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Protein

Cytohesin-interacting protein

Gene

CYTIP

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

Functioni

By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm.

GO - Biological processi

  1. regulation of cell adhesion Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Cytohesin-interacting protein
Alternative name(s):
Cytohesin binder and regulator
Short name:
CYBR
Cytohesin-associated scaffolding protein
Short name:
CASP
Cytohesin-binding protein HE
Short name:
Cbp HE
Pleckstrin homology Sec7 and coiled-coil domains-binding protein
Gene namesi
Name:CYTIP
Synonyms:PSCDBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9506. CYTIP.

Subcellular locationi

Cytoplasm. Early endosome
Note: Recruited from the cytosol to endosomes by SNX27.

GO - Cellular componenti

  1. cell cortex Source: MGI
  2. cytoplasm Source: HPA
  3. early endosome Source: UniProtKB-SubCell
  4. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 821K → E: No membrane-association. No change in the binding to CYTH1; when associated with A-90 and A-92. 1 Publication
Mutagenesisi90 – 901F → A: No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-92. 1 Publication
Mutagenesisi92 – 921I → A: No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-90. 1 Publication

Organism-specific databases

PharmGKBiPA164718652.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Cytohesin-interacting proteinPRO_0000097061Add
BLAST

Proteomic databases

MaxQBiO60759.
PaxDbiO60759.
PRIDEiO60759.

PTM databases

PhosphoSiteiO60759.

Expressioni

Tissue specificityi

Expressed in lymph nodes, thymus, spleen, lung, peripheral blood leukocytes and bone marrow.2 Publications

Inductioni

By TNF and bacterial lipopolysaccharides (LPS).1 Publication

Gene expression databases

BgeeiO60759.
CleanExiHS_CYTIP.
ExpressionAtlasiO60759. baseline and differential.
GenevestigatoriO60759.

Organism-specific databases

HPAiHPA007191.

Interactioni

Subunit structurei

Interacts with CYTH1 and SNX27.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CYTH1Q154382EBI-997814,EBI-997830

Protein-protein interaction databases

BioGridi114961. 9 interactions.
IntActiO60759. 4 interactions.
MINTiMINT-6176803.
STRINGi9606.ENSP00000264192.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi77 – 815Combined sources
Beta strandi89 – 946Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi109 – 1146Combined sources
Helixi119 – 1235Combined sources
Helixi144 – 15310Combined sources
Turni154 – 1563Combined sources
Beta strandi157 – 1615Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z17X-ray2.70A67-163[»]
ProteinModelPortaliO60759.
SMRiO60759. Positions 70-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60759.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 16690PDZPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni166 – 18823Interaction with CYTH1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili166 – 18823Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi241 – 32383Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG244814.
GeneTreeiENSGT00530000063734.
HOGENOMiHOG000231871.
HOVERGENiHBG053061.
InParanoidiO60759.
OMAiEMCTLIC.
OrthoDBiEOG72NRQP.
PhylomeDBiO60759.
TreeFamiTF316315.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60759-1) [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
MSLQRLLQHS SNGNLADFCA GPAYSSYSTL TGSLTMDDNR RIQMLADTVA
60 70 80 90 100
TLPRGRKQLA LTRSSSLSDF SWSQRKLVTV EKQDNETFGF EIQSYRPQNQ
110 120 130 140 150
NACSSEMFTL ICKIQEDSPA HCAGLQAGDV LANINGVSTE GFTYKQVVDL
160 170 180 190 200
IRSSGNLLTI ETLNGTMILK RTELEAKLQV LKQTLKQKWV EYRSLQLQEH
210 220 230 240 250
RLLHGDAANC PSLENMDLDE LSLFGPLPGP GPALVDRNRL SSESSCKSWL
260 270 280 290 300
SSMTMDSEDG YQTCVSEDSS RGAFSRQTST DDECFIPKEG DDFLRRSSSR
310 320 330 340 350
RNRSISNTSS GSMSPLWEGN LSSMFGTLPR KSRKGSVRKQ LLKFIPGLHR

AVEEEESRF
Length:359
Mass (Da):40,010
Last modified:September 27, 2005 - v2
Checksum:i76F0E0ED02EDD8C2
GO
Isoform 2 (identifier: O60759-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Note: No experimental confirmation available.

Show »
Length:253
Mass (Da):28,172
Checksum:iCE3E6B4FB0C6FA26
GO

Sequence cautioni

The sequence AAA16575.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti278 – 2781T → Q in AAA16575. (PubMed:8241278)Curated
Sequence conflicti339 – 3413KQL → RVA in AAA16575. (PubMed:8241278)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371D → N.1 Publication
Corresponds to variant rs1042038 [ dbSNP | Ensembl ].
VAR_023534
Natural varianti83 – 831Q → E.
Corresponds to variant rs2229345 [ dbSNP | Ensembl ].
VAR_051287
Natural varianti329 – 3291P → S Found in a renal cell carcinoma case; somatic mutation. 1 Publication
VAR_064706

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 106106Missing in isoform 2. 1 PublicationVSP_055502Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068836 mRNA. Translation: AAC19129.1.
AK301544 mRNA. Translation: BAG63041.1.
AC019201 Genomic DNA. Translation: AAY14898.1.
BC036449 mRNA. Translation: AAH36449.1.
L06633 mRNA. Translation: AAA16575.1. Different initiation.
CCDSiCCDS2204.1. [O60759-1]
PIRiS43424.
RefSeqiNP_004279.3. NM_004288.4. [O60759-1]
UniGeneiHs.270.

Genome annotation databases

EnsembliENST00000264192; ENSP00000264192; ENSG00000115165. [O60759-1]
GeneIDi9595.
KEGGihsa:9595.
UCSCiuc002tzj.1. human. [O60759-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068836 mRNA. Translation: AAC19129.1.
AK301544 mRNA. Translation: BAG63041.1.
AC019201 Genomic DNA. Translation: AAY14898.1.
BC036449 mRNA. Translation: AAH36449.1.
L06633 mRNA. Translation: AAA16575.1. Different initiation.
CCDSiCCDS2204.1. [O60759-1]
PIRiS43424.
RefSeqiNP_004279.3. NM_004288.4. [O60759-1]
UniGeneiHs.270.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z17X-ray2.70A67-163[»]
ProteinModelPortaliO60759.
SMRiO60759. Positions 70-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114961. 9 interactions.
IntActiO60759. 4 interactions.
MINTiMINT-6176803.
STRINGi9606.ENSP00000264192.

PTM databases

PhosphoSiteiO60759.

Proteomic databases

MaxQBiO60759.
PaxDbiO60759.
PRIDEiO60759.

Protocols and materials databases

DNASUi9595.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264192; ENSP00000264192; ENSG00000115165. [O60759-1]
GeneIDi9595.
KEGGihsa:9595.
UCSCiuc002tzj.1. human. [O60759-1]

Organism-specific databases

CTDi9595.
GeneCardsiGC02M158271.
HGNCiHGNC:9506. CYTIP.
HPAiHPA007191.
MIMi604448. gene.
neXtProtiNX_O60759.
PharmGKBiPA164718652.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG244814.
GeneTreeiENSGT00530000063734.
HOGENOMiHOG000231871.
HOVERGENiHBG053061.
InParanoidiO60759.
OMAiEMCTLIC.
OrthoDBiEOG72NRQP.
PhylomeDBiO60759.
TreeFamiTF316315.

Miscellaneous databases

EvolutionaryTraceiO60759.
GeneWikiiPSCDBP.
GenomeRNAii9595.
NextBioi35475724.
PROiO60759.
SOURCEiSearch...

Gene expression databases

BgeeiO60759.
CleanExiHS_CYTIP.
ExpressionAtlasiO60759. baseline and differential.
GenevestigatoriO60759.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH CYTH1.
  2. "Attenuation of cell adhesion in lymphocytes is regulated by CYTIP, a protein which mediates signal complex sequestration."
    Boehm T., Hofer S., Winklehner P., Kellersch B., Geiger C., Trockenbacher A., Neyer S., Fiegl H., Ebner S., Ivarsson L., Schneider R., Kremmer E., Heufler C., Kolanus W.
    EMBO J. 22:1014-1024(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, DOMAIN, TISSUE SPECIFICITY, INTERACTION WITH CYTH1, MUTAGENESIS OF LYS-82; PHE-90 AND ILE-92.
  3. "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: Mammary gland.
  4. "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].
  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] (ISOFORM 1).
    Tissue: Testis.
  6. "Cloning a cDNA from human NK/T cells which codes for an unusual leucine zipper containing protein."
    Dixon B., Sahely B., Liu L., Pohajdak B.
    Biochim. Biophys. Acta 1216:321-324(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-359 (ISOFORM 1), VARIANT ASN-37.
    Tissue: Blood.
  7. "Sorting nexin 27 interacts with the Cytohesin associated scaffolding protein (CASP) in lymphocytes."
    MacNeil A.J., Mansour M., Pohajdak B.
    Biochem. Biophys. Res. Commun. 359:848-853(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SNX27.
  8. Cited for: VARIANT SER-329.

Entry informationi

Entry nameiCYTIP_HUMAN
AccessioniPrimary (citable) accession number: O60759
Secondary accession number(s): B4DWH9, Q15630, Q8NE32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 27, 2005
Last modified: February 4, 2015
This is version 110 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 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.