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Q15438

- CYH1_HUMAN

UniProt

Q15438 - CYH1_HUMAN

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Protein

Cytohesin-1

Gene

CYTH1

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

Functioni

Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei281 – 2811Phosphatidylinositol 3,4,5-trisphosphateBy similarity
Binding sitei292 – 2921Phosphatidylinositol 3,4,5-trisphosphateBy similarity
Binding sitei302 – 3021Phosphatidylinositol 3,4,5-trisphosphateBy similarity
Binding sitei351 – 3511Phosphatidylinositol 3,4,5-trisphosphateBy similarity

GO - Molecular functioni

  1. ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
  2. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. establishment of epithelial cell polarity Source: Ensembl
  2. positive regulation of GTPase activity Source: GOC
  3. regulation of ARF protein signal transduction Source: InterPro
  4. regulation of cell adhesion Source: MGI
  5. vesicle-mediated transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytohesin-1
Alternative name(s):
PH, SEC7 and coiled-coil domain-containing protein 1
SEC7 homolog B2-1
Gene namesi
Name:CYTH1
Synonyms:D17S811E, PSCD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:9501. CYTH1.

Subcellular locationi

Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytosol By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: UniProtKB
  3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  4. plasma membrane Source: UniProtKB
  5. tight junction Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571E → A or K: Reduces guanine exchange factor activity by over 90%. 1 Publication
Mutagenesisi187 – 1871Y → A: Reduces guanine exchange factor activity by over 90%. 1 Publication
Mutagenesisi195 – 1951M → A: Reduces guanine exchange factor activity by over 90%. 1 Publication

Organism-specific databases

PharmGKBiPA164718528.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Cytohesin-1PRO_0000120194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15438.
PaxDbiQ15438.
PRIDEiQ15438.

PTM databases

PhosphoSiteiQ15438.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ15438.
CleanExiHS_CYTH1.
ExpressionAtlasiQ15438. baseline and differential.
GenevestigatoriQ15438.

Organism-specific databases

HPAiHPA047498.

Interactioni

Subunit structurei

Interacts with TRIM23 and CYTIP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CYTIPO607592EBI-997830,EBI-997814

Protein-protein interaction databases

BioGridi114688. 12 interactions.
IntActiQ15438. 3 interactions.
MINTiMINT-3031502.
STRINGi9606.ENSP00000354398.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 7512Combined sources
Helixi77 – 8610Combined sources
Helixi94 – 10310Combined sources
Helixi109 – 1168Combined sources
Helixi121 – 13313Combined sources
Turni137 – 1393Combined sources
Helixi141 – 15010Combined sources
Helixi158 – 17518Combined sources
Helixi183 – 20119Combined sources
Beta strandi203 – 2053Combined sources
Helixi211 – 2177Combined sources
Turni218 – 2214Combined sources
Helixi229 – 24113Combined sources
Beta strandi246 – 2483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BC9NMR-A58-256[»]
4A4PX-ray2.00A/B63-248[»]
ProteinModelPortaliQ15438.
SMRiQ15438. Positions 58-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15438.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 202130SEC7PROSITE-ProRule annotationAdd
BLAST
Domaini260 – 377118PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 2779Phosphatidylinositol 3,4,5-trisphosphate bindingBy similarity
Regioni388 – 3969C-terminal autoinhibitory regionBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili10 – 6758Sequence AnalysisAdd
BLAST

Domaini

Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate.By similarity
Autoinhibited by its C-terminal basic region.By similarity

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 SEC7 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00760000119036.
HOGENOMiHOG000253023.
HOVERGENiHBG002647.
InParanoidiQ15438.
KOiK18441.
OMAiVGLHEFT.
OrthoDBiEOG7RBZ9C.
PhylomeDBiQ15438.
TreeFamiTF352091.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48425. SSF48425. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50190. SEC7. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15438-1) [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
MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKDE IAEVANEIEN
60 70 80 90 100
LGSTEERKNM QRNKQVAMGR KKFNMDPKKG IQFLIENDLL KNTCEDIAQF
110 120 130 140 150
LYKGEGLNKT AIGDYLGERD EFNIQVLHAF VELHEFTDLN LVQALRQFLW
160 170 180 190 200
SFRLPGEAQK IDRMMEAFAQ RYCQCNNGVF QSTDTCYVLS FAIIMLNTSL
210 220 230 240 250
HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK NEPFKIPEDD
260 270 280 290 300
GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
310 320 330 340 350
PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG
360 370 380 390
NHTVYRISAP TPEEKEEWIK CIKAAISRDP FYEMLAARKK KVSSTKRH
Length:398
Mass (Da):46,413
Last modified:November 1, 1996 - v1
Checksum:i067FEE0FEA7A4C86
GO
Isoform 2 (identifier: Q15438-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     273-273: Missing.

Show »
Length:397
Mass (Da):46,356
Checksum:iCBD984BC348E6B15
GO
Isoform 3 (identifier: Q15438-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: Missing.

Note: No experimental confirmation available.

Show »
Length:339
Mass (Da):39,470
Checksum:iC08318AD7469BD02
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3619TVYRISAPT → MFTGSQLRR in AAF37737. (PubMed:15489334)Curated
Sequence conflicti353 – 3619TVYRISAPT → MFTGSQLRR in AAF37738. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5959Missing in isoform 3. 1 PublicationVSP_055884Add
BLAST
Alternative sequencei273 – 2731Missing in isoform 2. CuratedVSP_006034

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85169 mRNA. Translation: AAA36602.1.
AK293894 mRNA. Translation: BAH11620.1.
AK316277 mRNA. Translation: BAH14648.1.
AC022966 Genomic DNA. No translation available.
AC099804 Genomic DNA. No translation available.
BC038385 mRNA. Translation: AAH38385.1.
BC050452 mRNA. Translation: AAH50452.1.
AF125362
, AF125350, AF125351, AF125352, AF125353, AF125354, AF125355, AF125356, AF125357, AF125359, AF125360, AF125361 Genomic DNA. Translation: AAF37737.1.
AF125362
, AF125350, AF125351, AF125352, AF125353, AF125354, AF125355, AF125356, AF125357, AF125358, AF125359, AF125360, AF125361 Genomic DNA. Translation: AAF37738.1.
CCDSiCCDS32754.1. [Q15438-2]
CCDS42392.2. [Q15438-1]
PIRiS24168.
RefSeqiNP_001278947.1. NM_001292018.1. [Q15438-3]
NP_001278948.1. NM_001292019.1. [Q15438-3]
NP_004753.1. NM_004762.3. [Q15438-1]
NP_059430.2. NM_017456.3. [Q15438-2]
UniGeneiHs.191215.

Genome annotation databases

EnsembliENST00000361101; ENSP00000354398; ENSG00000108669. [Q15438-1]
ENST00000446868; ENSP00000389095; ENSG00000108669. [Q15438-1]
ENST00000585509; ENSP00000465940; ENSG00000108669. [Q15438-3]
ENST00000589297; ENSP00000466512; ENSG00000108669. [Q15438-3]
ENST00000591455; ENSP00000465665; ENSG00000108669. [Q15438-2]
GeneIDi9267.
KEGGihsa:9267.
UCSCiuc002jvw.3. human. [Q15438-2]
uc010wtw.1. human. [Q15438-1]

Polymorphism databases

DMDMi2498175.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85169 mRNA. Translation: AAA36602.1 .
AK293894 mRNA. Translation: BAH11620.1 .
AK316277 mRNA. Translation: BAH14648.1 .
AC022966 Genomic DNA. No translation available.
AC099804 Genomic DNA. No translation available.
BC038385 mRNA. Translation: AAH38385.1 .
BC050452 mRNA. Translation: AAH50452.1 .
AF125362
, AF125350 , AF125351 , AF125352 , AF125353 , AF125354 , AF125355 , AF125356 , AF125357 , AF125359 , AF125360 , AF125361 Genomic DNA. Translation: AAF37737.1 .
AF125362
, AF125350 , AF125351 , AF125352 , AF125353 , AF125354 , AF125355 , AF125356 , AF125357 , AF125358 , AF125359 , AF125360 , AF125361 Genomic DNA. Translation: AAF37738.1 .
CCDSi CCDS32754.1. [Q15438-2 ]
CCDS42392.2. [Q15438-1 ]
PIRi S24168.
RefSeqi NP_001278947.1. NM_001292018.1. [Q15438-3 ]
NP_001278948.1. NM_001292019.1. [Q15438-3 ]
NP_004753.1. NM_004762.3. [Q15438-1 ]
NP_059430.2. NM_017456.3. [Q15438-2 ]
UniGenei Hs.191215.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BC9 NMR - A 58-256 [» ]
4A4P X-ray 2.00 A/B 63-248 [» ]
ProteinModelPortali Q15438.
SMRi Q15438. Positions 58-391.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114688. 12 interactions.
IntActi Q15438. 3 interactions.
MINTi MINT-3031502.
STRINGi 9606.ENSP00000354398.

PTM databases

PhosphoSitei Q15438.

Polymorphism databases

DMDMi 2498175.

Proteomic databases

MaxQBi Q15438.
PaxDbi Q15438.
PRIDEi Q15438.

Protocols and materials databases

DNASUi 9267.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361101 ; ENSP00000354398 ; ENSG00000108669 . [Q15438-1 ]
ENST00000446868 ; ENSP00000389095 ; ENSG00000108669 . [Q15438-1 ]
ENST00000585509 ; ENSP00000465940 ; ENSG00000108669 . [Q15438-3 ]
ENST00000589297 ; ENSP00000466512 ; ENSG00000108669 . [Q15438-3 ]
ENST00000591455 ; ENSP00000465665 ; ENSG00000108669 . [Q15438-2 ]
GeneIDi 9267.
KEGGi hsa:9267.
UCSCi uc002jvw.3. human. [Q15438-2 ]
uc010wtw.1. human. [Q15438-1 ]

Organism-specific databases

CTDi 9267.
GeneCardsi GC17M076670.
HGNCi HGNC:9501. CYTH1.
HPAi HPA047498.
MIMi 182115. gene.
neXtProti NX_Q15438.
PharmGKBi PA164718528.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5307.
GeneTreei ENSGT00760000119036.
HOGENOMi HOG000253023.
HOVERGENi HBG002647.
InParanoidi Q15438.
KOi K18441.
OMAi VGLHEFT.
OrthoDBi EOG7RBZ9C.
PhylomeDBi Q15438.
TreeFami TF352091.

Miscellaneous databases

ChiTaRSi CYTH1. human.
EvolutionaryTracei Q15438.
GeneWikii CYTH1.
GenomeRNAii 9267.
NextBioi 34739.
PROi Q15438.
SOURCEi Search...

Gene expression databases

Bgeei Q15438.
CleanExi HS_CYTH1.
ExpressionAtlasi Q15438. baseline and differential.
Genevestigatori Q15438.

Family and domain databases

Gene3Di 1.10.1000.11. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF01369. Sec7. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00222. Sec7. 1 hit.
[Graphical view ]
SUPFAMi SSF48425. SSF48425. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS50190. SEC7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7."
    Liu L., Pohajdak B.
    Biochim. Biophys. Acta 1132:75-78(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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 3).
    Tissue: Cerebellum.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [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: Skin and Testis.
  5. "Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors."
    Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K., Kirby M., Moss J., Vaughan M.
    J. Biol. Chem. 275:3221-3230(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-398, FUNCTION, ALTERNATIVE SPLICING.
  6. "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)."
    Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W., Moss J., Vaughan M.
    J. Biol. Chem. 275:21331-21339(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM23.
  7. Cited for: INTERACTION WITH CYTIP.
  8. "The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane."
    Hofmann I., Thompson A., Sanderson C.M., Munro S.
    Curr. Biol. 17:711-716(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1."
    Betz S.F., Schnuchel A., Wang H., Olejniczak E.T., Meadows R.P., Lipsky B.P., Harris E.A., Staunton D.E., Fesik S.W.
    Proc. Natl. Acad. Sci. U.S.A. 95:7909-7914(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 58-256, FUNCTION, MUTAGENESIS OF GLU-157; TYR-187 AND MET-195.

Entry informationi

Entry nameiCYH1_HUMAN
AccessioniPrimary (citable) accession number: Q15438
Secondary accession number(s): A6NFW7
, B7Z1T4, Q9P123, Q9P124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 140 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 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3