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Protein

Glucosidase 2 subunit beta

Gene

PRKCSH

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

Functioni

Regulatory subunit of glucosidase II.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi213 – 236241PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. ion channel binding Source: UniProtKB
  3. phosphoprotein binding Source: UniProtKB
  4. protein kinase C binding Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. innate immune response Source: Reactome
  3. intracellular signal transduction Source: UniProtKB
  4. N-glycan processing Source: InterPro
  5. post-translational protein modification Source: Reactome
  6. protein folding Source: Reactome
  7. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.84. 2681.
ReactomeiREACT_23810. Calnexin/calreticulin cycle.
REACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
REACT_25195. Advanced glycosylation endproduct receptor signaling.
SignaLinkiP14314.
UniPathwayiUPA00957.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucosidase 2 subunit beta
Alternative name(s):
80K-H protein
Glucosidase II subunit beta
Protein kinase C substrate 60.1 kDa protein heavy chain
Short name:
PKCSH
Gene namesi
Name:PRKCSH
Synonyms:G19P1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9411. PRKCSH.

Subcellular locationi

Endoplasmic reticulum PROSITE-ProRule annotation

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. intracellular Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Polycystic liver disease2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA hepatobiliary disease characterized by overgrowth of biliary epithelium and supportive connective tissue, resulting in multiple liver cysts.

See also OMIM:174050

Organism-specific databases

MIMi174050. phenotype.
Orphaneti2924. Isolated polycystic liver disease.
PharmGKBiPA33774.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 14141 PublicationAdd
BLAST
Chaini15 – 528514Glucosidase 2 subunit betaPRO_0000004143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
Modified residuei89 – 891Phosphoserine; by PKCSequence Analysis
Modified residuei166 – 1661N6-succinyllysineBy similarity
Modified residuei383 – 3831Phosphoserine; by PKCSequence Analysis
Modified residuei390 – 3901Phosphoserine; by PKCSequence Analysis
Modified residuei434 – 4341Phosphoserine; by PKCSequence Analysis
Glycosylationi476 – 4761N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP14314.
PaxDbiP14314.
PRIDEiP14314.

PTM databases

PhosphoSiteiP14314.

Miscellaneous databases

PMAP-CutDBP14314.

Expressioni

Gene expression databases

BgeeiP14314.
CleanExiHS_PRKCSH.
ExpressionAtlasiP14314. baseline and differential.
GenevestigatoriP14314.

Organism-specific databases

HPAiCAB004465.
HPA041940.
HPA043560.

Interactioni

Subunit structurei

Heterodimer of a catalytic alpha subunit (GANAB) and a beta subunit (PRKCSH). Binds glycosylated PTPRC (By similarity).By similarity

Protein-protein interaction databases

BioGridi111575. 45 interactions.
IntActiP14314. 13 interactions.
MINTiMINT-1380114.
STRINGi9606.ENSP00000252455.

Structurei

3D structure databases

ProteinModelPortaliP14314.
SMRiP14314. Positions 423-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini209 – 24436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini245 – 29046EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini413 – 46856PRKCSHAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi525 – 5284Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi313 – 33624Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 PRKCSH domain.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG289998.
GeneTreeiENSGT00510000047770.
HOGENOMiHOG000007805.
HOVERGENiHBG051738.
InParanoidiP14314.
KOiK08288.
OrthoDBiEOG7DZ8JX.
PhylomeDBiP14314.
TreeFamiTF329550.

Family and domain databases

Gene3Di2.70.130.10. 1 hit.
4.10.400.10. 2 hits.
InterProiIPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR026874. Glucosidase_2_bsu.
IPR002172. LDrepeatLR_classA_rpt.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR028146. PRKCSH_N.
[Graphical view]
PANTHERiPTHR12630:SF1. PTHR12630:SF1. 1 hit.
PfamiPF13202. EF-hand_5. 2 hits.
PF12999. PRKCSH-like. 1 hit.
[Graphical view]
SMARTiSM00192. LDLa. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 1 hit.
SSF57424. SSF57424. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00014. ER_TARGET. 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. AlignAdd to basket

Isoform 1 (identifier: P14314-1) [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
MLLPLLLLLP MCWAVEVKRP RGVSLTNHHF YDESKPFTCL DGSATIPFDQ
60 70 80 90 100
VNDDYCDCKD GSDEPGTAAC PNGSFHCTNT GYKPLYIPSN RVNDGVCDCC
110 120 130 140 150
DGTDEYNSGV ICENTCKEKG RKERESLQQM AEVTREGFRL KKILIEDWKK
160 170 180 190 200
AREEKQKKLI ELQAGKKSLE DQVEMLRTVK EEAEKPEREA KEQHQKLWEE
210 220 230 240 250
QLAAAKAQQE QELAADAFKE LDDDMDGTVS VTELQTHPEL DTDGDGALSE
260 270 280 290 300
AEAQALLSGD TQTDATSFYD RVWAAIRDKY RSEALPTDLP APSAPDLTEP
310 320 330 340 350
KEEQPPVPSS PTEEEEEEEE EEEEEAEEEE EEEDSEEAPP PLSPPQPASP
360 370 380 390 400
AEEDKMPPYD EQTQAFIDAA QEARNKFEEA ERSLKDMEES IRNLEQEISF
410 420 430 440 450
DFGPNGEFAY LYSQCYELTT NEYVYRLCPF KLVSQKPKLG GSPTSLGTWG
460 470 480 490 500
SWIGPDHDKF SAMKYEQGTG CWQGPNRSTT VRLLCGKETM VTSTTEPSRC
510 520
EYLMELMTPA ACPEPPPEAP TEDDHDEL
Length:528
Mass (Da):59,425
Last modified:October 17, 2006 - v2
Checksum:i8DAD9776037E878E
GO
Isoform 2 (identifier: P14314-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     337-346: EAPPPLSPPQ → VQGEQPK

Show »
Length:525
Mass (Da):59,178
Checksum:iABACF156C534F30E
GO

Sequence cautioni

The sequence AAH15154.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3251Missing in AAA52493 (PubMed:2793184).Curated
Sequence conflicti325 – 3251Missing in AAA98668 (PubMed:9043864).Curated
Sequence conflicti325 – 3251Missing in AAP88860 (Ref. 4) Curated
Sequence conflicti325 – 3251Missing in AAH13586 (PubMed:15057824).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741S → N.
Corresponds to variant rs10406672 [ dbSNP | Ensembl ].
VAR_028761
Natural varianti291 – 2911A → T.2 Publications
Corresponds to variant rs11557488 [ dbSNP | Ensembl ].
VAR_028762
Natural varianti338 – 3381A → G.
Corresponds to variant rs35847588 [ dbSNP | Ensembl ].
VAR_048658

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei337 – 34610EAPPPLSPPQ → VQGEQPK in isoform 2. 2 PublicationsVSP_043749

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03075 mRNA. Translation: AAA52493.1.
U50326
, U50317, U50318, U50319, U50320, U50321, U50322, U50323, U50324, U50325 Genomic DNA. Translation: AAA98668.1.
AF144075 mRNA. Translation: AAF66686.1.
BT009858 mRNA. Translation: AAP88860.1.
AK290433 mRNA. Translation: BAF83122.1.
AC008481 Genomic DNA. No translation available.
AC024575 Genomic DNA. No translation available.
BC013586 mRNA. Translation: AAH13586.2.
BC015154 mRNA. Translation: AAH15154.1. Different initiation.
CCDSiCCDS32911.1. [P14314-1]
CCDS45977.1. [P14314-2]
PIRiA32469.
RefSeqiNP_001001329.1. NM_001001329.2. [P14314-2]
NP_001276031.1. NM_001289102.1. [P14314-2]
NP_002734.2. NM_002743.3. [P14314-1]
UniGeneiHs.610830.

Genome annotation databases

EnsembliENST00000587327; ENSP00000466012; ENSG00000130175. [P14314-2]
ENST00000589838; ENSP00000465461; ENSG00000130175. [P14314-1]
ENST00000591462; ENSP00000465489; ENSG00000130175. [P14314-2]
GeneIDi5589.
KEGGihsa:5589.
UCSCiuc002mrt.3. human. [P14314-1]
uc002mru.3. human. [P14314-2]

Polymorphism databases

DMDMi116242499.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03075 mRNA. Translation: AAA52493.1.
U50326
, U50317, U50318, U50319, U50320, U50321, U50322, U50323, U50324, U50325 Genomic DNA. Translation: AAA98668.1.
AF144075 mRNA. Translation: AAF66686.1.
BT009858 mRNA. Translation: AAP88860.1.
AK290433 mRNA. Translation: BAF83122.1.
AC008481 Genomic DNA. No translation available.
AC024575 Genomic DNA. No translation available.
BC013586 mRNA. Translation: AAH13586.2.
BC015154 mRNA. Translation: AAH15154.1. Different initiation.
CCDSiCCDS32911.1. [P14314-1]
CCDS45977.1. [P14314-2]
PIRiA32469.
RefSeqiNP_001001329.1. NM_001001329.2. [P14314-2]
NP_001276031.1. NM_001289102.1. [P14314-2]
NP_002734.2. NM_002743.3. [P14314-1]
UniGeneiHs.610830.

3D structure databases

ProteinModelPortaliP14314.
SMRiP14314. Positions 423-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111575. 45 interactions.
IntActiP14314. 13 interactions.
MINTiMINT-1380114.
STRINGi9606.ENSP00000252455.

PTM databases

PhosphoSiteiP14314.

Polymorphism databases

DMDMi116242499.

Proteomic databases

MaxQBiP14314.
PaxDbiP14314.
PRIDEiP14314.

Protocols and materials databases

DNASUi5589.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000587327; ENSP00000466012; ENSG00000130175. [P14314-2]
ENST00000589838; ENSP00000465461; ENSG00000130175. [P14314-1]
ENST00000591462; ENSP00000465489; ENSG00000130175. [P14314-2]
GeneIDi5589.
KEGGihsa:5589.
UCSCiuc002mrt.3. human. [P14314-1]
uc002mru.3. human. [P14314-2]

Organism-specific databases

CTDi5589.
GeneCardsiGC19P011546.
HGNCiHGNC:9411. PRKCSH.
HPAiCAB004465.
HPA041940.
HPA043560.
MIMi174050. phenotype.
177060. gene.
neXtProtiNX_P14314.
Orphaneti2924. Isolated polycystic liver disease.
PharmGKBiPA33774.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289998.
GeneTreeiENSGT00510000047770.
HOGENOMiHOG000007805.
HOVERGENiHBG051738.
InParanoidiP14314.
KOiK08288.
OrthoDBiEOG7DZ8JX.
PhylomeDBiP14314.
TreeFamiTF329550.

Enzyme and pathway databases

UniPathwayiUPA00957.
BRENDAi3.2.1.84. 2681.
ReactomeiREACT_23810. Calnexin/calreticulin cycle.
REACT_23878. N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
REACT_25195. Advanced glycosylation endproduct receptor signaling.
SignaLinkiP14314.

Miscellaneous databases

ChiTaRSiPRKCSH. human.
GeneWikiiPRKCSH.
GenomeRNAii5589.
NextBioi21678.
PMAP-CutDBP14314.
PROiP14314.
SOURCEiSearch...

Gene expression databases

BgeeiP14314.
CleanExiHS_PRKCSH.
ExpressionAtlasiP14314. baseline and differential.
GenevestigatoriP14314.

Family and domain databases

Gene3Di2.70.130.10. 1 hit.
4.10.400.10. 2 hits.
InterProiIPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR026874. Glucosidase_2_bsu.
IPR002172. LDrepeatLR_classA_rpt.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
IPR028146. PRKCSH_N.
[Graphical view]
PANTHERiPTHR12630:SF1. PTHR12630:SF1. 1 hit.
PfamiPF13202. EF-hand_5. 2 hits.
PF12999. PRKCSH-like. 1 hit.
[Graphical view]
SMARTiSM00192. LDLa. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 1 hit.
SSF57424. SSF57424. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80K protein."
    Sakai K., Masamichi H., Minoshima S., Kudoh J., Fukuyama R., Shimizu N.
    Genomics 5:309-315(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "A 3-Mb region for the familial hemiplegic migraine locus on 19p13.1-p13.2: exclusion of PRKCSH as a candidate gene."
    Ophoff R.A., Terwindt G.M., Vergouwe M.N., van Eijk R., Mohrenweiser H., Litt M., Hofker M.H., Haan J., Ferrari M.D., Frants R.R.
    Eur. J. Hum. Genet. 4:321-328(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo."
    Pelletier M.F., Marcil A., Sevigny G., Jakob C.A., Tessier D.C., Chevet E., Menard R., Bergeron J.J.M., Thomas D.Y.
    Glycobiology 10:815-827(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GANAB, SUBCELLULAR LOCATION.
    Tissue: Lymphocyte.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-528 (ISOFORM 1), VARIANT THR-291.
  5. "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).
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] OF 22-528 (ISOFORM 2), VARIANT THR-291.
    Tissue: Lung.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 15-21.
    Tissue: Platelet.
  9. "Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease."
    Li A., Davila S., Furu L., Qian Q., Tian X., Kamath P.S., King B.F., Torres V.E., Somlo S.
    Am. J. Hum. Genet. 72:691-703(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PCLD.
  10. "Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease."
    Drenth J.P.H., te Morsche R.H.M., Smink R., Bonifacino J.S., Jansen J.B.M.J.
    Nat. Genet. 33:345-347(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PCLD.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiGLU2B_HUMAN
AccessioniPrimary (citable) accession number: P14314
Secondary accession number(s): A8K318
, Q96BU9, Q96D06, Q9P0W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 17, 2006
Last modified: March 4, 2015
This is version 164 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.