Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O43865

- SAHH2_HUMAN

UniProt

O43865 - SAHH2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Putative adenosylhomocysteinase 2

Gene

AHCYL1

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

Functioni

Catalytic activityi

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

Cofactori

Binds 1 NAD per subunit.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateBy similarity
Binding sitei229 – 2291SubstrateBy similarity
Binding sitei254 – 2541SubstrateBy similarity
Binding sitei284 – 2841SubstrateBy similarity
Binding sitei288 – 2881SubstrateBy similarity
Binding sitei341 – 3411NAD1 Publication
Binding sitei376 – 3761NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi318 – 3225NAD1 Publication
Nucleotide bindingi397 – 3993NAD1 Publication

GO - Molecular functioni

  1. adenosylhomocysteinase activity Source: UniProtKB-EC

GO - Biological processi

  1. mRNA polyadenylation Source: Ensembl
  2. one-carbon metabolic process Source: UniProtKB-KW
  3. positive regulation of sodium ion transport Source: Ensembl
  4. protein export from nucleus Source: Ensembl
  5. regulation of anion transport Source: Ensembl
  6. regulation of ion transmembrane transporter activity Source: Ensembl
  7. regulation of mRNA 3'-end processing Source: Ensembl
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:
Putative adenosylhomocysteinase 2 (EC:3.3.1.1)
Short name:
AdoHcyase 2
Alternative name(s):
DC-expressed AHCY-like molecule
S-adenosyl-L-homocysteine hydrolase 2
S-adenosylhomocysteine hydrolase-like protein 1
Gene namesi
Name:AHCYL1
Synonyms:DCAL, XPVKONA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:344. AHCYL1.

Subcellular locationi

Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24637.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 530529Putative adenosylhomocysteinase 2PRO_0000116908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei40 – 401N6-acetyllysineBy similarity
Modified residuei391 – 3911Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO43865.
PaxDbiO43865.
PeptideAtlasiO43865.
PRIDEiO43865.

PTM databases

PhosphoSiteiO43865.

Miscellaneous databases

PMAP-CutDBO43865.

Expressioni

Tissue specificityi

Expressed in dendritic cells.1 Publication

Developmental stagei

Expression increases markedly during activation of blood and skin DC (Langerhans cells), but is diminished in terminally differentiated tonsil DC.1 Publication

Gene expression databases

BgeeiO43865.
CleanExiHS_AHCYL1.
ExpressionAtlasiO43865. baseline and differential.
GenevestigatoriO43865.

Organism-specific databases

HPAiHPA042589.

Interactioni

Subunit structurei

Interacts with ITPR1. Competes with IP3 for interaction with ITPR1 and attenuates IP3-induced Ca2+ release through the ITPR1 from the non-mitochondrial intracellular stores By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
tatP046085EBI-2371423,EBI-6164389From a different organism.

Protein-protein interaction databases

BioGridi115987. 111 interactions.
IntActiO43865. 9 interactions.
STRINGi9606.ENSP00000358814.

Structurei

Secondary structure

1
530
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi113 – 12412
Helixi128 – 13710
Turni142 – 1454
Beta strandi147 – 1526
Helixi156 – 16712
Beta strandi171 – 1755
Beta strandi177 – 1804
Helixi184 – 19310
Beta strandi196 – 1983
Helixi205 – 21612
Beta strandi224 – 2318
Helixi232 – 2409
Helixi242 – 2454
Beta strandi249 – 2535
Helixi256 – 26510
Turni266 – 2694
Beta strandi275 – 2773
Helixi282 – 29312
Helixi299 – 3057
Beta strandi313 – 3175
Helixi321 – 33313
Beta strandi336 – 3405
Helixi344 – 3529
Helixi360 – 3623
Turni363 – 3664
Beta strandi368 – 3725
Helixi382 – 3876
Beta strandi392 – 3965
Turni400 – 4034
Helixi406 – 4094
Beta strandi415 – 4206
Beta strandi423 – 4275
Beta strandi433 – 4375
Helixi438 – 4403
Helixi444 – 4463
Helixi452 – 47120
Beta strandi479 – 4824
Helixi486 – 49611
Helixi497 – 5004
Helixi509 – 5146
Beta strandi519 – 5213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTGX-ray2.64A/B89-530[»]
ProteinModelPortaliO43865.
SMRiO43865. Positions 101-530.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43865.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni65 – 9228PESTBy similarityAdd
BLAST
Regioni281 – 448168NAD bindingBy similarityAdd
BLAST
Regioni520 – 53011PDZ-bindingBy similarityAdd
BLAST

Domaini

The PEST region is essential for the interaction with ITPR1. The PDZ-binding region is required for maximal interaction with ITPR1 and is also responsible for the IP3-insensitive interaction with ITPR1 By similarity.By similarity

Sequence similaritiesi

Belongs to the adenosylhomocysteinase family.Curated

Phylogenomic databases

eggNOGiCOG0499.
GeneTreeiENSGT00390000003626.
HOGENOMiHOG000227986.
HOVERGENiHBG005041.
InParanoidiO43865.
KOiK01251.
OMAiKQIQFVE.
OrthoDBiEOG76739S.
PhylomeDBiO43865.
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]
PIRSFiPIRSF001109. Ad_hcy_hydrolase. 1 hit.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43865-1) [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
MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE
60 70 80 90 100
FTKFPTKTGR RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK
110 120 130 140 150
GSSNFCVKNI KQAEFGRREI EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG
160 170 180 190 200
CTHITAQTAV LIETLCALGA QCRWSACNIY STQNEVAAAL AEAGVAVFAW
210 220 230 240 250
KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK YPNVFKKIRG
260 270 280 290 300
IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG
310 320 330 340 350
LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA
360 370 380 390 400
CMDGFRVVKL NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS
410 420 430 440 450
NTEIDVTSLR TPELTWERVR SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV
460 470 480 490 500
PTFVLSITAT TQALALIELY NAPEGRYKQD VYLLPKKMDE YVASLHLPSF
510 520 530
DAHLTELTDD QAKYLGLNKN GPFKPNYYRY
Length:530
Mass (Da):58,951
Last modified:April 4, 2006 - v2
Checksum:i974D23361A245D04
GO
Isoform 2 (identifier: O43865-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Note: Derived from EST data.

Show »
Length:483
Mass (Da):53,753
Checksum:i18DFC7E74697E1D4
GO

Sequence cautioni

The sequence BI460083 differs from that shown. Reason: Frameshift at several positions.
The sequence AAC01960.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAB43223.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941K → M in T19009. (PubMed:7782076)Curated
Sequence conflicti99 – 991S → F in T19009. (PubMed:7782076)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2. 5 PublicationsVSP_021751Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF315687 mRNA. Translation: AAL26869.1.
AL036027 mRNA. No translation available.
AK303690 mRNA. Translation: BAG64680.1.
AK316110 mRNA. Translation: BAH14481.1.
AL049954 mRNA. Translation: CAB43223.2. Different initiation.
AL772411 Genomic DNA. Translation: CAH70965.1.
AL772411 Genomic DNA. Translation: CAH70966.1.
CH471122 Genomic DNA. Translation: EAW56426.1.
BC007576 mRNA. Translation: AAH07576.3.
BC010681 mRNA. Translation: AAH10681.3.
BC016942 mRNA. Translation: AAH16942.3.
BC065254 mRNA. Translation: AAH65254.2.
BC095476 mRNA. Translation: AAH95476.2.
BC110896 mRNA. Translation: AAI10897.2.
BI460083 mRNA. No translation available.
U82761 mRNA. Translation: AAC01960.1. Different initiation.
AU279527 mRNA. No translation available.
T19009 mRNA. No translation available.
BK005418 mRNA. Translation: DAA05763.1.
BK005417 mRNA. Translation: DAA05762.1.
CCDSiCCDS55620.1. [O43865-2]
CCDS818.1. [O43865-1]
PIRiT08681.
RefSeqiNP_001229602.1. NM_001242673.1. [O43865-2]
NP_001229603.1. NM_001242674.1. [O43865-2]
NP_001229604.1. NM_001242675.1. [O43865-2]
NP_001229605.1. NM_001242676.1. [O43865-2]
NP_006612.2. NM_006621.5. [O43865-1]
UniGeneiHs.743973.

Genome annotation databases

EnsembliENST00000359172; ENSP00000352092; ENSG00000168710. [O43865-2]
ENST00000369799; ENSP00000358814; ENSG00000168710. [O43865-1]
ENST00000393614; ENSP00000377238; ENSG00000168710. [O43865-2]
GeneIDi10768.
KEGGihsa:10768.
UCSCiuc001dyx.3. human. [O43865-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF315687 mRNA. Translation: AAL26869.1 .
AL036027 mRNA. No translation available.
AK303690 mRNA. Translation: BAG64680.1 .
AK316110 mRNA. Translation: BAH14481.1 .
AL049954 mRNA. Translation: CAB43223.2 . Different initiation.
AL772411 Genomic DNA. Translation: CAH70965.1 .
AL772411 Genomic DNA. Translation: CAH70966.1 .
CH471122 Genomic DNA. Translation: EAW56426.1 .
BC007576 mRNA. Translation: AAH07576.3 .
BC010681 mRNA. Translation: AAH10681.3 .
BC016942 mRNA. Translation: AAH16942.3 .
BC065254 mRNA. Translation: AAH65254.2 .
BC095476 mRNA. Translation: AAH95476.2 .
BC110896 mRNA. Translation: AAI10897.2 .
BI460083 mRNA. No translation available.
U82761 mRNA. Translation: AAC01960.1 . Different initiation.
AU279527 mRNA. No translation available.
T19009 mRNA. No translation available.
BK005418 mRNA. Translation: DAA05763.1 .
BK005417 mRNA. Translation: DAA05762.1 .
CCDSi CCDS55620.1. [O43865-2 ]
CCDS818.1. [O43865-1 ]
PIRi T08681.
RefSeqi NP_001229602.1. NM_001242673.1. [O43865-2 ]
NP_001229603.1. NM_001242674.1. [O43865-2 ]
NP_001229604.1. NM_001242675.1. [O43865-2 ]
NP_001229605.1. NM_001242676.1. [O43865-2 ]
NP_006612.2. NM_006621.5. [O43865-1 ]
UniGenei Hs.743973.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MTG X-ray 2.64 A/B 89-530 [» ]
ProteinModelPortali O43865.
SMRi O43865. Positions 101-530.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115987. 111 interactions.
IntActi O43865. 9 interactions.
STRINGi 9606.ENSP00000358814.

PTM databases

PhosphoSitei O43865.

Proteomic databases

MaxQBi O43865.
PaxDbi O43865.
PeptideAtlasi O43865.
PRIDEi O43865.

Protocols and materials databases

DNASUi 10768.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359172 ; ENSP00000352092 ; ENSG00000168710 . [O43865-2 ]
ENST00000369799 ; ENSP00000358814 ; ENSG00000168710 . [O43865-1 ]
ENST00000393614 ; ENSP00000377238 ; ENSG00000168710 . [O43865-2 ]
GeneIDi 10768.
KEGGi hsa:10768.
UCSCi uc001dyx.3. human. [O43865-1 ]

Organism-specific databases

CTDi 10768.
GeneCardsi GC01P110529.
HGNCi HGNC:344. AHCYL1.
HPAi HPA042589.
MIMi 607826. gene.
neXtProti NX_O43865.
PharmGKBi PA24637.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0499.
GeneTreei ENSGT00390000003626.
HOGENOMi HOG000227986.
HOVERGENi HBG005041.
InParanoidi O43865.
KOi K01251.
OMAi KQIQFVE.
OrthoDBi EOG76739S.
PhylomeDBi O43865.
TreeFami TF300415.

Enzyme and pathway databases

UniPathwayi UPA00314 ; UER00076 .

Miscellaneous databases

ChiTaRSi AHCYL1. human.
EvolutionaryTracei O43865.
GeneWikii AHCYL1.
GenomeRNAii 10768.
NextBioi 40889.
PMAP-CutDB O43865.
PROi O43865.
SOURCEi Search...

Gene expression databases

Bgeei O43865.
CleanExi HS_AHCYL1.
ExpressionAtlasi O43865. baseline and differential.
Genevestigatori O43865.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view ]
PANTHERi PTHR23420. PTHR23420. 1 hit.
Pfami PF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view ]
PIRSFi PIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTi SM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00936. ahcY. 1 hit.
PROSITEi PS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation."
    Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J., Hart D.N., Kato M.
    Immunogenetics 53:993-1001(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  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] (ISOFORM 2).
    Tissue: Kidney and Thalamus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-251 (ISOFORM 2).
    Tissue: Brain, Colon, Eye, Placenta, PNS and Testis.
  7. "Complementation of chromosomal instability in the xeroderma pigmentosum variant by a gene on human chromosome 1 with homology to S-adenosyl homocysteine hydrolase."
    Volpe J.P.G., McDowell M., Jostes R.F., Afzal V., Sadinski W., Trask B.J., Legerski R., Cleaver J.E.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-530 (ISOFORM 1).
    Tissue: Skin.
  8. "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis."
    Imabayashi H., Mori T., Gojo S., Kiyono T., Sugiyama T., Irie R., Isogai T., Hata J., Toyama Y., Umezawa A.
    Exp. Cell Res. 288:35-50(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-164 (ISOFORM 2).
    Tissue: Chondrocyte.
  9. "Characterization of a large population of mRNAs from human testis."
    Pawlak A., Toussaint C., Levy I., Bulle F., Poyard M., Barouki R., Guellaen G.
    Genomics 26:151-158(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-105 (ISOFORM 2).
    Tissue: Testis.
  10. "Suppression and overexpression of adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) influences zebrafish embryo development: a possible role for AHCYL1 in inositol phospholipid signaling."
    Cooper B.J., Key B., Carter A., Angel N.Z., Hart D.N.J., Kato M.
    J. Biol. Chem. 281:22471-22484(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 2).
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein."
    Structural genomics consortium (SGC)
    Submitted (MAY-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 89-530 IN COMPLEX WITH NAD, COFACTOR.

Entry informationi

Entry nameiSAHH2_HUMAN
AccessioniPrimary (citable) accession number: O43865
Secondary accession number(s): B4E168
, Q2TAJ6, Q502W8, Q5VSM0, Q6P171, Q96PK4, Q9UG84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 4, 2006
Last modified: October 29, 2014
This is version 139 of the entry and version 2 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3