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Protein

Prolactin regulatory element-binding protein

Gene

PREB

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

Functioni

Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription (By similarity). Guanine nucleotide exchange factor that activates SARA2. Required for the formation of COPII transport vesicles from the ER.By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. COPII vesicle coating Source: Reactome
  4. endoplasmic reticulum unfolded protein response Source: Reactome
  5. ER to Golgi vesicle-mediated transport Source: Reactome
  6. membrane organization Source: Reactome
  7. post-translational protein modification Source: Reactome
  8. protein N-linked glycosylation via asparagine Source: Reactome
  9. protein transport Source: UniProtKB-KW
  10. regulation of transcription, DNA-templated Source: ProtInc
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
REACT_18273. XBP1(S) activates chaperone genes.
SignaLinkiQ9HCU5.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolactin regulatory element-binding protein
Alternative name(s):
Mammalian guanine nucleotide exchange factor mSec12
Gene namesi
Name:PREB
Synonyms:SEC12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9356. PREB.

Subcellular locationi

Nucleus By similarity. Endoplasmic reticulum membrane By similarity; Single-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 388388CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei389 – 40921HelicalSequence AnalysisAdd
BLAST
Topological domaini410 – 4178LumenalSequence Analysis

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. Golgi membrane Source: GOC
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33727.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 417417Prolactin regulatory element-binding proteinPRO_0000051154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Nitrated tyrosineBy similarity

Keywords - PTMi

Nitration

Proteomic databases

MaxQBiQ9HCU5.
PaxDbiQ9HCU5.
PeptideAtlasiQ9HCU5.
PRIDEiQ9HCU5.

PTM databases

PhosphoSiteiQ9HCU5.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

BgeeiQ9HCU5.
CleanExiHS_PREB.
ExpressionAtlasiQ9HCU5. baseline and differential.
GenevestigatoriQ9HCU5.

Organism-specific databases

HPAiHPA013582.
HPA014133.

Interactioni

Subunit structurei

Binds SARA2.

Protein-protein interaction databases

BioGridi115419. 6 interactions.
IntActiQ9HCU5. 5 interactions.
MINTiMINT-4539832.
STRINGi9606.ENSP00000260643.

Structurei

3D structure databases

ProteinModelPortaliQ9HCU5.
SMRiQ9HCU5. Positions 152-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati152 – 19140WD 1Add
BLAST
Repeati194 – 23239WD 2Add
BLAST
Repeati298 – 33740WD 3Add
BLAST

Sequence similaritiesi

Contains 3 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, WD repeat

Phylogenomic databases

eggNOGiNOG309181.
GeneTreeiENSGT00390000018031.
HOGENOMiHOG000045302.
HOVERGENiHBG002027.
InParanoidiQ9HCU5.
KOiK14003.
OMAiKASVWQK.
OrthoDBiEOG7XM305.
PhylomeDBiQ9HCU5.
TreeFamiTF314383.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 2 hits.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HCU5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRRRAPELY RAPFPLYALQ VDPSTGLLIA AGGGGAAKTG IKNGVHFLQL
60 70 80 90 100
ELINGRLSAS LLHSHDTETR ATMNLALAGD ILAAGQDAHC QLLRFQAHQQ
110 120 130 140 150
QGNKAEKAGS KEQGPRQRKG AAPAEKKCGA ETQHEGLELR VENLQAVQTD
160 170 180 190 200
FSSDPLQKVV CFNHDNTLLA TGGTDGYVRV WKVPSLEKVL EFKAHEGEIE
210 220 230 240 250
DLALGPDGKL VTVGRDLKAS VWQKDQLVTQ LHWQENGPTF SSTPYRYQAC
260 270 280 290 300
RFGQVPDQPA GLRLFTVQIP HKRLRQPPPC YLTAWDGSNF LPLRTKSCGH
310 320 330 340 350
EVVSCLDVSE SGTFLGLGTV TGSVAIYIAF SLQCLYYVRE AHGIVVTDVA
360 370 380 390 400
FLPEKGRGPE LLGSHETALF SVAVDSRCQL HLLPSRRSVP VWLLLLLCVG
410
LIIVTILLLQ SAFPGFL
Length:417
Mass (Da):45,468
Last modified:November 23, 2004 - v2
Checksum:i7FD490A641202D19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191L → F in AAG01692. (PubMed:10920239)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226684 mRNA. Translation: AAG01692.1.
AF203687 mRNA. Translation: AAF19192.1.
AF227166 Genomic DNA. Translation: AAF74572.1.
AK023064 mRNA. Translation: BAB14385.1.
AC013403 Genomic DNA. Translation: AAX93170.1.
CH471053 Genomic DNA. Translation: EAX00627.1.
BC002765 mRNA. Translation: AAH02765.1.
BC012890 mRNA. Translation: AAH12890.1.
BC016472 mRNA. Translation: AAH16472.1.
BC041032 mRNA. Translation: AAH41032.1.
CCDSiCCDS1738.1.
RefSeqiNP_037520.1. NM_013388.4.
UniGeneiHs.279784.

Genome annotation databases

EnsembliENST00000260643; ENSP00000260643; ENSG00000138073.
GeneIDi10113.
KEGGihsa:10113.
UCSCiuc002rix.1. human.

Polymorphism databases

DMDMi55977881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226684 mRNA. Translation: AAG01692.1.
AF203687 mRNA. Translation: AAF19192.1.
AF227166 Genomic DNA. Translation: AAF74572.1.
AK023064 mRNA. Translation: BAB14385.1.
AC013403 Genomic DNA. Translation: AAX93170.1.
CH471053 Genomic DNA. Translation: EAX00627.1.
BC002765 mRNA. Translation: AAH02765.1.
BC012890 mRNA. Translation: AAH12890.1.
BC016472 mRNA. Translation: AAH16472.1.
BC041032 mRNA. Translation: AAH41032.1.
CCDSiCCDS1738.1.
RefSeqiNP_037520.1. NM_013388.4.
UniGeneiHs.279784.

3D structure databases

ProteinModelPortaliQ9HCU5.
SMRiQ9HCU5. Positions 152-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115419. 6 interactions.
IntActiQ9HCU5. 5 interactions.
MINTiMINT-4539832.
STRINGi9606.ENSP00000260643.

PTM databases

PhosphoSiteiQ9HCU5.

Polymorphism databases

DMDMi55977881.

Proteomic databases

MaxQBiQ9HCU5.
PaxDbiQ9HCU5.
PeptideAtlasiQ9HCU5.
PRIDEiQ9HCU5.

Protocols and materials databases

DNASUi10113.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260643; ENSP00000260643; ENSG00000138073.
GeneIDi10113.
KEGGihsa:10113.
UCSCiuc002rix.1. human.

Organism-specific databases

CTDi10113.
GeneCardsiGC02M027353.
HGNCiHGNC:9356. PREB.
HPAiHPA013582.
HPA014133.
MIMi606395. gene.
neXtProtiNX_Q9HCU5.
PharmGKBiPA33727.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG309181.
GeneTreeiENSGT00390000018031.
HOGENOMiHOG000045302.
HOVERGENiHBG002027.
InParanoidiQ9HCU5.
KOiK14003.
OMAiKASVWQK.
OrthoDBiEOG7XM305.
PhylomeDBiQ9HCU5.
TreeFamiTF314383.

Enzyme and pathway databases

ReactomeiREACT_12507. COPII (Coat Protein 2) Mediated Vesicle Transport.
REACT_18273. XBP1(S) activates chaperone genes.
SignaLinkiQ9HCU5.

Miscellaneous databases

ChiTaRSiPREB. human.
GeneWikiiPREB.
GenomeRNAii10113.
NextBioi38259.
PROiQ9HCU5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCU5.
CleanExiHS_PREB.
ExpressionAtlasiQ9HCU5. baseline and differential.
GenevestigatoriQ9HCU5.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 2 hits.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of human PREB; a gene that maps to a genomic region associated with trisomy 2p syndrome."
    Taylor Clelland C.L., Levy B., McKie J.M., Duncan A.M.V., Hirschhorn K., Bancroft C.
    Mamm. Genome 11:675-681(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
  2. "The human and mouse homologues of rat prolactin regulatory element binding protein."
    Edgar A.J., Polak J.M.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The gene structure and expression of human ABHD1: overlapping polyadenylation signal sequence with Sec12."
    Edgar A.J.
    BMC Genomics 4:18-18(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  4. "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].
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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].
    Tissue: Brain, Lung and Uterus.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPREB_HUMAN
AccessioniPrimary (citable) accession number: Q9HCU5
Secondary accession number(s): Q53SZ8, Q9UH94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 23, 2004
Last modified: January 7, 2015
This is version 124 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. 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.