2]
NP_001124194.2. NM_001130722.2. [Q96HN2-3]
NP_001124195.1. NM_001130723.2. [Q96HN2-4]
NP_056143.1. NM_015328.3. [Q96HN2-1]
UniGeneiHs.600789.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GVPX-ray2.25A/B/C/D175-607[»]
ProteinModelPortaliQ96HN2.
SMRiQ96HN2. Positions 176-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116958. 46 interactions.
IntActiQ96HN2. 7 interactions.
MINTiMINT-5005542.
STRINGi9606.ENSP00000315931.

PTM databases

PhosphoSiteiQ96HN2.

Polymorphism and mutation databases

BioMutaiAHCYL2.
DMDMi21759427.

Proteomic databases

MaxQBiQ96HN2.
PaxDbiQ96HN2.
PRIDEiQ96HN2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325006; ENSP00000315931; ENSG00000158467.
ENST00000446544; ENSP00000413639; ENSG00000158467. [Q96HN2-2]
ENST00000474594; ENSP00000420459; ENSG00000158467. [Q96HN2-4]
ENST00000490911; ENSP00000420801; ENSG00000158467. [Q96HN2-3]
GeneIDi23382.
KEGGihsa:23382.
UCSCiuc003vot.3. human. [Q96HN2-2]
uc011kov.2. human. [Q96HN2-1]
uc011kox.2. human. [Q96HN2-3]

Organism-specific databases

CTDi23382.
GeneCardsiGC07P128865.
HGNCiHGNC:22204. AHCYL2.
HPAiHPA053128.
neXtProtiNX_Q96HN2.
PharmGKBiPA162376046.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0499.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227986.
HOVERGENiHBG005041.
InParanoidiQ96HN2.
KOiK01251.
OMAiAENWQPN.
OrthoDBiEOG76739S.
PhylomeDBiQ96HN2.
TreeFamiTF300415.

Enzyme and pathway databases

UniPathwayiUPA00314; UER00076.

Miscellaneous databases

ChiTaRSiAHCYL2. human.
EvolutionaryTraceiQ96HN2.
GenomeRNAii23382.
NextBioi45489.
PROiQ96HN2.

Gene expression databases

BgeeiQ96HN2.
CleanExiHS_AHCYL2.
ExpressionAtlasiQ96HN2. baseline and differential.
GenevisibleiQ96HN2. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERiPTHR23420. PTHR23420. 1 hit.
PfamiPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
SMARTiSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00936. ahcY. 1 hit.
PROSITEiPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Tissue: Colon mucosa and Hippocampus.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung and Uterus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. "An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage."
    Ando H., Mizutani A., Mikoshiba K.
    J. Neurochem. 109:539-550(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AHCYL1, INTERACTION WITH ITPR1, PHOSPHORYLATION AT SER-149; SER-152; SER-155 AND SER-158.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Human S-adenosyl homocysteine hydrolase-like 2 protein crystal structure."
    Structural genomics consortium (SGC)
    Submitted (JUN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 175-607 IN COMPLEX WITH NAD, SUBUNIT.

Entry informationi

Entry nameiSAHH3_HUMAN
AccessioniPrimary (citable) accession number: Q96HN2
Secondary accession number(s): B4DIZ5, D9N155, O94917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: December 1, 2001
Last modified: July 22, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.