SubmitCancel

Skip Header

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

P50238

- CRIP1_HUMAN

UniProt

P50238 - CRIP1_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

Cysteine-rich protein 1

Gene
CRIP1, CRIP, CRP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.

GO - Molecular functioni

  1. AT DNA binding Source: UniProtKB
  2. DNA binding, bending Source: UniProtKB
  3. peptide binding Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cellular response to antibiotic Source: UniProtKB
  3. cellular response to UV-B Source: UniProtKB
  4. heart development Source: UniProtKB
  5. immune response Source: UniProtKB
  6. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  7. prostate gland stromal morphogenesis Source: UniProtKB
  8. regulation of gene expression Source: UniProtKB
  9. response to organic substance Source: UniProtKB
  10. response to zinc ion Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine-rich protein 1
Short name:
CRP-1
Alternative name(s):
Cysteine-rich heart protein
Short name:
CRHP
Short name:
hCRHP
Cysteine-rich intestinal protein
Short name:
CRIP
Gene namesi
Name:CRIP1
Synonyms:CRIP, CRP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:2360. CRIP1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26878.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 7776Cysteine-rich protein 1PRO_0000075707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysine1 Publication
Modified residuei22 – 221N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP50238.
PaxDbiP50238.
PeptideAtlasiP50238.
PRIDEiP50238.

PTM databases

PhosphoSiteiP50238.

Expressioni

Gene expression databases

BgeeiP50238.
CleanExiHS_CRIP1.
GenevestigatoriP50238.

Organism-specific databases

HPAiHPA042462.

Interactioni

Protein-protein interaction databases

BioGridi107786. 5 interactions.
IntActiP50238. 3 interactions.
MINTiMINT-3018274.
STRINGi9606.ENSP00000332449.

Structurei

3D structure databases

ProteinModelPortaliP50238.
SMRiP50238. Positions 2-77.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6362LIM zinc-bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 709Gly-rich

Sequence similaritiesi

Keywords - Domaini

LIM domain

Phylogenomic databases

eggNOGiNOG246818.
HOGENOMiHOG000264233.
HOVERGENiHBG051118.
InParanoidiP50238.
OMAiCNKTLSA.
PhylomeDBiP50238.

Family and domain databases

Gene3Di2.10.110.10. 1 hit.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00132. LIM. 1 hit.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P50238-1 [UniParc]FASTAAdd to Basket

« Hide

MPKCPKCNKE VYFAERVTSL GKDWHRPCLK CEKCGKTLTS GGHAEHEGKP   50
YCNHPCYAAM FGPKGFGRGG AESHTFK 77
Length:77
Mass (Da):8,533
Last modified:January 23, 2007 - v3
Checksum:iB342436418DBC021
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581A → V in AAA64537. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09770 mRNA. Translation: AAA64537.1.
U58630 mRNA. Translation: AAB61158.1.
BT007181 mRNA. Translation: AAP35845.1.
AL928654 Genomic DNA. No translation available.
BC002738 mRNA. Translation: AAH02738.1.
CCDSiCCDS10004.1.
PIRiG02666.
JC2431.
RefSeqiNP_001302.1. NM_001311.4.
UniGeneiHs.70327.

Genome annotation databases

EnsembliENST00000330233; ENSP00000332449; ENSG00000213145.
ENST00000392531; ENSP00000376315; ENSG00000213145.
ENST00000409393; ENSP00000386340; ENSG00000213145.
ENST00000603619; ENSP00000473914; ENSG00000270784.
ENST00000604460; ENSP00000474660; ENSG00000270784.
ENST00000604601; ENSP00000474287; ENSG00000270784.
GeneIDi1396.
KEGGihsa:1396.
UCSCiuc001yri.4. human.

Polymorphism databases

DMDMi20981688.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09770 mRNA. Translation: AAA64537.1 .
U58630 mRNA. Translation: AAB61158.1 .
BT007181 mRNA. Translation: AAP35845.1 .
AL928654 Genomic DNA. No translation available.
BC002738 mRNA. Translation: AAH02738.1 .
CCDSi CCDS10004.1.
PIRi G02666.
JC2431.
RefSeqi NP_001302.1. NM_001311.4.
UniGenei Hs.70327.

3D structure databases

ProteinModelPortali P50238.
SMRi P50238. Positions 2-77.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107786. 5 interactions.
IntActi P50238. 3 interactions.
MINTi MINT-3018274.
STRINGi 9606.ENSP00000332449.

PTM databases

PhosphoSitei P50238.

Polymorphism databases

DMDMi 20981688.

Proteomic databases

MaxQBi P50238.
PaxDbi P50238.
PeptideAtlasi P50238.
PRIDEi P50238.

Protocols and materials databases

DNASUi 1396.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330233 ; ENSP00000332449 ; ENSG00000213145 .
ENST00000392531 ; ENSP00000376315 ; ENSG00000213145 .
ENST00000409393 ; ENSP00000386340 ; ENSG00000213145 .
ENST00000603619 ; ENSP00000473914 ; ENSG00000270784 .
ENST00000604460 ; ENSP00000474660 ; ENSG00000270784 .
ENST00000604601 ; ENSP00000474287 ; ENSG00000270784 .
GeneIDi 1396.
KEGGi hsa:1396.
UCSCi uc001yri.4. human.

Organism-specific databases

CTDi 1396.
GeneCardsi GC14P105952.
HGNCi HGNC:2360. CRIP1.
HPAi HPA042462.
MIMi 123875. gene.
neXtProti NX_P50238.
PharmGKBi PA26878.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG246818.
HOGENOMi HOG000264233.
HOVERGENi HBG051118.
InParanoidi P50238.
OMAi CNKTLSA.
PhylomeDBi P50238.

Miscellaneous databases

GeneWikii CRIP1.
GenomeRNAii 1396.
NextBioi 5713.
PROi P50238.
SOURCEi Search...

Gene expression databases

Bgeei P50238.
CleanExi HS_CRIP1.
Genevestigatori P50238.

Family and domain databases

Gene3Di 2.10.110.10. 1 hit.
InterProi IPR001781. Znf_LIM.
[Graphical view ]
Pfami PF00412. LIM. 1 hit.
[Graphical view ]
SMARTi SM00132. LIM. 1 hit.
[Graphical view ]
PROSITEi PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a cDNA that codes for a LIM-containing protein which is developmentally regulated in heart."
    Tsui S.K.W., Yam N.Y., Lee C.-Y., Waye M.M.Y.
    Biochem. Biophys. Res. Commun. 205:497-505(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Human cysteine-rich intestinal protein: cDNA cloning and expression of recombinant protein and identification in human peripheral blood mononuclear cells."
    Khoo C., Blanchard R.K., Sullivan V.K., Cousins R.J.
    Protein Expr. Purif. 9:379-387(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Small intestine.
  3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Uterus.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCRIP1_HUMAN
AccessioniPrimary (citable) accession number: P50238
Secondary accession number(s): H3BPI2
, Q13628, Q53XY7, Q96J34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 121 of the entry and version 3 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 14
    Human chromosome 14: 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