O60759 (CYTIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CYTIP
Synonyms:	PSCDBP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Interacts with CYTH1 and SNX27. Ref.1 Ref.2 Ref.6
Subcellular location	Cytoplasm. Early endosome. Note: Recruited from the cytosol to endosomes by SNX27. Ref.2 Ref.6
Tissue specificity	Expressed in lymph nodes, thymus, spleen, lung, peripheral blood leukocytes and bone marrow. Ref.1 Ref.2
Induction	By TNF and bacterial lipopolysaccharides (LPS). Ref.2
Sequence similarities	Contains 1 PDZ (DHR) domain.
Sequence caution	The sequence AAA16575.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Endosome
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of cell adhesion Inferred from direct assay Ref.2. Source: MGI
Cellular_component	cell cortex Inferred from direct assay Ref.2. Source: MGI early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CYTH1	Q15438	2	EBI-997814,EBI-997830

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 359

359

Cytohesin-interacting protein

PRO_0000097061

Regions

Domain

77 – 166

90

PDZ

Region

166 – 188

23

Interaction with CYTH1

Coiled coil

166 – 188

23

Potential

Compositional bias

241 – 323

83

Ser-rich

Natural variations

Natural variant

37

1

D → N. Ref.5
Corresponds to variant rs1042038 [ dbSNP | Ensembl ].

VAR_023534

Natural variant

83

1

Q → E.
Corresponds to variant rs2229345 [ dbSNP | Ensembl ].

VAR_051287

Natural variant

329

1

P → S Found in a renal cell carcinoma case; somatic mutation. Ref.7

VAR_064706

Experimental info

Mutagenesis

82

1

K → E: No membrane-association. No change in the binding to CYTH1; when associated with A-90 and A-92. Ref.2

Mutagenesis

90

1

F → A: No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-92. Ref.2

Mutagenesis

92

1

I → A: No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-90. Ref.2

Sequence conflict

278

1

T → Q in AAA16575. Ref.5

Sequence conflict

339 – 341

3

KQL → RVA in AAA16575. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

359

Helix Strand Turn

Details...

Beta strand

77 – 81

5

Beta strand

89 – 94

6

Beta strand

101 – 103

3

Beta strand

109 – 114

6

Helix

119 – 123

5

Helix

144 – 153

10

Turn

154 – 156

3

Beta strand

157 – 161

5

Sequences

	Sequence		Length	Mass (Da)
	O60759 [UniParc]. Last modified September 27, 2005. Version 2. Checksum: 76F0E0ED02EDD8C2	FASTA	359	40,010
	10 20 30 40 50 60 MSLQRLLQHS SNGNLADFCA GPAYSSYSTL TGSLTMDDNR RIQMLADTVA TLPRGRKQLA 70 80 90 100 110 120 LTRSSSLSDF SWSQRKLVTV EKQDNETFGF EIQSYRPQNQ NACSSEMFTL ICKIQEDSPA 130 140 150 160 170 180 HCAGLQAGDV LANINGVSTE GFTYKQVVDL IRSSGNLLTI ETLNGTMILK RTELEAKLQV 190 200 210 220 230 240 LKQTLKQKWV EYRSLQLQEH RLLHGDAANC PSLENMDLDE LSLFGPLPGP GPALVDRNRL 250 260 270 280 290 300 SSESSCKSWL SSMTMDSEDG YQTCVSEDSS RGAFSRQTST DDECFIPKEG DDFLRRSSSR 310 320 330 340 350 RNRSISNTSS GSMSPLWEGN LSSMFGTLPR KSRKGSVRKQ LLKFIPGLHR AVEEEESRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates its activity." Tang P., Cheng T.P., Agnello D., Wu C.-Y., Hissong B.D., Watford W.T., Ahn H.-J., Galon J., Moss J., Vaughan M., O'Shea J.J., Gadina M. Proc. Natl. Acad. Sci. U.S.A. 99:2625-2629(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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], SUBCELLULAR LOCATION, INDUCTION, DOMAIN, TISSUE SPECIFICITY, INTERACTION WITH CYTH1, MUTAGENESIS OF LYS-82; PHE-90 AND ILE-92.
[3]	"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].
[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]. Tissue: Testis.
[5]	"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, VARIANT ASN-37. Tissue: Blood.
[6]	"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.
[7]	"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A. Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-329.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF068836 mRNA. Translation: AAC19129.1.
AC019201 Genomic DNA. Translation: AAY14898.1.
BC036449 mRNA. Translation: AAH36449.1.
L06633 mRNA. Translation: AAA16575.1. Different initiation.

IPI

IPI00003591.

PIR

S43424.

RefSeq

NP_004279.3. NM_004288.4.

UniGene

Hs.270.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z17	X-ray	2.70	A	64-163	[»]

ProteinModelPortal

O60759.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60759. 4 interactions.

STRING

9606.ENSP00000264192.

PTM databases

PhosphoSite

O60759.

Proteomic databases

PaxDb

O60759.

PRIDE

O60759.

Protocols and materials databases

DNASU

9595.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264192; ENSP00000264192; ENSG00000115165.

GeneID

9595.

KEGG

hsa:9595.

UCSC

uc002tzj.1. human.

Organism-specific databases

CTD

9595.

GeneCards

GC02M158271.

HGNC

HGNC:9506. CYTIP.

HPA

HPA007191.

MIM

604448. gene.

neXtProt

NX_O60759.

PharmGKB

PA164718652.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG244814.

HOGENOM

HOG000231871.

HOVERGEN

HBG053061.

InParanoid

O60759.

OMA

TDDECFV.

OrthoDB

EOG4JQ3Z3.

PhylomeDB

O60759.

Gene expression databases

ArrayExpress

O60759.

Bgee

O60759.

CleanEx

HS_CYTIP.

Genevestigator

O60759.

GermOnline

ENSG00000115165. Homo sapiens.

Family and domain databases

InterPro

IPR001478. PDZ.
[Graphical view]

Pfam

PF00595. PDZ. 1 hit.
[Graphical view]

SMART

SM00228. PDZ. 1 hit.
[Graphical view]

SUPFAM

SSF50156. PDZ. 1 hit.

PROSITE

PS50106. PDZ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O60759.

GenomeRNAi

9595.

NextBio

36003.

SOURCE

Search...

Entry information

Entry name

CYTIP_HUMAN

Accession

Primary (citable) accession number: O60759
Secondary accession number(s): Q15630, Q8NE32

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	September 27, 2005
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.